]> Dumontier Lab application/rdf+xml Michel Dumontier Enzyme Commission Ontology (primitive) Biochemical reactions as defined by the enzyme commission. 2007-10-01 en 1.0 Oxidoreductases Acting on the CH-OH group of donors With NAD(+) or NADP(+) as acceptor Aldehyde reductase Alcohol dehydrogenase The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols. Acts on primary or secondary alcohols or hemiacetals. Zinc or iron An alcohol + NAD(+) = an aldehyde or ketone + NADH. L-xylulose reductase http://purl.uniprot.org/mim/260800 Xylitol + NADP(+) = L-xylulose + NADPH. 3-oxoacyl-[acyl-carrier-protein] reductase Exhibits a marked preference for [acyl-carrier-protein] derivatives over CoA derivatives as substrates. (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH. Palmitoyldihydroxyacetone-phosphate reductase Acylglycerone-phosphate reductase Also acts on alkylglycerone 3-phosphate and alkylglycerol 3-phosphate. 1-palmitoylglycerol 3-phosphate + NADP(+) = palmitoylglycerone phosphate + NADPH. 3-dehydrosphinganine reductase KTS reductase 3-oxosphinganine reductase D-3-oxosphinganine reductase 3-ketosphinganine reductase 3-oxosphinganine:NADPH oxidoreductase D-3-oxosphinganine:B-NADPH oxidoreductase D-3-dehydrosphinganine reductase DSR Sphinganine + NADP(+) = 3-dehydrosphinganine + NADPH. L-threonine 3-dehydrogenase L-threonine + NAD(+) = L-2-amino-3-oxobutanoate + NADH. The product spontaneously decarboxylates to aminoacetone. Hydroxyproline oxidase 4-oxoproline reductase http://purl.uniprot.org/mim/237000 4-hydroxy-L-proline + NAD(+) = 4-oxoproline + NADH. Retinol dehydrogenase http://purl.uniprot.org/mim/136800 Retinol + NAD(+) = retinal + NADH. Panthothenase Pantoate 4-dehydrogenase (R)-pantoate + NAD(+) = (R)-4-dehydropantoate + NADH. Pyridoxal 4-dehydrogenase Pyridoxal + NAD(+) = 4-pyridoxolactone + NADH. The enzyme acts on the hemiacetal form of the substrate. Carnitine 3-dehydrogenase Carnitine + NAD(+) = 3-dehydrocarnitine + NADH. D-arabinitol 4-dehydrogenase D-arabinitol + NAD(+) = D-xylulose + NADH. Indolelactate dehydrogenase Indole-3-lactate dehydrogenase (Indol-3-yl)lactate + NAD(+) = (indol-3-yl)pyruvate + NADH. 3-(imidazol-5-yl)lactate dehydrogenase (S)-3-(imidazol-5-yl)lactate + NAD(P)(+) = 3-(imidazol-5-yl)pyruvate + NAD(P)H. Indanol dehydrogenase Indan-1-ol + NAD(P)(+) = indanone + NAD(P)H. 3(20)-alpha-hydroxysteroids are also oxidized, more slowly. L-xylose 1-dehydrogenase Also oxidizes D-arabinose and D-lyxose. L-xylose + NADP(+) = L-xylono-1,4-lactone + NADPH. Apiose 1-reductase D-apiose reductase D-apiitol reductase D-apiitol + NAD(+) = D-apiose + NADH. NADP-pentose-dehydrogenase Ribose 1-dehydrogenase (NADP(+)) Also acts, more slowly, on D-xylose and other pentoses. D-ribose + NADP(+) + H(2)O = D-ribonate + NADPH. D-arabinose 1-dehydrogenase D-arabinose + NAD(+) = D-arabinono-1,4-lactone + NADH. D-arabinose 1-dehydrogenase (NAD(P)(+)) D-arabinose + NAD(P)(+) = D-arabinono-1,4-lactone + NAD(P)H. Also acts on L-galactose, 6-deoxy-and 3,6-dideoxy-L-galactose. Glucose 1-dehydrogenase (NAD(+)) D-glucose + NAD(+) = D-glucono-1,5-lactone + NADH. Glucose 1-dehydrogenase (NADP(+)) Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D-mannose. D-glucose + NADP(+) = D-glucono-1,5-lactone + NADPH. L-arabinitol 4-dehydrogenase L-arabinitol + NAD(+) = L-xylulose + NADH. Galactose 1-dehydrogenase (NADP(+)) D-galactose + NADP(+) = D-galactonolactone + NADPH. Also acts on L-arabinose, 6-deoxy-and 2-deoxy-D-galactose. Aldose 1-dehydrogenase D-aldose + NAD(+) = D-aldonolactone + NADH. Acts on D-glucose, 2-deoxy-and 6-deoxy-D-glucose, D-galactose, 6-deoxy-D-galactose, 2-deoxy-L-arabinose and D-xylose. (2S,3R)-aldose dehydrogenase D-threo-aldose 1-dehydrogenase L-fucose dehydrogenase The animal enzyme was also shown to act on L-arabinose, and the enzyme from Pseudomonas caryophylli on L-glucose. Acts on L-fucose, D-arabinose and L-xylose. A D-threo-aldose + NAD(+) = a D-threo-aldono-1,5-lactone + NADH. Sorbose 5-dehydrogenase (NADP(+)) 5-ketofructose reductase L-sorbose + NADP(+) = 5-dehydro-D-fructose + NADPH. 5-ketofructose reductase (NADP+) 5-ketofructose reductase (NADP(+)) Fructose 5-dehydrogenase (NADP(+)) D-fructose + NADP(+) = 5-dehydro-D-fructose + NADPH. 2-keto-3-deoxygluconate oxidoreductase 2-deoxy-D-gluconate 3-dehydrogenase 2-deoxy-D-gluconate + NAD(+) = 3-dehydro-2-deoxy-D-gluconate + NADH. 2-keto-3-deoxy-D-gluconate dehydrogenase 2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase 2-dehydro-3-deoxy-D-gluconate + NADP(+) = (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate + NADPH. 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase 2-keto-3-deoxygluconate dehydrogenase 2-dehydro-3-deoxy-D-gluconate + NAD(+) = (4S)-4,6-dihydroxy-2,5-dioxohexanoate + NADH. The enzyme from Pseudomonas acts equally well on NAD(+) or NADP(+), while those from Erwinia chrysanthemi and Escherichia coli are more specific for NAD(+). 5-ketogluconate 2-reductase L-idonate 2-dehydrogenase L-idonate + NADP(+) = 5-dehydro-D-gluconate + NADPH. L-threonic acid dehydrogenase L-threonate 3-dehydrogenase L-threonate + NAD(+) = 3-dehydro-L-threonate + NADH. L-arabinitol 2-dehydrogenase L-arabinitol 2-dehydrogenase (ribulose forming) L-arabinitol + NAD(+) = L-ribulose + NADH. 3-keto-L-gulonate dehydrogenase 3-dehydro-L-gulonate 2-dehydrogenase 2,3-diketo-L-gulonate reductase 3-dehydro-L-gulonate + NAD(P)(+) = (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate + NAD(P)H. Mannonate dehydrogenase Mannuronate reductase D-mannonate + NAD(P)(+) = D-mannuronate + NAD(P)H. GDP-mannose 6-dehydrogenase GDP-D-mannose + 2 NAD(+) + H(2)O = GDP-D-mannuronate + 2 NADH. Also uses the corresponding deoxynucleoside diphosphate derivative as a substrate. dTDP-4-keto-L-rhamnose reductase dTDP-4-dehydrorhamnose reductase dTDP-6-deoxy-L-mannose dehydrogenase In the reverse direction, reduction on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyzes epimerization at C-3 and C-5; the complex has been referred to as dTDP-L-rhamnose synthase. dTDP-6-deoxy-L-mannose + NADP(+) = dTDP-4-dehydro-6-deoxy-L-mannose + NADPH. dTDP-6-deoxy-L-talose 4-dehydrogenase Oxidation on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyzes epimerization at C-3 and C-5. dTDP-6-deoxy-L-talose + NADP(+) = dTDP-4-dehydro-6-deoxy-L-mannose + NADPH. GDP-6-deoxy-D-talose 4-dehydrogenase GDP-6-deoxy-D-talose + NAD(P)(+) = GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H. UDP-N-acetylglucosamine 6-dehydrogenase UDP-N-acetyl-D-glucosamine + 2 NAD(+) + H(2)O = UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH. Ribitol-5-phosphate 2-dehydrogenase D-ribitol 5-phosphate + NAD(P)(+) = D-ribulose 5-phosphate + NAD(P)H. NADP-dependent mannitol dehydrogenase Mannitol 2-dehydrogenase (NADP(+)) D-mannitol + NADP(+) = D-fructose + NADPH. Polyol dehydrogenase Glucitol dehydrogenase L-iditol 2-dehydrogenase Sorbitol dehydrogenase L-iditol + NAD(+) = L-sorbose + NADH. Also acts on D-glucitol (giving D-fructose) and other closely related sugar alcohols. http://purl.uniprot.org/mim/182500 Ketosephosphate reductase Glucitol-6-phosphate dehydrogenase Sorbitol-6-phosphate 2-dehydrogenase D-sorbitol 6-phosphate + NAD(+) = D-fructose 6-phosphate + NADH. 15-hydroxyprostaglandin dehydrogenase (NAD(+)) Acts on prostaglandins E(2), F(2-alpha) and B(1), but not on prostaglandin D(2) (cf. EC 1.1.1.196 and EC 1.1.1.197). (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprost-13-enoate + NAD(+) = (5Z,13E)-11-alpha-hydroxy-9,15-dioxoprost-13-enoate + NADH. D-pinitol dehydrogenase 1D-3-O-methyl-chiro-inositol + NADP(+) = 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADPH. Sequoyitol dehydrogenase 5-O-methyl-myo-inositol + NAD(+) = 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADH. Perillyl-alcohol dehydrogenase Oxidizes a number of primary alcohols with the alcohol group allylic to an endocyclic double bond and a 6-membered ring, either aromatic or hydroaromatic. Perillyl alcohol + NAD(+) = perillyl aldehyde + NADH. 3-beta-hydroxy-5-ene steroid dehydrogenase Progesterone reductase 3-beta-hydroxy-Delta(5)-steroid dehydrogenase Acts on 3-beta-hydroxyandrost-5-en-17-one to form androst-4-ene-3,17-dione and on 3-beta-hydroxypregn-5-en-20-one to form progesterone. http://purl.uniprot.org/mim/201810 A 3-beta-hydroxy-Delta(5)-steroid + NAD(+) = a 3-oxo-Delta(5)-steroid + NADH. 11-beta-hydroxysteroid dehydrogenase Corticosteroid 11-beta-dehydrogenase http://purl.uniprot.org/mim/207765 http://purl.uniprot.org/mim/604931 http://purl.uniprot.org/mim/218030 An 11-beta-hydroxysteroid + NADP(+) = an 11-oxosteroid + NADPH. 16-alpha-hydroxysteroid dehydrogenase A 16-alpha-hydroxysteroid + NAD(P)(+) = a 16-oxosteroid + NAD(P)H. Estradiol 17-alpha-dehydrogenase Estradiol-17-alpha + NAD(P)(+) = estrone + NAD(P)H. 20-alpha-hydroxysteroid dehydrogenase A-specific with respect to NAD(P)(+) (cf. EC 1.1.1.62). 17-alpha,20-alpha-dihydroxypregn-4-en-3-one + NAD(P)(+) = 17-alpha-hydroxyprogesterone + NAD(P)H. D-iditol 2-dehydrogenase D-iditol + NAD(+) = D-sorbose + NADH. Also converts xylitol into L-xylulose and L-glucitol into L-fructose. 21-hydroxysteroid dehydrogenase (NAD(+)) Pregnan-21-ol + NAD(+) = pregnan-21-al + NADH. Acts on a number of 21-hydroxycorticosteroids. 21-hydroxysteroid dehydrogenase (NADP(+)) NADP-21-hydroxysteroid dehydrogenase 21-hydroxy steroid dehydrogenase (nicotinamide adenine dinucleotide phosphate) 21-hydroxy steroid (nicotinamide adenine dinucleotide phosphate) dehydrogenase 21-hydroxy steroid dehydrogenase Acts on a number of 21-hydroxycorticosteroids. Pregnan-21-ol + NADP(+) = pregnan-21-al + NADPH. 3-alpha-hydroxy-5-beta-androstane-17-one 3-alpha-dehydrogenase Etiocholanolone 3-alpha-dehydrogenase 3-alpha-hydroxy-5-beta-androstane-17-one + NAD(+) = 5-beta-androstane-3,17-dione + NADH. Sepiapterin reductase 7,8-dihydrobiopterin + NADP(+) = sepiapterin + NADPH. http://purl.uniprot.org/mim/182125 Ureidoglycolate dehydrogenase (S)-ureidoglycolate + NAD(P)(+) = oxalureate + NAD(P)H. Glycerol 2-dehydrogenase (NADP(+)) Dihydroxyacetone reductase Glycerol + NADP(+) = glycerone + NADPH. 3-hydroxybutyryl-CoA dehydrogenase BHBD Beta-hydroxybutyryl-CoA dehydrogenase (S)-3-hydroxybutanoyl-CoA + NADP(+) = 3-acetoacetyl-CoA + NADPH. UDP-N-acetylmuramate dehydrogenase UDP-N-acetylglucosamine-enoylpyruvate reductase UDP-N-acetylenolpyruvoylglucosamine reductase Uridine diphospho-N-acetylglucosamine-enolpyruvate reductase UDP-GlcNAc-enoylpyruvate reductase Uridine diphosphoacetylpyruvoylglucosamine reductase Uridine-5'-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP-oxidoreductase FAD UDP-N-acetylmuramate + NADP(+) = UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH. Sodium dithionite, sodium borohydride and, to a lesser extent, NADH can replace NADPH. 7-alpha-hydroxysteroid dehydrogenase Catalyzes the oxidation of the 7-alpha-hydroxy group of bile acids and alcohols both in their free and conjugated forms. 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + NAD(+) = 3-alpha,12-alpha-dihydroxy-7-oxo-5-beta-cholanate + NADH. The Bacteroides fragilis and Clostridium enzymes can also utilize NADP(+). Galactitol 2-dehydrogenase Galactitol + NAD(+) = D-tagatose + NADH. Also converts other alditols containing an L-threo-configuration adjacent to a primary alcohol group into the corresponding sugars. Dihydrobunolol dehydrogenase Bunolol reductase (+-)-5-((tert-butylamino)-2'-hydroxypropoxy)-1,2,3,4-tetrahydro-1-naphthol + NADP(+) = (+-)-5-((tert-butylamino)-2'-hydroxypropoxy)-3,4-dihydro-1(2H)-naphthalenone + NADPH. Also acts, more slowly, with NAD(+). TEHC-NAD oxidoreductase Cholestanetetraol 26-dehydrogenase 5-beta-cholestane-3-alpha,7-alpha,12-alpha,26-tetraol + NAD(+) = 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-al + NADH. D-erythrulose reductase Erythrulose reductase Also acts, more slowly, with NAD(+). Erythritol + NADP(+) = D-erythrulose + NADPH. Cyclopentanol dehydrogenase Cyclopentanol + NAD(+) = cyclopentanone + NADH. 4-methylcyclohexanol and cyclohexanol can also act as substrates. Hexadecanol dehydrogenase The Euglena enzyme also oxidizes the corresponding aldehydes to fatty acids. Hexadecanol + NAD(+) = hexadecanal + NADH. The liver enzyme acts on long-chain alcohols from C(8) to C(16). 2-alkyn-1-ol dehydrogenase 2-butyne-1,4-diol + NAD(+) = 4-hydroxy-2-butynal + NADH. NADP(+) also acts as acceptor, but more slowly. Acts on a variety of 2-alkyn-1-ols, and also on 1,4-butanediol. Hydroxycyclohexanecarboxylate dehydrogenase Acts on hydroxycyclohexanecarboxylates that have an equatorial carboxy group at C-1, an axial hydroxy group at C-3 and an equatorial hydroxy or carbonyl group at C-4, including (-)-quinate and (-)-shikimate. (1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate + NAD(+) = (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate + NADH. Hydroxymalonate dehydrogenase Hydroxymalonate + NAD(+) = oxomalonate + NADH. 2-dehydropantoyl-lactone reductase (A-specific) 2-ketopantoyl lactone reductase Ketopantoyl lactone reductase 2-dehydropantolactone reductase (A-specific) The enzyme from Saccharomyces cerevisiae differs from that from Escherichia coli (EC 1.1.1.214), which is specific for the B-face of NADP, and in receptor requirements from EC 1.1.99.26. (R)-pantolactone + NADP(+) = 2-dehydropantolactone + NADPH. Ketopantoate reductase 2-dehydropantoate 2-reductase Ketopantoic acid reductase KPA reductase (R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH. Mannitol-1-phosphate 5-dehydrogenase D-mannitol 1-phosphate + NAD(+) = D-fructose 6-phosphate + NADH. 3-beta-hydroxy-4-beta-methylcholestenecarboxylate 3-dehydrogenase (decarboxylating) 3-beta-hydroxy-4-beta-methylcholestenoate dehydrogenase Sterol-4-alpha-carboxylate 3-dehydrogenase (decarboxylating) 3-beta-hydroxy-4-alpha-methylcholestenecarboxylate 3-dehydrogenase (decarboxylating) Sterol 4-alpha-carboxylic decarboxylase Also acts on 3-beta-hydroxy-5-alpha-cholest-7-ene-4-alpha-carboxylate. 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)(+) = 4-alpha-methyl-5-alpha-cholest-7-en-3-one + CO(2) + NAD(P)H. 2-ketoadipate reductase 2-oxoadipate reductase Alpha-ketoadipate reductase 2-hydroxyadipate + NAD(+) = 2-oxoadipate + NADH. L-rhamnose 1-dehydrogenase L-rhamnofuranose + NAD(+) = L-rhamno-1,4-lactone + NADH. Cyclohexane-1,2-diol dehydrogenase Also oxidizes, more slowly, the cis isomer and 2-hydroxycyclohexanone. Trans-cyclohexane-1,2-diol + NAD(+) = 2-hydroxycyclohexan-1-one + NADH. D-xylose 1-dehydrogenase NAD-D-xylose dehydrogenase NAD-linked D-xylose dehydrogenase D-xylose dehydrogenase D-xylose + NAD(+) = D-xylonolactone + NADH. 12-alpha-hydroxysteroid dehydrogenase Also acts on bile alcohols. 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + NADP(+) = 3-alpha,7-alpha-dihydroxy-12-oxo-5-beta-cholanate + NADPH. Catalyzes the oxidation of the 12-alpha-hydroxy group of bile acids, both in their free and conjugated form. Glycerol-3-phosphate 1-dehydrogenase (NADP(+)) sn-glycerol 3-phosphate + NADP(+) = D-glyceraldehyde 3-phosphate + NADPH. 3-hydroxy-2-methylbutyryl-CoA dehydrogenase 2-methyl-3-hydroxybutyryl-CoA dehydrogenase Also acts, more slowly, on (2S,3S)-2-hydroxy-3-methylpentanoyl-CoA. (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD(+) = 2-methylacetoacetyl-CoA + NADH. D-xylose-NADP dehydrogenase D-xylose 1-dehydrogenase (NADP(+)) D-xylose + NADP(+) = D-xylono-1,5-lactone + NADPH. Also acts, more slowly, on L-arabinose and D-ribose. Myo-inositol 2-dehydrogenase Inositol 2-dehydrogenase Myo-inositol + NAD(+) = 2,4,6/3,5-pentahydroxycyclohexanone + NADH. 3-beta-hydroxy-Delta(5)-C(27)-steroid oxidoreductase Cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase Cholest-5-ene-3-beta,7-alpha-diol + NAD(+) = 7-alpha-hydroxycholest-4-en-3-one + NADH. Highly specific for 3-beta-hydroxy-C(27)-steroids with Delta(5)-double bond. Geraniol dehydrogenase Geraniol + NADP(+) = geranial + NADPH. Also acts, more slowly, on nerol, farnesol and citronellol. NADPH-dependent carbonyl reductase Prostaglandin 9-ketoreductase Aldehyde reductase I Carbonyl reductase (NADPH) Xenobiotic ketone reductase R-CHOH-R' + NADP(+) = R-CO-R' + NADPH. B-specific with respect to NADPH (cf. EC 1.1.1.2). Acts on a wide range of carbonyl compounds, including quinones, aromatic aldehydes, ketoaldehydes, daunorubicin, and prostaglandins E and F, reducing them to the corresponding alcohol. L-glycol dehydrogenase An L-glycol + NAD(P)(+) = a 2-hydroxycarbonyl compound + NAD(P)H. In the reverse direction, vicinal diketones, glyceraldehyde, glyoxal, methylglyoxal, 2-oxo-hydroxyketones and 2-ketoacid esters can be reduced. The 2-hydroxycarbonyl compound formed can be further oxidized to a vicinal dicarbonyl compound. dTDP-galactose 6-dehydrogenase Thymidine-diphosphate-galactose dehydrogenase dTDP-D-galactose + 2 NADP(+) + H(2)O = dTDP-D-galacturonate + 2 NADPH. GDP-4-keto-6-deoxy-D-mannose reductase GDP-4-keto-D-rhamnose reductase GDP-4-dehydro-D-rhamnose reductase Guanosine diphosphate-4-keto-D-rhamnose reductase GDP-6-deoxy-D-mannose + NAD(P)(+) = GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H. In the reverse reaction, a mixture of GDP-D-rhamnose and its C-4 epimer is formed. Prostaglandin-D(2) 11-reductase Prostaglandin-D(2) ketoreductase Prostaglandin-D(2) 11-ketoreductase PGD(2) 11-ketoreductase PGF synthetase Prostaglandin-F synthetase Prostaglandin 11-ketoreductase Prostaglandin-F synthase Reduces prostaglandin D(2) and prostaglandin H(2) to prostaglandin F(2); prostaglandin D(2) is not an intermediate in the reduction of prostaglandin H(2). Also catalyzes the reduction of a number of carbonyl compounds, such as 9,10-phenanthroquinone and 4-nitroacetophenone. (5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate + NADP(+) = (5Z,13E)-(15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH. Prostaglandin-E(2) 9-reductase 9-keto-prostaglandin E(2) reductase Prostaglandin-E2 9-reductase 9-ketoprostaglandin reductase PGE(2) 9-oxoreductase Prostaglandin-E(2) 9-oxoreductase PGE(2) 9-ketoreductase (5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate + NADP(+) = (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH. Reduces prostaglandin E(2) to prostaglandin F(2)-alpha. May be identical with EC 1.1.1.197. A number of other 9-oxo-and 15-oxo-prostaglandin derivatives can also be reduced to the corresponding hydroxy compounds. D-glucuronate reductase Glucuronate dehydrogenase D-glucuronate dehydrogenase TPN-L-gulonate dehydrogenase L-glucuronate reductase Glucuronate reductase NADP-L-gulonate dehydrogenase Aldehyde reductase II Aldehyde reductase L-gulonate + NADP(+) = D-glucuronate + NADPH. Also reduces D-galacturonate. May be identical with EC 1.1.1.2. Indoleacetaldehyde reductase Indole-3-acetaldehyde reductase (NADH) (Indol-3-yl)ethanol + NAD(+) = (indol-3-yl)acetaldehyde + NADH. Indole-3-acetaldehyde reductase (NADPH) (Indol-3-yl)ethanol + NADP(+) = (indol-3-yl)acetaldehyde + NADPH. Long-chain-alcohol dehydrogenase Fatty alcohol oxidoreductase A long-chain alcohol + 2 NAD(+) + H(2)O = a long-chain carboxylate + 2 NADH. Hexadecanol is a good substrate. 5-amino-6-(5-phosphoribosylamino)uracil reductase 5-amino-6-(5-phosphoribitylamino)uracil + NADP(+) = 5-amino-6-(5-phosphoribosylamino)uracil + NADPH. Coniferyl-alcohol dehydrogenase Coniferyl alcohol + NADP(+) = coniferyl aldehyde + NADPH. Specific for coniferyl alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or sinapyl alcohol. CAD Cinnamyl-alcohol dehydrogenase Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194). Cinnamyl alcohol + NADP(+) = cinnamaldehyde + NADPH. Prostaglandin-D 15-dehydrogenase (NADP(+)) Prostaglandin-D 15-dehydrogenase (NADP+) 15-hydroxyprostaglandin-D dehydrogenase (NADP(+)) Specific for prostaglandins D (cf. EC 1.1.1.141 and EC 1.1.1.197). (5Z,13E)-(15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADP(+) = (5Z,13E)-9-alpha-hydroxy-11,15-dioxoprosta-5,13-dienoate + NADPH. 15-hydroxyprostaglandin dehydrogenase (NADP(+)) Acts on prostaglandins E(2), F(2)-alpha and B(1), but not on prostaglandin D(2) (cf. EC 1.1.1.141 and EC 1.1.1.196). May be identical with EC 1.1.1.189. (13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP(+) = (13E)-11-alpha-hydroxy-9,15-dioxoprost-13-enoate + NADPH. (+)-borneol dehydrogenase (+)-borneol + NAD(+) = (+)-camphor + NADH. NADP(+) can also act, more slowly. (S)-usnate reductase In the reverse direction, (S)-usnate is reduced by NADH with cleavage of the ether bond to form a 7-hydroxy group. Aldehyde reductase (NADPH) Alcohol dehydrogenase (NADP(+)) A-specific with respect to NADPH. Zinc May be identical with EC 1.1.1.19, EC 1.1.1.33 and EC 1.1.1.55. An alcohol + NADP(+) = an aldehyde + NADPH. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. Glucuronolactone reductase L-gulono-1,4-lactone + NADP(+) = D-glucurono-3,6-lactone + NADPH. NADP-dependent D-sorbitol-6-phosphate dehydrogenase Aldose-6-phosphate reductase (NADPH) In the reverse reaction, acts also on D-galactose 6-phosphate and, more slowly, on D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate. D-sorbitol 6-phosphate + NADP(+) = D-glucose 6-phosphate + NADPH. NADP-dependent 7-beta-hydroxysteroid dehydrogenase 7-beta-hydroxysteroid dehydrogenase (NADP(+)) A 7-beta-hydroxysteroid + NADP(+) = a 7-oxosteroid + NADPH. Catalyzes the oxidation of the 7-beta-hydroxy group of bile acids such as ursodeoxycholate. 1,3-propanediol dehydrogenase 3-hydroxypropionaldehyde reductase 1,3-propanediol oxidoreductase Propane-1,3-diol + NAD(+) = 3-hydroxypropanal + NADH. Uronic acid dehydrogenase Uronate dehydrogenase Also acts on D-glucuronate. D-galacturonate + NAD(+) + H(2)O = D-galactarate + NADH. Inosinic acid dehydrogenase Inosine 5'-monophosphate dehydrogenase IMP oxidoreductase Inosine monophosphate oxidoreductase IMP dehydrogenase Inosinate dehydrogenase http://purl.uniprot.org/mim/180105 The enzyme acts on the hydroxy group of the hydrated derivative of the substrate. Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH. Tropine dehydrogenase Tropine + NADP(+) = tropinone + NADPH. Also oxidizes other tropan-3-alpha-ols, but not the corresponding beta-derivatives. Monoterpenoid dehydrogenase (-)-menthol dehydrogenase (-)-menthol + NADP(+) = (-)-menthone + NADPH. Not identical with EC 1.1.1.208. Acts on a number of other cyclohexanols and cyclohexenols. (+)-neomenthol dehydrogenase Monoterpenoid dehydrogenase Not identical with EC 1.1.1.207. (+)-neomenthol + NADP(+) = (-)-menthone + NADPH. Acts on a number of other cyclohexanols and cyclohexenols. 3(or 17)-alpha-hydroxysteroid dehydrogenase Androsterone + NAD(P)(+) = 5-alpha-androstane-3,17-dione + NAD(P)H. Acts on the 3-alpha-hydroxy group of androgens of the 5-alpha-androstane series; and also, more slowly, on the 17-alpha-hydroxyl group of both androgenic and estrogenic substrates (cf. EC 1.1.1.51). Aldose reductase Polyol dehydrogenase (NADP(+)) Aldehyde reductase Wide specificity. Alditol + NAD(P)(+) = aldose + NAD(P)H. Progesterone reductase 3-beta-HSD 3-beta-(or 20-alpha)-hydroxysteroid dehydrogenase Also acts on 20-alpha-hydroxysteroids. 5-alpha-androstan-3-beta,17-beta-diol + NADP(+) = 17-beta-hydroxy-5-alpha-androstan-3-one + NADPH. Beta-hydroxyacyl-CoA dehydrogenase Long-chain-3-hydroxyacyl-CoA dehydrogenase http://purl.uniprot.org/mim/609016 http://purl.uniprot.org/mim/609015 Acts most rapidly on derivatives with chain length C(8) or C(10) (cf. EC 1.1.1.35). (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH. 3-oxoacyl-[acyl-carrier-protein] reductase (NADH) Forms part of the fatty acid synthase system in plants. (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NAD(+) = 3-oxoacyl-[acyl-carrier-protein] + NADH. Can be separated from EC 1.1.1.100. 3-alpha-hydroxysteroid dehydrogenase (A-specific) A-specific with respect to NAD(+) or NADP(+) (cf. EC 1.1.1.50). Also acts on other 3-alpha-hydroxysteroids. Androsterone + NAD(P)(+) = 5-alpha-androstane-3,17-dione + NAD(P)H. 2-ketopantoyl lactone reductase 2-dehydropantolactone reductase (B-specific) 2-dehydropantoyl-lactone reductase (B-specific) Ketopantoyl lactone reductase (R)-pantolactone + NADP(+) = 2-dehydropantolactone + NADPH. The Escherichia coli enzyme differs from that from Saccharomyces cerevisiae (EC 1.1.1.168), which is specific for the A-face of NADP, and in receptor requirements from EC 1.1.99.26. 2-keto-D-gluconate reductase 2-ketogluconate reductase Gluconate 2-dehydrogenase D-gluconate + NADP(+) = 2-dehydro-D-gluconate + NADPH. Also acts on L-idonate, D-galactonate and D-xylonate. Farnesol dehydrogenase 2-trans,6-trans-farnesol + NADP(+) = 2-trans,6-trans-farnesal + NADPH. Also acts, more slowly, on 2-cis,6-trans-farnesol, geraniol, citronerol and nerol. Benzyl 2-methyl-3-hydroxybutyrate dehydrogenase Benzyl-2-methyl-hydroxybutyrate dehydrogenase Also acts on benzyl (2S,3S)-2-methyl-3-hydroxybutanoate; otherwise highly specific. Benzyl (2R,3S)-2-methyl-3-hydroxybutanoate + NADP(+) = benzyl 2-methyl-3-oxobutanoate + NADPH. Naloxone reductase Morphine 6-dehydrogenase In the reverse direction, also reduces naloxone to the 6-alpha-hydroxy analog. Activated by 2-mercaptoethanol. Also acts on some other alkaloids, including codeine, normorphine and ethylmorphine, but only very slowly on 7,8-saturated derivatives such as dihydromorphine and dihydrocodeine. Morphine + NAD(P)(+) = morphinone + NAD(P)H. Dihydroflavanol 4-reductase NADPH-dihydromyricetin reductase Dihydrokaempferol 4-reductase Dihydroflavonol 4-reductase Cis-3,4-leucopelargonidin + NADP(+) = (+)-dihydrokaempferol + NADPH. Involved in the biosynthesis of anthocyanidins in plants. NAD(+) can act instead of NADP(+), but more slowly. Also acts, in the reverse direction, on (+)-dihydroquercetin and (+)-dihydromyricetin; each dihydroflavonol is reduced to the corresponding cis-flavan-3,4-diol. UDP-glucose 6-dehydrogenase UDP-glucose + 2 NAD(+) + H(2)O = UDP-glucuronate + 2 NADH. Also acts on UDP-2-deoxyglucose. 6-pyruvoyltetrahydropterin 2'-reductase 6PPH4(2'-oxo) reductase 6-pyruvoyl-tetrahydropterin 2'-reductase Pyruvoyl-tetrahydropterin reductase 6-pyruvoyl tetrahydropterin (2'-oxo)reductase 6-lactoyl-5,6,7,8-tetrahydropterin + NADP(+) = 6-pyruvoyltetrahydropterin + NADPH. Not identical with EC 1.1.1.153. Vomifoliol 4'-dehydrogenase (+-)-6-hydroxy-3-oxo-alpha-ionol + NAD(+) = (+-)-6-hydroxy-3-oxo-alpha-ionone + NADH. Oxidizes vomifoliol to dehydrovomifoliol; involved in the metabolism of abscisic acid in Corynebacterium sp. (R)-4-hydroxyphenyllactate dehydrogenase (R)-aromatic lactate dehydrogenase Also acts, more slowly, on (R)-3-phenyllactate, (R)-3-(indol-3-yl)lactate and (R)-lactate. (R)-3-(4-hydroxyphenyl)lactate + NAD(P)(+) = 3-(4-hydroxyphenyl)pyruvate + NAD(P)H. Isopiperitenol dehydrogenase Involved in the biosynthesis of menthol and related monoterpenes in peppermint (Mentha piperita) leaves. (-)-trans-isopiperitenol + NAD(+) = (-)-isopiperitenone + NADH. Acts on (-)-trans-isopiperitenol, (+)-trans-piperitenol and (+)-trans-pulegol. NADPH-dependent M6P reductase Mannose-6-phosphate 6-reductase NADPH-mannose-6-P reductase D-mannitol 1-phosphate + NADP(+) = D-mannose 6-phosphate + NADPH. Involved in the biosynthesis of mannitol in celery (Apium graveolens) leaves. CDR Chlordecone reductase Chlordecone, an organochlorine pesticide, is 1,1a,3,3a,4,5,5a,5b,6-decachlorooctahydro-1,3,4-metheno-2H-cyclobuta[cd]pentalen-2-one. Chlordecone alcohol + NADP(+) = chlordecone + NADPH. 4-hydroxycyclohexanecarboxylate dehydrogenase The enzyme from Corynebacterium cyclohexanicum is highly specific for the trans-4-hydroxy derivative. Trans-4-hydroxycyclohexanecarboxylate + NAD(+) = 4-oxocyclohexanecarboxylate + NADH. (-)-borneol dehydrogenase (-)-borneol + NAD(+) = (-)-camphor + NADH. NADP(+) can also act, more slowly. (+)-sabinol dehydrogenase (+)-cis-sabinol + NAD(+) = (+)-sabinone + NADH. NADP(+) can also act, more slowly. Involved in the biosynthesis of (+)-3-thujone and (-)-3-isothujone. Diethyl 2-methyl-3-oxosuccinate reductase Also acts on diethyl (2S,3R)-2-methyl-3-hydroxysuccinate; and on the corresponding dimethyl esters. Diethyl (2R,3R)-2-methyl-3-hydroxysuccinate + NADP(+) = diethyl 2-methyl-3-oxosuccinate + NADPH. Histidinol dehydrogenase The Neurospora enzyme also catalyzes the reactions of EC 3.5.4.19 and EC 3.6.1.31. Also oxidizes L-histidinal. L-histidinol + 2 NAD(+) = L-histidine + 2 NADH. 3-alpha-hydroxyglycyrrhetinate dehydrogenase Highly specific to 3-alpha-hydroxy derivatives of glycyrrhetinate and its analogs. 3-alpha-hydroxyglycyrrhetinate + NADP(+) = 3-oxoglycyrrhetinate + NADPH. Not identical to EC 1.1.1.50. 15-hydroxyprostaglandin-I dehydrogenase (NADP(+)) PG I2 dehydrogenase Prostacyclin dehydrogenase (5Z,13E)-(15S)-6,9-alpha-epoxy-11-alpha,15-dihydroxyprosta-5,13-dienoate + NADP(+) = (5Z,13E)-6,9-alpha-epoxy-11-alpha-hydroxy-15-oxoprosta-5,13-dienoate + NADPH. Specific for prostaglandin I(2). 15-hydroxyicosatetraenoate dehydrogenase (15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)(+) = 15-oxo-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)H. N-acyl-D-mannosamine dehydrogenase N-acylmannosamine 1-dehydrogenase N-acylmannosamine dehydrogenase N-acetyl-D-mannosamine dehydrogenase Acts on acetyl-D-mannosamine and glycolyl-D-mannosamine. Highly specific. N-acyl-D-mannosamine + NAD(+) = N-acyl-D-mannosaminolactone + NADH. Flavanone 4-reductase Involved in the biosynthesis of 3-deoxyanthocyanidins from flavanones such as naringenin or eriodictyol. (2S)-flavan-4-ol + NADP(+) = (2S)-flavanone + NADPH. 8-oxocoformycin reductase B-specific with respect to NADPH. Coformycin + NADP(+) = 8-oxocoformycin + NADPH. Also reduces 8-oxodeoxy-coformycin to the nucleoside antibiotic deoxycoformycin. Tropinone reductase Pseudotropine forming tropinone reductase Tropinone reductase II Pseudotropine + NADP(+) = tropinone + NADPH. Hydroxyphenylpyruvate reductase Also acts on 3-(3,4-dihydroxyphenyl)lactate. Involved with EC 2.3.1.140 in the biosynthesis of rosmarinic acid. 3-(4-hydroxyphenyl)lactate + NAD(+) = 3-(4-hydroxyphenyl)pyruvate + NADH. 12-beta-hydroxysteroid dehydrogenase Acts on a number of bile acids, both in their free and conjugated forms. 3-alpha,7-alpha,12-beta-trihydroxy-5-beta-cholanate + NADP(+) = 3-alpha,7-alpha-dihydroxy-12-oxo-5-beta-cholanate + NADPH. 3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+)) Also acts on other 17-beta-hydroxysteroids, on the 3-alpha-hydroxy group of pregnanes and bile acids, and on benzene dihydrodiol. Testosterone + NAD(+) = androst-4-ene-3,17-dione + NADH. Different from EC 1.1.1.50 or EC 1.1.1.213. Quinate:NAD oxidoreductase Quinic dehydrogenase Quinate:NAD(+) 5-oxidoreductase Quinate 5-dehydrogenase Quinate dehydrogenase The enzyme is specific for quinate as substrate; phenylpyruvate, phenylalanine, cinnamate and shikimate will not act as substrates. NAD(+) cannot be replaced by NADP(+). Quinate + NAD(+) = 3-dehydroquinate + NADH. N-acetylhexosamine 1-dehydrogenase Also acts on N-acetylgalactosamine and, more slowly, on N-acetylmannosamine. N-acetyl-D-glucosamine + NAD(+) = N-acetyl-D-glucosaminate + NADH. 6-endo-hydroxycineole dehydrogenase 6-endo-hydroxycineole + NAD(+) = 6-oxocineole + NADH. Carveol dehydrogenase (-)-trans-carveol + NADP(+) = (-)-carvone + NADPH. Methanol dehydrogenase Methanol + NAD(+) = formaldehyde + NADH. Cyclohexanol dehydrogenase Cyclohexanol + NAD(+) = cyclohexanone + NADH. Also oxidizes some other alicyclic alcohols and diols. Pterocarpin synthase Medicarpin + NADP(+) = vestitone + NADPH. Catalyzes the final step in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain. Codeinone reductase (NADPH) Catalyzes the reversible reduction of codeinone to codeine, which is a direct precursor of morphine in the opium poppy plant, Papaver somniferum. Codeine + NADP(+) = codeinone + NADPH. Salutaridine reductase (NADPH) Salutaridinol + NADP(+) = salutaridine + NADPH. Catalyzes the reversible reduction of salutaridine to salutaridinol, which is a direct precursor of morphinan alkaloids in the poppy plant. Shikimate dehydrogenase Dehydroshikimic reductase Shikimate:NADP(+) 5-oxidoreductase DHS reductase Shikimate oxidoreductase 5-dehydroshikimic reductase Shikimate:NADP(+) oxidoreductase Shikimate 5-dehydrogenase 5-dehydroshikimate reductase Shikimate + NADP(+) = 3-dehydroshikimate + NADPH. In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10. NAD(+) cannot replace NADP(+). D-arabinitol 2-dehydrogenase (ribulose-forming) D-arabinitol 2-dehydrogenase D-arabinitol + NAD(+) = D-ribulose + NADH. Galactitol-1-phosphate 5-dehydrogenase Galactitol-1-phosphate + NAD(+) = L-tagatose 6-phosphate + NADH. Zinc Tetrahydroxynaphthalene reductase T4HN reductase Reduces 1,3,6,8-tetrahydroxynaphthalene to scytalone and also reduces 1,3,8-trihydroxynaphthalene to vermelone. Involved with EC 4.2.1.94 in the biosynthesis of melanin in pathogenic fungi. Scytalone + NADP(+) = 1,3,6,8-tetrahydroxynaphthalene + NADPH. D-carnitine dehydrogenase (S)-carnitine 3-dehydrogenase Specific for the (S)-enantiomer of carnitine, i.e., the enantiomer of the substrate of EC 1.1.1.108. (S)-carnitine + NAD(+) = 3-dehydrocarnitine + NADH. MTD Mannitol dehydrogenase NAD-dependent mannitol dehydrogenase The enzyme is specific for NAD(+) and does not use NADP(+). The enzyme from Apium graveolens (celery) oxidizes alditols with a minimum requirement of 2R chirality at the carbon adjacent to the primary carbon undergoing the oxidation. D-mannitol + NAD(+) = D-mannose + NADH. Fluoren-9-ol dehydrogenase Fluoren-9-ol + 2 NAD(P)(+) = fluoren-9-one + 2 NAD(P)H. Involved in the pathway for fluorene metabolism in Arthrobacter sp. 4-(hydroxymethyl)benzenesulfonate dehydrogenase 4-(hydroxymethyl)benzenesulfonate + NAD(+) = 4-formylbenzenesulfonate + NADH. Involved in the toluene-4-sulfonate degradation pathway in Comamonas testosteroni. 6-hydroxyhexanoate dehydrogenase 6-hydroxyhexanoate + NAD(+) = 6-oxohexanoate + NADH. Involved in the cyclohexanol degradation pathway in Acinetobacter NCIB 9871. 3-hydroxypimeloyl-CoA dehydrogenase 3-hydroxypimeloyl-CoA + NAD(+) = 3-oxopimeloyl-CoA + NADH. Involved in the anaerobic pathway of benzoate degradation in bacteria. NADH-dependent glyoxylate reductase Glycolate reductase Glyoxylic acid reductase Glyoxylate reductase Reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate. Glycolate + NAD(+) = glyoxylate + NADH. Sulcatone reductase Sulcatol + NAD(+) = sulcatone + NADH. Studies on the effects of growth-stage and nutrient supply on the stereochemistry of sulcatone reduction in Clostridia pasteurianum, C.tyrobutyricum and Lactobacillus brevis suggest that there may be at least two sulcatone reductases with different stereospecificities. Glycerol-1-phosphate dehydrogenase (NAD(P)(+)) sn-glycerol-1-phosphate + NAD(P)(+) = glycerone phosphate + NAD(P)H. Responsible for the formation of archaea-specific glycerophosphate and is stereospecifically different from EC 1.1.1.94. L-threonine 4-phosphate dehydrogenase 4-(phosphohydroxy)-L-threonine dehydrogenase 4-hydroxythreonine-4-phosphate dehydrogenase NAD(+)-dependent threonine 4-phosphate dehydrogenase The product of the reaction undergoes decarboxylation to give 3-amino-2-oxopropyl phosphate. 4-(phosphonooxy)-L-threonine + NAD(+) = (2S)-2-amino-3-oxo-4-phosphonooxybutanoate + NADH. In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72, EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5. 1,5-anhydro-D-fructose reductase AF reductase 1,5-anhydro-D-glucitol + NADP(+) = 1,5-anhydro-D-fructose + NADPH. Acetaldehyde, 2-dehydroglucose (glucosone) and glucuronate are poor substrates, but there is no detectable action on glucose, mannose and fructose. Also reduces pyridine-3-aldehyde and 2,3-butanedione. L-idonate 5-dehydrogenase The enzyme from Escherichia coli cannot oxidize D-gluconate to form 5-dehydrogluconate, a reaction that is catalyzed by EC 1.1.1.69. Zinc L-idonate + NAD(P)(+) = 5-dehydrogluconate + NAD(P)H. 3-methylbutanal reductase The enzyme purified from Saccharomyces cerevisiae catalyzes the reduction of a number of straight-chain and branched aldehydes, as well as some aromatic aldehydes. 3-methylbutanol + NAD(P)(+) = 3-methylbutanal + NAD(P)H. dTDP-4-keto-6-deoxyglucose reductase dTDP-4-dehydro-6-deoxyglucose reductase dTDP-D-fucose + NADP(+) = dTDP-4-dehydro-6-deoxy-D-glucose + NADPH. The enzyme from the Gram-negative bacterium Actinobacillus actinomycetemcomitans forms activated fucose for incorporation into capsular polysaccharide. 1-deoxy-D-xylulose-5-phosphate reductoisomerase DXP-reductoisomerase 1-deoxyxylulose-5-phosphate reductoisomerase 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + NADPH. Manganese or cobalt or magnesium The enzyme from several eubacteria, including Escherichia coli, forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. 2-(R)-hydroxypropyl-CoM dehydrogenase 2-(2-(R)-hydroxypropylthio)ethanesulfonate dehydrogenase Forms component III of a four-component enzyme system (comprising EC 4.4.1.23 (component I), EC 1.8.1.5 (component II), EC 1.1.1.268 (component III) and EC 1.1.1.269 (component IV)) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2. Highly specific for (R)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.269, which is highly specific for the (S)-enantiomer. 2-(R)-hydroxypropyl-CoM + NAD(+) = 2-oxopropyl-CoM + NADH. 2-(S)-hydroxypropyl-CoM dehydrogenase 2-(2-(S)-hydroxypropylthio)ethanesulfonate dehydrogenase 2-(S)-hydroxypropyl-CoM + NAD(+) = 2-oxopropyl-CoM + NADH. Forms component IV of a four-component enzyme system (comprising EC 4.4.1.23 (component I), EC 1.8.1.5 (component II), EC 1.1.1.268 (component III) and EC 1.1.1.269 (component IV)) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2. Highly specific for (S)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.268, which is highly specific for the (R)-enantiomer. L-lactic acid dehydrogenase L-lactic dehydrogenase L-lactate dehydrogenase (S)-lactate + NAD(+) = pyruvate + NADH. http://purl.uniprot.org/mim/150100 Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP(+) acts, more slowly, with the animal, but not the bacterial, enzyme. http://purl.uniprot.org/mim/150000 3-KSR 3-keto-steroid reductase Also acts on 5-alpha-cholest-7-en-3-one. 4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NADP(+) = 4-alpha-methyl-5-alpha-cholest-7-en-3-one + NADPH. GDP-fucose synthetase GDP-L-fucose synthase GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase GDP-L-fucose + NADP(+) = GDP-4-dehydro-6-deoxy-D-mannose + NADPH. Both human and Escherichia coli enzymes can use NADH in place of NADPH to a slight extent. (R)-sulfolactate:NAD(P)(+) oxidoreductase L-sulfolactate dehydrogenase (R)-2-hydroxyacid dehydrogenase (2R)-3-sulfolactate + NAD(P)(+) = 3-sulfopyruvate + NAD(P)H. This dehydrogenase also acts on (S)-malate and (S)-2-hydroxyglutarate i.e. with the same configuration as (R)-sulfolactate. Vellosimine dehydrogenase 10-deoxysarpagine + NADP(+) = vellosimine + NADPH. Also acts on related alkaloids with an endo-aldehyde group such as vellosimine (same stereochemistry at C-16) but only slight activity with exo-aldehydes (epimeric at C-16). Detected in many cell suspension cultures of plants from the family Apocynaceae. 2,5-didehydrogluconate reductase 2,5-diketo-D-gluconate reductase The identification of a bacterial beta-keto ester reductase as a 2,5-didehydrogluconate reductase links two previously separate areas of biocatalysis, i.e., asymmetric carbonyl reduction and microbial vitamin C production. Key enzyme in the microbial production of ascorbate. Can also reduce ethyl 2-methylacetoacetate stereoselectively to ethyl (2R)-methyl-(3S)-hydroxybutanoate and can also accept some other beta-keto esters. 2-dehydro-D-gluconate + NADP(+) = 2,5-didehydro-D-gluconate + NADPH. (+)-trans-carveol dehydrogenase Carveol dehydrogenase NADP(+) cannot replace NAD(+). Forms part of the monoterpenoid biosynthesis pathway in Carum carvi (caraway) seeds. (+)-trans-carveol + NAD(+) = (+)-(S)-carvone + NADH. Serine 3-dehydrogenase NAD(+) cannot replace NADP(+). L-serine + NADP(+) = 2-ammoniomalonate semialdehyde + NADPH. The product 2-ammoniomalonate semialdehyde is spontaneously converted into 2-aminoacetaldehyde and CO(2). 3-beta-hydroxy-5-beta-steroid dehydrogenase 3-beta-hydroxysteroid 5-beta-oxidoreductase 3-beta-hydroxysteroid 5-beta-progesterone oxidoreductase 3-beta-hydroxy-5-beta-pregnane-20-one + NADP(+) = 5-beta-pregnan-3,20-dione + NADPH. 3-beta-hydroxy-5-alpha-steroid dehydrogenase 3-beta-hydroxy-5-alpha-pregnane-20-one + NADP(+) = 5-alpha-pregnan-3,20-dione + NADPH. (R)-3-hydroxyacid-ester dehydrogenase 3-oxo ester (R)-reductase Also acts on ethyl (R)-3-oxobutanoate and some other (R)-3-hydroxy acid esters. Ethyl (R)-3-hydroxyhexanoate + NADP(+) = ethyl 3-oxohexanoate + NADPH. A subunit of Saccharomyces cerevisiae EC 2.3.1.86. Cf. EC 1.1.1.280. The (R)-symbol is allotted on the assumption that no substituents change the order of priority from O-3>C-2>C-4. D-lactate dehydrogenase D-lactic acid dehydrogenase D-lactic dehydrogenase (R)-lactate + NAD(+) = pyruvate + NADH. 3-oxo ester (S)-reductase (S)-3-hydroxyacid-ester dehydrogenase Cf. EC 1.1.1.279. Ethyl (S)-3-hydroxyhexanoate + NADP(+) = ethyl 3-oxohexanoate + NADPH. Also acts on 4-oxo-and 5-oxo-fatty acids and their esters. GDP-4-keto-6-deoxy-D-mannose reductase GDP-4-dehydro-6-deoxy-D-mannose reductase GDP-6-deoxy-D-lyxo-4-hexulose reductase GDP-6-deoxy-D-mannose + NAD(P)(+) = GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H. D-rhamnose is a constituent of lipopolysaccharides of Gram-negative plant and human pathogenic bacteria. Differs from EC 1.1.1.187 in that the only product formed is GDP-D-rhamnose (GDP-6-deoxy-D-mannose). Quinate/shikimate dehydrogenase (1) L-quinate + NAD(P)(+) = 3-dehydroquinate + NAD(P)H. This is the second shikimate dehydrogenase enzyme found in Escherichia coli and differs from EC 1.1.1.25, in that it can use both quinate and shikimate as substrate and either NAD(+) or NADP(+) as acceptor. (2) Shikimate + NAD(P)(+) = 3-dehydroshikimate + NAD(P)H. Methylglyoxal reductase (NADPH-dependent) Lactaldehyde dehydrogenase (NADP(+)) Lactaldehyde + NADP(+) = methylglyoxal + NADPH. It also acts on phenylglyoxal and glyoxal. It differs in coenzyme requirement from EC 1.1.1.78, which is found in mammals. The enzyme from the yeast Saccharomyces cerevisiae catalyzes the conversion of methylglyoxal into lactaldehyde; the reverse reaction has not been demonstrated. NAD- and glutathione-dependent formaldehyde dehydrogenase GD-FALDH ADH3 FDH S-(hydroxymethyl)glutathione dehydrogenase Formaldehyde dehydrogenase (glutathione) Chi-ADH Formaldehyde dehydrogenase NAD-linked formaldehyde dehydrogenase Glutathione-dependent formaldehyde dehydrogenase GS-FDH Class III alcohol dehydrogenase NAD-dependent formaldehyde dehydrogenase Formic dehydrogenase S-(hydroxymethyl)glutathione + NAD(P)(+) = S-formylglutathione + NAD(P)H. Also specifically reduces S-nitrosylglutathione. Forms part of the pathway that detoxifies formaldehyde, since the product is hydrolyzed by EC 3.1.2.12. The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22. 3''-deamino-3''-oxonicotianamine reductase 2'-deoxymugineic acid + NAD(P)(+) = 3''-deamino-3''-oxonicotianamine + NAD(P)H. Homoisocitrate--isocitrate dehydrogenase Isocitrate--homoisocitrate dehydrogenase Potassium or ammonium May play a role in both the lysine and glutamate biosynthesis pathways. Manganese Unlike EC 1.1.1.41 and EC 1.1.1.87, this enzyme, from Pyrococcus horikoshii, can use both isocitrate and homoisocitrate as substrate. (1) Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + NADH. (2) (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD(+) = 2-oxoadipate + CO(2) + NADH. NADP(+)-dependent D-arabinitol dehydrogenase D-arabinitol dehydrogenase (NADP(+)) D-arabinitol dehydrogenase 1 (1) D-arabinitol + NADP(+) = D-xylulose + NADPH. D-arabinitol is capable of quenching reactive oxygen species involved in defense reactions of the host plant. This enzyme carries out the reactions of both EC 1.1.1.11 and EC 1.1.1.250, but unlike them, uses NADP(+) rather than NAD(+) as cofactor. The enzyme from the rust fungus Uromyces fabae can use D-arabinitol and D-mannitol as substrates in the forward direction and D-xylulose, D-ribulose and, to a lesser extent, D-fructose as substrates in the reverse direction. (2) D-arabinitol + NADP(+) = D-ribulose + NADPH. Xanthoxin oxidase Xanthoxin dehydrogenase Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.2.3.14, EC 1.13.11.51 and EC 1.14.13.93. Molybdenum Xanthoxin + NAD(+) = abscisic aldehyde + NADH. NADP(+) cannot replace NAD(+) and short-chain alcohols such as ethanol, isopropanol, butanol and cyclohexanol cannot replace xanthoxin as substrate. Sorbose reductase This enzyme can also convert D-fructose into D-mannitol, but more slowly. D-glucitol + NADP(+) = L-sorbose + NADPH. The reaction occurs predominantly in the reverse direction. Glycerate dehydrogenase Hydroxypyruvate reductase Hydroxypyruvate dehydrogenase (R)-glycerate + NAD(+) = hydroxypyruvate + NADH. http://purl.uniprot.org/mim/260000 Erythronate-4-phosphate dehydrogenase 4-phosphoerythronate dehydrogenase 4-O-phosphoerythronate dehydrogenase 4PE dehydrogenase 4-phospho-D-erythronate + NAD(+) = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH. This enzyme catalyzes the second step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate in Escherichia coli. Other enzymes involved in this pathway are EC 1.2.1.72, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5. The reaction occurs predominantly in the reverse direction. 2-hydroxymethylglutarate dehydrogenase (S)-2-hydroxymethylglutarate + NAD(+) = 2-formylglutarate + NADH. Other enzymes involved in this pathway are EC 1.17.1.5, EC 1.3.7.1, EC 3.5.2.18, EC 5.4.99.4, EC 5.3.3.6, EC 4.2.1.85 and EC 4.1.3.32. NADP(+) cannot replace NAD(+). Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. 1,5-anhydro-D-fructose reductase AFR 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) In Sinorhizobium morelense, the product of the reaction, 1,5-anhydro-D-mannitol, can be further metabolized to D-mannose. Also reduces 1,5-anhydro-D-erythro-hexo-2,3-diulose and 2-ketoaldoses (called osones), such as D-glucosone (D-arabino-hexos-2-ulose) and 6-deoxy-D-glucosone. 1,5-anhydro-D-mannitol + NADP(+) = 1,5-anhydro-D-fructose + NADPH. Does not reduce common aldoses and ketoses, or non-sugar aldehydes and ketones. Differs from hepatic 1,5-anhydro-D-fructose reductase, which yields 1,5-anhydro-D-glucitol as the product (see EC 1.1.1.263). Present in some but not all Rhizobium species. Homoserine dehydrogenase The enzyme from Saccharomyces cerevisiae acts most rapidly with NAD(+); the Neurospora enzyme with NADP(+). L-homoserine + NAD(P)(+) = L-aspartate 4-semialdehyde + NAD(P)H. The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 2.7.2.4. 3-hydroxybutyrate dehydrogenase D-beta-hydroxybutyrate dehydrogenase Also oxidizes other 3-hydroxymonocarboxylic acids. (R)-3-hydroxybutanoate + NAD(+) = acetoacetate + NADH. 3-hydroxyisobutyrate dehydrogenase 3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + NADH. Mevaldate reductase (R)-mevalonate + NAD(+) = mevaldate + NADH. Mevaldate reductase (NADPH) (R)-mevalonate + NADP(+) = mevaldate + NADPH. May be identical with EC 1.1.1.2. 3-hydroxy-3-methylglutaryl-coenzyme A reductase HMG-CoA reductase Hydroxymethylglutaryl-CoA reductase (NADPH) (R)-mevalonate + CoA + 2 NADP(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH. The enzyme is inactivated by EC 2.7.11.31 and reactivated by EC 3.1.3.47. Beta-hydroxyacyl dehydrogenase Beta-keto-reductase 3-hydroxyacyl-CoA dehydrogenase http://purl.uniprot.org/mim/261515 (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH. Broad specificity to acyl chain-length (cf. EC 1.1.1.211). http://purl.uniprot.org/mim/231530 Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3-hydroxyacylhydrolipoate. http://purl.uniprot.org/mim/609975 Some enzymes act, more slowly, with NADP(+). http://purl.uniprot.org/mim/300438 Acetoacetyl-CoA reductase (R)-3-hydroxyacyl-CoA + NADP(+) = 3-oxoacyl-CoA + NADPH. Malic dehydrogenase Malate dehydrogenase Also oxidizes some other 2-hydroxydicarboxylic acids. (S)-malate + NAD(+) = oxaloacetate + NADH. Malic enzyme Pyruvic-malic carboxylase NAD-malic enzyme Malate dehydrogenase (oxaloacetate-decarboxylating) (S)-malate + NAD(+) = pyruvate + CO(2) + NADH. Also decarboxylates added oxaloacetate. NAD-malic enzyme Pyruvic-malic carboxylase Malate dehydrogenase (decarboxylating) Malic enzyme Does not decarboxylate added oxaloacetate. (S)-malate + NAD(+) = pyruvate + CO(2) + NADH. 1-amino-2-propanol dehydrogenase Aminopropanol oxidoreductase 1-amino-2-propanol oxidoreductase Butylene glycol dehydrogenase D-aminopropanol dehydrogenase D-1-amino-2-propanol:NAD(2) oxidoreductase D-(-)-butanediol dehydrogenase D-butanediol dehydrogenase Diacetyl (acetoin) reductase D-1-amino-2-propanol dehydrogenase 2,3-butanediol dehydrogenase (R)-diacetyl reductase (R)-2,3-butanediol dehydrogenase (R,R)-butanediol dehydrogenase Butyleneglycol dehydrogenase (R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + NADH. Also converts diacetyl into acetoin with NADH as reductant. Pyruvic-malic carboxylase Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP(+)) NADP-malic enzyme Malic enzyme (S)-malate + NADP(+) = pyruvate + CO(2) + NADPH. Also decarboxylates added oxaloacetate. Nicotinamide adenine dinucleotide isocitrate dehydrogenase Isocitrate dehydrogenase (NAD(+)) Isocitric dehydrogenase IDH NAD isocitric dehydrogenase NAD-linked isocitrate dehydrogenase NAD isocitrate dehydrogenase NAD-specific isocitrate dehydrogenase Isocitric acid dehydrogenase Isocitrate dehydrogenase (NAD) NAD dependent isocitrate dehydrogenase Beta-ketoglutaric-isocitric carboxylase Unlike EC 1.1.1.42, oxalosuccinate cannot be used as a substrate. Manganese or magnesium The enzyme from some species can also use NADP(+) but much more slowly. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD(+)-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP(+)-linked enzyme that is found in both mitochondria and cytoplasm. Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + NADH. IDP Dual-cofactor-specific isocitrate dehydrogenase Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase NADP(+)-ICDH Oxalosuccinate decarboxylase NADP isocitric dehydrogenase Oxalsuccinic decarboxylase NADP(+)-IDH Isocitrate (NADP) dehydrogenase Isocitrate dehydrogenase (NADP) NADP(+)-linked isocitrate dehydrogenase NADP-linked isocitrate dehydrogenase NADP-dependent isocitrate dehydrogenase Triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase NADP-dependent isocitric dehydrogenase NADP-specific isocitrate dehydrogenase IDH Isocitrate dehydrogenase (NADP-dependent) Isocitrate dehydrogenase (NADP(+)) In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD(+)-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP(+)-linked enzyme that is found in both mitochondria and cytoplasm. Unlike EC 1.1.1.41, oxalosuccinate can be used as a substrate. (1) Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. The enzyme from some species can also use NAD(+) but much more slowly. (2) Oxalosuccinate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Manganese or magnesium 6-phosphogluconic dehydrogenase Phosphogluconate 2-dehydrogenase 6-phosphogluconate 2-dehydrogenase 6-phospho-D-gluconate + NAD(P)(+) = 6-phospho-2-dehydro-D-gluconate + NAD(P)H. 6-phosphogluconic dehydrogenase 6-phosphogluconic carboxylase Phosphogluconate dehydrogenase (decarboxylating) Phosphogluconic acid dehydrogenase 6PGD 6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO(2) + NADPH. http://purl.uniprot.org/mim/172200 L-3-aldonate dehydrogenase L-gulonate 3-dehydrogenase L-gulonate + NAD(+) = 3-dehydro-L-gulonate + NADH. Also oxidizes other L-3-hydroxyacids. L-arabinose 1-dehydrogenase L-arabinose + NAD(+) = L-arabinono-1,4-lactone + NADH. Glucose 1-dehydrogenase Beta-D-glucose + NAD(P)(+) = D-glucono-1,5-lactone + NAD(P)H. http://purl.uniprot.org/mim/604931 Also oxidizes D-xylose. Galactose 1-dehydrogenase D-galactose 1-dehydrogenase D-galactose + NAD(+) = D-galactono-1,4-lactone + NADH. G6PD Glucose-6-phosphate 1-dehydrogenase Certain preparations reduce NAD(+) as well as NADP(+). D-glucose 6-phosphate + NADP(+) = D-glucono-1,5-lactone 6-phosphate + NADPH. http://purl.uniprot.org/mim/305900 Also acts slowly on beta-D-glucose and other sugars. Acetoin dehydrogenase Diacetyl reductase Acetoin + NAD(+) = diacetyl + NADH. NADP(+) also acts. Hydroxyprostaglandin dehydrogenase 3-alpha-HSD 3-alpha-hydroxysteroid dehydrogenase (B-specific) Acts on other 3-alpha-hydroxysteroids and on 9-, 11-and 15-hydroxyprostaglandin. Androsterone + NAD(P)(+) = 5-alpha-androstane-3,17-dione + NAD(P)H. B-specific with respect to NAD(+) or NADP(+) (cf. EC 1.1.1.213). 3(or 17)-beta-hydroxysteroid dehydrogenase Also acts on other 3-beta-or 17-beta-hydroxysteroids (cf. EC 1.1.1.209). Testosterone + NAD(P)(+) = androst-4-ene-3,17-dione + NAD(P)H. 3-alpha-hydroxycholanate dehydrogenase 3-alpha-hydroxy-5-beta-cholanate + NAD(+) = 3-oxo-5-beta-cholanate + NADH. Also acts on other 3-alpha-hydroxysteroids with an acidic side-chain. 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase Cortisone reductase (R)-20-hydroxysteroid dehydrogenase The 3-alpha-hydroxy group or 20-beta-hydroxy group of pregnane and androstane steroids can act as donor. Androstan-3-alpha,17-beta-diol + NAD(+) = 17-beta-hydroxyandrostan-3-one + NADH. Allyl-alcohol dehydrogenase Also acts on saturated primary alcohols. Allyl alcohol + NADP(+) = acrolein + NADPH. Lactaldehyde reductase (NADPH) May be identical with EC 1.1.1.2. Propane-1,2-diol + NADP(+) = L-lactaldehyde + NADPH. Ribitol 2-dehydrogenase Ribitol + NAD(+) = D-ribulose + NADH. D-mannonate oxidoreductase Mannonic dehydrogenase Fructuronate reductase D-mannonate dehydrogenase Also reduces D-tagaturonate. D-mannonate + NAD(+) = D-fructuronate + NADH. Altronic oxidoreductase Altronate dehydrogenase Altronate oxidoreductase Tagaturonate dehydrogenase Tagaturonate reductase D-altronate + NAD(+) = D-tagaturonate + NADH. 3-hydroxypropionate dehydrogenase 3-hydroxypropanoate + NAD(+) = 3-oxopropanoate + NADH. NAD-linked glycerol dehydrogenase Glycerol dehydrogenase Also acts on 1,2-propanediol. Glycerol + NAD(+) = glycerone + NADH. 2-hydroxy-3-oxopropionate reductase Tartronate semialdehyde reductase (R)-glycerate + NAD(P)(+) = 2-hydroxy-3-oxopropanoate + NAD(P)H. 4-hydroxybutyrate dehydrogenase 4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH. 17-beta-HSD 17-beta-hydroxysteroid dehydrogenase 17-beta-estradiol dehydrogenase Estrogen 17-oxidoreductase 20-alpha-hydroxysteroid dehydrogenase Estradiol 17-beta-dehydrogenase Also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds, oxidizing the (S)-20-group. B-specific with respect to NAD(P)(+) (cf. EC 1.1.1.149). Estradiol-17-beta + NAD(P)(+) = estrone + NAD(P)H. 17-beta-HSD 17-ketoreductase Testosterone 17-beta-dehydrogenase Testosterone + NAD(+) = androst-4-ene-3,17-dione + NADH. 17-ketoreductase Testosterone 17-beta-dehydrogenase (NADP(+)) http://purl.uniprot.org/mim/264300 Also oxidizes 3-hydroxyhexobarbital to 3-oxohexobarbital. Testosterone + NADP(+) = androst-4-ene-3,17-dione + NADPH. PL reductase Pyridoxine 4-dehydrogenase Pyridoxal reductase Pyridoxine dehydrogenase Pyridoxin dehydrogenase Pyridoxine + NADP(+) = pyridoxal + NADPH. Also oxidizes pyridoxine phosphate. Omega-hydroxydecanoate dehydrogenase 10-hydroxydecanoate + NAD(+) = 10-oxodecanoate + NADH. Also acts, more slowly, on 9-hydroxynonanoate and 11-hydroxyundecanoate. Mannitol dehydrogenase Mannitol 2-dehydrogenase D-mannitol + NAD(+) = D-fructose + NADH. 5-keto-D-gluconate 5-reductase 5-ketogluconate reductase Gluconate 5-dehydrogenase 5-ketogluconate 5-reductase D-gluconate + NAD(P)(+) = 5-dehydro-D-gluconate + NAD(P)H. Propanediol-phosphate dehydrogenase Propane-1,2-diol 1-phosphate + NAD(+) = hydroxyacetone phosphate + NADH. Retinal reductase Alcohol dehydrogenase (NAD(P)(+)) Also reduces retinal to retinol. Reduces aliphatic aldehydes of chain length from C2 to C14, with greatest activity on C4, C6 and C8 aldehydes. An alcohol + NAD(P)(+) = an aldehyde + NAD(P)H. Glycerol dehydrogenase (NADP(+)) Glycerol + NADP(+) = D-glyceraldehyde + NADPH. Octanol dehydrogenase Acts, less rapidly, on other long-chain alcohols. 1-octanol + NAD(+) = 1-octanal + NADH. (R)-aminopropanol dehydrogenase (R)-1-aminopropan-2-ol + NAD(+) = aminoacetone + NADH. Potassium (S,S)-butanediol dehydrogenase (S,S)-butane-2,3-diol + NAD(+) = acetoin + NADH. Lactaldehyde reductase Propanediol oxidoreductase (1) (R)-propane-1,2-diol + NAD(+) = (R)-lactaldehyde + NADH. (2) (S)-propane-1,2-diol + NAD(+) = (S)-lactaldehyde + NADH. Methylglyoxal reductase D-lactaldehyde dehydrogenase Methylglyoxal reductase (NADH-dependent) This mammalian enzyme differs from the yeast enzyme, EC 1.1.1.283, in using NADH rather than NADPH as reductant. It oxidizes HO-CH(2)-CHOH-CHO (glyceraldehyde) as well as CH(3)-CHOH-CHO (lactaldehyde). (R)-lactaldehyde + NAD(+) = methylglyoxal + NADH. Glyoxylate reductase (NADP(+)) Has some affinity for NAD(+). Glycolate + NADP(+) = glyoxylate + NADPH. Also reduces hydroxypyruvate to glycerate. Glycerol 1-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase (NAD(+)) Glycerophosphate dehydrogenase (NAD) L-alpha-glycerophosphate dehydrogenase Alpha-glycerol phosphate dehydrogenase (NAD) NAD-L-glycerol-3-phosphate dehydrogenase NAD-alpha-glycerophosphate dehydrogenase NAD-linked glycerol 3-phosphate dehydrogenase Glycerol phosphate dehydrogenase (NAD) NAD-dependent glycerol phosphate dehydrogenase L-alpha-glycerol phosphate dehydrogenase Hydroglycerophosphate dehydrogenase L-glycerophosphate dehydrogenase NADH-dihydroxyacetone phosphate reductase L-glycerol phosphate dehydrogenase Alpha-glycerophosphate dehydrogenase (NAD) NAD-dependent glycerol-3-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase (NAD) sn-glycerol 3-phosphate + NAD(+) = glycerone phosphate + NADH. Also acts on propane-1,2-diol phosphate and glycerone sulfate (but with a much lower affinity). Isopropanol dehydrogenase (NADP(+)) Also acts on other short-chain secondary alcohols and, slowly, on primary alcohols. Propan-2-ol + NADP(+) = acetone + NADPH. D-glycerate dehydrogenase Hydroxypyruvate reductase D-glycerate + NAD(P)(+) = hydroxypyruvate + NAD(P)H. Malate dehydrogenase (NADP(+)) NADP-linked malate dehydrogenase (S)-malate + NADP(+) = oxaloacetate + NADPH. Activated by light. D-malate dehydrogenase (decarboxylating) (R)-malate + NAD(+) = pyruvate + CO(2) + NADH. Dimethylmalate dehydrogenase Manganese or cobalt Also acts on (R)-malate. (R)-3,3-dimethylmalate + NAD(+) = 3-methyl-2-oxobutanoate + CO(2) + NADH. Potassium or ammonia Beta-IPM dehydrogenase IMDH Beta-isopropylmalate dehydrogenase 3-isopropylmalate dehydrogenase 3-carboxy-2-hydroxy-4-methylpentanoate + NAD(+) = 3-carboxy-4-methyl-2-oxopentanoate + NADH. The product decarboxylates spontaneously to yield 4-methyl-2-oxopentanoate. Dihydroxyisovalerate dehydrogenase (isomerizing) Ketol-acid reductoisomerase Acetohydroxy acid isomeroreductase Alpha-keto-beta-hydroxylacyl reductoisomerase (1) (R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. (2) (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. Homoisocitrate dehydrogenase (-)-1-hydroxy-1,2,4-butanetricarboxylate:NAD(+) oxidoreductase (decarboxylating) Homoisocitric dehydrogenase 2-hydroxy-3-carboxyadipate dehydrogenase 3-carboxy-2-hydroxyadipate dehydrogenase 3-carboxy-2-hydroxyadipate:NAD(+) oxidoreductase (decarboxylating) (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD(+) = 2-oxoadipate + CO(2) + NADH. Forms part of the lysine biosynthesis pathway in fungi. HMG-CoA reductase 3-hydroxy-3-methylglutaryl-coenzyme A reductase Beta-hydroxy-beta-methylglutaryl CoA-reductase Hydroxymethylglutaryl coenzyme A reductase Beta-hydroxy-beta-methylglutaryl coenzyme A reductase Hydroxymethylglutaryl-CoA reductase (R)-mevalonate + CoA + 2 NAD(+) = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH. Xylitol dehydrogenase D-xylulose reductase Xylitol + NAD(+) = D-xylulose + NADH. Also acts as an L-erythrulose reductase. Aryl-alcohol dehydrogenase Benzyl alcohol dehydrogenase p-hydroxybenzyl alcohol dehydrogenase A group of enzymes with broad specificity toward primary alcohols with an aromatic or cyclohex-1-ene ring, but with low or no activity toward short-chain aliphatic alcohols. An aromatic alcohol + NAD(+) = an aromatic aldehyde + NADH. Aryl-alcohol dehydrogenase (NADP(+)) Also acts on some aliphatic aldehydes, but cinnamaldehyde was the best substrate found. An aromatic alcohol + NADP(+) = an aromatic aldehyde + NADPH. Oxaloglycolate reductase (decarboxylating) Also reduces hydroxypyruvate to D-glycerate and glyoxylate to glycolate. D-glycerate + NAD(P)(+) + CO(2) = 2-hydroxy-3-oxosuccinate + NAD(P)H. Tartrate dehydrogenase Mesotartrate dehydrogenase Monovalent cation (1) Tartrate + NAD(+) = oxaloglycolate + NADH. (2) Meso-tartrate + NAD(+) = oxaloglycolate + NADH. (3) (R,R)-tartrate + NAD(+) = oxaloglycolate + NADH. Manganese Glycerol-3-phosphate dehydrogenase (NAD(P)(+)) Glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide (phosphate)) Glycerol 3-phosphate dehydrogenase (NAD(P)) Glycerol 3-phosphate dehydrogenase (NADP) L-glycerol-3-phosphate:NAD(P) oxidoreductase The enzyme from Escherichia coli shows specificity for the B side of NADPH. sn-glycerol 3-phosphate + NAD(P)(+) = glycerone phosphate + NAD(P)H. Phosphoglycerate oxidoreductase PGDH Glycerate 3-phosphate dehydrogenase Phosphoglyceric acid dehydrogenase 3-phosphoglycerate dehydrogenase Glycerate-1,3-phosphate dehydrogenase Alpha-phosphoglycerate dehydrogenase Alpha-KG reductase 3PHP reductase 3-phosphoglyceric acid dehydrogenase Phosphoglycerate dehydrogenase D-3-phosphoglycerate dehydrogenase (2) 2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH. The enzyme is unusual in that it also acts as a D-and L-2-hydroxyglutarate dehydrogenase (with the D-form being the better substrate) and as a 2-oxoglutarate reductase. (1) 3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH. http://purl.uniprot.org/mim/601815 Reaction (1) occurs predominantly in the reverse direction and is inhibited by serine and glycine. Catalyzes the first committed step in the phosphoserine pathway of serine biosynthesis in Escherichia coli. Diiodophenylpyruvate reductase Substrates contain an aromatic ring with a pyruvate side chain. Compounds with hydroxy or amino groups in the 3 or 5 position are inactive. 3-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD(+) = 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + NADH. The most active substrates are halogenated derivatives. 3-hydroxybenzyl-alcohol dehydrogenase m-hydroxybenzyl alcohol dehydrogenase 3-hydroxybenzyl alcohol + NADP(+) = 3-hydroxybenzaldehyde + NADPH. (R)-2-hydroxy-fatty-acid dehydrogenase D-2-hydroxy fatty acid dehydrogenase (R)-2-hydroxystearate + NAD(+) = 2-oxostearate + NADH. (S)-2-hydroxy-fatty-acid dehydrogenase L-2-hydroxy fatty acid dehydrogenase (S)-2-hydroxystearate + NAD(+) = 2-oxostearate + NADH. With a cytochrome as acceptor Mannitol dehydrogenase (cytochrome) Polyol dehydrogenase D-mannitol + ferricytochrome c = D-fructose + ferrocytochrome c. Acts on polyols with a D-lyxo configuration, such as D-mannitol and D-sorbitol. L-lactate ferricytochrome c oxidoreductase L-lactate dehydrogenase (cytochrome) Cytochrome b2 Lactic acid dehydrogenase FMN (S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H(+). Protoheme IX D-lactate dehydrogenase (cytochrome) Lactic acid dehydrogenase D-lactate ferricytochrome c oxidoreductase FAD (R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c. D-lactate dehydrogenase (cytochrome c-553) From Desulfovibrio vulgaris. (R)-lactate + 2 ferricytochrome c-553 = pyruvate + 2 ferrocytochrome c-553. With oxygen as acceptor Pyranose oxidase Glucose 2-oxidase Also oxidizes D-xylose, L-sorbose and D-glucono-1,5-lactone, which have the same ring conformation and configuration at C-2, C-3 and C-4. D-glucose + O(2) = 2-dehydro-D-glucose + H(2)O(2). FAD L-sorbose oxidase 2,6-dichloroindophenol can act as acceptor. Also acts on D-glucose, D-galactose and D-xylose, but not on D-fructose. L-sorbose + O(2) = 5-dehydro-D-fructose + H(2)O(2). Pyridoxin 4-oxidase Pyridoxine 4-oxidase 2,6-dichloroindophenol can act as acceptor. FAD Pyridoxine + O(2) = pyridoxal + H(2)O(2). AOX Alcohol oxidase Methanol oxidase Acts on lower primary alcohols and unsaturated alcohols but branched-chain and secondary alcohols are not attacked. FAD A primary alcohol + O(2) = an aldehyde + H(2)O(2). Catechol oxidase (dimerizing) 4 catechol + 3 O(2) = 2 dibenzo[1,4]dioxin-2,3-dione + 6 H(2)O. Hydroxy-acid oxidase A (S)-2-hydroxy-acid oxidase Glycolate oxidase Hydroxy-acid oxidase B FMN (S)-2-hydroxy acid + O(2) = 2-oxo acid + H(2)O(2). The rat isoenzyme B also acts as EC 1.4.3.2. Exists as two major isoenzymes; the A form preferentially oxidizes short-chain aliphatic hydroxy acids; the B form preferentially oxidizes long-chain and aromatic hydroxy acids. Ecdysone oxidase 2,6-dichloroindophenol can act as acceptor. Ecdysone + O(2) = 3-dehydroecdysone + H(2)O(2). Choline oxidase Also oxidizes betaine aldehyde to betaine. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 and EC 2.1.1.157. Different enzymes are involved in the first reaction. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. The enzyme involved in the second step, EC 1.2.1.8, appears to be the same in plants, animals and bacteria. In plants, this reaction is catalyzed by EC 1.14.15.7, whereas in animals and many bacteria, it is catalyzed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17). FAD Choline + O(2) = betaine aldehyde + H(2)O(2). Secondary-alcohol oxidase Acts on secondary alcohols with five or more carbons, and polyvinyl alcohols with molecular mass over 300 Da. Iron A secondary alcohol + O(2) = a ketone + H(2)O(2). 4-hydroxymandelate oxidase FAD (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O(2) = 4-hydroxybenzaldehyde + CO(2) + H(2)O(2). Manganese Long-chain-alcohol oxidase 2 long-chain alcohol + O(2) = 2 long-chain aldehyde + 2 H(2)O. Oxidizes long-chain fatty alcohols; best substrate is dodecyl alcohol. Alpha-glycerophosphate oxidase Glycerol-3-phosphate oxidase sn-glycerol 3-phosphate + O(2) = glycerone phosphate + H(2)O(2). FAD Thiamine oxidase Thiamine dehydrogenase The product differs from thiamine in replacement of -CH(2)-CH(2)-OH by -CH(2)-COOH; the two-step oxidation proceeds without the release of the intermediate aldehyde from the enzyme. FAD Thiamine + 2 O(2) + H(2)O = thiamine acetic acid + 2 H(2)O(2). Hydroxyphytanate oxidase L-2-hydroxyphytanate + O(2) = 2-oxophytanate + H(2)O(2). Nucleoside oxidase Other purine and pyrimidine nucleosides (as well as 2'-deoxynucleosides) are substrates, but ribose and nucleotides are not substrates. Inosine + O(2) = 9-riburonosylhypoxanthine + 2 H(2)O. The overall reaction takes place in two separate steps: (1) 2 inosine + O(2) = 2 5'-dehydroinosine + 2 H(2)O. (2) 2 5'-dehydroinosine + O(2) = 2 9-riburonosylhypoxanthine + 2 H(2)O. Differs from EC 1.1.3.39 as it produces water rather than hydrogen peroxide. The 5'-dehydro nucleoside is being released from the enzyme to serve as substrate for the second reaction. N-acylhexosamine oxidase Also acts on N-glycolylglucosamine, N-acetylgalactosamine and, more slowly, on N-acetylmannosamine. N-acetyl-D-glucosamine + O(2) = N-acetyl-D-glucosaminate + H(2)O(2). Malate oxidase Malic oxidase (S)-malate + O(2) = oxaloacetate + H(2)O(2). FAD Polyvinyl-alcohol oxidase PVA oxidase Polyvinyl alcohol + O(2) = oxidized polyvinyl alcohol + H(2)O(2). D-arabinono-1,4-lactone oxidase FAD D-arabinono-1,4-lactone + O(2) = D-erythro-ascorbate + H(2)O(2). 4-hydroxy-2-methoxybenzyl alcohol oxidase Vanillyl-alcohol oxidase Vanillyl alcohol + O(2) = vanillin + H(2)O(2). Converts a wide range of 4-hydroxybenzyl alcohols and 4-hydroxybenzylamines into the corresponding aldehydes. The allyl group of 4-allylphenols is also converted into the -CH=CH-CH(2)OH group. FAD Nucleoside oxidase (H(2)O(2)-forming) Differs from EC 1.1.3.28 as it produces hydrogen peroxide rather than water. Other purine and pyrimidine nucleosides (as well as 2'-deoxynucleosides and arabinosides) are substrates, but ribose and nucleotides are not substrates. Adenosine + 2 O(2) = 9-riburonosyladenine + 2 H(2)O(2). The overall reaction takes place in two separate steps: (1) Adenosine + O(2) = 5'-dehydroadenosine + H(2)O(2). (2) 5'-dehydroadenosine + O(2) = 9-riburonosyladenine + H(2)O(2). Heme The 5'-dehydro nucleoside is being released from the enzyme to serve as substrate for the second reaction. FAD Beta-D-glucose:oxygen 1-oxido-reductase Glucose oxyhydrase GOD Glucose aerodehydrogenase Glucose oxidase D-glucose-1-oxidase FAD Beta-D-glucose + O(2) = D-glucono-1,5-lactone + H(2)O(2). D-arabinitol oxidase D-mannitol oxidase Mannitol oxidase Also catalyzes the oxidation of D-arabinitol and, to a lesser extent, D-glucitol (sorbitol), whereas L-arabinitol is not a good substrate. Mannitol + O(2) = mannose + H(2)O(2). The enzyme from the snails Helix aspersa and Arion ater is found in a specialized tubular organelle that has been termed the mannosome. Xylitol oxidase The enzyme also oxidizes D-sorbitol. Xylitol + O(2) = xylose + H(2)O(2). FAD Hexose oxidase Also oxidizes D-galactose, D-mannose, maltose, lactose and cellobiose. Copper Beta-D-glucose + O(2) = D-glucono-1,5-lactone + H(2)O(2). Cholesterol-O(2) oxidoreductase Cholesterol oxidase Cholesterol + O(2) = cholest-4-en-3-one + H(2)O(2). FAD Veratryl alcohol oxidase Aryl-alcohol oxidase An aromatic primary alcohol + O(2) = an aromatic aldehyde + H(2)O(2). Oxidizes many primary alcohols containing an aromatic ring; best substrates are (2-naphthyl)methanol and 3-methoxybenzyl alcohol. L-gulonolactone oxidase L-gulono-gamma-lactone oxidase GLO The product spontaneously isomerizes to L-ascorbate. (1) L-gulono-1,4-lactone + O(2) = L-xylo-hex-2-ulono-1,4-lactone + H(2)O(2). FAD While most higher animals can synthesize ascorbic acid, primates and guinea pigs cannot. (2) L-xylo-hex-2-ulono-1,4-lactone = L-ascorbate. Galactose oxidase Beta-galactose oxidase D-galactose + O(2) = D-galacto-hexodialdose + H(2)O(2). Copper With a disulfide as acceptor Vitamin K1 epoxide reductase Phylloquinone epoxide reductase Vitamin-K-epoxide reductase (warfarin-sensitive) In the reverse reaction, vitamin K 2,3-epoxide is reduced to vitamin K and possibly to vitamin K hydroquinone by 1,4-dithioerythritol, which is oxidized to a disulfide; some other dithiols and 4-butanethiol can also act. 2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol. Inhibited strongly by warfarin (cf. EC 1.1.4.2). Vitamin K 2,3-epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive) Not inhibited by warfarin (cf. EC 1.1.4.1). In the reverse reaction, vitamin K 2,3-epoxide is reduced to 3-hydroxy-(and 2-hydroxy-) vitamin K by 1,4-dithioerythritol, which is oxidized to a disulfide. 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol. With a quinone or similar compound as acceptor Glucose dehydrogenase (PQQ-dependent) Glucose dehydrogenase (pyrroloquinoline-quinone) Quinoprotein glucose dehydrogenase D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase Quinoprotein D-glucose dehydrogenase Magnesium or calcium This is a PQQ-containing quinoprotein that catalyzes a direct oxidation of D-glucose to D-gluconate in the periplasm of some bacteria and concomitantly transfers electrons to ubiquinol oxidase through ubiquinone in the respiratory chain. D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol. PQQ With other acceptors Choline-cytochrome c reductase Choline oxidase Choline dehydrogenase PQQ Choline + acceptor = betaine aldehyde + reduced acceptor. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. In plants, this reaction is catalyzed by EC 1.14.15.7, whereas in animals and many bacteria, it is catalyzed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17). In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 and EC 2.1.1.157. Different enzymes are involved in the first reaction. The enzyme involved in the second step, EC 1.2.1.8, appears to be the same in plants, animals and bacteria. Glucose dehydrogenase (acceptor) Glucose dehydrogenase (Aspergillus) D-glucose + acceptor = D-glucono-1,5-lactone + reduced acceptor. FAD 2,6-dichloroindophenol can act as acceptor. Fructose 5-dehydrogenase D-fructose dehydrogenase 2,6-dichloroindophenol can act as acceptor. D-fructose + acceptor = 5-dehydro-D-fructose + reduced acceptor. Sorbose dehydrogenase 2,6-dichloroindophenol can act as acceptor. L-sorbose + acceptor = 5-dehydro-D-fructose + reduced acceptor. D-aldohexopyranoside dehydrogenase Glucoside 3-dehydrogenase The enzyme acts on D-glucose, D-galactose, D-glucosides and D-galactosides, but D-glucosides react more rapidly than D-galactosides. FAD Sucrose + acceptor = 3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside + reduced acceptor. Glycolic acid dehydrogenase Glycolate dehydrogenase Glycolate oxidoreductase Also acts on (R)-lactate. Glycolate + acceptor = glyoxylate + reduced acceptor. 2,6-dichloroindophenol and phenazine methosulfate can act as acceptors. Malate dehydrogenase (acceptor) FAD (S)-malate + acceptor = oxaloacetate + reduced acceptor. Cellobiose dehydrogenase Cellobiose oxidase CBOR Cellobiose oxidoreductase CDH Cellobiose dehydrogenase (quinone) Cellobiose dehydrogenase (acceptor) Cellobiose-quinone oxidoreductase The enzyme from the white rot fungus Phanerochaete chrysosporium is unusual in having two redoxin domains, one containing a flavin and the other a protoheme group. Cellobiose + acceptor = cellobiono-1,5-lactone + reduced acceptor. 2,6-dichloroindophenol can act as acceptor. FAD Heme Also acts, more slowly, on cello-oligosaccharides, lactose and D-glucosyl-1,4-beta-D-mannose. Includes EC 1.1.5.1, which is now known to be a proteolytic product of this enzyme. It transfers reducing equivalents from cellobiose to two types of redox acceptor: two-electron oxidants, including redox dyes, benzoquinones and molecular oxygen and one-electron oxidants, including semiquinone species, Fe(2+) complexes and the model acceptor cytochrome c. L-alpha-hydroxyglutarate dehydrogenase Hydroxyglutaric dehydrogenase 2-hydroxyglutarate dehydrogenase Alpha-hydroxyglutarate dehydrogenase Alpha-ketoglutarate reductase Alpha-hydroxyglutarate oxidoreductase FAD (S)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor. http://purl.uniprot.org/mim/236792 Polyethylene glycol dehydrogenase Alkan-1-ol dehydrogenase (acceptor) Primary alcohol + acceptor = aldehyde + reduced acceptor. PQQ 2,6-dichloroindophenol can act as acceptor. Acts on C(3)-C(16) linear-chain saturated primary alcohols, C(4)-C(7) aldehydes and on non-ionic surfactants containing polyethylene glycol residues, such as Tween 40 and 60, but not on methanol and only very slowly on ethanol. D-sorbitol dehydrogenase (acceptor) FAD D-sorbitol + acceptor = L-sorbose + reduced acceptor. Glycerol dehydrogenase (acceptor) PQQ Glycerol + acceptor = glycerone + reduced acceptor. Also acts, more slowly, on a number of other polyols including D-sorbitol, D-arabinitol, meso-erythritol, adonitol and propylene glycol. Polyvinyl-alcohol dehydrogenase (acceptor) PVA dehydrogenase Polyvinyl alcohol + acceptor = oxidized polyvinyl alcohol + reduced acceptor. Phenazine methosulfate and 2,6-dichloroindophenol can act as acceptors. Also acts, more slowly, on 2-hexanol and some other secondary alcohols (cf. EC 1.1.99.8 and EC 1.1.99.20). PQQ Hydroxyacid--oxoacid transhydrogenase (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2-hydroxyglutarate. 4-hydroxybutanoate and (R)-2-hydroxyglutarate can also act as donors; 4-oxobutanoate can also act as acceptor. Quinate dehydrogenase (pyrroloquinoline-quinone) NAD(P)-independent quinate dehydrogenase Quinate:pyrroloquinoline-quinone 5-oxidoreductase Quinate + pyrroloquinoline-quinone = 3-dehydroquinate + reduced pyrroloquinoline-quinone. 3-hydroxycyclohexanone dehydrogenase 2,6-dichloroindophenol and methylene blue can act as acceptors. 3-hydroxycyclohexanone + acceptor = cyclohexane-1,3-dione + reduced acceptor. (R)-pantoyllactone dehydrogenase (flavin) 2-dehydropantolactone reductase (flavin) 2-dehydropantoyl-lactone reductase (flavin) (R)-pantolactone dehydrogenase (flavin) High specificity for (R)-pantolactone. FMN Phenazine methosulfate (PMS) can act as acceptor. The enzyme has been studied in Nocardia asteroides and shown to be membrane-bound and induced by 1,2-propanediol. (R)-pantolactone + acceptor = 2-dehydropantolactone + reduced acceptor. Glucose--fructose oxidoreductase D-mannose, D-xylose, D-galactose, 2-deoxy-D-glucose and L-arabinose will function as aldose substrates, but with low affinities. Xylulose and glycerone (dihydroxyacetone) will replace fructose, but they are poor substrates. The apparent affinity for fructose is low, because little of the fructose substrate is in the open-chain form. D-glucose + D-fructose = D-gluconolactone + D-glucitol. The enzyme from Zymomonas mobilis contains tightly bound NADP(+). The ketose substrate must be in the open-chain form. Pyranose dehydrogenase Pyranose dehydrogenase (acceptor) Quinone-dependent pyranose dehydrogenase Pyranose-quinone oxidoreductase PDH (2) Pyranose + acceptor = 3-dehydropyranose + reduced acceptor. (3) Pyranose + acceptor = 2,3-dehydropyranose + reduced acceptor. A number of aldoses and ketoses in pyranose form, as well as glycosides, gluco-oligosaccharides, sucrose and lactose can act as a donor. FAD The enzyme also acts on 1->4-alpha-and 1->4-beta-gluco-oligosaccharides, non-reducing gluco-oligosaccharides and L-arabinose, which are not substrates of EC 1.1.3.10. D-glucose is exclusively or preferentially oxidized at C-3 (depending on the enzyme source), but can also be oxidized at C-2 + C-3. (5) A pyranoside + acceptor = a 3,4-dehydropyranoside + reduced acceptor. (4) A pyranoside + acceptor = a 3-dehydropyranoside + reduced acceptor. 1,4-benzoquinone or ferricenium ion (ferrocene oxidized by removal of one electron) can serve as acceptor. Unlike EC 1.1.3.10, this fungal enzyme does not interact with O(2) and exhibits extremely broad substrate tolerance with variable regioselectivity (C-3, C-2 or C-3 + C-2 or C-3 + C-4) for (di)oxidation of different sugars. (1) Pyranose + acceptor = 2-dehydropyranose + reduced acceptor. Sugars are oxidized in their pyranose but not in their furanose form. Gluconate 2-dehydrogenase (acceptor) FAD D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor. 2-oxoacid reductase HVOR (2R)-hydroxycarboxylate-viologen-oxidoreductase 2-oxo-acid reductase Mononucleotide molybdenum (pyranopterin) cofactor The enzyme from Proteus sp. is inactivated by oxygen. Branching in a substrate at the C-3 position results in loss of activity. A (2R)-hydroxy-carboxylate + acceptor = a 2-oxo-carboxylate + reduced acceptor. Iron-sulfur Has broad substrate specificity, with 2-oxo-monocarboxylates and 2-oxo-dicarboxylates acting as substrates. MDH (S)-mandelate dehydrogenase L(+)-mandelate dehydrogenase Transfers the electron pair from FMNH(2) to a component of the electron transport chain, most probably ubiquinone. It also prefers substrates that, like (S)-mandelate, have beta unsaturation, e.g. (indol-3-yl)glycolate compared with (indol-3-yl)lactate. (S)-2-hydroxy-2-phenylacetate + acceptor = 2-oxo-2-phenylacetate + reduced acceptor. Has a large active-site pocket and preferentially binds substrates with longer sidechains, e.g. 2-hydroxyoctanoate rather than 2-hydroxybutyrate. While all enzymes of this family oxidize the (S)-enantiomer of an alpha-hydroxy acid to an alpha-oxo acid, the ultimate oxidant (oxygen, intramolecular heme or some other acceptor) depends on the particular enzyme. Esters of mandelate, such as methyl (S)-mandelate, are also substrates. It is part of a metabolic pathway in Pseudomonads that allows these organisms to utilize mandelic acid, derivatized from the common soil metabolite amygdalin, as the sole source of carbon and energy. Dehydrogluconate dehydrogenase Ketogluconate dehydrogenase 2-dehydro-D-gluconate + acceptor = 2,5-didehydro-D-gluconate + reduced acceptor. Flavoprotein Glycerol-3-phosphate dehydrogenase Flavin sn-glycerol 3-phosphate + acceptor = glycerone phosphate + reduced acceptor. D-2-hydroxy-acid dehydrogenase (R)-lactate + acceptor = pyruvate + reduced acceptor. Acts on a variety of (R)-2-hydroxy acids. FAD Zinc Lactate--malate transhydrogenase (S)-lactate + oxaloacetate = pyruvate + malate. Contains tightly bound nicotinamide nucleotide in its active center. Catalyzes hydrogen transfer from C(3) or C(4) (S)-2-hydroxy acids to 2-oxo acids. This prosthetic group cannot be removed without denaturation of the protein. Methanol dehydrogenase Alcohol dehydrogenase (acceptor) Acts on a wide range of primary alcohols, including methanol. PQQ A primary alcohol + acceptor = an aldehyde + reduced acceptor. Pyridoxol 5-dehydrogenase Pyridoxine 5-dehydrogenase Pyridoxine + acceptor = isopyridoxal + reduced acceptor. FAD Acting on diphenols and related substances as donors With NAD(+) or NADP(+) as acceptor Trans-acenaphthene-1,2-diol dehydrogenase (+-)-trans-acenaphthene-1,2-diol + 2 NADP(+) = acenaphthenequinone + 2 NADPH. Some preparations also utilize NAD(+). With a cytochrome as acceptor L-ascorbate--cytochrome-b5 reductase L-ascorbate + ferricytochrome b5 = monodehydroascorbate + ferrocytochrome b5 + H(+). Ubiquinone--cytochrome-c oxidoreductase Complex III (mitochondrial electron transport) Cytochrome bc1 complex Ubiquinol--cytochrome-c reductase Depending on the organism and physiological conditions, either two or four protons are extruded from the cytoplasmic to the non-cytoplasmic compartment (cf. EC 1.6.99.3). QH(2) + 2 ferricytochrome c = Q + 2 ferrocytochrome c + 2 H(+). Contains cytochrome b-562, cytochrome b-566, cytochrome c1, and 2-iron ferredoxin. With oxygen as acceptor Catechol oxidase o-diphenolase Diphenol oxidase Polyphenol oxidase Phenolase Tyrosinase Copper Many of these enzymes also catalyze the reaction listed under EC 1.14.18.1; this is especially true for the classical tyrosinase. Also acts on a variety of substituted catechols. 2 catechol + O(2) = 2 1,2-benzoquinone + 2 H(2)O. Laccase Urishiol oxidase The semiquinone may react further either enzymically or non-enzymically. A group of multi-copper proteins of low specificity. Copper 4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O. Acts on both o-and p-quinols, and often acting also on aminophenols and phenylenediamine. Ascorbase L-ascorbate oxidase Copper 2 L-ascorbate + O(2) = 2 dehydroascorbate + 2 H(2)O. o-aminophenol oxidase Isophenoxazine synthase Flavoprotein Copper or manganese Two molecules of the product 6-iminocyclohexa-2,4-dienone (i.e. 1,2-benzoquinone monoimine) spontaneously condense with oxidation to yield 2-aminophenoxazin-3-one. While the enzyme from the plant Tecoma stans is activated by Mn(2+), that from the bacterium Streptomyces griseus (GriF) requires Cu(2+) for maximal activity. 3-amino-4-hydroxybenzaldehyde, which has a -CHO group at the para-position with respect to the hydroxy group of 2-aminophenol, was found to be the best substrate for GriF. 2 2-aminophenol + O(2) + oxidant = 2-aminophenoxazin-3-one + 2 H(2)O + reduced oxidant. 3-hydroxyanthranilate oxidase 3-hydroxyanthranilic acid oxidase 3-hydroxyanthranilate + O(2) = 6-imino-5-oxocyclohexa-1,3-dienecarboxylate + H(2)O(2). Rifamycin-B oxidase Also acts on benzene-1,4-diol and, more slowly, on some other p-quinols. Rifamycin B + O(2) = rifamycin O + H(2)O(2). Not identical with EC 1.10.3.1, EC 1.10.3.2, EC 1.10.3.4 or EC 1.10.3.5. With other acceptors Plastoquinol--plastocyanin reductase Cytochrome b6f complex A cytochrome f,b6 complex separated from chloroplasts. Plastoquinol-1 + 2 oxidized plastocyanin = plastoquinone + 2 reduced plastocyanin. Cytochrome c-552 can act instead of plastocyanin, but more slowly. Also acts, more slowly, on plastoquinol-9 and ubiquinols. NAD(P)H:quinone oxidoreductase 2 Ribosyldihydronicotinamide dehydrogenase (quinone) N-ribosyldihydronicotinamide dehydrogenase (quinone) NQO(2) Quinone reductase 2 NRH:quinone oxidoreductase 2 QR2 1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(beta-D-ribofuranosyl)nicotinamide + a hydroquinone. FAD This enzyme can catalyze both 2-electron and 4-electron reductions, but one-electron acceptors, such as potassium ferricyanide, cannot be reduced. Polycyclic aromatic hydrocarbons, such as benz[a]anthracene, and the estrogens 17-beta-estradiol and diethylstilbestrol are potent inhibitors, but dicoumarol is only a very weak inhibitor. Zinc Unlike EC 1.6.5.2, this quinone reductase cannot use NADH or NADPH; instead it uses N-ribosyl-and N-alkyldihydronicotinamides. VDE Violaxanthin de-epoxidase It is activated by a low pH of the thylakoid lumen (produced by high light intensity). Zeaxanthin induces the dissipation of excitation energy in the chlorophyll of the light-harvesting protein complex of photosystem II. Along with EC 1.14.13.90, this enzyme forms part of the xanthophyll (or violaxanthin) cycle for controlling the concentration of zeaxanthin in chloroplasts. (2) Antheraxanthin + ascorbate = zeaxanthin + dehydroascorbate + H(2)O. In higher plants the enzyme reacts with all-trans-diepoxides, such as violaxanthin, and all-trans-monoepoxides, but in the alga Mantoniella squamata, only the diepoxides are good substrates. (1) Violaxanthin + ascorbate = antheraxanthin + dehydroascorbate + H(2)O. Acting on a peroxide as acceptor Peroxidases NADH peroxidase NADH + H(2)O(2) = NAD(+) + 2 H(2)O. FAD Ferricyanide, quinones, etc., can replace H(2)O(2). Chloride peroxidase Chloroperoxidase Also acts on bromide and iodide. 2 RH + 2 Cl(-) + H(2)O(2) = 2 RCl + 2 H(2)O. Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds. Heme L-ascorbate peroxidase Ascorbic acid peroxidase L-ascorbate + H(2)O(2) = dehydroascorbate + 2 H(2)O. Phospholipid-hydroperoxide glutathione peroxidase Peroxidation-inhibiting protein Also acts on H(2)O(2), but much more slowly (cf. EC 1.11.1.9). The products of action of EC 1.13.11.12 on phospholipids can act as acceptor. Selenium 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H(2)O. Mn-dependent peroxidase Manganese peroxidase 2 Mn(2+) + 2 H(+) + H(2)O(2) = 2 Mn(3+) + 2 H(2)O. Involved in the oxidative degradation of lignin in white rot Basidiomycetes. Heme Diarylpropane oxygenase Ligninase I Lignin peroxidase LiP Diarylpropane peroxidase Involved in the oxidative breakdown of lignin in white rot basidiomycetes. Also oxidizes benzyl alcohols to aldehydes, via an aromatic cation radical. Heme Brings about the oxidative cleavage of C-C and ether (C-O-C) bonds in a number of lignin model compounds (of the diarylpropane and arylpropane-aryl ether type). Molecular oxygen may be involved in the reaction of some isoenzymes under aerobic conditions. 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H(2)O(2) = 3,4-dimethoxybenzaldehyde + 1-(3,4-dimethoxyphenyl)ethane-1,2-diol + H(2)O. TrxPx Peroxiredoxin Tryparedoxin peroxidase TXNPx AhpC Prx Alkyl hydroperoxide reductase C22 Thioredoxin peroxidase PRDX In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. The peroxidase reaction comprises two steps centered around a redox-active cysteine called the peroxidatic cysteine. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. VP Hybrid peroxidase Polyvalent peroxidase Versatile peroxidase (1) Reactive Black 5 + H(2)O(2) = oxidized Reactive Black 5 + 2 H(2)O. Also able to oxidize phenols, hydroquinones and both low-and high-redox-potential dyes, due to a hybrid molecular architecture that involves multiple binding sites for substrates. (2) Donor + H(2)O(2) = oxidized donor + 2 H(2)O. This ligninolytic peroxidase combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, EC 1.11.1.13 and EC 1.11.1.14. Heme NADPH peroxidase NADPH + H(2)O(2) = NADP(+) + 2 H(2)O. Fatty-acid peroxidase Acts on long-chain fatty acids from dodecanoic to octadecanoic acid. Palmitate + 2 H(2)O(2) = pentadecanal + CO(2) + 3 H(2)O. Cytochrome-c peroxidase 2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O. Heme Catalase 2 H(2)O(2) = O(2) + 2 H(2)O. http://purl.uniprot.org/mim/115500 A manganese protein containing Mn(3+) in the resting state, which also belongs here, is often called pseudocatalase. Heme Manganese This enzyme can also act as an EC 1.11.1.7 for which several organic substances, especially ethanol, can act as a hydrogen donor. Enzymes from some microorganisms, such as Penicillium simplicissimum, which exhibit both catalase and peroxidase activity, have sometimes been referred to as catalase-peroxidase. Myeloperoxidase Lactoperoxidase Peroxidase http://purl.uniprot.org/mim/261500 Donor + H(2)O(2) = oxidized donor + 2 H(2)O. http://purl.uniprot.org/mim/254600 Heme Thyroid peroxidase TPO Iodide peroxidase Iodotyrosine deiodase Thyroperoxidase Iodinase Iodotyrosine deiodinase Heme http://purl.uniprot.org/mim/274500 2 iodide + H(2)O(2) + 2 H(+) = 2 iodine + 2 H(2)O. Glutathione peroxidase 2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O. Selenium http://purl.uniprot.org/mim/138320 Steroid and lipid hydroperoxides, but not the product of reaction of EC 1.13.11.12 on phospholipids, can act as acceptor, but more slowly than H(2)O(2) (cf. EC 1.11.1.12). Acting on hydrogen as donor With NAD(+) or NADP(+) as acceptor Hydrogen dehydrogenase Hydrogenase Bidirectional hydrogenase NAD-linked hydrogenase H(2):NAD(+) oxidoreductase Iron-sulfur Nickel H(2) + NAD(+) = H(+) + NADH. FMN or FAD Hydrogen dehydrogenase (NADP(+)) NADP-reducing hydrogenase NADP-linked hydrogenase Flavoprotein H(2) + NADP(+) = H(+) + NADPH. Iron-sulfur With a cytochrome as acceptor Cytochrome-c3 hydrogenase H(2):ferricytochrome c3 oxidoreductase Cytochrome c3 reductase Cytochrome hydrogenase Some forms of the enzyme contain nickel ([NiFe]-hydrogenases) and, of these, some contain selenocysteine ([NiFeSe]-hydrogenases). Iron-sulfur Nickel Methylene blue and other acceptors can also be reduced. 2 H(2) + ferricytochrome c3 = 4 H(+) + ferrocytochrome c3. With a quinone or similar compound as acceptor Membrane-bound hydrogenase Hydrogen:quinone oxidoreductase Hydrogen-ubiquinone oxidoreductase Quinone-reactive Ni/Fe-hydrogenase Hydrogen:menaquinone oxidoreductase Also catalyzes the reduction of water-soluble quinones (e.g. 2,3-dimethylnaphthoquinone) or viologen dyes (benzyl viologen or methyl viologen) by H(2). H(2) + menaquinone = menaquinol. Iron-sulfur Nickel With an iron-sulfur protein as acceptor H(2) oxidizing hydrogenase Hydrogenase (ferredoxin) H(2) producing hydrogenase Hydrogenase I Uptake hydrogenase Hydrogenlyase Hydrogenase II Hydrogen-lyase Hydrogenase Bidirectional hydrogenase Ferredoxin hydrogenase H(2) + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H(+). Nickel Iron-sulfur Can use molecular hydrogen for the reduction of a variety of substances. With other known acceptors Coenzyme F420-dependent hydrogenase Coenzyme F420 hydrogenase F420-reducing hydrogenase 8-hydroxy-5-deazaflavin-reducing hydrogenase The hydrogen acceptor coenzyme F420 is a deazaflavin derivative. FAD H(2) + coenzyme F420 = reduced coenzyme F420. The enzyme from some sources contains selenocysteine. Nickel The enzyme also reduces the riboflavin analog of F420, flavins and methylviologen, but to a lesser extent. Iron N(5),N(10)-methenyltetrahydromethanopterin hydrogenase H(2)-dependent methylene-H(4)MPT dehydrogenase H(2)-forming N(5),N(10)-methylenetetrahydromethanopterin dehydrogenase Hydrogen:N(5),N(10)-methenyltetrahydromethanopterin oxidoreductase Nonmetal hydrogenase 5,10-methenyltetrahydromethanopterin hydrogenase Does not contain nickel or iron-sulfur clusters. Does not catalyze the reduction of artificial dyes. Does not by itself catalyze a H(2)/H(+) exchange reaction. H(2) + 5,10-methenyltetrahydromethanopterin = H(+) + 5,10-methylenetetrahydromethanopterin. Methylviologen-reducing hydrogenase Methanophenazine hydrogenase Methanosarcina-phenazine hydrogenase H(2) + 2-(2,3-dihydropentaprenyloxy)phenazine = 2-dihydropentaprenyloxyphenazine. Iron-sulfur Nickel The enzyme from some sources contains selenocysteine. With other acceptors Hydrogenase (acceptor) Hydrogenlyase Uptake hydrogenase H(2) producing hydrogenase Hydrogen-lyase H(2) + A = AH(2). Iron-sulfur Uses molecular hydrogen for the reduction of a variety of substances. Nickel Acting on single donors with incorporation of molecular oxygen With incorporation of two atoms of oxygen Catechol 1,2-dioxygenase Pyrocatechase Catechase Iron Catechol + O(2) = cis,cis-muconate. Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida. 7,8-dihydroxykynurenate 8,8a-dioxygenase 7,8-dihydroxykynurenate oxygenase Iron 7,8-dihydroxykynurenate + O(2) = 5-(3-carboxy-3-oxopropenyl)-4,6-dihydroxypyridine-2-carboxylate. Indoleamine 2,3-dioxygenase Tryptophan 2,3-dioxygenase Tryptophan peroxidase L-tryptophan pyrrolase Tryptamine 2,3-dioxygenase L-tryptophan 2,3-dioxygenase Tryptophan oxygenase Indolamine 2,3-dioxygenase Tryptamin 2,3-dioxygenase Tryptophanase Tryptophan pyrrolase Specific for tryptophan as substrate, but is far more active with L-tryptophan than with D-tryptophan. Catalyzes, together with EC 1.13.11.52, the first and rate-limiting step in the kynurenine pathway, the major pathway of tryptophan metabolism. L-tryptophan + O(2) = N-formyl-L-kynurenine. Heme Lipoxygenase Lipoperoxidase Carotene oxidase Lipoxidase Also oxidizes other methylene-interrupted polyunsaturated fatty acids. Iron Linoleate + O(2) = (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate. Ascorbate 2,3-dioxygenase Ascorbate + O(2) + H(2)O = oxalate + threonate. Iron 2,3-dihydroxybenzoate 3,4-dioxygenase o-pyrocatechuate oxygenase 2,3-dihydroxybenzoic oxygenase 2,3-dihydroxybenzoate + O(2) = 3-carboxy-2-hydroxymuconate semialdehyde. 3,4-dihydroxyphenylacetate 2,3-dioxygenase HPC dioxygenase Homoprotocatechuate 2,3-dioxygenase 3,4-dihydroxyphenylacetate + O(2) = 2-hydroxy-5-carboxymethylmuconate semialdehyde. Iron 3-carboxyethylcatechol 2,3-dioxygenase Iron 3-(2,3-dihydroxyphenyl)propanoate + O(2) = 2-hydroxy-6-oxonona-2,4-diene-1,9-dioate. Indole oxidase Indole 2,3-dioxygenase Flavoprotein A second enzyme from Tecoma stans, which is not a flavoprotein, uses four atoms of oxygen and forms anthranilate as the final product. Copper One enzyme from Tecoma stans is also a flavoprotein containing copper and uses three atoms of oxygen per molecule of indole, to form anthranil (3,4-benzisoxazole). The enzyme from Jasminum is a flavoprotein containing copper, and forms anthranilate as the final product. Indole + O(2) = 2-formylaminobenzaldehyde. Sulfur dioxygenase Sulfur oxygenase Glutathione (GSH) plays a catalytic role in elemental sulfur activation, but is not consumed during the enzymic reaction. The sulfite can be further converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO(3)(-)) non-enzymically. Iron GSH and elemental sulfur react non-enzymically to yield S-sulfanylglutathione and it is only in this form that the sulfur can be oxidized to yield sulfite. Sulfur + O(2) + H(2)O = sulfite + 2 H(+). Cysteamine oxygenase Cysteamine dioxygenase Persulfurase 3-aminopropanethiol (homocysteamine) and 2-mercaptoethanol can also act as substrates, but glutathione, cysteine, and cysteine ethyl-and methyl esters are not good substrates. 2-aminoethanethiol + O(2) = hypotaurine. Involved in the biosynthesis of taurine. Requires catalytic amounts of a cofactor-like compound, such as sulfur, sufide, selenium or methylene blue for maximal activity. Iron 2,3-pyrocatechase Catechol 2,3-dioxygenase Metapyrocatechase Cato2ase Catechol + O(2) = 2-hydroxymuconate semialdehyde. The enzyme from Alcaligenes sp. strain O-1 has also been shown to catalyze the reaction: 2,3-dihydroxybenzenesulfonate + O(2) + H(2)O = 2-hydroxymuconate + bisulfite and has been referred to as 2,3-dihydroxybenzenesulfonate 2,3-dioxygenase. Further work will be necessary to show whether or not this is a distinct enzyme. Iron Cysteine dioxygenase Iron NAD(P)H L-cysteine + O(2) = 3-sulfinoalanine. Caffeate 3,4-dioxygenase 3,4-dihydroxy-trans-cinnamate + O(2) = 3-(2-carboxyethenyl)-cis,cis-muconate. 2,3-dihydroxyindole 2,3-dioxygenase 2,3-dihydroxyindole + O(2) + H(+) = anthranilate + CO(2). Quercetin 2,3-dioxygenase Copper or iron Quercetin + O(2) = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H(+). Quercetin is a flavonol (5,7,3',4'-tetrahydroxyflavonol). Steroid 4,5-dioxygenase 3-alkylcatechol 2,3-dioxygenase 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase Also acts on 3-isopropylcatechol and 3-tert-butyl-5-methylcatechol. Iron 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + O(2) = 3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-dien-4-oate. Pyrrolooxygenase Tryptophan pyrrolooxygenase Peptide-tryptophan 2,3-dioxygenase Also acts on tryptophan. Peptide tryptophan + O(2) = peptide formylkynurenine. 4-hydroxyphenylpyruvate hydroxylase p-hydroxyphenylpyruvate oxidase 4-hydroxyphenylpyruvate dioxygenase p-hydroxyphenylpyruvate dioxygenase 4-hydroxyphenylpyruvate + O(2) = homogentisate + CO(2). http://purl.uniprot.org/mim/140350 http://purl.uniprot.org/mim/276710 Iron 2,3-dihydroxybenzoate 2,3-dioxygenase Also acts, more slowly, with 2,3-dihydroxy-4-methylbenzoate and 2,3-dihydroxy-4-isopropylbenzoate. 2,3-dihydroxybenzoate + O(2) = 2-carboxy-cis,cis-muconate. Stizolobate synthase Zinc The intermediate product undergoes ring closure and oxidation, with NAD(P)(+) as acceptor, to stizolobic acid. 3,4-dihydroxy-L-phenylalanine + O(2) = 4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde. Protocatechuate 3,4-dioxygenase Protocatechuate oxygenase Iron 3,4-dihydroxybenzoate + O(2) = 3-carboxy-cis,cis-muconate. Stizolobinate synthase 3,4-dihydroxy-L-phenylalanine + O(2) = 5-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde. The intermediate product undergoes ring closure and oxidation, with NAD(P)(+) as acceptor, to stizolobinic acid. Zinc Arachidonate 12-lipoxygenase 12-lipoxygenase The product is rapidly reduced to the corresponding 12S-hydroxy compound. Iron Arachidonate + O(2) = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate. 2-nitropropane dioxygenase 2-NPD Nitroalkane oxidase 2 2-nitropropane + O(2) = 2 acetone + 2 nitrite. While the enzyme from the fungus Neurospora crassa contains non-covalently bound FMN as the cofactor, that from the yeast Williopsis mrakii contains FAD. FAD or FMN Some other nitroalkanes, including nitroethane, 1-nitropropane and 3-nitropentan-2-ol, can act as donors, but more slowly. Has broad substrate specificity that is independent of substrate size. Differs from EC 1.7.3.1 in that the preferred substrates are anionic nitronates rather than neutral nitroalkanes. 15-lipoxygenase Arachidonate 15-lipoxygenase Arachidonate omega(6) lipoxygenase The product is rapidly converted to the corresponding 15S-hydroxy compound. Arachidonate + O(2) = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate. Iron 5-lipoxygenase Arachidonic 5-lipoxygenase Leukotriene-A(4) synthase Delta(5)-lipoxygenase Arachidonic acid 5-lipoxygenase 5-Delta-lipoxygenase C-5-lipoxygenase Arachidonate 5-lipoxygenase LTA synthase Iron (1) Arachidonate + O(2) = (6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyicosa-6,8,11,14-tetraenoate. (2) (6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyicosa-6,8,11,14-tetraenoate = (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H(2)O. The product of the second reaction, (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate, is leukotriene A(4). Pyrogallol 1,2-oxygenase 1,2,3-trihydroxybenzene + O(2) = (Z)-5-oxohex-2-enedioate. Chloridazon-catechol dioxygenase 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O(2) = 5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone. Not identical with EC 1.13.11.1, EC 1.13.11.2 or EC 1.13.11.5. Iron Involved in the breakdown of the herbicide chloridazon. Hydroxyquinol 1,2-dioxygenase The product isomerizes to 2-maleylacetate (cis-hexenedioate). Highly specific; catechol and pyrogallol are acted on at less than 1% of the rate at which hydroxyquinol is oxidized. Benzene-1,2,4-triol + O(2) = 3-hydroxy-cis,cis-muconate. Iron 1-hydroxy-2-naphthoate 1,2-dioxygenase 1-hydroxy-2-naphthoic acid dioxygenase 1-hydroxy-2-naphthoate-degrading enzyme Involved, with EC 4.1.2.34, in the metabolism of phenanthrene in bacteria. 1-hydroxy-2-naphthoate + O(2) = (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate. Iron 2,3-dihydroxybiphenyl dioxygenase Biphenyl-2,3-diol 1,2-dioxygenase Biphenyl-2,3-diol + O(2) = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H(2)O. Not identical with EC 1.13.11.2. Also acts on 3-isopropylcatechol, forming 7-methyl-2-hydroxy-6-oxo-octa-2,4-dienoate. Gentisate 1,2-dioxygenase Gentisate oxygenase Gentisic acid oxidase Iron 2,5-dihydroxybenzoate + O(2) = maleylpyruvate. 8-lipoxygenase Arachidonate 8-lipoxygenase Arachidonate + O(2) = (5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate. An enzyme from the coral Pseudoplexaura porosa. Iron 2,4'-dihydroxyacetophenone dioxygenase 2,4'-dihydroxyacetophenone + O(2) = 4-hydroxybenzoate + formate. Lignostilbene alpha-beta-dioxygenase The enzyme catalyzes oxidative cleavage of the interphenyl double bond in the synthetic substrate and lignin-derived stilbenes. Iron It is responsible for the degradation of a diarylpropane-type structure in lignin. 1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene + O(2) = 2 vanillin. Linoleate (8R)-dioxygenase Linoleate diol synthase Linoleate 8-dioxygenase Heme Linoleate + O(2) = (9Z,12Z)-(7S,8S)-dihydroxyoctadeca-9,12-dienoate. Oleate and linolenate are also substrates, whereas stearate, elaidate, gamma-linolenate, arachidonate and eicosapentaenate are not. This enzyme differs from EC 1.13.11.12 because it catalyzes the formation of a hydroperoxide without affecting the double bonds of the substrate. Manganese lipoxygenase Linoleate 11-lipoxygenase Linoleate dioxygenase Linoleate + O(2) = (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate. It also acts on alpha-linolenate, whereas gamma-linolenate is a poor substrate. Oleate and arachidonate are not substrates. The product (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate, is converted, more slowly, into (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate. The enzyme from the fungus Gaeumannomyces graminis requires Mn(2+). 4-hydroxyphenylpyruvate dioxygenase II 4-hydroxymandelate synthase Involved in the biosynthesis of the vancomycin group of glycopeptide antibiotics. 4-hydroxyphenylpyruvate + O(2) = 4-hydroxymandelate + CO(2). Iron Quinoline-3,4-diol 2,4-dioxygenase (1H)-3-hydroxy-4-oxoquinoline 2,4-dioxygenase 3-hydroxy-4-oxoquinoline 2,4-dioxygenase 3-hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase 3-hydroxy-4(1H)-one, 2,4-dioxygenase The enzyme from Pseudomonas putida is highly specific for this substrate. 3-hydroxy-1H-quinolin-4-one + O(2) = N-formylanthranilate + CO. Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide. Does not contain a metal center or organic cofactor. (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase The enzyme from Arthrobacter sp. can also act on 3-hydroxy-4-oxoquinoline, forming N-formylanthranilate and CO (cf. EC 1.13.11.47), but more slowly. Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide. Does not contain a metal center or organic cofactor. 3-hydroxy-2-methyl-1H-quinolin-4-one + O(2) = N-acetylanthranilate + CO. Chlorite dismutase Chlorite O(2)-lyase Reaction occurs in the reverse direction in chlorate-and perchlorate-reducing bacteria. Chloride + O(2) = chlorite. There is no activity when chlorite is replaced by hydrogen peroxide, perchlorate, chlorate or nitrite. The term 'chlorite dismutase' is misleading as the reaction does not involve dismutation/disproportionation. Iron Protoheme IX Homogentisate 1,2-dioxygenase Homogentisicase Homogentisate oxygenase Homogentisic acid oxidase Homogentisate + O(2) = 4-maleylacetoacetate. Iron http://purl.uniprot.org/mim/203500 Diketone cleaving enzyme Diketone cleaving dioxygenase Acetylacetone dioxygenase Acetylacetone-cleaving enzyme Forms the first step in the acetylacetone degradation pathway of Acinetobacter johnsonii. Iron While acetylacetone is by far the best substrate, heptane-3,5-dione, octane-2,4-dione, 2-acetylcyclohexanone and ethyl acetoacetate can also act as substrates. Pentane-2,4-dione + O(2) = acetate + 2-oxopropanal. VP14 Nine-cis-epoxycarotenoid dioxygenase NCED 9-cis-epoxycarotenoid dioxygenase (1) A 9-cis-epoxycarotenoid + O(2) = 2-cis,4-trans-xanthoxin + a 12'-apo-carotenal. In vitro, it will cleave 9-cis-zeaxanthin. (3) 9'-cis-neoxanthin + O(2) = 2-cis,4-trans-xanthoxin + (3S,5R,6R)-5,6-dihydroxy-6,7-didehydro-5,6-dihydro-12'-apo-beta-caroten-12'-al. (2) 9-cis-violaxanthin + O(2) = 2-cis,4-trans-xanthoxin + (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-dihydro-12'-apo-beta-caroten-12'-al. Acts on 9-cis-violaxanthin and 9'-cis-neoxanthin but not on the all-trans isomers. Iron The other enzymes involved in the abscisic-acid biosynthesis pathway are EC 1.1.1.288, EC 1.2.3.14 and EC 1.14.13.93. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids in chloroplasts, in response to water stress. IDO Tryptophan pyrrolase Indoleamine 2,3-dioxygenase Heme (2) L-tryptophan + O(2) = N-formyl-L-kynurenine. Has broader substrate specificity than EC 1.13.11.11. While the enzyme is more active with D-tryptophan than L-tryptophan, its only known function to date is in the metabolism of L-tryptophan. Superoxide radicals can replace O(2) as oxygen donor. (1) D-tryptophan + O(2) = N-formyl-D-kynurenine. Requires ascorbic acid and methylene blue for activity. Is induced in response to pathological conditions and host-defense mechanisms. E-2 Acireductone dioxygenase 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase ARD Acireductone dioxygenase (Ni(2+)-requiring) The enzyme from Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC 8724 is involved in the methionine salvage pathway. Nickel If Fe(2+) is bound instead of Ni(2+), the reaction catalyzed by EC 1.13.11.54 occurs instead. 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O(2) = 3-(methylthio)propanoate + formate + CO. Acireductone dioxygenase (Fe(2+)-requiring) 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase E-2' ARD' Acireductone dioxygenase The enzyme from Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC 8724 is involved in the methionine salvage pathway. Iron(2+) 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O(2) = 4-(methylthio)-2-oxobutanoate + formate. If Ni(2+) is bound instead of Fe(2+), the reaction catalyzed by EC 1.13.11.53 occurs instead. Sulfur oxygenase Sulfur oxygenase/reductase Sulfur oxygenase reductase Another reaction product is thiosulfate, but this is probably formed non-enzymically at elevated temperature from sulfite and sulfur. 4 sulfur + 4 H(2)O + O(2) = 2 H(2)S + 2 HSO(3)(-) + 2 H(+). This enzyme differs from EC 1.13.11.18 and EC 1.97.1.3 in that both activities are found together. Elemental sulfur is both the electron donor and one of the two known acceptors, the other being oxygen. Iron 3-hydroxyanthranilic acid oxidase 3-hydroxyanthranilic acid dioxygenase 3-hydroxyanthranilate 3,4-dioxygenase 3-hydroxyanthranilate oxygenase Iron The product of the reaction spontaneously rearrange to quinolinic acid (quin). 3-hydroxyanthranilate + O(2) = 2-amino-3-carboxymuconate semialdehyde. Protocatechuate 4,5-oxygenase Protocatechuate 4,5-dioxygenase Iron Protocatechuate + O(2) = 4-carboxy-2-hydroxymuconate semialdehyde. 2,5-dihydroxypyridine 5,6-dioxygenase Pyridine-2,5-diol dioxygenase 2,5-dihydroxypyridine oxygenase 2,5-dihydroxypyridine + O(2) + H(2)O = maleamate + formate. Iron With incorporation of one atom of oxygen Arginine 2-monooxygenase Arginine decarboxylase Arginine decarboxy-oxidase Arginine oxygenase (decarboxylating) L-arginine + O(2) = 4-guanidinobutanamide + CO(2) + H(2)O. Flavoprotein Also acts on canavanine and homoarginine. Apo-beta-carotenoid-14',13'-dioxygenase Unlike EC 1.14.99.36, it is not active toward beta-carotene. A thiol-dependent enzyme. 8'-apo-beta-carotenol + O(2) = 14'-apo-beta-carotenal + H(2)O. Presumably 2-methyl-6-oxohepta-2,4-dienal is also formed in this reaction. Oplophorus luciferase Oplophorus-luciferin 2-monooxygenase Oplophorus luciferin + O(2) = oxidized Oplophorus luciferin + CO(2) + light. The luciferase from the deep sea shrimp Oplophorus gracilorostris is a complex composed of more than one protein. The enzyme's specificity is quite broad, with both coelenterazine and bisdeoxycoelenterazine being good substrates. CAO Cholorophyll-b synthase Chlorophyllide a oxygenase Chlorophyllide-a oxygenase (1) Chlorophyllide a + O(2) + NADPH = 7-hydroxychlorophyllide a + H(2)O + NADP(+). (2) 7-hydroxychlorophyllide a + O(2) + NADPH = chlorophyllide b + 2 H(2)O + NADP(+). Catalyzes two successive hydroxylations at the 7-methyl group of chlorophyllide a. Iron The second step yields the aldehyde hydrate, which loses H(2)O spontaneously to form chlorophyllide b. Chlorophyll a and protochlorophyllide a are not substrates. Lysine oxygenase Lysine 2-monooxygenase FAD Also acts on other diamino acids. L-lysine + O(2) = 5-aminopentanamide + CO(2) + H(2)O. Tryptophan 2-monooxygenase L-tryptophan + O(2) = (indol-3-yl)acetamide + CO(2) + H(2)O. Lactate oxidase Lactate 2-monooxygenase Lactate oxygenase Lactate oxidative decarboxylase FMN (S)-lactate + O(2) = acetate + CO(2) + H(2)O. Renilla-luciferin 2-monooxygenase Aequorin Renilla-type luciferase Luciferase In vitro, Renilla luciferase emits blue light in the absence of any green fluorescent protein. In vivo, the excited state luciferin--luciferase complex undergoes the process of nonradiative energy transfer to an accessory protein, Renilla green fluorescent protein, which results in green bioluminescence. From the soft coral coelenterate Renilla reniformis. The luciferin is bound to a luciferin-binding protein (BP-LH2). The bioluminescent reaction between the luciferin complex, luciferase and oxygen is triggered by calcium ions. Renilla luciferin + O(2) = oxidized Renilla luciferin + CO(2) + light. Cypridina-type luciferase Cypridina-luciferin 2-monooxygenase Luciferase The enzyme may be assayed by measurement of light emission. Cypridina luciferin is (3-(3,7-dihydro-6-(1H-indol-3-yl)-2-((S)-1-methyl-6-propyl)-3-oxoimidazo-[1,2-a]pyrazin-8-yl)propyl)guanidine. Cypridina luciferin + O(2) = oxidized Cypridina luciferin + CO(2) + light. Luciferase Firefly luciferase Photinus pyralis luciferase Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing) The first step in the reaction is the formation of an acid anhydride between the carboxylic group and AMP, with the release of diphosphate. Photinus luciferin + O(2) + ATP = oxidized Photinus luciferin + CO(2) + AMP + diphosphate + light. The enzyme may be assayed by measurement of light emission. Photinus luciferin is (S)-4,5-dihydro-2-(6-hydroxy-2-benzo-thiazoloyl)-4-thiazolecarboxylic acid. Watasenia-type luciferase Watasenia-luciferin 2-monooxygenase Luciferase The enzyme may be assayed by measurement of light emission. Watasenia luciferin + O(2) = oxidized Watasenia luciferin + CO(2) + light. Watasenia luciferin is 8-(phenylmethyl)-6-(4-sulfooxyphenyl)-2-((4-sulfooxyphenyl)methyl)imidazo[1,2-a]pyrazin-3(7H)-one. L-phenylalanine oxidase (deaminating and decarboxylating) Phenylalanine 2-monooxygenase Phenylalanine (deaminating, decarboxylating) oxidase The reaction shown above is about 80% of the reaction catalyzed; the remaining 20% is: L-phenylalanine + O(2) + H(2)O = 3-phenylpyruvic acid + NH(3) + H(2)O(2), a reaction similar to that of EC 1.4.3.2. L-phenylalanine + O(2) = 2-phenylacetamide + CO(2) + H(2)O. Miscellaneous (requires further characterization) Inositol oxygenase Myo-inositol oxygenase MOO Meso-inositol oxygenase Myo-inositol + O(2) = D-glucuronate + H(2)O. Iron Tryptophan 2'-dioxygenase Indole-3-alkane alpha-hydroxylase Tryptophan side-chain alpha,beta-oxidase TSO Tryptophan side-chain oxidase Best substrates are L-tryptophan and 5-hydroxy-L-tryptophan. Acts on a number of indole-3-alkane derivatives, oxidizing the 3-side-chain in the 2'-position. L-tryptophan + O(2) = (indol-3-yl)glycolaldehyde + CO(2) + NH(3). Heme Acting on paired donors, with incorporation or reduction of molecular oxygen With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors Gamma-butyrobetaine hydroxylase Gamma-butyrobetaine,2-oxoglutarate dioxygenase Gamma-butyrobetaine dioxygenase Gamma-BBH Ascorbate 4-trimethylammoniobutanoate + 2-oxoglutarate + O(2) = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO(2). Iron Deoxyuridine-uridine 1'-dioxygenase Pyrimidine-deoxynucleoside 1'-dioxygenase Pyrimidine-deoxynucleoside,2-oxoglutarate 1'-dioxygenase Ascorbate Cf. EC 1.14.11.3. 2'-deoxyuridine + 2-oxoglutarate + O(2) = uracil + 2-deoxyribonolactone + succinate + CO(2). Iron Hyoscyamine (6S)-hydroxylase Hyoscyamine 6-beta-hydroxylase Hyoscyamine (6S)-dioxygenase Iron Ascorbate L-hyoscyamine + 2-oxoglutarate + O(2) = (6S)-hydroxyhyoscyamine + succinate + CO(2). Gibberellin-44 dioxygenase Gibberellin A44 oxidase Iron Gibberellin 44 + 2-oxoglutarate + O(2) = gibberellin 19 + succinate + CO(2). Gibberellin 2-beta-dioxygenase Gibberellin 2-beta-hydroxylase Also acts on a number of other gibberellins. Iron Gibberellin 1 + 2-oxoglutarate + O(2) = 2-beta-hydroxygibberellin 1 + succinate + CO(2). Hydroxyhyoscyamine dioxygenase 6-beta-hydroxyhyoscyamine epoxidase (6S)-6-hydroxyhyoscyamine + 2-oxoglutarate + O(2) = scopolamine + succinate + CO(2). Iron Ascorbate Gibberellin 3-beta-hydroxylase Gibberellin 3-beta-dioxygenase Iron Gibberellin 20 + 2-oxoglutarate + O(2) = gibberellin 1 + succinate + CO(2). Ascorbate Aspartate beta-hydroxylase Peptide-aspartate beta-dioxygenase Aspartyl/asparaginyl beta-hydroxylase Peptide L-aspartate + 2-oxoglutarate + O(2) = peptide 3-hydroxy-L-aspartate + succinate + CO(2). Some vitamin K-dependent coagulation factors, as well as synthetic peptides based on the structure of the first epidermal growth factor domain of human coagulation factor IX or X, can act as acceptors. Iron Taurine dioxygenase Alpha-ketoglutarate-dependent taurine dioxygenase 2-aminoethanesulfonate dioxygenase The enzyme from Escherichia coli also acts on pentanesulfonate, 3-(N-morpholino)propanesulfonate and 2-(1,3-dioxoisoindolin-2-yl)ethanesulfonate, but at lower rates. Iron Ascorbate Taurine + 2-oxoglutarate + O(2) = sulfite + aminoacetaldehyde + succinate + CO(2). Phytanoyl-CoA alpha-hydroxylase Phytanoyl-CoA 2-hydroxylase Phytanoyl-CoA 2 oxoglutarate dioxygenase Phytanoyl-CoA dioxygenase Phytanoyl-CoA hydroxylase Iron Phytanoyl-CoA + 2-oxoglutarate + O(2) = 2-hydroxyphytanoyl-CoA + succinate + CO(2). Part of the peroxisomal phytanic acid alpha-oxidation pathway. http://purl.uniprot.org/mim/266500 Ascorbate Anthocyanidin synthase Leucoanthocyanidin dioxygenase Leucocyanidin oxygenase Involved in the pathway by which many flowering plants make anthocyanin (glycosylated anthocyandin) flower pigments. Ascorbate Acidification of the products gives anthocyanidin, which, however, may not be a natural precursor of the anthocyanins. Iron The intermediates are transformed into cis-and trans-dihydroquercetin, which the enzyme can also oxidize to quercetin. Leucocyanidin + 2-oxoglutarate + O(2) = cis- and trans-dihydroquercetins + succinate + CO(2). Protocollagen hydroxylase Proline,2-oxoglutarate 4-dioxygenase Prolyl hydroxylase Procollagen-proline dioxygenase Procollagen-proline,2-oxoglutarate-4-dioxygenase Prolyl 4-hydroxylase Procollagen-proline 4-dioxygenase Proline hydroxylase Ascorbate Procollagen L-proline + 2-oxoglutarate + O(2) = procollagen trans-4-hydroxy-L-proline + succinate + CO(2). Iron D17H Desacetoxyvindoline 4-hydroxylase Desacetoxyvindoline-4-hydroxylase Desacetyoxyvindoline-17-hydroxylase Desacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase (4-beta-hydroxylating) Iron Ascorbate Also acts on 3-hydroxy-16-methoxy-2,3-dihydrotabersonine and to a lesser extent on 16-methoxy-2,3-dihydrotabersonine. Desacetoxyvindoline + 2-oxoglutarate + O(2) = desacetylvindoline + succinate + CO(2). Clavaminate synthase Clavaminic acid synthase Iron (2) Proclavaminate + 2-oxoglutarate + O(2) = dihydroclavaminate + succinate + CO(2) + 2 H(2)O. Catalyzes three separate oxidative reactions in the pathway for the biosythesis of the beta-lactamase inhibitor clavulanate in Streptomyces clavuligerus. (1) Deoxyamidinoproclavaminate + 2-oxoglutarate + O(2) = amidinoproclavaminate + succinate + CO(2) + H(2)O. The three reactions are all catalyzed at the same nonheme iron site. The first step (hydroxylation) is separated from the latter two (oxidative cyclization and desaturation) by the action of EC 3.5.3.22. (3) Dihydroclavaminate + 2-oxoglutarate + O(2) = clavaminate + succinate + CO(2) + 2 H(2)O. FNS I Flavone synthase I Flavone synthase Iron Ascorbate A flavanone + 2-oxoglutarate + O(2) = a flavone + succinate + CO(2) + H(2)O. FLS Flavonoid 2-oxoglutarate-dependent dioxygenase Flavonol synthase A dihydroflavonol + 2-oxoglutarate + O(2) = a flavonol + succinate + CO(2) + H(2)O. In addition to the desaturation of (2R,3R)-dihydroflavonols to flavonols, the enzyme from the satsuma Citrus unshiu also has a non-specific activity that trans-hydroxylates the flavanones (2S)-naringenin and the unnatural (2R)-naringenin at C-3 to kaempferol and (2R,3R)-dihydrokaempferol, respectively. Iron IDS3 2'-deoxymugineic-acid 2'-dioxygenase Iron It is also likely that this enzyme can catalyze the hydroxylation of 3-epihydroxy-2'-deoxymugineic acid to form 3-epihydroxymugineic acid. 2'-deoxymugineic acid + 2-oxoglutarate + O(2) = mugineic acid + succinate + CO(2). Mugineic-acid 3-dioxygenase IDS2 (2) 2'-deoxymugineic acid + 2-oxoglutarate + O(2) = 3-epihydroxy-2'-deoxymugineic acid + succinate + CO(2). Iron(2+) (1) Mugineic acid + 2-oxoglutarate + O(2) = 3-epihydroxymugineic acid + succinate + CO(2). Deacetoxycephalosporin C hydroxylase DAOC hydroxylase 3'-methylcephem hydroxylase DACS Deacetoxycephalosporin-C hydroxylase Deacetylcephalosporin C synthase Iron The enzyme can also use 3-exomethylenecephalosporin C as a substrate to form deacetoxycephalosporin C, although more slowly. In Acremonium chrysogenum, the enzyme forms part of a bifunctional protein along with EC 1.14.20.1. It is a separate enzyme in Streptomyces clavuligerus. Deacetoxycephalosporin C + 2-oxoglutarate + O(2) = deacetylcephalosporin C + succinate + CO(2). H3-K36-specific demethylase JmjC domain-containing histone demethylase 1A Histone demethylase [Histone H3]-lysine-36 demethylase Histone-lysine (H3-K36) demethylase JHDM1A Of the seven potential methylation sites in histones H3 (K4, K9, K27, K36, K79) and H4 (K20, R3) from HeLa cells, the enzyme is specific for Lys-36. Lysine residues exist in three methylation states (mono-, di-and trimethylated). It can also demethylate the monomethyl-but not the trimethyl form of Lys-36. The enzyme preferentially demethylates the dimethyl form of Lys-36 (K36me2), which is its natural substrate, to form the monomethyl and unmethylated forms of Lys-36. (1) Protein N(6),N(6)-dimethyl-L-lysine + 2-oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO(2). (2) Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O(2) = protein L-lysine + succinate + formaldehyde + CO(2). Iron(2+) P-3-H Proline 3-hydroxylase The enzyme is specific for L-proline as D-proline, trans-4-hydroxy-L-proline, cis-4-hydroxy-L-proline and 3,4-dehydro-DL-proline are not substrates. Unlike the proline hydroxylases involved in collagen biosynthesis (EC 1.14.11.2 and EC 1.14.11.7), this enzyme does not require ascorbate for activity although it does increase the activity of the enzyme. L-proline + 2-oxoglutarate + O(2) = cis-3-hydroxy-L-proline + succinate + CO(2). Iron(2+) Thymidine 2-oxoglutarate dioxygenase Deoxyuridine 2'-dioxygenase Thymidine dioxygenase Thymidine 2'-dioxygenase Thymidine 2'-hydroxylase Pyrimidine-deoxynucleoside 2'-dioxygenase Pyrimidine-deoxynucleoside,2-oxoglutarate 2'-dioxygenase Deoxyuridine 2'-hydroxylase Pyrimidine deoxyribonucleoside 2'-hydroxylase 2'-deoxyuridine + 2-oxoglutarate + O(2) = uridine + succinate + CO(2). Iron Also acts on thymidine (cf. EC 1.14.11.10). Ascorbate Procollagen-lysine 5-dioxygenase Lysine hydroxylase Lysine,2-oxoglutarate 5-dioxygenase Procollagen-lysine,2-oxoglutarate 5-dioxygenase Lysyl hydroxylase Ascorbate http://purl.uniprot.org/mim/609220 Iron http://purl.uniprot.org/mim/225400 Procollagen L-lysine + 2-oxoglutarate + O(2) = procollagen 5-hydroxy-L-lysine + succinate + CO(2). Thymine dioxygenase Thymine,2-oxoglutarate dioxygenase Thymine 7-hydroxylase Also acts on 5-hydroxymethyluracil to oxidize its -CH(2)-OH group first to -CHO and then to -COOH. Ascorbate Iron Thymine + 2-oxoglutarate + O(2) = 5-hydroxymethyluracil + succinate + CO(2). Prolyl 3-hydroxylase Proline,2-oxoglutarate 3-dioxygenase Procollagen-proline 3-dioxygenase Procollagen-proline,2-oxoglutarate 3-dioxygenase Procollagen L-proline + 2-oxoglutarate + O(2) = procollagen trans-3-hydroxy-L-proline + succinate + CO(2). Iron Ascorbate TML-alpha-ketoglutarate dioxygenase TML hydroxylase Epsilon-trimethyllysine 2-oxoglutarate dioxygenase Trimethyllysine alpha-ketoglutarate dioxygenase Trimethyllysine dioxygenase TMLD Trimethyllysine,2-oxoglutarate dioxygenase TML dioxygenase Iron(2+) Ascorbate N(6),N(6),N(6)-trimethyl-L-lysine + 2-oxoglutarate + O(2) = 3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine + succinate + CO(2). Flavanone synthase I Flavanone 3-beta-hydroxylase Naringenin 3-dioxygenase Naringenin,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating) Flavanone 3-hydroxylase Naringenin 3-hydroxylase (2S)-flavanone 3-hydroxylase Flavanone 3-dioxygenase Iron Ascorbate A flavanone + 2-oxoglutarate + O(2) = a dihydroflavonol + succinate + CO(2). With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into one donor Anthranilate 1,2-dioxygenase (deaminating, decarboxylating) Anthranilate hydroxylase Anthranilic acid hydroxylase Anthranilic hydroxylase Iron Anthranilate + NAD(P)H + O(2) = catechol + CO(2) + NAD(P)(+) + NH(3). Benzoate hydroxylase Benzoic hydroxylase Benzoate 1,2-dioxygenase A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), and an iron-sulfur oxygenase. Benzoate + NADH + O(2) = 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD(+). Iron Toluene dioxygenase Toluene 1,2-dioxygenase A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), an iron-sulfur oxygenase, and a ferredoxin. Some other aromatic compounds, including ethylbenzene, 4-xylene and some halogenated toluenes, are converted into the corresponding cis-dihydrodiols. Toluene + NADH + O(2) = (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD(+). Naphthalene 1,2-dioxygenase A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), an iron-sulfur oxygenase, and ferredoxin. Naphthalene + NADH + O(2) = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD(+). Iron 2-chlorobenzoate 1,2-dioxygenase 2-chlorobenzoate + NADH + O(2) = catechol + chloride + NAD(+) + CO(2). Iron 2-aminosulfobenzene 2,3-dioxygenase 2-aminobenzenesulfonate 2,3-dioxygenase 2-aminobenzenesulfonate + NADH + O(2) = 2,3-dihydroxybenzenesulfonate + NH(3) + NAD(+). 1,4-dicarboxybenzoate 1,2-dioxygenase Terephthalate 1,2-dioxygenase Benzene-1,4-dicarboxylate 1,2-dioxygenase Terephthalate + NADH + O(2) = (1R,6S)-dihydroxycyclohexa-2,4-diene-1,4-dicarboxylate + NAD(+). In Comamonas testoteroni, contains a Rieske [2Fe-2S] center. 2-hydroxyquinoline 5,6-dioxygenase Quinolin-2-ol 5,6-dioxygenase 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase Quinolin-2(1H)-one 5,6-dioxygenase Quinolin-2-ols exist largely as their quinolin-2(1H)-one tautomers. Quinolin-2-ol + NADH + O(2) = 2,5,6-trihydroxy-5,6-dihydroquinoline + NAD(+). 3-methylquinolin-2-ol, quinolin-8-ol and quinolin-2,8-diol are also substrates. Nitric oxide dioxygenase NOD Heme 2 NO + 2 O(2) + NAD(P)H = 2 NO(3)(-) + NAD(P)(+). FAD It has been proposed that FAD functions as the electron carrier from NADPH to the ferric heme prosthetic group. Biphenyl 2,3-dioxygenase Biphenyl dioxygenase The enzyme from Burkholderia fungorum strain LB400 (previously Pseudomonas sp.) is part of a multicomponent system composed of an NADH:ferredoxin oxidoreductase (FAD cofactor), a [2Fe-2S] Rieske-type ferredoxin, and a terminal oxygenase that contains a [2Fe-2S] Rieske-type iron-sulfur cluster and a catalytic mononuclear nonheme iron center. Chlorine-substituted biphenyls can also act as substrates. Similar to the three-component enzyme systems EC 1.14.12.3 and EC 1.14.12.11. Iron Biphenyl + NADH + O(2) = (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD(+). HcaA1A2CD 3-phenylpropanoate dioxygenase Hca dioxygenase 3-phenylpropionate dioxygenase 3-phenylpropanoate + NADH + O(2) = 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD(+). The product, 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate, is then converted into 3-(2,3-dihydroxyphenyl)propanoate, by a dehydrogenase, with the concomitant regeneration of NADH. Iron This enzyme catalyzes the insertion of both atoms of molecular oxygen into positions 2 and 3 of the phenyl ring of 3-phenylpropanoate. The enzyme also acts on (2E)-3-phenylprop-2-enoate (cinnamate). Benzene hydroxylase Benzene 1,2-dioxygenase FAD Iron Benzene + NADH + O(2) = cis-cyclohexa-3,5-diene-1,2-diol + NAD(+). Iron-sulfur A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), an iron-sulfur oxygenase and ferredoxin. Methylhydroxypyridinecarboxylate oxidase Methylhydroxypyridine carboxylate dioxygenase 3-hydroxy-2-methylpyridinecarboxylate dioxygenase 3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + O(2) = 2-(acetamidomethylene)succinate + NAD(P)(+). FAD 5-pyridoxate dioxygenase 5-pyridoxate oxidase 3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + O(2) = 2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP(+). Flavoprotein Phthalate 4,5-dioxygenase PDO Phthalate dioxygenase Iron Phthalate + NADH + O(2) = cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD(+). FMN Iron-sulfur A system, containing a reductase which is an iron-sulfur flavoprotein (FMN), an iron-sulfur oxygenase, and no independent ferredoxin. 4-sulfobenzoate 3,4-dioxygenase Iron FMN Iron-sulfur A system, containing a reductase which is an iron-sulfur flavoprotein (FMN), an iron-sulfur oxygenase, and no independent ferredoxin. 4-sulfobenzoate + NADH + O(2) = 3,4-dihydroxybenzoate + sulfite + NAD(+). 4-chlorophenylacetate 3,4-dioxygenase Iron Also acts on 4-bromophenyl acetate. A system, containing a reductase and an iron-sulfur oxygenase, and no independent ferredoxin. 4-chlorophenylacetate + NADH + O(2) = 3,4-dihydroxyphenylacetate + chloride + NAD(+). With NADH or NADPH as one donor, and incorporation of one atom of oxygen Salicylate hydroxylase Salicylic hydroxylase Salicylate 1-monooxygenase FAD Salicylate + NADH + O(2) = catechol + NAD(+) + H(2)O + CO(2). 2,6-dihydroxypyridine 3-monooxygenase Flavoprotein 2,6-dihydroxypyridine + NADH + O(2) = 2,3,6-trihydroxypyridine + NAD(+) + H(2)O. 25-hydroxycholesterol 7-alpha-monooxygenase 25-hydroxycholesterol 7-alpha-hydroxylase (1) Cholest-5-ene-3-beta,25-diol + NADPH + O(2) = cholest-5-ene-3-beta,7-alpha,25-triol + NADP(+) + H(2)O. Unlike EC 1.14.13.99 which is specific for its oxysterol substrate, this enzyme can also metabolize the oxysterols 24,25-epoxycholesterol, 22-hydroxycholesterol and 24-hydroxycholesterol, but to a lesser extent. (2) Cholest-5-ene-3-beta,27-diol + NADPH + O(2) = cholest-5-ene-3-beta,7-alpha,27-triol + NADP(+) + H(2)O. Heme-thiolate http://purl.uniprot.org/mim/603711 Senecionine N-oxygenase Senecionine monooxygenase (N-oxide-forming) Senecionine N-oxide is used by insects as a chemical defense: it is non-toxic, but it is bioactivated to a toxic form by the action of cytochrome P-450 oxidase when absorbed by insectivores. Senecionine + NADPH + O(2) = senecionine N-oxide + NADP(+) + H(2)O. While pyrrolizidine alkaloids of the senecionine and monocrotaline types are generally good substrates (e.g. senecionine, retrorsine and monocrotaline), the enzyme does not use ester alkaloids lacking an hydroxy group at C-7 (e.g. supinine and phalaenopsine), 1,2-dihydro-alkaloids (e.g. sarracine) or unesterified necine bases (e.g. senkirkine) as substrates. NADH cannot replace NADPH. Psoralen synthase Furanocoumarins protect plants from fungal invasion and herbivore attack. (+)-marmesin + NADPH + O(2) = psoralen + NADP(+) + acetone + 2 H(2)O. Specific for (+)-marmesin, and to a much lesser extent 5-hydroxymarmesin, as substrate. (+)-columbianetin, the angular furanocoumarin analog of the linear furanocoumarin (+)-marmesin, is not a substrate for the enzyme but it is a competitive inhibitor. CA4H Cinnamic acid 4-hydroxylase Cinnamate 4-monooxygenase Cinnamic acid 4-monooxygenase Cinnamate 4-hydroxylase Trans-cinnamate 4-monooxygenase Trans-cinnamate + NADPH + O(2) = 4-hydroxycinnamate + NADP(+) + H(2)O. Heme-thiolate Also acts on NADH, more slowly. p-hydroxybenzoate hydroxylase Benzoate 4-monooxygenase Benzoic acid 4-hydroxylase Benzoate-p-hydroxylase Benzoate-para-hydroxylase Benzoate 4-hydroxylase Iron Benzoate + NADPH + O(2) = 4-hydroxybenzoate + NADP(+) + H(2)O. Tetrahydropteridine 25-hydroxycholecalciferol-1-hydroxylase Calcidiol 1-monooxygenase 25-OHD-1 alpha-hydroxylase 25-hydroxycholecalciferol 1-monooxygenase 25-hydroxyvitamin D-1 alpha hydroxylase http://purl.uniprot.org/mim/264700 Calcidiol + NADPH + O(2) = calcitriol + NADP(+) + H(2)O. Heme-thiolate Trans-cinnamate 2-monooxygenase Cinnamic acid 2-hydroxylase Cinnamic 2-hydroxylase Trans-cinnamate + NADPH + O(2) = 2-hydroxycinnamate + NADP(+) + H(2)O. 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 26-hydroxylase Sterol 27-hydroxylase Cytochrome P450 27A1' Cholestanetriol 26-monooxygenase Cholesterol 27-hydroxylase Cholestanetriol 26-hydroxylase Sterol 26-hydroxylase 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol hydroxylase Heme-thiolate 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol + NADPH + O(2) = (25R)-5-beta-cholestane-3-alpha,7-alpha,12-alpha,26-tetraol + NADP(+) + H(2)O. With prolonged treatment, 26-hydroxycholesterol is converted into the corresponding 27-aldehyde and 27-oic acid. With cholesterol as well as 26-hydroxycholesterol, 24-hydroxy-and 25-hydroxycholesterol are also formed. Requires ferrodoxin. http://purl.uniprot.org/mim/213700 Acts on cholesterol, cholest-5-en-3-beta,7-alpha-diol, 7-alpha-hydroxycholest-4-en-3-one, 5-beta-cholestane-3-alpha,7-alpha-diol as well as 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol. Cyclopentanone monooxygenase Cyclopentanone 1,2-monooxygenase Cyclopentanone + NADPH + O(2) = 5-valerolactone + NADP(+) + H(2)O. Cholesterol 7-alpha-monooxygenase Cholesterol 7-alpha-hydroxylase Cholesterol + NADPH + O(2) = 7-alpha-hydroxycholesterol + NADP(+) + H(2)O. Heme-thiolate 4-hydroxyphenylacetic 1-hydroxylase 4-hydroxyphenylacetate 1-hydroxylase 4-hydroxyphenylacetate 1-monooxygenase 4-HPA 1-hydroxylase 4-hydroxyphenylacetate + NAD(P)H + O(2) = homogentisate + NAD(P)(+) + H(2)O. Also acts on 4-hydroxyhydratropate forming 2-methylhomogentisate and on 4-hydroxyphenoxyacetate forming hydroquinone and glycolate. FAD Taxifolin 8-monooxygenase Converts a flavanol into a flavanone. Flavoprotein Taxifolin + NAD(P)H + O(2) = 2,3-dihydrogossypetin + NAD(P)(+) + H(2)O. Also acts on fustin, but not on catechin, quercetin or mollisacacidin. 4-hydroxybenzoate 3-monooxygenase p-hydroxybenzoic acid hydroxylase p-hydroxybenzoate hydroxylase Para-hydroxybenzoate hydroxylase Most enzymes from Pseudomonas are highly specific for NAD(P)H (cf. EC 1.14.13.33). 4-hydroxybenzoate + NADPH + O(2) = protocatechuate + NADP(+) + H(2)O. FAD 2,4-dichlorophenol hydroxylase 2,4-dichlorophenol 6-monooxygenase FAD 2,4-dichlorophenol + NADPH + O(2) = 3,5-dichlorocatechol + NADP(+) + H(2)O. Also acts, more slowly, on 4-chlorophenol and 4-chloro-2-methylphenol. NADH can act instead of NADPH, but more slowly. Flavonoid 3'-monooxygenase Flavonoid 3'-hydroxylase Acts on a number of flavonoids, including naringenin and dihydrokaempferol. A flavonoid + NADPH + O(2) = a 3'-hydroxyflavonoid + NADP(+) + H(2)O. Does not act on 4-coumarate or 4-coumaroyl-CoA. Cyclohexanone oxygenase Cyclohexanone 1,2-monooxygenase Cyclohexanone:NADPH:oxygen oxidoreductase (6-hydroxylating, 1,2-lactonizing) Cyclohexanone monooxygenase In the catalytic mechanism of this enzyme, the nucleophilic species that attacks the carbonyl group is a peroxyflavin intermediate that is generated by reaction of the enzyme-bound flavin cofactor with NAD(P)H and oxygen. This enzyme is able to catalyze a wide range of oxidative reactions, including enantioselective Baeyer-Villiger reactions, sulfoxidations, amine oxidations and epoxidations. FAD Cyclohexanone + NADPH + O(2) = hexano-6-lactone + NADP(+) + H(2)O. 3-hydroxybenzoate 4-hydroxylase 3-hydroxybenzoate 4-monooxygenase 3-hydroxybenzoate + NADPH + O(2) = 3,4-dihydroxybenzoate + NADP(+) + H(2)O. FAD Also acts on a number of analogs of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions. 3-hydroxybenzoic acid-6-hydroxylase 3-hydroxybenzoate 6-hydroxylase 3-hydroxybenzoate 6-monooxygenase NADPH can act instead of NADH, more slowly. 3-hydroxybenzoate + NADH + O(2) = 2,5-dihydroxybenzoate + NAD(+) + H(2)O. Also acts on a number of analogs of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions. FAD Methane monooxygenase Methane hydroxylase Broad specificity; many alkanes can be hydroxylated, and alkenes are converted into the corresponding epoxides; CO is oxidized to CO(2), ammonia is oxidized to hydroxylamine, and some aromatic compounds and cyclic alkanes can also be hydroxylated, more slowly. Methane + NAD(P)H + O(2) = methanol + NAD(P)(+) + H(2)O. Phosphatidylcholine 12-monooxygenase Oleate Delta(12)-hydroxylase Ricinoleic acid synthase 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + NADH + O(2) = 1-acyl-2-((S)-12-hydroxyoleoyl)-sn-glycero-3-phosphocholine + NAD(+) + H(2)O. 4-aminobenzoate hydroxylase 4-aminobenzoate dehydrogenase 4-aminobenzoate 1-monooxygenase FAD 4-aminobenzoate + NAD(P)H + O(2) = 4-hydroxyaniline + NAD(P)(+) + H(2)O + CO(2). Acts on anthranilate and 4-aminosalicylate but not on salicylate (cf. EC 1.14.13.1). 3,9-dihydroxypterocarpan 6A-monooxygenase 3,9-dihydroxypterocarpan 6A-hydroxylase (6aR,11aR)-3,9-dihydroxypterocarpan + NADPH + O(2) = (6aS,11aS)-3,6a,9-trihydroxypterocarpan + NADP(+) + H(2)O. Heme-thiolate The product of the reaction is the biosynthetic precursor of the phytoalexin glyceollin in soybean. 4-nitrophenol-2-hydroxylase 4-nitrophenol hydroxylase 4-nitrophenol 2-monooxygenase FAD 4-nitrophenol + NADH + O(2) = 4-nitrocatechol + NAD(+) + H(2)O. 4-hydroxyphenylacetic acid-3-hydroxylase 4 HPA 3-hydroxylase 4-hydroxyphenylacetate 3-monooxygenase p-hydroxyphenylacetate 3-hydroxylase 4-hydroxyphenylacetate + NADH + O(2) = 3,4-dihydroxyphenylacetate + NAD(+) + H(2)O. FAD LTB(4) omega-hydroxylase Leukotriene-B(4) omega-hydroxylase Leukotriene-B(4) 20-monooxygenase LTB(4) 20-hydroxylase Leukotriene-B(4) 20-hydroxylase Heme-thiolate (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + NADPH + O(2) = (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + NADP(+) + H(2)O. Not identical with EC 1.14.13.34. 2-nitrophenol 2-monooxygenase Nitrophenol oxygenase 2-nitrophenol + NADPH + O(2) = catechol + nitrite + NADP(+) + H(2)O. Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida. Albendazole sulfoxidase Albendazole monooxygenase Albendazole + NADPH + O(2) = albendazole S-oxide + NADP(+) + H(2)O. FAD 4-hydroxybenzoate 3-hydroxylase 4-hydroxybenzoate 3-monooxygenase (NAD(P)H) The enzyme from Corynebacterium cyclohexanicum is highly specific for 4-hydroxybenzoate, but uses NADH and NADPH at approximately equal rates (cf. EC 1.14.13.2). 4-hydroxybenzoate + NAD(P)H + O(2) = 3,4-dihydroxybenzoate + NAD(P)(+) + H(2)O. FAD It is less specific for NADPH than EC 1.14.13.2. Leukotriene-E(4) 20-monooxygenase Leukotriene-E(4) omega-hydroxylase Also acts on N-acetyl-leukotriene E(4), more slowly. (7E,9E,11Z,14Z)-(5S,6R)-6-(cystein-S-yl)-5-hydroxyicosa-7,9,11,14-tetraenoate + NADPH + O(2) = 20-hydroxyleukotriene E(4) + NADP(+) + H(2)O. Not identical with EC 1.14.13.30. Anthranilate 3-monooxygenase (deaminating) Anthranilate hydroxylase Anthranilate 2,3-hydroxylase (deaminating) Anthranilate + NADPH + O(2) = 2,3-dihydroxybenzoate + NADP(+) + NH(3). The enzyme from Aspergillus niger is an iron protein; that from the yeast Trichosporon cutaneum is a flavoprotein (FAD). 5-O-(4-coumaroyl)-D-quinate/shikimate 3'-hydroxylase 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase Also acts on trans-5-O-(4-coumaroyl)shikimate. Trans-5-O-(4-coumaroyl)-D-quinate + NADPH + O(2) = trans-5-O-caffeoyl-D-quinate + NADP(+) + H(2)O. Methyltetrahydroprotoberberine 14-monooxygenase Methyltetrahydroprotoberberine 14-hydroxylase (S)-cis-N-methyltetrahydroprotoberberine-14-hydroxylase Heme-thiolate (S)-N-methylcanadine + NADPH + O(2) = allocryptopine + NADP(+) + H(2)O. Anhydrotetracycline oxygenase ATC oxygenase Anhydrotetracycline monooxygenase Anhydrotetracycline + NADPH + O(2) = 12-dehydrotetracycline + NADP(+) + H(2)O. Involved in the biosynthesis of tetracyclines in Streptomyces sp. Endothelium-derived relaxing factor synthase Nitric-oxide synthase NADPH-diaphorase Nitric-oxide synthetase NO synthase Endothelium-derived relaxation factor-forming enzyme The stoichiometry is not clear, but may involve a two-electron and a one-electron oxidation step. L-arginine + n NADPH + m O(2) = citrulline + nitric oxide + n NADP(+). The enzyme in brain, but not that induced in lung or liver by endotoxin, requires calcium. http://purl.uniprot.org/mim/163729 Melilotate 3-monooxygenase 2-hydroxyphenylpropionate hydroxylase Melilotate hydroxylase Melilotic hydroxylase FAD 3-(2-hydroxyphenyl)propanoate + NADH + O(2) = 3-(2,3-dihydroxyphenyl)propanoate + NAD(+) + H(2)O. 2-aminobenzoyl-CoA monooxygenase/reductase Anthraniloyl-CoA monooxygenase FAD 2-aminobenzoyl-CoA + 2 NAD(P)H + O(2) = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H(2)O + 2 NAD(P)(+). The non-aromatic product is unstable and releases CO(2) and NH(3), forming 1,4-cyclohexanedione. Tyrosine N-hydroxylase CYP79A1 Tyrosine N-monooxygenase Heme-thiolate (3) N,N-dihydroxy-L-tyrosine = (Z)-(4-hydroxyphenylacetaldehyde oxime) + CO(2) + H(2)O. (1) L-tyrosine + O(2) + NADPH = N-hydroxy-L-tyrosine + NADP(+) + H(2)O. Involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum, along with EC 1.14.13.68 and EC 2.4.1.85. Some 2-(4-hydroxyphenyl)-1-nitroethane is formed as a side product. (2) N-hydroxy-L-tyrosine + O(2) + NADPH = N,N-dihydroxy-L-tyrosine + NADP(+) + H(2)O. 4-hydroxyphenylacetonitrile hydroxylase Hydroxyphenylacetonitrile 2-monooxygenase Heme-thiolate 4-hydroxyphenylacetonitrile + NADPH + O(2) = 4-hydroxymandelonitrile + NADP(+) + H(2)O. Questin oxygenase Questin monooxygenase The enzyme cleaves the anthraquinone ring of questin to form a benzophenone. Involved in the biosynthesis of the seco-anthraquinone (+)-geodin. Questin + NADPH + O(2) = sulochrin + NADP(+) + H(2)O. 2-hydroxybiphenyl 3-monooxygenase 2-hydroxybiphenyl + NADH + O(2) = 2,3-dihydroxybiphenyl + NAD(+) + H(2)O. Also converts 2,2'-dihydroxybiphenyl into 2,2',3-trihydroxy-biphenyl. (-)-menthol monooxygenase (-)-menthol + NADPH + O(2) = p-menthane-3,8-diol + NADP(+) + H(2)O. (-)-limonene 3-hydroxylase (-)-limonene 3-monooxygenase (S)-limonene 3-monooxygenase (-)-limonene,NADPH:oxygen oxidoreductase (3-hydroxylating) High specificity, but NADH can act instead of NADPH, although more slowly. (-)-(S)-limonene + NADPH + O(2) = (-)-trans-isopiperitenol + NADP(+) + H(2)O. Heme-thiolate (-)-limonene 6-hydroxylase (-)-limonene,NADPH:oxygen oxidoreductase (6-hydroxylating) (S)-limonene 6-monooxygenase (-)-limonene 6-monooxygenase (-)-(S)-limonene + NADPH + O(2) = (-)-trans-carveol + NADP(+) + H(2)O. Heme-thiolate High specificity, but NADH can act instead of NADPH, although more slowly. (-)-limonene 7-monooxygenase (S)-limonene 7-monooxygenase (-)-limonene monooxygenase (-)-limonene hydroxylase (-)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating) (-)-(S)-limonene + NADPH + O(2) = (-)-perillyl alcohol + NADP(+) + H(2)O. Heme-thiolate High specificity, but NADH can act instead of NADPH, although more slowly. Imidazoleacetate 4-monooxygenase Imidazoleacetic monooxygenase Imidazoleacetate hydroxylase FAD 4-imidazoleacetate + NADH + O(2) = 5-hydroxy-4-imidazoleacetate + NAD(+) + H(2)O. PCB 4-monooxygenase Pentachlorophenol dehalogenase Pentachlorophenol monooxygenase Pentachlorophenol dechlorinase Pentachlorophenol hydroxylase PCB4MO PCP hydroxylase Pentachlorophenol 4-monooxygenase FAD If C-4 carries a halogen substituent, reaction 1 is catalyzed, e.g. 2,4,6-triiodophenol is oxidized to 2,6-diiodohydroquinone; if C-4 is unsubstituted, reaction 2 is catalyzed. The enzyme displaces a diverse range of substituents from the 4-position of polyhalogenated phenols but requires that a halogen substituent be present at the 2-position. The enzyme converts many polyhalogenated phenols into hydroquinones, and requires that a halogen substituent be present at C-2. (1) Pentachlorophenol + 2 NADPH + O(2) = 2,3,5,6-tetrachlorohydroquinone + 2 NADP(+) + chloride + H(2)O. (2) 2,3,5,6-tetrachlorophenol + NADPH + O(2) = 2,3,5,6-tetrachlorohydroquinone + NADP(+) + H(2)O. 6-oxocineole dehydrogenase 6-oxocineole + NADPH + O(2) = 1,6,6-trimethyl-2,7-dioxabicyclo-[3.2.2]nonan-3-one + NADP(+) + H(2)O. The product undergoes non-enzymic cleavage and subsequent ring closure to form the lactone 4,5-dihydro-5,5-dimethyl-4-(3-oxobutyl)furan-2(3H)-one. Isoflavone 3'-hydroxylase Also acts on biochanin A and other isoflavones with a 4'-methoxy group. Involved in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain. Formononetin + NADPH + O(2) = calycosin + NADP(+) + H(2)O. Heme-thiolate Isoflavone 2'-hydroxylase Isoflavone 2'-monooxygenase 4'-methoxyisoflavone 2'-hydroxylase EC 1.14.13.89 is less specific and acts on other isoflavones as well as 4'-methoxyisoflavones. Formononetin + NADPH + O(2) = 2'-hydroxyformononetin + NADP(+) + H(2)O. Involved in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain. Heme-thiolate Acts on isoflavones with a 4'-methoxy group, such as formononetin and biochanin A. Steroid-ketone monooxygenase Ketosteroid monooxygenase The possibility that a single enzyme is responsible for the reactions ascribed to EC 1.14.99.4 and EC 1.14.99.12 in other tissues cannot be excluded. (1) Ketosteroid + NADPH + O(2) = steroid ester/lactone + NADP(+) + H(2)O. (3) Androstenedione + NADPH + O(2) = testololactone + NADP(+) + H(2)O. (2) Progesterone + NADPH + O(2) = testosterone acetate + NADP(+) + H(2)O. The oxidative lactonization of a number of derivatives of androstenedione to produce the 13,17-secoandrosteno-17,13-alpha-lactone, such as testololactone, is shown in reaction (3). reaction (2) is also catalyzed by EC 1.14.99.4 and reactions (3) and (4) correspond to that catalyzed by EC 1.14.99.12. The oxidative esterification of a number of derivatives of progesterone to produce the corresponding 17-alpha-hydroxysteroid 17-acetate ester, such as testosterone acetate, is shown in reaction (2). (4) 17-alpha-hydroxyprogesterone + NADPH + O(2) = androstenedione + NADP(+) + H(2)O. FAD The oxidative cleavage of the 17-beta-side-chain of 17-alpha-hydroxyprogesterone to produce androstenedione and acetate is shown in reaction (4). A single FAD-containing enzyme catalyzes three types of monooxygenase (Baeyer-Villiger oxidation) reaction. Protopine 6-monooxygenase Protopine 6-hydroxylase Heme-thiolate Protopine + NADPH + O(2) = 6-hydroxyprotopine + NADP(+) + H(2)O. Involved in benzophenanthridine alkaloid synthesis in higher plants. Dihydrosanguinarine 10-hydroxylase Dihydrosanguinarine 10-monooxygenase Involved in benzophenanthridine alkaloid synthesis in higher plants. Dihydrosanguinarine + NADPH + O(2) = 10-hydroxydihydrosanguinarine + NADP(+) + H(2)O. Heme-thiolate Dihydrochelirubine 12-hydroxylase Dihydrochelirubine 12-monooxygenase Heme-thiolate Dihydrochelirubine + NADPH + O(2) = 12-hydroxydihydrochelirubine + NADP(+) + H(2)O. Benzoyl-CoA 3-hydroxylase Benzoyl-CoA 3-monooxygenase Benzoate is not a substrate. FAD or FMN Benzoyl-CoA + NADPH + O(2) = 3-hydroxybenzoyl-CoA + NADP(+) + H(2)O. L-lysine 6-monooxygenase (NADPH) Lysine N(6)-hydroxylase L-lysine + NADPH + O(2) = N(6)-hydroxy-L-lysine + NADP(+) + H(2)O. The enzyme from strain EN 222 of Escherichia coli is highly specific for L-lysine; L-ornithine and L-homolysine are, for example, not substrates. FAD Orcinol hydroxylase Orcinol 2-monooxygenase FAD Orcinol + NADH + O(2) = 2,3,5-trihydroxytoluene + NAD(+) + H(2)O. 27-hydroxycholesterol 7-alpha-hydroxylase 27-hydroxycholesterol 7-alpha-monooxygenase Heme-thiolate 27-hydroxycholesterol + NADPH + O(2) = 7-alpha,27-dihydroxycholesterol + NADP(+) + H(2)O. The enzyme from mammalian liver differs from EC 1.14.13.17 in having no activity toward cholesterol. 2-oxo-1,2-dihydroquinoline 8-monooxygenase 2-hydroxyquinoline 8-monooxygenase Quinolin-2-ol exists largely as the quinolin-2(1H)-one tautomer. Quinolin-2-ol + NADH + O(2) = quinolin-2,8-diol + NAD(+) + H(2)O. Iron 1-H-4-oxoquinoline 3-monooxygenase Quinolin-4(1H)-one 3-monooxygenase 4-hydroxyquinoline 3-monooxygenase Quinolin-4-ol exists largely as the quinolin-4(1H)-one tautomer. Quinolin-4-ol + NADH + O(2) = quinolin-3,4-diol + NAD(+) + H(2)O. 3-hydroxyphenylacetate 6-monooxygenase 3-hydroxyphenylacetate 6-hydroxylase 3-hydroxyphenylacetate 6-hydroxylase from Flavobacterium sp. is highly specific for 3-hydroxyphenylacetate and uses NADH and NADPH as electron donors with similar efficiency. FAD 3-hydroxyphenylacetate + NAD(P)H + O(2) = 2,5-dihydroxyphenylacetate + NAD(P)(+) + H(2)O. 4-hydroxybenzoate 1-hydroxylase 4-hydroxybenzoate 1-monooxygenase The enzyme from Candida parapsilosis is specific for 4-hydroxybenzoate derivatives and prefers NADH to NADPH as electron donor. 4-hydroxybenzoate + NAD(P)H + O(2) = hydroquinone + NAD(P)(+) + H(2)O + CO(2). FAD 2-hydroxycyclohexanone 2-monooxygenase 2-hydroxycyclohexan-1-one + NADPH + O(2) = 6-hydroxyhexan-6-olide + NADP(+) + H(2)O. The product decomposes spontaneously to 6-oxohexanoic acid (adipic semialdehyde). Nifedipine oxidase Quinine 3-monooxygenase Quinine 3-hydroxylase Quinine + NADPH + O(2) = 3-hydroxyquinine + NADP(+) + H(2)O. Heme-thiolate CYP71E1 4-hydroxyphenylacetaldehyde oxime monooxygenase Cytochrome P450-II-dependent monooxygenase 4-hydroxybenzeneacetaldehyde oxime monooxygenase (Z)-4-hydroxyphenylacetaldehyde oxime + NADPH + O(2) = (S)-4-hydroxymandelonitrile + NADP(+) + 2 H(2)O. Involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum, along with EC 1.14.13.41 and EC 2.4.1.85. Heme-thiolate Alkene monooxygenase Alkene epoxygenase Iron Propene + NADH + O(2) = 1,2-epoxypropane + NAD(+) + H(2)O. The enzyme oxygenates C(2) to C(6) aliphatic alkenes. The enzyme from Xanthobacter sp. strain Py2 is a multicomponent enzyme comprising: (1) an NADH reductase, which provides the reductant for O(2) activation. (2) a Rieske-type ferredoxin, which is an electron-transfer protein. (3) an oxygenase, which contains the catalytic center for alkene epoxidation. (4) a small protein of unknown function that is essential for activity. With 1,2-epoxypropane as substrate, the stereospecificity of the epoxypropane formed is 95% (R) and 5% (S). Phenol 2-monooxygenase Phenol hydroxylase Phenol o-hydroxylase Phenol + NADPH + O(2) = catechol + NADP(+) + H(2)O. FAD Also active with resorcinol and o-cresol. Sterol 14-alpha-demethylase Obtusufoliol 14-demethylase Sterol 14-demethylase Lanosterol 14-demethylase Lanosterol 14-alpha-demethylase Cytochrome P450 51 The enzyme (P450) catalyzes successive hydroxylations of the 14-alpha-methyl group and C-15, followed by elimination as formate leaving the 14(15) double bond. Heme-thiolate This enzyme acts on a range of steroids with a 14-alpha-methyl group. Obtusifoliol + 3 O(2) + 3 NADPH = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP(+) + 4 H(2)O. N-methylcoclaurine 3'-monooxygenase N-methylcoclaurine 3'-hydroxylase Cytochrome P450 80B1 (S)-N-methylcoclaurine 3'-hydroxylase (S)-N-methylcoclaurine + NADPH + O(2) = (S)-3'-hydroxy-N-methylcoclaurine + NADP(+) + H(2)O. A P450 protein involved in benzylisoquinoline alkaloid synthesis in higher plants. Heme-thiolate Methylsterol monooxygenase 4-methylsterol oxidase Methylsterol hydroxylase Also acts on 4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol. The sterol can be based on cycloartenol as well as lanosterol. (1) 4,4-dimethyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O(2) = 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)(+) + H(2)O. (3) 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)H + O(2) = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)(+) + H(2)O. Requires cytochrome b5. (2) 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O(2) = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)(+) + 2 H(2)O. Tabersonine 16-hydroxylase Heme-thiolate Tabersonine + NADPH + O(2) = 16-hydroxytabersonine + NADP(+) + H(2)O. 7-deoxyloganin 7-hydroxylase Heme-thiolate 7-deoxyloganin + NADPH + O(2) = loganin + NADP(+) + H(2)O. Vinorine hydroxylase Heme-thiolate Forms a stage in the biosynthesis of the indole alkaloid ajmaline. Vinorine + NADPH + O(2) = vomilenine + NADP(+) + H(2)O. 5-alpha-taxadienol-10-beta-hydroxylase Taxane 10-beta-hydroxylase Heme-thiolate Taxa-4(20),11-dien-5-alpha-yl acetate + NADPH + O(2) = 10-beta-hydroxytaxa-4(20),11-dien-5-alpha-yl acetate + NADP(+) + H(2)O. Taxane 13-alpha-hydroxylase Taxa-4(20),11-dien-5-alpha-ol + NADPH + O(2) = taxa-4(20),11-dien-5-alpha,13-alpha-diol + NADP(+) + H(2)O. Heme-thiolate Ent-kaurene oxidase (3) Ent-kaur-16-en-19-al + NADPH + O(2) = ent-kaur-16-en-19-oate + NADP(+) + H(2)O. Catalyzes three sucessive oxidations of the 4-methyl group of ent-kaurene giving kaurenoic acid. (2) Ent-kaur-16-en-19-ol + NADPH + O(2) = ent-kaur-16-en-19-al + NADP(+) + 2 H(2)O. (1) Ent-kaur-16-ene + NADPH + O(2) = ent-kaur-16-en-19-ol + NADP(+) + H(2)O. Requires cytochrome P450. Ent-kaurenoic acid oxidase In Cucurbita maxima, ent-6-alpha,7-alpha-dihydroxykaur-16-en-19-oate is also formed. Requires cytochrome P450. (1) Ent-kaur-16-en-19-oate + NADPH + O(2) = ent-7-alpha-hydroxykaur-16-en-19-oate + NADP(+) + H(2)O. (3) Gibberellin A(12) aldehyde + NADPH + O(2) = gibberellin A(12) + NADP(+) + H(2)O. (2) Ent-7-alpha-hydroxykaur-16-en-19-oate + NADPH + O(2) = gibberellin A(12) aldehyde + NADP(+) + 2 H(2)O. The second step includes a ring-B contraction giving the gibbane skeleton. Catalyzes three sucessive oxidations of ent-kaurenoic acid. Flavin mixed function oxidase Flavin-containing monooxygenase FMO FAD-containing monooxygenase Dimethylaniline N-oxidase Dimethylaniline monooxygenase (N-oxide-forming) DMA oxidase Mixed-function amine oxidase Flavin monooxygenase N,N-dimethylaniline monooxygenase Ziegler's enzyme Methylphenyltetrahydropyridine N-monooxygenase Dimethylaniline oxidase For example, N-oxygenation is largely responsible for the detoxification of the dopaminergic neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). FAD N,N-dimethylaniline + NADPH + O(2) = N,N-dimethylaniline N-oxide + NADP(+) + H(2)O. Is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate. http://purl.uniprot.org/mim/602079 A broad spectrum monooxygenase that accepts substrates as diverse as hydrazines, phosphines, boron-containing compounds, sulfides, selenides, iodide, as well as primary, secondary and tertiary amines. Generally converts nucleophilic heteroatom-containing chemicals and drugs into harmless, readily excreted metabolites. (+)-limonene-6-hydroxylase (+)-limonene 6-monooxygenase (R)-limonene 6-monooxygenase Forms part of the carvone biosynthesis pathway in Carum carvi (caraway) seeds. Heme-thiolate (S)-Limonene, the substrate for EC 1.14.13.48 is not a substrate. The reaction is stereospecific with over 95% yield of (+)-trans-carveol from (R)-limonene. http://purl.uniprot.org/mim/609535 (+)-(R)-limonene + NADPH + O(2) = (+)-trans-carveol + NADP(+) + H(2)O. Magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase Mg-protoporphyrin IX monomethyl ester oxidative cyclase Iron (1) Magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + O(2) = 13(1)-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + NADP(+) + H(2)O. The cyclase activity in Chlamydomonas reinhardtii is associated exclusively with the membranes, whereas that from cucumber cotyledons requires both membrane and soluble fractions for activity. (2) 13(1)-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + O(2) = 13(1)-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + NADP(+) + 2 H(2)O. (3) 13(1)-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + O(2) = divinylprotochlorophyllide + NADP(+) + 2 H(2)O. 4-hydroxy-3-methoxybenzoate demethylase Vanillate demethylase Vanillate monooxygenase Vanillate + O(2) + NADH = 3,4-dihydroxybenzoate + NAD(+) + H(2)O + formaldehyde. Forms part of the vanillin degradation pathway in Arthrobacter sp. Precorrin-3X synthase Precorrin-3B synthase In the aerobic cobalamin biosynthesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A. Precorrin-3A + NADH + O(2) = precorrin-3B + NAD(+) + H(2)O. This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin-4, precorrin-5 and precorrin-6A, respectively. Iron-sulfur An oxygen atom from dioxygen is incorporated into the macrocycle at C-20. This enzyme carries out the first of the four steps, yielding precorrin-3B as the product. HAPMO 4-hydroxyacetophenone monooxygenase Highest activity occurs with compounds bearing an electron-donating substituent at the para position of the aromatic ring. (4-hydroxyphenyl)ethan-1-one + NADPH + O(2) = 4-hydroxyphenyl acetate + NADP(+) + H(2)O. In the absence of substrate, the enzyme can act as an NADPH oxidase (EC 1.6.3.1). The enzyme from Pseudomonas fluorescens ACB catalyzes the conversion of a wide range of acetophenone derivatives. FAD Dimethylallyl-3,6a,9-trihydroxypterocarpan cyclase Glyceollin synthase Heme-thiolate 2-(or 4-)dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan + NADPH + O(2) = glyceollin + NADP(+) + 2 H(2)O. Glyceollins II and III are formed from 2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan whereas glyceollin I is formed from the 4-isomer. 2-HIS 2-hydroxyisoflavanone synthase Apigenin + 2 NADPH + O(2) = 2-hydroxy-2,3-dihydrogenistein + 2 NADP(+) + H(2)O. Heme-thiolate EC 4.2.1.105 acts on 2-hydroxy-2,3-dihydrogenistein with loss of water and formation of genistein; this may occur spontaneously. Licodione synthase (2S)-flavanone 2-hydroxylase It probably forms 2-hydroxyliquiritigenin which spontaneously forms licodione. Heme-thiolate Liquiritigenin + NADPH + O(2) = licodione + NADP(+) + H(2)O. NADH can act instead of NADPH, but more slowly. Flavonoid 3',5'-hydroxylase F3',5'H F3'5'H Heme-thiolate NADH is not a good substitute for NADPH. (1) A flavanone + NADPH + O(2) = a 3'-hydroxyflavanone + NADP(+) + H(2)O. The enzyme catalyzes the hydroxylation of 5,7,4'-trihydroxyflavanone (naringenin) at either the 3' position to form eriodictyol or at both the 3' and 5' positions to form 5,7,3',4',5'-pentahydroxyflavanone (dihydrotricetin). The enzyme also catalyzes the hydroxylation of 3,5,7,3',4'-pentahydroxyflavanone (taxifolin) at the 5' position, forming ampelopsin. In Petunia hybrida the enzyme acts on naringenin, eriodictyol, dihydroquercetin (taxifolin) and dihydrokaempferol (aromadendrin). The 3',5'-dihydroxyflavanone is formed via the 3'-hydroxyflavanone. (2) A 3'-hydroxyflavanone + NADPH + O(2) = a 3',5'-dihydroxyflavanone + NADP(+) + H(2)O. Isoflavone 2'-hydroxylase Isoflavone 2'-monooxygenase CYP Ge-3 CYP81E1 Acts on daidzein, formononetin and genistein. Heme-thiolate An isoflavone + NADPH + O(2) = a 2'-hydroxyisoflavone + NADP(+) + H(2)O. EC 1.14.13.53 has the same reaction but is more specific as it requires a 4'-methoxyisoflavone. Kynurenine 3-hydroxylase Kynurenine 3-monooxygenase L-kynurenine + NADPH + O(2) = 3-hydroxy-L-kynurenine + NADP(+) + H(2)O. FAD Zeaxanthin epoxidase Zea-epoxidase FAD (2) Antheraxanthin + NAD(P)H + O(2) = violaxanthin + NAD(P)(+) + H(2)O. (1) Zeaxanthin + NAD(P)H + O(2) = antheraxanthin + NAD(P)(+) + H(2)O. It will also epoxidize lutein in some higher-plant species. Along with EC 1.10.99.3, this enzyme forms part of the xanthophyll (or violaxanthin) cycle, which is involved in protecting the plant against damage by excess light. Active under conditions of low light. Deoxysarpagine hydroxylase DOSH Heme-thiolate 10-deoxysarpagine + NADPH + O(2) = sarpagine + NADP(+) + H(2)O. PAMO Phenylacetone monooxygenase In addition to phenylacetone, which is the best substrate found to date, this Baeyer-Villiger monooxygenase can oxidize other aromatic ketones (1-(4-hydroxyphenyl)propan-2-one, 1-(4-hydroxyphenyl)propan-2-one and 3-phenylbutan-2-one), some alipatic ketones (e.g. dodecan-2-one) and sulfides (e.g. 1-methyl-4-(methylsulfanyl)benzene). FAD Phenylacetone + NADPH + O(2) = benzyl acetate + NADP(+) + H(2)O. NADH cannot replace NADPH as coenzyme. (+)-ABA 8'-hydroxylase (+)-abscisic acid 8'-hydroxylase ABA 8'-hydroxylase (+)-abscisate + NADPH + O(2) = 8'-hydroxyabscisate + NADP(+) + H(2)O. CO inhibits the reaction, but its effects can be reversed by the presence of blue light. The 8'-hydroxyabscisate formed can be converted into (-)-phaseic acid, most probably spontaneously. Catalyzes the first step in the oxidative degradation of abscisic acid and is considered to be the pivotal enzyme in controlling the rate of degradation of this plant hormone. Heme-thiolate Other enzymes involved in the abscisic-acid biosynthesis pathway are EC 1.1.1.288, EC 1.2.3.14 and EC 1.13.11.51. Lithocholate 6-beta-hydroxylase Lithocholate 6-beta-monooxygenase 6-beta-hydroxylase Cytochrome P450 3A10/lithocholic acid 6-beta-hydroxylase Expression of the gene for this enzyme is 50-fold higher in male compared to female hamsters. Lithocholate + NADPH + O(2) = 6-beta-hydroxylithocholate + NADP(+) + H(2)O. Heme-thiolate HCO 12-alpha-hydroxylase 7-alpha-hydroxy-4-cholesten-3-one 12-alpha-monooxygenase 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase Sterol 12-alpha-hydroxylase Requires EC 1.6.2.4 and cytochrome b5 for maximal activity. Heme-thiolate Important in bile acid biosynthesis, being responsible for the balance between the formation of cholic acid and chenodeoxycholic acid. 7-alpha-hydroxycholest-4-en-3-one + NADPH + O(2) = 7-alpha,12-alpha-dihydroxycholest-4-en-3-one + NADP(+) + H(2)O. Sterol 12-alpha-hydroxylase 5-beta-cholestane-3-alpha,7-alpha-diol 12-alpha-monooxygenase Cytochrome P450 8B1 5-beta-cholestane-3-alpha,7-alpha-diol 12-alpha-hydroxylase Can also hydroxylate the substrate at the 25 and 26 position, but to a lesser extent. Key enzyme in the biosynthesis of the bile acid cholic acid (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanoic acid). Heme-thiolate 5-beta-cholestane-3-alpha,7-alpha-diol + NADPH + O(2) = 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol + NADP(+) + H(2)O. The activity determines the biosynthetic ratio between cholic acid and chenodeoxycholic acid. Taurochenodeoxycholate 6-alpha-hydroxylase Taurochenodeoxycholate 6-alpha-monooxygenase Acts on taurochenodeoxycholate, taurodeoxycholate and less readily on lithocholate and chenodeoxycholate. (1) Taurochenodeoxycholate + NADPH + O(2) = taurohyocholate + NADP(+) + H(2)O. Requires cytochrome b5 for maximal activity. Heme-thiolate In adult pig (Sus scrofa), hyocholic acid replaces cholic acid as a primary bile acid. (2) Lithocholate + NADPH + O(2) = hyodeoxycholate + NADP(+) + H(2)O. Cholesterol 24-hydroxylase Cholesterol 24-monooxygenase Cholesterol 24S-hydroxylase Cytochrome P450 46A1 Heme-thiolate Can also produce 25-hydroxycholesterol. This reaction is the first step in the enzymatic degradation of cholesterol in the brain as hydroxycholesterol can pass the blood-brain barrier whereas cholesterol cannot. Cholesterol + NADPH + O(2) = (24S)-24-hydroxycholesterol + NADP(+) + H(2)O. In addition, it can further hydroxylate the product to 24,25-dihydroxycholesterol and 24,27-dihydroxycholesterol. 24-hydroxycholesterol 7-alpha-monooxygenase 24-hydroxycholesterol 7-alpha-hydroxylase (24R)-cholest-5-ene-3-beta,24-diol + NADPH + O(2) = (24R)-cholest-5-ene-3-beta,7-alpha,24-triol + NADP(+) + H(2)O. Specific for (24R)-cholest-5-ene-3-beta,24-diol as substrate. Heme-thiolate Found in liver microsomes and in ciliary non-pigmented epithelium. With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen Flavoprotein-linked monooxygenase Unspecific monooxygenase Cytochrome p450 Aryl hydrocarbon hydroxylase Aryl-4-monooxygenase Xenobiotic monooxygenase Microsomal monooxygenase Microsomal p450 Reactions catalyzed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S-and O-dealkylations, desulfation, deamination, and reduction of azo, nitro, and N-oxide groups. Acts on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins. Heme-thiolate RH + reduced flavoprotein + O(2) = ROH + oxidized flavoprotein + H(2)O. Bacterial luciferase Alkanal monooxygenase (FMN-linked) Aldehyde monooxygenase The reaction involves incorporation of a molecule of oxygen into reduced FMN, and subsequent reaction with the aldehyde to form an activated FMN.H(2)O complex which breaks down with emission of light. RCHO + reduced FMN + O(2) = RCOOH + FMN + H(2)O + light. The enzyme is highly specific for reduced FMN, and for long-chain aliphatic aldehydes with 8 carbons or more. Sulfate starvation-induced protein 6 FMNH(2)-dependent aliphatic sulfonate monooxygenase Alkanesulfonate monooxygenase An alkanesufonate (R-CH(2)-SO(3)H) + FMNH(2) + O(2) = an aldehyde (R-CHO) + FMN + sulfite + H(2)O. Instead, it uses reduced FMN (i.e., FMNH(2)) as a substrate. FMNH(2) is provided by SsuE, the associated FMN reductase (EC 1.5.1.29). Does not use FMN as a bound cofactor. Does not desulfonate taurine (2-aminoethanesulfonate) or aromatic sulfonates. The enzyme from Escherichia coli catalyzes the desulfonation of a wide range of aliphatic sulfonates (unsubstituted C(1)-to C(14)-sulfonates as well as substituted C(2)-sulfonates). With a reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen Camphor 5-monooxygenase Cytochrome p450-cam Camphor 5-exo-methylene hydroxylase (+)-camphor + putidaredoxin + O(2) = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H(2)O. Also acts on (-)-camphor and 1,2-campholide, forming 5-exo-hydroxy-1,2-campholide. Heme-thiolate 2,5-diketocamphane lactonizing enzyme Camphor ketolactonase I Camphor 1,2-monooxygenase (+)-bornane-2,5-dione + reduced rubredoxin + O(2) = 5-oxo-1,2-campholide + oxidized rubredoxin + H(2)O. Iron Alkane 1-hydroxylase Lauric acid omega-hydroxylase Fatty acid omega-hydroxylase Alkane 1-monooxygenase Omega-hydroxylase Also hydroxylates fatty acids in the omega-position. Some enzyme of this group are heme-thiolated proteins (P450). Octane + reduced rubredoxin + O(2) = 1-octanol + oxidized rubredoxin + H(2)O. Steroid 11-beta/18-hydroxylase Steroid 11-beta-monooxygenase Steroid 11-beta-hydroxylase Cytochrome p450 XIB1 Heme-thiolate Also hydroxylates steroids at the 18-position, and converts 18-hydroxycorticosterone into aldosterone. A steroid + reduced adrenal ferredoxin + O(2) = an 11-beta-hydroxysteroid + oxidized adrenal ferredoxin + H(2)O. http://purl.uniprot.org/mim/103900 http://purl.uniprot.org/mim/202010 Corticosterone methyl oxidase Corticosterone 18-monooxygenase Corticosterone 18-hydroxylase Heme-thiolate Corticosterone + reduced adrenal ferredoxin + O(2) = 18-hydroxycorticosterone + oxidized adrenal ferredoxin + H(2)O. http://purl.uniprot.org/mim/610600 http://purl.uniprot.org/mim/203400 Cholesterol monooxygenase (side-chain-cleaving) Steroid 20-22 desmolase Cytochrome p450(scc) Cholesterol side-chain-cleaving enzyme Cholesterol side-chain cleavage enzyme Cholesterol desmolase Cholesterol 20-22-desmolase Cholesterol C(20-22) desmolase Steroid 20-22-lyase Cytochrome P-450(scc) The reaction proceeds in three stages, with hydroxylation at C-20 and C-22 preceding scission of the side-chain at C-20. http://purl.uniprot.org/mim/201710 Cholesterol + reduced adrenal ferredoxin + O(2) = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H(2)O. Heme-thiolate Choline monooxygenase The enzyme involved in the second step, EC 1.2.1.8, appears to be the same in plants, animals and bacteria. Iron-sulfur Magnesium In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. In plants, the reaction is catalyzed by this enzyme whereas in animals and many bacteria, it is catalyzed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17). Choline + O(2) + 2 reduced ferredoxin + 2 H(+) = betaine aldehyde hydrate + H(2)O + 2 oxidized ferredoxin. Different enzymes are involved in the first reaction. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 and EC 2.1.1.157. Catalyzes the first step of glycine betaine synthesis. With reduced pteridine as one donor, and incorporation of one atom of oxygen Phenylalanine 4-monooxygenase Phenylalanine hydroxylase Phenylalaninase Phenylalanine 4-hydroxylase PAH http://purl.uniprot.org/mim/261600 Iron The reaction involves an arene oxide which rearranges to give the phenolic hydroxy group. This results in the hydrogen at C-4 migrating to C-3 and in part being retained, a process known as the NIH-shift. L-phenylalanine + tetrahydrobiopterin + O(2) = L-tyrosine + 4a-hydroxytetrahydrobiopterin. The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC 1.5.1.34, or slowly rearranges into the more stable compound 7,8-dihydrobiopterin. The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7-dihydrobiopterin, both spontaneously and by the action of EC 4.2.1.96. Tyrosine hydroxylase L-tyrosine hydroxylase Tyrosine 3-hydroxylase Tyrosine 3-monooxygenase Iron The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC 1.5.1.34, or slowly rearranges into the more stable compound 7,8-dihydrobiopterin. http://purl.uniprot.org/mim/605407 Activated by phosphorylation, catalyzed by EC 2.7.11.27. The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7-dihydrobiopterin, both spontaneously and by the action of EC 4.2.1.96. L-tyrosine + tetrahydrobiopterin + O(2) = 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin. Anthranilate 3-hydroxylase Anthranilic hydroxylase Anthranilate 3-monooxygenase Anthranilic acid hydroxylase Anthranilate + tetrahydrobiopterin + O(2) = 3-hydroxyanthranilate + dihydrobiopterin + H(2)O. Iron Tryptophan hydroxylase Tryptophan 5-hydroxylase Tryptophan 5-monooxygenase Indoleacetic acid-5-hydroxylase L-tryptophan hydroxylase The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7-dihydrobiopterin, both spontaneously and by the action of EC 4.2.1.96. L-tryptophan + tetrahydrobiopterin + O(2) = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin. Activated by phosphorylation, catalyzed by a Ca(2+)-activated protein kinase. http://purl.uniprot.org/mim/608516 The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC 1.5.1.34, or slowly rearranges into the more stable compound 7,8-dihydrobiopterin. Iron Glyceryl etherase Glyceryl-ether cleaving enzyme Glyceryl-ether monooxygenase Requires phospholipids for full activity. 1-alkyl-sn-glycerol + tetrahydrobiopterin + O(2) = 1-hydroxyalkyl-sn-glycerol + dihydrobiopterin + H(2)O. Glutathione The product spontaneously breaks down to form a fatty aldehyde and glycerol. L-mandelate 4-hydroxylase Mandelate 4-monooxygenase Mandelic acid 4-hydroxylase (S)-2-hydroxy-2-phenylacetate + tetrahydrobiopterin + O(2) = (S)-4-hydroxymandelate + dihydrobiopterin + H(2)O. Iron With reduced ascorbate as one donor, and incorporation of one atom of oxygen Dopamine beta-hydroxylase Dopamine beta-monooxygenase 3,4-dihydroxyphenethylamine + ascorbate + O(2) = noradrenaline + dehydroascorbate + H(2)O. Stimulated by fumarate. http://purl.uniprot.org/mim/223360 Copper PAM Peptidylglycine 2-hydroxylase Peptidylglycine alpha-amidating monooxygenase Peptidylglycine monooxygenase Peptidyl alpha-amidating enzyme Copper Peptidylglycine + ascorbate + O(2) = peptidyl(2-hydroxyglycine) + dehydroascorbate + H(2)O. The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalyzed by EC 4.3.2.5. Involved in the final step of biosynthesis of alpha-melanotropin and related biologically active peptides. Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme. 1-aminocyclopropane-1-carboxylate oxidase ACC oxidase Aminocyclopropanecarboxylate oxidase Ethylene-forming enzyme In the enzyme from plants, the ethylene has signaling functions such as stimulation of fruit-ripening. Requires CO(2) for activity. Iron 1-aminocyclopropane-1-carboxylate + ascorbate + O(2) = ethylene + cyanide + dehydroascorbate + CO(2) + 2 H(2)O. With another compound as one donor, and incorporation of one atom of oxygen Phenolase Monophenol oxidase Cresolase Monophenol monooxygenase Tyrosinase http://purl.uniprot.org/mim/203100 A group of copper proteins that also catalyze the reaction of EC 1.10.3.1, if only 1,2-benzenediols are available as substrate. http://purl.uniprot.org/mim/606952 L-tyrosine + L-dopa + O(2) = L-dopa + dopaquinone + H(2)O. Copper http://purl.uniprot.org/mim/103470 CMP-N-acetylneuraminate hydroxylase CMP-Neu5Ac hydroxylase CMP-N-acetylneuraminate monooxygenase Cytidine monophosphoacetylneuraminate monooxygenase CMP-N-acetylneuraminic acid hydroxylase The enzyme can be activated by Fe(2+) or Fe(3+). Iron Iron-sulfur The ferricytochrome b5 produced is reduced by NADH and EC 1.6.2.2. CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O(2) + 2 H(+) = CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H(2)O. With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water Stearoyl-CoA 9-desaturase Fatty acid desaturase Stearoyl-CoA desaturase Delta(9)-desaturase Acyl-CoA desaturase The ferricytochrome b5 produced is reduced by NADH and EC 1.6.2.2. Stearoyl-CoA + 2 ferrocytochrome b5 + O(2) + 2 H(+) = oleoyl-CoA + 2 ferricytochrome b5 + 2 H(2)O. Iron The liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2. Acyl-[acyl-carrier-protein] desaturase Stearyl-ACP desaturase Stearyl acyl carrier protein desaturase Requires ferredoxin. Stearoyl-[acyl-carrier-protein] + reduced acceptor + O(2) = oleoyl-[acyl-carrier-protein] + acceptor + 2 H(2)O. The enzyme from safflower is specific for stearoyl-CoA; that from Euglena acts on derivatives of a number of long-chain fatty acids. Linoleoyl-coenzyme A desaturase Delta(6)-desaturase Fatty acid Delta(6)-desaturase Linoleate desaturase Linoleic acid desaturase Fatty acid 6-desaturase Delta(6)-fatty acyl-CoA desaturase Long-chain fatty acid Delta(6)-desaturase Linoleoyl CoA desaturase Linoleic desaturase Linoleoyl-CoA desaturase Delta(6)-acyl CoA desaturase Linoleoyl-CoA + AH(2) + O(2) = gamma-linolenoyl-CoA + A + 2 H(2)O. Iron The rat liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2. With 2-oxoglutarate as one donor, and the other dehydrogenated Penicillin N expandase DAOCS DAOC synthase Deacetoxycephalosporin-C synthase Penicillin N + 2-oxoglutarate + O(2) = deacetoxycephalosporin C + succinate + CO(2) + H(2)O. Forms part of the penicillin biosynthesis pathway. With NADH or NADPH as one donor, and the other dehydrogenated (S)-cheilanthifoline oxidase (methylenedioxy-bridge-forming) (S)-stylopine synthase Catalyzes an oxidative reaction that does not incorporate oxygen into the product. Forms the second methylenedioxy bridge of the protoberberine alkaloid stylopine from oxidative ring closure of adjacent phenolic and methoxy groups of cheilanthifoline. (S)-cheilanthifoline + NADPH + O(2) = (S)-stylopine + NADP(+) + 2 H(2)O. Heme-thiolate (S)-scoulerine oxidase (methylenedioxy-bridge-forming) (S)-cheilanthifoline synthase Catalyzes an oxidative reaction that does not incorporate oxygen into the product. Heme-thiolate Forms the methylenedioxy bridge of the protoberberine alkaloid cheilanthifoline from oxidative ring closure of adjacent phenolic and methoxy groups of scoulerine. (S)-scoulerine + NADPH + O(2) = (S)-cheilanthifoline + NADP(+) + 2 H(2)O. Berbamunine synthase (S)-N-methylcoclaurine oxidase (C-O phenol-coupling) Reaction of 2 molecules of (R)-N-methylcoclaurine gives the dimer guattagaumerine. Heme-thiolate (S)-N-methylcoclaurine + (R)-N-methylcoclaurine + NADPH + O(2) = berbamunine + NADP(+) + 2 H(2)O. Forms the bisbenzylisoquinoline alkaloid berbamunine by phenol oxidation of N-methylcoclaurine without the incorporation of oxygen into the product. Salutaridine synthase (R)-reticuline oxidase (C-C phenol-coupling) Forms the morphinan alkaloid salutaridine by intramolecular phenol oxidation of reticuline without the incorporation of oxygen into the product. Heme-thiolate (R)-reticuline + NADPH + O(2) = salutaridine + NADP(+) + 2 H(2)O. (S)-tetrahydrocolumbamine oxidase (methylenedioxy-bridge-forming) (S)-canadine synthase (S)-tetrahydroberberine synthase Catalyzes an oxidative reaction that does not incorporate oxygen into the product. Heme-thiolate Oxidation of the methoxyphenol group of the alkaloid tetrahydrocolumbamine results in the formation of the methylenedioxy bridge of canadine. (S)-tetrahydrocolumbamine + NADPH + O(2) = (S)-canadine + NADP(+) + 2 H(2)O. Lathosterol 5-desaturase Delta(7)-sterol 5-desaturase 5-DES Delta(7)-sterol Delta(5)-dehydrogenase Lathosterol oxidase Delta(7)-sterol-C5(6)-desaturase This enzyme catalyzes the introduction of a C5 double bond into the B ring of Delta(7)-sterols to yield the corresponding Delta(5,7)-sterols in mammals, yeast and plants. http://purl.uniprot.org/mim/607330 5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O(2) = cholesta-5,7-dien-3-beta-ol + NAD(P)(+) + 2 H(2)O. Forms part of the plant sterol biosynthesis pathway. Miscellaneous (requires further characterization) PG synthetase Prostaglandin G/H synthase Prostaglandin-endoperoxide synthase Prostaglandin synthase Prostaglandin synthetase Acts both as a dioxygenase and as a peroxidase. Arachidonate + AH(2) + 2 O(2) = prostaglandin H(2) + A + H(2)O. Steroid 21-hydroxylase Cytochrome p450 XXIA1 Steroid 21-monooxygenase A steroid + AH(2) + O(2) = a 21-hydroxysteroid + A + H(2)O. http://purl.uniprot.org/mim/201910 Heme-thiolate Estradiol 6-beta-monooxygenase Estradiol 6-beta-hydroxylase Estradiol-17-beta + AH(2) + O(2) = 6-beta-hydroxyestradiol-17-beta + A + H(2)O. Androstenedione monooxygenase Androstene-3,17-dione hydroxylase 4-androstene-3,17-dione monooxygenase Androst-4-ene-3,17-dione monooxygenase Androst-4-ene-3,17-dione 17-oxidoreductase Androst-4-ene-3,17-dione + AH(2) + O(2) = 3-oxo-13,17-secoandrost-4-ene-17,13-alpha-lactone + A + H(2)O. A single enzyme from Cylindrocarpon radicicola (EC 1.14.13.54) catalyzes both this reaction and that catalyzed by EC 1.14.99.4. Has a wide specificity. Progesterone 11-alpha-monooxygenase Progesterone 11-alpha-hydroxylase Progesterone + AH(2) + O(2) = 11-alpha-hydroxyprogesterone + A + H(2)O. 4-methoxybenzoate O-demethylase 4-methoxybenzoate monooxygenase (O-demethylating) Also acts on 4-ethoxybenzoate, N-methyl-4-aminobenzoate and toluate. The fungal enzyme acts best on veratrate. Iron-sulfur Flavoprotein The bacterial enzyme consists of a ferredoxin-type protein and an iron-sulfur flavoprotein (FMN). 4-methoxybenzoate + AH(2) + O(2) = 4-hydroxybenzoate + formaldehyde + A + H(2)O. Plasmanylethanolamine desaturase Alkylacylglycerophosphoethanolamine desaturase Either NADPH or NADH can act as AH(2). Requires ATP. May involve cytochrome b5. O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine + AH(2) + O(2) = O-1-alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine + A + 2 H(2)O. Magnesium Kynurenine 7,8-hydroxylase Kynurenate + AH(2) + O(2) = 7,8-dihydro-7,8-dihydroxykynurenate + A. Phylloquinone epoxidase Phylloquinone monooxygenase (2,3-epoxidizing) Phylloquinone + AH(2) + O(2) = 2,3-epoxyphylloquinone + A + H(2)O. Latia-luciferin monooxygenase (demethylating) Flavoprotein The reaction possibly involves two enzymes, an oxygenase followed by a monooxygenase for the actual light-emitting step. Latia luciferin is (E)-2-methyl-4-(2,6,6-trimethyl-1-cyclohex-1-yl)-1-buten-1-ol formate. Latia luciferin + AH(2) + 2 O(2) = oxidized Latia luciferin + CO(2) + formate + A + H(2)O + light. Ecdysone 20-monooxygenase Ecdysone + AH(2) + O(2) = 20-hydroxyecdysone + A + H(2)O. Heme-thiolate An enzyme from insect fat body or malpighian tubules. NADPH can act as ultimate hydrogen donor. 3-hydroxybenzoate 2-hydroxylase 3-hydroxybenzoate 2-monooxygenase 3-hydroxybenzoate + AH(2) + O(2) = 2,3-dihydroxybenzoate + A + H(2)O. Steroid 9-alpha-hydroxylase Steroid 9-alpha-monooxygenase Pregna-4,9(11)-diene-3,20-dione + AH(2) + O(2) = 9,11-alpha-epoxypregn-4-ene-3,20-dione + A + H(2)O. Iron-sulfur FMN An enzyme system involving a flavoprotein (FMN) and two iron-sulfur proteins. 2-hydroxypyridine oxygenase 2-hydroxypyridine 5-monooxygenase Also oxidizes 2,5-dihydroxypyridine, but does not act on 3-hydroxypyridine, 4-hydroxypyridine or 2,6-dihydroxypyridine. 2-hydroxypyridine + AH(2) + O(2) = 2,5-dihydroxypyridine + A + H(2)O. Juglone 3-monooxygenase Also acts on 1,4-naphthoquinone, naphthazarin and 2-chloro-1,4-naphthoquinone, but not on other related compounds. 5-hydroxy-1,4-naphthoquinone + AH(2) + O(2) = 3,5-dihydroxy-1,4-naphthoquinone + A + H(2)O. Linalool 8-monooxygenase Heme-thiolate 3,7-dimethylocta-1,6-dien-3-ol + AH(2) + O(2) = (E)-3,7-dimethylocta-1,6-dien-3,8-diol + A + H(2)O. Deoxyhypusine dioxygenase DOHH Deoxyhypusine monooxygenase Deoxyhypusine hydroxylase Protein N(6)-(4-aminobutyl)-L-lysine + AH(2) + O(2) = protein N(6)-((R)-4-amino-2-hydroxybutyl)-L-lysine + A + H(2)O. Catalyzes the final step in the formation of the amino acid hypusine in eukaryotic initiation factor 5A (eIF-5A) (formerly eIF-4D). Heme oxygenase (decyclizing) Heme oxygenase Heme oxidase The central iron is kept in the reduced state by NAD(P)H. Heme + 3 AH(2) + 3 O(2) = biliverdin + Fe(2+) + CO + 3 A + 3 H(2)O. http://purl.uniprot.org/mim/141250 The third oxygen molecule provides the oxygen atom that converts the alpha-carbon to CO. The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules. Requires NAD(P)H and EC 1.6.2.4. Carotene 7,8-desaturase Zeta-carotene desaturase Neurosporene + AH(2) + O(2) = lycopene + A + 2 H(2)O. Also acts on zeta-carotene twice to give lycopene and converts beta-zeacarotene to gamma-carotene, and pro-zeta-carotene to prolycopene (via double reaction). Myristoyl-CoA 11-(E) desaturase EC 1.14.99.32 forms the Z-isomer by stereospecific cleavage of pro-R H at C-11 and C-12. Myristoyl-CoA + NAD(P)H + O(2) = (E)-11-tetradecenoyl-CoA + NAD(P)(+) + 2 H(2)O. Involved in sex pheromone synthesis in Spodoptera littoralis. (E)-11-tetradecenoyl-CoA is formed by stereospecific removal of the pro-R H at C-11 and the pro-S H at C-12. Myristoyl-CoA 11-(Z) desaturase Involved in sex pheromone synthesis in Spodoptera littoralis. Myristoyl-CoA + NAD(P)H + O(2) = (Z)-11-tetradecenoyl-CoA + NAD(P)(+) + 2 H(2)O. (Z)-11-tetradecenoyl-CoA is formed by stereospecific removal of H from the pro-R positions at C-11 and C-12. EC 1.14.99.31 forms the E-isomer by removing the pro-R H group at C-11 and the pro-S H group at C-12. Delta-12 fatty acid acetylenase Linoleate Delta-12-fatty acid acetylenase (desaturase) Crepenynate synthase Delta(12)-fatty acid dehydrogenase Linoleate + AH(2) + O(2) = crepenynate + A + H(2)O. Iron Monoprenyl isoflavone epoxidase Monoprenyl isoflavone monooxygenase The enzyme has a high specificity for monoprenyl isoflavone. It is slowly and nonenzymically converted into the corresponding dihydrofurano derivative. The product of the prenyl epoxidation reaction contains an oxygen atom derived from O(2), but not from H(2)O. 7-O-methylluteone + NADPH + O(2) = dihydrofurano derivatives + NADP(+) + H(2)O. FAD Thiophene-2-carboxyl-CoA hydroxylase Thiophene-2-carbonyl-CoA monooxygenase Thiophene-2-carboxyl-CoA dehydrogenase Thiophene-2-carboxyl-CoA monooxygenase Thiophene-2-carbonyl-CoA + AH(2) + O(2) = 5-hydroxythiophene-2-carbonyl-CoA + A + H(2)O. Highly specific for thiophene-2-carbonyl-CoA. Molybdenum Tetrazolium salts can act as electron acceptors. Carotene 15,15'-dioxygenase Carotene dioxygenase Beta-carotene 15,15'-monooxygenase Beta-carotene 15,15'-dioxygenase The reaction proceeds in three stages, epoxidation of the 15,15'-double bond, hydration of the double bond leading to ring opening, and oxidative cleavage of the diol formed (cf. EC 1.14.15.6). Beta-carotene + O(2) = 2 retinal. Bile salts Iron Thus only one atom of the dioxygen is incorporated into retinal. Taxadiene 5-alpha-hydroxylase The reaction includes rearrangement of the 4(5)-double bond to a 4(20)-double bond, possibly through allylic oxidation. Requires P450. Taxa-4,11-diene + AH(2) + O(2) = taxa-4(20),11-dien-5-alpha-ol + A + H(2)O. Cholesterol 25-hydroxylase Cholesterol 25-monooxygenase Cholesterol + AH(2) + O(2) = 25-hydroxycholesterol + A + H(2)O. In cell cultures, this enzyme down-regulates cholesterol synthesis and the processing of sterol regulatory element binding proteins (SREBPs). Instead, it uses diiron cofactors to catalyze the hydroxylation of hydrophobic substrates. Iron The diiron cofactor can be either Fe-O-Fe or Fe-OH-Fe and is bound to the enzyme through interactions with clustered histidine or glutamate residues. Unlike most other sterol hydroxylases, this enzyme is not a cytochrome P-450. Progesterone hydroxylase Progesterone monooxygenase Has a wide specificity. A single enzyme from Cylindrocarpon radicicola (EC 1.14.13.54) catalyzes both this reaction and that catalyzed by EC 1.14.99.12. Progesterone + AH(2) + O(2) = testosterone acetate + A + H(2)O. Squalene epoxidase Squalene monooxygenase This enzyme, together with EC 5.4.99.7, was formerly known as squalene oxidocyclase. Squalene + AH(2) + O(2) = (S)-squalene-2,3-epoxide + A + H(2)O. FAD Steroid 17-alpha-monooxygenase Steroid 17-alpha-hydroxylase Cytochrome p450 XVIIA1 Steroid 17-alpha-hydroxylase/17,20 lyase Heme-thiolate A steroid + AH(2) + O(2) = a 17-alpha-hydroxysteroid + A + H(2)O. http://purl.uniprot.org/mim/202110 Acting on superoxide as acceptor Acting on superoxide as acceptor Superoxide dismutase http://purl.uniprot.org/mim/105400 Copper and zinc or iron or manganese 2 superoxide + 2 H(+) = O(2) + H(2)O(2). Superoxide reductase Desulfoferrodoxin Neelaredoxin Reduced rubredoxin + superoxide + 2 H(+) = rubredoxin + H(2)O(2). Iron Oxidizing metal ions With NAD(+) or NADP(+) as acceptor Mercury(II) reductase Mercuric reductase Hg + NADP(+) + H(+) = Hg(2+) + NADPH. Transferrin reductase Diferric-transferrin reductase Transferrin-[Fe(2+)](2) + NAD(+) = transferrin-[Fe(3+)](2) + NADH. Aquocobalamin reductase Vitamin B(12a) reductase Aquacobalamin reductase B(12a) reductase NADH:cob(III)alamin oxidoreductase NADH-linked aquacobalamin reductase Flavoprotein 2 cob(II)alamin + NAD(+) = 2 aquacob(III)alamin + NADH. Cob(II)alamin reductase B(12r) reductase NADH:cob(II)alamin oxidoreductase Vitamin B(12r) reductase Flavoprotein 2 cob(I)alamin + NAD(+) = 2 cob(II)alamin + NADH. Aquacobalamin reductase (NADPH) NADPH:aquacob(III)alamin oxidoreductase Aquacobalamin (reduced nicotinamide adenine dinucleotide phosphate) reductase NADPH-linked aquacobalamin reductase Acts on aquacob(III)alamin and hydroxycobalamin, but not on cyanocobalamin. 2 cob(II)alamin + NADP(+) = 2 aquacob(III)alamin + NADPH. Flavoprotein Cyanocobalamin reductase (NADPH; CN-eliminating) Cyanocobalamin reductase Cyanocobalamin reductase (cyanide-eliminating) Cyanocobalamin reductase (NADPH, cyanide-eliminating) NADPH:cyanocob(III)alamin oxidoreductase (cyanide-eliminating) Cob(I)alamin + cyanide + NADP(+) = cyanocob(III)alamin + NADPH. Flavoprotein Ferric chelate reductase NADH:Fe(3+) oxidoreductase Iron chelate reductase Ferric-chelate reductase NADH:Fe(3+)-EDTA reductase 2 Fe(2+) + NAD(+) = 2 Fe(3+) + NADH. Involved in the transport of iron across plant plasma membranes. FAD Methionine synthase cob(II)alamin reductase (methylating) [Methionine synthase] reductase [Methionine synthase]-cobalamin methyltransferase (cob(II)alamin reducing) Methionine synthase reductase FAD The substrate of the enzyme is the inactivated [Co(II)] form of EC 2.1.1.13. FMN Electrons are transferred from NADPH to FAD to FMN. 2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP(+) = 2 [methionine synthase]-cob(II)alamin + NADPH + 2 S-adenosyl-L-methionine. http://purl.uniprot.org/mim/236270 With oxygen as acceptor Ferroxidase Ceruloplasmin 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O. http://purl.uniprot.org/mim/604290 Copper http://purl.uniprot.org/mim/134770 With flavin as acceptor Cob(II)yrinic acid a,c-diamide reductase 2 cob(II)yrinic acid a,c-diamide + FMN + 2 H(+) = 2 cob(I)yrinic acid a,c-diamide + FMNH(2). Also uses FAD and NADH but not NADPH. This enzyme also catalyzes the reduction of cob(II)yric acid, cob(II)inamide, cob(II)inamide phosphate, GDP-cob(II)inamide and cob(II)alamin although cob(II)yrinic acid a,c-diamide is thought to be the physiological substrate. Acting on CH or CH(2) groups With NAD(+) or NADP(+) as acceptor CDP-4-keto-deoxy-glucose reductase Cytidine diphospho-4-keto-6-deoxy-D-glucose reductase NAD(P)H:CDP-4-keto-6-deoxy-D-glucose oxidoreductase CDP-4-dehydro-6-deoxyglucose reductase Cytidine diphosphate 4-keto-6-deoxy-D-glucose-3-dehydrogenase CDP-4-keto-6-deoxyglucose reductase CDP-4-keto-6-deoxy-D-glucose-3-dehydrogenase system The enzyme consists of two proteins. The second catalyzes the reduction of this adduct by NAD(P)H and release of the CDP-4-dehydro-3,6-dideoxy-D-glucose and pyridoxamine phosphate. CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)(+) + H(2)O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H. One forms an enzyme-bound adduct of the CDP-4-dehydro-6-deoxyglucose with pyridoxamine phosphate, in which the 3-hydroxy group has been removed. 4-hydroxy-3-methylbut-2-enyl diphosphate reductase Forms part of an alternative, nonmevalonate pathway for terpenoid biosynthesis. The enzyme acts in the reverse direction producing a 5:1 mixture of isopentenyl diphosphate and dimethyallyl diphosphate. Isopentenyl diphosphate + NAD(P)(+) + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. Leucocyanidin reductase Leucoanthocyanidin reductase While 2,3-trans-3,4-cis-leucocyanidin is the preferred flavan-3,4-diol substrate, 2,3-trans-3,4-cis-leucodelphinidin and 2,3-trans-3, 4-cis-leucopelargonidin can also act as substrates, but more slowly. Catalyzes the synthesis of catechin-4-beta-ol and the related flavan-3-ols afzelechin and gallocatechin, which are initiating monomers in the synthesis of plant polymeric proanthocyanidins or condensed tannins. (2R,3S)-catechin + NADP(+) + H(2)O = 2,3-trans-3,4-cis-leucocyanidin + NADPH. NADH can replace NADPH but is oxidized more slowly. Xanthine oxidoreductase Xanthine dehydrogenase Xanthine/NAD(+) oxidoreductase Xanthine-NAD oxidoreductase NAD-xanthine dehydrogenase Xanthine + NAD(+) + H(2)O = urate + NADH. FAD The animal enzyme can be interconverted to EC 1.17.3.2 (the oxidase form). Iron-sulfur Acts on a variety of purines and aldehydes, including hypoxanthine. This enzyme can also be converted into EC 1.17.3.2 by EC 1.8.4.7 in the presence of glutathione disulfide. In other animal tissues, the enzyme exists almost entirely as EC 1.17.3.2, but can be converted into the dehydrogenase form by 1,4-dithioerythritol. That from liver exists in vivo mainly in the dehydrogenase form, but can be converted into EC 1.17.3.2 by storage at -20 degrees Celsius, by treatment with proteolytic agents or organic solvents, or by thiol reagents such as Cu(2+), N-ethylmaleamide or 4-hydroxymercuribenzoate. http://purl.uniprot.org/mim/278300 The effect of thiol reagents can be reversed by thiols such as 1,4-dithioerythritol. Molybdenum Nicotinate hydroxylase Nicotinate dehydrogenase Nicotinic acid hydroxylase Flavoprotein Nicotinate + H(2)O + NADP(+) = 6-hydroxynicotinate + NADPH. Other enzymes involved in this pathway are EC 1.3.7.1, EC 3.5.2.18, EC 1.1.1.291, EC 5.4.99.4, EC 5.3.3.6, EC 4.2.1.85 and EC 4.1.3.32. The enzyme from Clostridium barkeri also possesses a catalytically essential, labile selenium that can be removed by reaction with cyanide. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. The enzyme is capable of acting on a variety of nicotinate analogs to varying degrees, including pyrazine-2-carboxylate, pyrazine 2,3-dicarboxylate, trigonelline and 6-methylnicotinate. Iron With oxygen as acceptor Pteridine oxidase Different from EC 1.17.3.2. 2-amino-4-hydroxypteridine + O(2) = 2-amino-4,7-dihydroxypteridine + (?). Does not act on hypoxanthine. Xanthine oxidoreductase Hypoxanthine:oxygen oxidoreductase Schardinger enzyme Xanthine:O(2) oxidoreductase Hypoxanthine-xanthine oxidase Xanthine:xanthine oxidase Xanthine oxidase Hypoxanthine oxidase That from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20 degrees Celsius, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu(2+), N-ethylmaleamide or 4-mercuribenzoate. Xanthine + H(2)O + O(2) = urate + H(2)O(2). The Micrococcus enzyme can use ferredoxin as acceptor. Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes (i.e. possesses the activity of EC 1.2.3.1). http://purl.uniprot.org/mim/278300 Molybdopterin FAD Iron-sulfur The enzyme from animal tissues can be converted into EC 1.17.1.4. The effect of thiol reagents can be reversed by thiols such as 1,4-dithioerythritol. EC 1.17.1.4 can also be converted into this enzyme by EC 1.8.4.7 in the presence of glutathione disulfide. Under some conditions the product is mainly superoxide rather than peroxide: R-H + H(2)O + 2 O(2) = ROH + 2 O(2)(.-) + 2 H(+). 6-hydroxynicotinate hydroxylase 6-hydroxynicotinic acid dehydrogenase 6-hydroxynicotinate dehydrogenase 6-hydroxynicotinic acid hydroxylase 6-hydroxynicotinate + H(2)O + O(2) = 2,6-dihydroxynicotinate + H(2)O(2). Iron-sulfur Molybdopterin FAD The enzyme also has a catalytically essential, labile selenium that can be removed by reaction with cyanide. In Bacillus niacini, this enzyme is required for growth on nicotinic acid. With a disulfide as acceptor Ribonucleotide reductase Ribonucleoside-diphosphate reductase ATP Iron 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin. Ribonucleoside-triphosphate reductase Ribonucleotide reductase ATP Cobalt 2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H(2)O = ribonucleoside triphosphate + thioredoxin. 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H(2)O + protein-disulfide = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + protein-dithiol. Forms, in the reverse direction, part of an alternative, nonmevalonate pathway for terpenoid biosynthesis. With a quinone or similar compound as acceptor Phenylacetyl-CoA dehydrogenase Phenylacetyl-CoA:acceptor oxidoreductase Phenylacetate, acetyl-CoA, benzoyl-CoA, propanoyl-CoA, crotonyl-CoA, succinyl-CoA and 3-hydroxybenzoyl-CoA cannot act as substrates. The enzyme is specific for phenylacetyl-CoA as substrate. Iron-sulfur Molybdopterin The oxygen atom introduced into the product, phenylglyoxylyl-CoA, is derived from water and not molecular oxygen. Duroquinone, menaquinone and 2,6-dichlorophenolindophenol (DCPIP) can act as acceptor, but the likely physiological acceptor is ubiquinone. A second enzyme, EC 3.1.2.25 converts the phenylglyoxylyl-CoA formed into phenylglyoxylate. Phenylacetyl-CoA + H(2)O + 2 quinone = phenylglyoxylyl-CoA + 2 quinol. With other acceptors 4-cresol dehydrogenase (hydroxylating) p-cresol-(acceptor) oxidoreductase (hydroxylating) p-cresol methylhydroxylase FAD 4-cresol + acceptor + H(2)O = 4-hydroxybenzaldehyde + reduced acceptor. A quinone methide is probably formed as intermediate. The first hydroxylation forms 4-hydroxybenzyl alcohol; a second hydroxylation converts this into 4-hydroxybenzaldehyde. Phenazine methosulfate can act as acceptor. Ethylbenzene hydroxylase Ethylbenzene dehydrogenase Toluene is not oxidized. Ethylbenzene + H(2)O + acceptor = (S)-1-phenylethanol + reduced acceptor. Heme p-benzoquinone or ferrocenium can act as electron acceptor. Iron-sulfur Involved in the anaerobic catabolism of ethylbenzene by denitrifying bacteria. Molybdopterin Ethylbenzene is the preferred substrate; the enzyme from some strains oxidizes propylbenzene, 1-ethyl-4-fluorobenzene, 3-methylpent-2-ene and ethylidenecyclohexane. 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase THCA-CoA oxidase 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase Trihydroxycoprostanoyl-CoA oxidase THC-CoA oxidase 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate 24-hydroxylase However, in amphibians such as the Oriental fire-bellied toad (Bombina orientalis), it is probable that the product is formed via direct hydroxylation of the saturated side chain of (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate and not via hydration of a 24(25) double bond. Requires ATP. The reaction in mammals possibly involves dehydrogenation to give a 24(25)-double bond followed by hydration. (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oyl-CoA + H(2)O + acceptor = (24R,25R)-3-alpha,7-alpha,12-alpha,24-tetrahydroxy-5-beta-cholestan-26-oyl-CoA + reduced acceptor. In microsomes, the free acid is preferred to the coenzyme A ester, whereas in mitochondria, the coenzyme A ester is preferred to the free-acid form of the substrate. Uracil/thymine dehydrogenase Uracil-thymine oxidase Uracil dehydrogenase Uracil oxidase (1) Uracil + H(2)O + acceptor = barbiturate + reduced acceptor. Mammals, plants and other microorganisms utilize the reductive pathway, comprising EC 1.3.1.1 or EC 1.3.1.2, EC 3.5.2.2 and EC 3.5.1.6, with the ultimate degradation products being an L-amino acid, NH(3) and CO(2). (2) Thymine + H(2)O + acceptor = 5-methylbarbiturate + reduced acceptor. Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 3.5.2.1 and EC 3.5.1.95. Bile-acid 7-alpha-dehydroxylase 7-alpha-dehydroxylase Cholate 7-alpha-dehydroxylase Bile acid 7-dehydroxylase This unusual regulation by the NAD(+)/NADH ratio is most likely the result of the intermediates being linked at C-24 by an anhydride bond to the 5'-diphosphate of 3'-phospho-ADP. Highly specific for bile-acid substrates and requires a free C-24 carboxy group and an unhindered 7-alpha-hydroxy group on the B-ring of the steroid nucleus for activity, as found in cholate and chenodeoxycholate. The reaction is stimulated by the presence of NAD(+) but is inhibited by excess NADH. (1) Deoxycholate + FAD + H(2)O = cholate + FADH(2). Under physiological conditions, the reactions occur in the reverse direction to that shown above. Allo-deoxycholate is also formed as a side-product of the 7-alpha-dehydroxylation of cholate. (2) Lithocholate + FAD + H(2)O = chenodeoxycholate + FADH(2). Acting on iron-sulfur proteins as donors With NAD(+) or NADP(+) as acceptor Rubredoxin reductase Dihydronicotinamide adenine dinucleotide--rubredoxin reductase Rubredoxin--NAD reductase Rubredoxin--NAD(+) reductase Rubredoxin--nicotinamide adenine dinucleotide reductase NADH--rubredoxin oxidoreductase NADH--rubredoxin reductase Reduced nicotinamide adenine dinucleotide--rubredoxin reductase FAD 2 reduced rubredoxin + NAD(+) = 2 oxidized rubredoxin + NADH. Iron The reaction does not occur when NADPH is substituted for NADH. The enzyme from Clostridium acetobutylicum reduces rubredoxin, ferricyanide and dichlorophenolindophenol, but not ferredoxin or flavodoxin. NADPH:adrenodoxin oxidoreductase Ferredoxin--NADP(+) reductase Adrenodoxin reductase Also acts on adrenodoxin. FAD 2 reduced ferredoxin + NADP(+) = 2 oxidized ferredoxin + NADPH. Ferredoxin--NAD(+) reductase Reduced ferredoxin + NAD(+) = oxidized ferredoxin + NADH. Dinucleotide phosphate reductase Rubredoxin--NAD(P)(+) reductase Rubredoxin--nicotinamide adenine dinucleotide (phosphate) reductase Rubredoxin--nicotinamide adenine NAD(P)H--rubredoxin oxidoreductase NAD(P)--rubredoxin oxidoreductase Ferredoxin is not utilized. FAD Reduced rubredoxin + NAD(P)(+) = oxidized rubredoxin + NAD(P)H. The enzyme reduces a number of electron carriers, including benzyl viologen, menadione and 2,6-dichloroindophenol, but rubredoxin is the most efficient. With dinitrogen as acceptor Nitrogenase Composed of two proteins that can be separated but are both required for nitrogenase activity. Acetylene is reduced to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia. Dinitrogenase is a molybdenum-iron protein that reduces dinitrogen in three succesive two-electron reductions from nitrogen to diimine to hydrazine to two molecules of ammonia; the molybdenum may be replaced by vanadium or iron. Molybdenum or vanadium 8 reduced ferredoxin + 8 H(+) + N(2) + 16 ATP + 16 H(2)O = 8 oxidized ferredoxin + H(2) + 2 NH(3) + 16 ADP + 16 phosphate. Ferredoxin may be replaced by flavodoxin (see EC 1.19.6.1). Iron-sulfur The electron is transferred to the other protein, dinitrogenase (molybdoferredoxin). The reduction is initiated by formation of hydrogen in stoichiometric amounts. In the absence of a suitable substrate, hydrogen is slowly formed. Dinitrogen reductase is a [4Fe-4S] protein, which, with two molecules of ATP and ferredoxin, generates an electron. Acting on reduced flavodoxin as donor With dinitrogen as acceptor Nitrogenase (flavodoxin) Iron-sulfur 6 reduced flavodoxin + 6 H(+) + N(2) + n ATP = 6 oxidized flavodoxin + 2 NH(3) + n ADP + n phosphate. Molybdenum Acting on the aldehyde or oxo group of donors With NAD(+) or NADP(+) as acceptor Acylating acetaldehyde dehydrogenase Aldehyde dehydrogenase (acylating) Acetaldehyde dehydrogenase (acetylating) Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH. It is the final enzyme in the meta-cleavage pathway for the degradation of phenols, cresols and catechol, converting the acetaldehyde produced by EC 4.1.3.39 into acetyl-CoA. NADP(+) can replace NAD(+) but the rate of reaction is much slower. Also acts, more slowly, on glycolaldehyde, propanal and butanal. In Pseudomonas species, this enzyme forms part of a bifunctional enzyme with EC 4.1.3.39. Aspartate-semialdehyde dehydrogenase ASA dehydrogenase L-aspartate-beta-semialdehyde dehydrogenase Aspartic semialdehyde dehydrogenase L-aspartate 4-semialdehyde + phosphate + NADP(+) = L-4-aspartyl phosphate + NADPH. Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) Triosephosphate dehydrogenase GAPDH NAD-dependent glyceraldehyde-3-phosphate dehydrogenase D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. Also acts very slowly on D-glyceraldehyde and some other aldehydes. Thiols can replace phosphate. Glyceraldehyde-3-phosphate dehydrogenase (NADP(+)) (phosphorylating) Triosephosphate dehydrogenase (NADP(+)) Triosephosphate dehydrogenase (NADP+) NADP-dependent glyceraldehyde-3-phosphate dehydrogenase D-glyceraldehyde 3-phosphate + phosphate + NADP(+) = 3-phospho-D-glyceroyl phosphate + NADPH. Malonate-semialdehyde dehydrogenase 3-oxopropanoate + NAD(P)(+) + H(2)O = malonate + NAD(P)H. Succinate-semialdehyde dehydrogenase (NAD(P)(+)) Succinate semialdehyde + NAD(P)(+) + H(2)O = succinate + NAD(P)H. Glyoxylate dehydrogenase (acylating) Glyoxylate + CoA + NADP(+) = oxalyl-CoA + NADPH. Malonate-semialdehyde dehydrogenase (acetylating) 3-oxopropanoate + CoA + NAD(P)(+) = acetyl-CoA + CO(2) + NAD(P)H. 4-aminobutanal dehydrogenase ABALDH 1-pyrroline dehydrogenase Gamma-guanidinobutyraldehyde dehydrogenase Aminobutyraldehyde dehydrogenase As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate. The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates. The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54). 4-aminobutanal + NAD(+) + H(2)O = 4-aminobutanoate + NADH. Formate dehydrogenase Together with EC 1.12.1.2, forms a system previously known as formate hydrogenlyase. Formate + NAD(+) = CO(2) + NADH. Glutarate-semialdehyde dehydrogenase Glutarate semialdehyde + NAD(+) + H(2)O = glutarate + NADH. Glycolaldehyde dehydrogenase Glycolaldehyde + NAD(+) + H(2)O = glycolate + NADH. Lactaldehyde dehydrogenase (S)-lactaldehyde + NAD(+) + H(2)O = (S)-lactate + NADH. Alpha-ketoaldehyde dehydrogenase 2-oxoaldehyde dehydrogenase (NAD(+)) Methylglyoxal dehydrogenase A 2-oxoaldehyde + NAD(+) + H(2)O = a 2-oxo acid + NADH. Not identical with EC 1.2.1.49. Succinate-semialdehyde dehydrogenase http://purl.uniprot.org/mim/271980 Succinate semialdehyde + NAD(+) + H(2)O = succinate + NADH. 2-oxoisovalerate dehydrogenase (acylating) Also acts on (S)-3-methyl-2-oxopentanoate and 4-methyl-2-oxopentanoate. 3-methyl-2-oxobutanoate + CoA + NAD(+) = 2-methylpropanoyl-CoA + CO(2) + NADH. 2,5-dioxovalerate dehydrogenase 2,5-dioxopentanoate + NADP(+) + H(2)O = 2-oxoglutarate + NADPH. Methylmalonate-semialdehyde dehydrogenase (acylating) MMSA dehydrogenase MSDH http://purl.uniprot.org/mim/603178 2-methyl-3-oxopropanoate + CoA + H(2)O + NAD(+) = propanoyl-CoA + HCO(3)(-) + NADH. The reaction occurs in two steps with the decarboxylation process preceding CoA-binding. Bicarbonate rather than CO(2) is released as a final product. Also converts 3-oxopropanoate into acetyl-CoA. Benzaldehyde dehydrogenase (NAD(+)) Benzaldehyde + NAD(+) + H(2)O = benzoate + NADH. Aryl-aldehyde dehydrogenase Oxidizes a number of aromatic aldehydes, but not aliphatic aldehydes. An aromatic aldehyde + NAD(+) + H(2)O = an aromatic acid + NADH. Aldehyde dehydrogenase (NAD(+)) http://purl.uniprot.org/mim/270200 Wide specificity, including oxidation of D-glucuronolactone to D-glucarate. An aldehyde + NAD(+) + H(2)O = an acid + NADH. http://purl.uniprot.org/mim/100650 Aryl-aldehyde dehydrogenase (NADP(+)) An aromatic aldehyde + NADP(+) + AMP + diphosphate + H(2)O = an aromatic acid + NADPH + ATP. Aminoadipate semialdehyde dehydrogenase L-alpha-aminoadipate delta-semialdehyde oxidoreductase L-alpha-aminoadipate delta-semialdehyde:NAD oxidoreductase L-aminoadipate-semialdehyde dehydrogenase L-alpha-aminoadipate delta-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase 2-aminoadipic semialdehyde dehydrogenase Alpha-aminoadipate reductase Alpha-aminoadipate-semialdehyde dehydrogenase 2-aminoadipate semialdehyde dehydrogenase L-2-aminoadipate 6-semialdehyde + NAD(P)(+) + H(2)O = L-2-aminoadipate + NAD(P)H. http://purl.uniprot.org/mim/266100 Aminomuconate-semialdehyde dehydrogenase 2-aminomuconate 6-semialdehyde + NAD(+) + H(2)O = 2-aminomuconate + NADH. Also acts on 2-hydroxymuconate semialdehyde. D-aldopantoate dehydrogenase (R)-dehydropantoate dehydrogenase (R)-4-dehydropantoate + NAD(+) + H(2)O = (R)-3,3-dimethylmalate + NADH. Retinal dehydrogenase FAD Acts on both the 11-trans-and 13-cis-forms of retinal. Retinal + NAD(+) + H(2)O = retinoate + NADH. N-acetyl-gamma-glutamyl-phosphate reductase NAGSA dehydrogenase N-acetyl-glutamate semialdehyde dehydrogenase N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. Phenylacetaldehyde dehydrogenase Phenylacetaldehyde + NAD(+) + H(2)O = phenylacetate + NADH. Aldehyde dehydrogenase (NADP(+)) An aldehyde + NADP(+) + H(2)O = an acid + NADPH. 3-alpha,7-alpha,12-alpha-trihydroxycholestan-26-al 26-oxidoreductase 3-alpha,7-alpha,12-alpha-trihydroxycholestan-26-al 26-dehydrogenase 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-al + NAD(+) + H(2)O = 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate + NADH. Glutamyl-gamma-semialdehyde dehydrogenase Glutamate-5-semialdehyde dehydrogenase Gamma-glutamylphosphate reductase Beta-glutamylphosphate reductase L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH. Fatty acyl-CoA reductase Hexadecanal dehydrogenase (acylating) Hexadecanal + CoA + NAD(+) = hexadecanoyl-CoA + NADH. Also acts, more slowly, on octadecanoyl-CoA. Formate dehydrogenase (NADP(+)) Formate + NADP(+) = CO(2) + NADPH. Selenium Iron Tungsten Cinnamoyl-CoA reductase Cinnamaldehyde + CoA + NADP(+) = cinnamoyl-CoA + NADPH. Also acts on a number of substituted cinnamoyl esters of coenzyme A. 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase Does not act on unsubstituted aliphatic or aromatic aldehydes or glucose. NAD(+) can replace NADP(+), but with lower affinity. 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP(+) = 4-carboxy-2-hydroxy-cis,cis-muconate + NADPH. Formaldehyde dehydrogenase Formaldehyde + NAD(+) + H(2)O = formate + NADH. 4-trimethylammoniobutyraldehyde dehydrogenase 4-trimethylammoniobutanal + NAD(+) + H(2)O = 4-trimethylammoniobutanoate + NADH. Long-chain-aldehyde dehydrogenase The best substrate is dodecylaldehyde. A long-chain aldehyde + NAD(+) + H(2)O = a long-chain acid anion + NADH. Methylglyoxal dehydrogenase Alpha-ketoaldehyde dehydrogenase 2-oxoaldehyde dehydrogenase (NADP(+)) A 2-oxoaldehyde + NADP(+) + H(2)O = a 2-oxo acid + NADPH. Not identical with EC 1.2.1.23. Aldehyde dehydrogenase (NAD(P)(+)) An aldehyde + NAD(P)(+) + H(2)O = an acid + NAD(P)H. Long-chain-fatty-acyl-CoA reductase Acyl-CoA reductase A long-chain aldehyde + CoA + NADP(+) = a long-chain acyl-CoA + NADPH. Together with EC 6.2.1.19 forms a fatty acid reductase system which produces the substrate of EC 1.14.14.3, thus being part of the bacterial luciferase system. Pyruvate dehydrogenase (NADP(+)) Pyruvate:NADP(+) oxidoreductase Pyruvate + CoA + NADP(+) = acetyl-CoA + CO(2) + NADPH. The Euglena enzyme can also use FAD or methyl viologen as acceptor, more slowly. Inhibited by oxygen. Oxoglutarate dehydrogenase (NADP(+)) 2-oxoglutarate + CoA + NADP(+) = succinyl-CoA + CO(2) + NADPH. The Euglena enzyme can also use NAD(+) as acceptor, but more slowly. 4-hydroxyphenylacetaldehyde dehydrogenase With EC 4.2.1.87, brings about the metabolism of octopamine in Pseudomonas. 4-hydroxyphenylacetaldehyde + NAD(+) + H(2)O = 4-hydroxyphenylacetate + NADH. Gamma-guanidinobutyraldehyde dehydrogenase Involved in the degradation of arginine in Pseudomonas putida (cf. EC 1.2.1.19). 4-guanidinobutanal + NAD(+) + H(2)O = 4-guanidinobutanoate + NADH. Butanal dehydrogenase Butanal + CoA + NAD(P)(+) = butanoyl-CoA + NAD(P)H. Also acts on acetaldehyde, but more slowly. Phenylglyoxylate dehydrogenase (acylating) FAD Also reduces viologen dyes. Phenylglyoxylate + NAD(+) + CoA-SH = benzoyl-S-CoA + CO(2) + NADH. Iron-sulfur 2-oxoisovalerate is oxidized at 15% of the rate for phenylglyoxylate. The enzyme from Azoarcus evansii is specific for phenylglyoxylate. Thiamine diphosphate Triosephosphate dehydrogenase (NAD(P)(+)) NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase Triosephosphate dehydrogenase (NAD(P)) Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)(+)) (phosphorylating) D-glyceraldehyde 3-phosphate + phosphate + NAD(P)(+) = 3-phospho-D-glyceroyl phosphate + NAD(P)H. NAD(+) and NADP(+) can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 and EC 1.2.1.13, which are NAD(+)-and NADP(+)-dependent, respectively. 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase Carboxymethylhydroxymuconic semialdehyde dehydrogenase 5-carboxymethyl-2-hydroxymuconate semialdehyde + H(2)O + NAD(+) = 5-carboxymethyl-2-hydroxymuconate + NADH. Involved in the tyrosine degradation pathway in Arthrobacter sp. 4-hydroxymuconic-semialdehyde dehydrogenase Involved in the 4-nitrophenol degradation pathway. 4-hydroxymuconic semialdehyde + NAD(+) + H(2)O = maleylacetate + NADH. 4-formylbenzenesulfonate dehydrogenase 4-formylbenzenesulfonate + NAD(+) + H(2)O = 4-sulfobenzoate + NADH. Involved in the toluene-4-sulfonate degradation pathway. 6-oxohexanoate dehydrogenase Last step in the cyclohexanol degradation pathway in Acinetobacter sp. 6-oxohexanoate + NADP(+) + H(2)O = adipate + NADPH. 4-hydroxybenzaldehyde dehydrogenase p-hydroxybenzaldehyde dehydrogenase 4-hydroxybenzaldehyde + NAD(+) + H(2)O = 4-hydroxybenzoate + NADH. Involved in the toluene degradation pathway in Pseudomonas mendocina. Salicylaldehyde dehydrogenase Salicylaldehyde + NAD(+) + H(2)O = salicylate + NADH. Involved in the naphthalene degradation pathway in some bacteria. Mycothiol-dependent formaldehyde dehydrogenase NAD/factor-dependent formaldehyde dehydrogenase The S-formylmycothiol formed hydrolyzes to mycothiol and formate. Zinc Formaldehyde + mycothiol + NAD(+) = S-formylmycothiol + NADH. Vanillin dehydrogenase Vanillin + NAD(+) + H(2)O = vanillate + NADH. Coniferyl-aldehyde dehydrogenase Also oxidizes other aromatic aldehydes, but not aliphatic aldehydes. Coniferyl aldehyde + H(2)O + NAD(P)(+) = ferulate + NAD(P)H. Fluoroacetaldehyde dehydrogenase The enzyme from Streptomyces cattleya has a high affinity for fluoroacetate and glycolaldehyde but not for acetaldehyde. Fluoroacetaldehyde + NAD(+) + H(2)O = fluoroacetate + NADH. Benzaldehyde dehydrogenase (NADP(+)) Benzaldehyde + NADP(+) + H(2)O = benzoate + NADPH. Glutamyl-tRNA reductase However, in the alpha-proteobacteria EC 2.3.1.37 is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. Forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway, which is used in most eubacteria, and in all archaebacteria, algae and plants. L-glutamate 1-semialdehyde + NADP(+) + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37. This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic alpha-proteobacterium. SGSD Succinylglutamic semialdehyde dehydrogenase N-succinylglutamate 5-semialdehyde dehydrogenase Succinylglutamate-semialdehyde dehydrogenase This is the fourth enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. N-succinyl-L-glutamate 5-semialdehyde + NAD(+) + H(2)O = N-succinyl-L-glutamate + NADH. The five enzymes involved in this pathway are EC 2.3.1.109, EC 3.5.3.23, EC 2.6.1.11, EC 1.2.1.71 and EC 3.5.1.96. E4P dehydrogenase E4PDH Erythrose-4-phosphate dehydrogenase Erythrose 4-phosphate dehydrogenase Forms part of the pyridoxal-5'-phosphate coenzyme biosynthesis pathway in Escherichia coli, along with EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5. Was originally thought to be an EC 1.2.1.12, but this has since been disproved, as glyceraldehyde 3-phosphate is not a substrate. D-erythrose 4-phosphate + NAD(+) + H(2)O = 4-phosphoerythronate + NADH. Betaine aldehyde oxidase BADH Betaine-aldehyde dehydrogenase Betaine aldehyde dehydrogenase Betaine aldehyde + NAD(+) + H(2)O = betaine + NADH. In plants, this reaction is catalyzed by EC 1.14.15.7, whereas in animals and many bacteria, it is catalyzed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17). In contrast, different enzymes are involved in the first reaction. In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 and EC 2.1.1.157. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. Triosephosphate dehydrogenase Glyceraldehyde-3-phosphate dehydrogenase (NADP(+)) D-glyceraldehyde 3-phosphate + NADP(+) + H(2)O = 3-phospho-D-glycerate + NADPH. With a cytochrome as acceptor Formate dehydrogenase (cytochrome) Formate + 2 ferricytochrome b1 = CO(2) + 2 ferrocytochrome b1 + 2 H(+). Pyruvic dehydrogenase Pyruvate dehydrogenase (cytochrome) Pyruvate dehydrogenase Pyruvate + ferricytochrome b1 + H(2)O = acetate + CO(2) + ferrocytochrome b1. Thiamine diphosphate Formate dehydrogenase (cytochrome c-553) Formate + ferricytochrome c-553 = CO(2) + ferrocytochrome c-553. Saccharomyces cerevisiae cytochrome c, ferricyanide and phenazine methosulfate can act as acceptors. Carbon monoxide:methylene blue oxidoreductase Carbon-monoxide dehydrogenase (cytochrome b-561) Carbon monoxide oxygenase (cytochrome b-561) Carbon monoxide oxidase Iron-sulfur Molybdopterin cytosine dinucleotide FAD Oxygen, methylene blue and iodonitrotetrazolium chloride can act as nonphysiological electron acceptors. CO + H(2)O + 2 ferricytochrome b-561 = CO(2) + 2 H(+) + 2 ferrocytochrome b-561. With oxygen as acceptor Aldehyde oxidase Quinoline oxidase May be identical with EC 1.2.3.11. Also oxidizes quinoline and pyridine derivatives. Molybdenum FAD An aldehyde + H(2)O + O(2) = a carboxylic acid + H(2)O(2). Iron-sulfur Retinene oxidase Retinal oxidase Retinal + O(2) + H(2)O = retinoate + H(2)O(2). May be the same as EC 1.2.3.1. 4-hydroxyphenylpyruvate oxidase Involved in tyrosine degradation pathway in Arthrobacter sp. 4-hydroxyphenylpyruvate + 0.5 O(2) = 4-hydroxyphenylacetate + CO(2). Abscisic-aldehyde oxidase AO-delta While abscisic aldehyde is the best substrate, the enzyme also acts with indole-3-aldehyde, 1-naphthaldehyde and benzaldehyde as substrates, but more slowly. Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.1.1.288, EC 1.13.11.51 and EC 1.14.13.93. Abscisic aldehyde + H(2)O + O(2) = abscisate + H(2)O(2). Acts on both (+)-and (-)-abscisic aldehyde. Pyruvate oxidase Phosphate-dependent pyruvate oxidase Pyruvic oxidase Pyruvate + phosphate + O(2) = acetyl phosphate + CO(2) + H(2)O(2). Two reducing equivalents are transferred from the resonant carbanion/enamine forms of 2-hydroxyethyl-thiamine-diphosphate to the adjacent flavin cofactor, yielding 2-acetyl-thiamine diphosphate (AcThDP) and reduced flavin. FADH is reoxidized by O(2) to yield H(2)O(2) and FAD and AcThDP is cleaved phosphorolytically to acetyl phosphate and thiamine diphosphate. FAD Thiamine diphosphate Oxalate oxidase Oxalate + O(2) + 2 H(+) = 2 CO(2) + H(2)O(2). Manganese Glyoxylate oxidase Glyoxylate + H(2)O + O(2) = oxalate + H(2)O(2). Pyruvate oxidase (CoA-acetylating) FAD Pyruvate + CoA + O(2) = acetyl-CoA + CO(2) + H(2)O(2). May be identical with EC 1.2.7.1. IAAld oxidase Indole-3-acetaldehyde oxidase IAA oxidase Indoleacetaldehyde oxidase While (indol-3-yl)acetaldehyde is the preferred substrate, it also oxidizes indole-3-carbaldehyde and acetaldehyde, but more slowly. Has a preference for aldehydes having an indole-ring structure as substrate. FAD Isoform of EC 1.2.3.1. May play a role in plant hormone biosynthesis as its activity is higher in the auxin-overproducing mutant, super-root1, than in wild-type Arabidopsis thaliana. (Indol-3-yl)acetaldehyde + H(2)O + O(2) = (indol-3-yl)acetate + H(2)O(2). Heme Molybdenum Pyridoxal oxidase Molybdenum Pyridoxal + H(2)O + O(2) = 4-pyridoxate + H(2)O(2). Aryl-aldehyde oxidase An aromatic aldehyde + O(2) + H(2)O = an aromatic carboxylic acid + H(2)O(2). Acts on benzaldehyde, vanillin and a number of other aromatic aldehydes, but not on aliphatic aldehydes or sugars. With a disulfide as acceptor Pyruvic dehydrogenase Pyruvate dehydrogenase Pyruvate decarboxylase Pyruvic acid dehydrogenase Pyruvate dehydrogenase (acetyl-transferring) MtPDC (mitochondrial pyruvate dehydogenase complex) Pyruvate dehydrogenase (lipoamide) Pyruvate dehydrogenase complex Pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-acetylating) Thiamine diphosphate http://purl.uniprot.org/mim/312170 http://purl.uniprot.org/mim/179060 Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12. OGDC Alpha-oxoglutarate dehydrogenase Ketoglutaric dehydrogenase Oxoglutarate dehydrogenase (succinyl-transferring) Oxoglutarate dehydrogenase (lipoamide) Oxoglutarate decarboxylase Alpha-ketoglutaric dehydrogenase 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-succinylating) AKGDH Oxoglutarate dehydrogenase 2-oxoglutarate: lipoate oxidoreductase Alpha-ketoglutaric acid dehydrogenase Alpha-ketoglutarate dehydrogenase 2-ketoglutarate dehydrogenase 2-oxoglutarate dehydrogenase Thiamine diphosphate It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61. http://purl.uniprot.org/mim/203740 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2). It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, which also binds multiple copies of EC 1.8.1.4. Branched-chain keto acid dehydrogenase Alpha-keto-alpha-methylvalerate dehydrogenase Dehydrogenase, 2-oxoisovalerate (lipoate) 2-oxoisocaproate dehydrogenase 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) BCOAD Dehydrogenase, branched chain alpha-keto acid Branched-chain (-2-oxoacid) dehydrogenase (BCD) Branched-chain alpha-oxo acid dehydrogenase Alpha-ketoisocaproic-alpha-keto-alpha-methylvaleric dehydrogenase Branched-chain ketoacid dehydrogenase Alpha-ketoisocaproate dehydrogenase Branched-chain alpha-keto acid dehydrogenase 2-oxoisovalerate (lipoate) dehydrogenase Branched-chain 2-oxo acid dehydrogenase Branched-chain 2-keto acid dehydrogenase BCKDH Alpha-oxoisocaproate dehydrogenase Alpha-ketoisocaproic dehydrogenase Branched chain keto acid dehydrogenase 3-methyl-2-oxobutanoate:lipoamide oxidoreductase (decarboxylating and acceptor-2-methylpropanoylating) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) Alpha-ketoisovalerate dehydrogenase http://purl.uniprot.org/mim/248600 It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, which also binds multiple copies of EC 1.8.1.4. Thiamine diphosphate It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168. 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO(2). It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. With an iron-sulfur protein as acceptor Pyruvate:ferredoxin oxidoreductase Pyruvate synthase Pyruvate synthetase Pyruvate oxidoreductase Pyruvic-ferredoxin oxidoreductase Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+). Thiamine diphosphate Iron-sulfur 2-oxobutyrate synthase 2-oxobutanoate + CoA + oxidized ferredoxin = propanoyl-CoA + CO(2) + reduced ferredoxin. KGOR Alpha-ketoglutarate-ferredoxin oxidoreductase Alpha-ketoglutarate synthase 2-ketoglutarate ferredoxin oxidoreductase 2-oxoglutarate synthase 2-oxoglutarate ferredoxin oxidoreductase Thiamine diphosphate 2-oxoglutarate + CoA + 2 oxidized ferredoxin = succinyl-CoA + CO(2) + 2 reduced ferredoxin. Highly specific for 2-oxoglutarate. This enzyme is one of four 2-oxoacid oxidoreductases that are differentiated by their abilities to oxidatively decarboxylate different 2-oxoacids and form their CoA derivatives (see also EC 1.2.7.1, EC 1.2.7.7 and EC 1.2.7.8). Iron-sulfur Carbon-monoxide dehydrogenase (ferredoxin) The enzyme from Moorella thermoacetica exists as a complex with EC 2.3.1.169, which catalyzes the overall reaction: methylcorrinoid protein + CoA + CO(2) + reduced ferredoxin = acetyl-CoA + corrinoid protein + H(2)O + oxidized ferredoxin. Zinc CO + H(2)O + oxidized ferredoxin = CO(2) + reduced ferredoxin. Methyl viologen can act as acceptor. Nickel Iron Tungsten-containing aldehyde ferredoxin oxidoreductase AOR Aldehyde ferredoxin oxidoreductase Can use ferredoxin or methyl viologen but not NAD(P)(+) as electron acceptor. This is an oxygen-sensitive enzyme. Tungsten-molybdopterin Iron-sulfur However, it does not oxidize glyceraldehyde 3-phosphate (see EC 1.2.7.6). Catalyzes the oxidation of aldehydes (including crotonaldehyde, acetaldehyde, formaldehyde and glyceraldehyde) to their corresponding acids. An aldehyde + H(2)O + 2 oxidized ferredoxin = an acid + 2 H(+) + 2 reduced ferredoxin. Glyceraldehyde-3-phosphate Fd oxidoreductase Glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) Glyceraldehyde-3-phosphate ferredoxin reductase GAPOR Tungsten-molybdopterin Specific for glyceraldehyde-3-phosphate. Iron-sulfur Thought to function in place of glyceraldehyde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhof-type glycolytic pathway found in Pyrococcus furiosus. D-glyceraldehyde-3-phosphate + H(2)O + 2 oxidized ferredoxin = 3-phospho-D-glycerate + 2 H(+) + 2 reduced ferredoxin. Ketoisovalerate oxidoreductase 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) Branched-chain ketoacid ferredoxin reductase Ketoisovalerate ferredoxin reductase 3-methyl-2-oxobutanoate synthase (ferredoxin) Keto-valine-ferredoxin oxidoreductase Branched-chain oxo acid ferredoxin reductase 2-ketoisovalerate ferredoxin reductase 2-oxoisovalerate ferredoxin reductase VOR Iron-sulfur Tungsten-molybdopterin One of four 2-oxoacid oxidoreductases that are differentiated by their abilities to oxidatively decarboxylate different 2-oxoacids and form their CoA derivatives (see also EC 1.2.7.1, EC 1.2.7.3 and EC 1.2.7.8). Coenzyme-A 3-methyl-2-oxobutanoate + CoA + oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO(2) + reduced ferredoxin. Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo-pentanoate, 2-oxobutyrate and 3-methylthiopropanamine. 3-(indol-3-yl)pyruvate synthase (ferredoxin) Indolepyruvate ferredoxin oxidoreductase IOR Thiamine diphosphate This enzyme, which is found in archaea, is one of four 2-oxoacid oxidoreductases that are differentiated by their abilities to oxidatively decarboxylate different 2-oxoacids and form their CoA derivatives (see also EC 1.2.7.1, EC 1.2.7.3 and EC 1.2.7.7). Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and 4-hydroxyphenylpyruvate as substrates. (Indol-3-yl)pyruvate + CoA + oxidized ferredoxin = S-2-(indol-3-yl)acetyl-CoA + CO(2) + reduced ferredoxin. Iron-sulfur With other acceptors Carbon monoxide oxygenase Carbon-monoxide dehydrogenase (acceptor) Carbon-monoxide dehydrogenase Anaerobic carbon monoxide dehydrogenase CO + H(2)O + A = CO(2) + AH(2). Forms part of a membrane-bound multienzyme complex with EC 1.12.99.6, which catalyzes the overall reaction: CO + H(2)O = CO(2) + H(2). Iron-sulfur Nickel It uses many electron acceptors, including ferredoxin, methyl viologen and benzyl viologen and flavins, but not pyridine nucleotides. Aldehyde dehydrogenase (pyrroloquinoline-quinone) Aldehyde dehydrogenase (acceptor) PQQ Wide specificity; acts on straight-chain aldehydes up to C(10), aromatic aldehydes, glyoxylate and glyceraldehyde. An aldehyde + acceptor + H(2)O = a carboxylate + reduced acceptor. Formaldehyde dismutase Formaldehyde and acetaldehyde can act as donors; formaldehyde, acetaldehyde and propanal can act as acceptors. 2 formaldehyde + H(2)O = formate + methanol. Formylmethanofuran dehydrogenase Methyl viologen can act as acceptor. Molybdenum Formylmethanofuran + H(2)O + acceptor = CO(2) + methanofuran + reduced acceptor. Also oxidizes N-furfurylformamide. Carboxylate reductase Methyl viologen can act as acceptor. In the reverse direction, non-activated acids are reduced by reduced viologens to aldehydes, but not to the corresponding alcohols. Tungsten An aldehyde + acceptor + H(2)O = a carboxylate + reduced acceptor. AORDd Aldehyde oxidoreductase Aldehyde dehydrogenase (FAD-independent) Aldehyde oxidase Molybdopterin cytosine dinucleotide An aldehyde + H(2)O + acceptor = a carboxylate + reduced acceptor. Iron-sulfur Acting on phosphorus or arsenic in donors Acting on phosphorus or arsenic in donors, with NAD(P)(+) as acceptor Phosphite dehydrogenase Phosphonate dehydrogenase NAD-dependent phosphite dehydrogenas NAD:phosphite oxidoreductase NADP(+) is a poor substitute for NAD(+) in the enzyme from Pseudomonas stutzeri WM88. Phosphonate + NAD(+) + H(2)O = phosphate + NADH. Acting on phosphorus or arsenic in donors, with disulfide as acceptor Arsenate reductase (glutaredoxin) Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 3.6.3.16. Molybdenum Thioredoxins reduced by NADPH and thioredoxin reductase can act as alternative substrates. Arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H(2)O. The glutaredoxins catalyze glutathione-disulfide oxidoreductions and have a redox-active disulfide/dithiol in the active site (-Cys-Pro-Tyr-Cys-) that forms a disulfide bond in the oxidized form. The enzyme is part of a system for detoxifying arsenate. Glutaredoxins have a binding site for glutathione, which is required to reduce them to the dithiol form. In other organisms, arsenite can be methylated by EC 2.1.1.137 in a pathway to non-toxic organoarsenical compounds. MMA(V) reductase Methylarsonate reductase Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H(2)O. The product, Me-As(OH)(2) (methylarsonous acid), is biologically methylated by EC 2.1.1.137 to form cacodylic acid (dimethylarsinic acid). Acting on phosphorus or arsenic in donors, with other, known acceptors Arsenite oxidase Arsenate reductase (azurin) Iron-sulfur Molybdenum Molybdopterin The enzyme also uses a c-type cytochrome or O(2) as acceptors. Arsenite + H(2)O + 2 azurin(ox) = arsenate + 2 azurin(red) + 2 H(+). Acting on phosphorus or arsenic in donors, with other acceptors Arsenate reductase (donor) Unlike EC 1.20.4.1 reduced glutaredoxin cannot serve as a reductant. Arsenite + acceptor = arsenate + reduced acceptor. Benzyl viologen can act as an acceptor. Acting on x-H and y-H to form an x-y bond With oxygen as acceptor Isopenicillin-N synthase Forms part of the penicillin biosynthesis pathway. N-((5S)-5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + O(2) = isopenicillin N + 2 H(2)O. Berberine synthase Columbamine oxidase Iron 2 columbamine + O(2) = 2 berberine + 2 H(2)O. Oxidation of the O-methoxyphenol structure forms the methylenedioxy group of berberine. Reticuline oxidase Berberine-bridge-forming enzyme Tetrahydroprotoberberine synthase Berberine bridge enzyme The product of the reaction, (S)-scoulerine, is a precursor of protopine, protoberberine and benzophenanthridine alkaloid biosynthesis in plants. FAD (S)-reticuline + O(2) = (S)-scoulerine + H(2)O(2). Acts on (S)-reticuline and related compounds, converting the N-methyl group into the methylene bridge ('berberine bridge') of (S)-tetrahydroprotoberberines. Sulochrin oxidase Sulochrin oxidase ((+)-bisdechlorogeodin-forming) Involved in the biosynthesis of mold metabolites related to the antibiotic griseofulvin. Also acts on several diphenols and phenylenediamines, but has low affinity for these substrates. 2 sulochrin + O(2) = 2 (+)-bisdechlorogeodin + 2 H(2)O. Sulochrin oxidase Sulochrin oxidase ((-)-bisdechlorogeodin-forming) Involved in the biosynthesis of mold metabolites related to the antibiotic griseofulvin. 2 sulochrin + O(2) = 2 (-)-bisdechlorogeodin + 2 H(2)O. Also acts on several diphenols and phenylenediamines, but has low affinity for these substrates. Aureusidin synthase Plays a key role in the yellow coloration of flowers such as snapdragon. Copper (1) 2',4,4',6'-tetrahydroxychalcone + O(2) = aureusidin + H(2)O. The enzyme is a homolog of plant polyphenol oxidase and catalyzes two separate chemical transformations, i.e. 3-hydroxylation and oxidative cyclization (2',alpha-dehydrogenation). (2) 2',3,4,4',6'-pentahydroxychalcone + 0.5 O(2) = aureusidin + H(2)O. H(2)O(2) activates reaction (1) but inhibits reaction (2). With a disulfide as acceptor D-proline reductase (dithiol) 5-aminopentanoate + lipoate = D-proline + dihydrolipoate. Other dithiols can function as reducing agents; the enzyme contains a pyruvoyl group and a selenocysteine residue, both essential for activity. Pyruvate The reaction is observed only in the direction of D-proline reduction. Glycine reductase Only subunit B distinguishes this enzyme from EC 1.21.4.3 and EC 1.21.4.4. The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C. The reaction is observed only in the direction of glycine reduction. Subunit A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by subunit C to produce acetyl phosphate. Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Acetyl phosphate + NH(3) + thioredoxin disulfide + H(2)O = glycine + phosphate + thioredoxin. Sarcosine reductase Only subunit B distinguishes this enzyme from EC 1.21.4.2 and EC 1.21.4.4. Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for sarcosine binding and methylamine release. Acetyl phosphate + methylamine + thioredoxin disulfide = N-methylglycine + phosphate + thioredoxin. The reaction is observed only in the direction of sarcosine reduction. Subunit A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by subunit C to produce acetyl phosphate. The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C. Betaine reductase Only subunit B distinguishes this enzyme from EC 1.21.4.2 and EC 1.21.4.3. The reaction is observed only in the direction of betaine reduction. The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C. Acetyl phosphate + trimethylamine + thioredoxin disulfide = N,N,N-trimethylglycine + phosphate + thioredoxin. Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Subunit A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by subunit C to produce acetyl phosphate. With other acceptors Beta-cyclopiazonic oxidocyclase Beta-cyclopiazonate dehydrogenase Beta-cyclopiazonate oxidocyclase FAD Cytochrome c and various dyes can act as acceptor. Beta-cyclopiazonate + acceptor = alpha-cyclopiazonate + reduced acceptor. Cyclopiazonate is a microbial toxin. Acting on the CH-CH group of donors With NAD(+) or NADP(+) as acceptor Dihydrouracil dehydrogenase (NAD(+)) 5,6-dihydrouracil + NAD(+) = uracil + NADH. Enoyl acyl-carrier-protein reductase Enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) Acyl-ACP dehydrogenase Enoyl-ACP reductase NADPH 2-enoyl Co A reductase Acyl-[acyl-carrier-protein] + NADP(+) = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH. The Saccharomyces cerevisiae and Escherichia coli enzymes are B-specific with respect to NADP(+) (cf. EC 1.3.1.9). Catalyzes the reduction of enoyl-acyl-[acyl-carrier-protein] derivatives of carbon chain length from 4 to 16. Melilotate dehydrogenase 2-coumarate reductase 3-(2-hydroxyphenyl)propanoate + NAD(+) = 2-coumarate + NADH. Hydroxyphenylpyruvate synthase Prephenate dehydrogenase Chorismate mutase--prephenate dehydrogenase Prephenate + NAD(+) = 4-hydroxyphenylpyruvate + CO(2) + NADH. This enzyme in the enteric bacteria also possesses EC 5.4.99.5 activity and converts chorismate into prephenate. Prephenate dehydrogenase (NADP(+)) Prephenate + NADP(+) = 4-hydroxyphenylpyruvate + CO(2) + NADPH. Orotate reductase (NADH) FMN (S)-dihydroorotate + NAD(+) = orotate + NADH. FAD Orotate reductase (NADPH) Flavoprotein (S)-dihydroorotate + NADP(+) = orotate + NADPH. Beta-nitroacrylate reductase 3-nitropropanoate + NADP(+) = 3-nitroacrylate + NADPH. 3-methyleneoxindole reductase 3-methyl-1,3-dihydroindol-2-one + NADP(+) = 3-methylene-1,3-dihydro-2H-indol-2-one + NADPH. Kynurenate-7,8-dihydrodiol dehydrogenase 7,8-dihydro-7,8-dihydroxykynurenate + NAD(+) = 7,8-dihydroxykynurenate + NADH. Cis-1,2-dihydrobenzene-1,2-diol dehydrogenase Cis-benzene glycol dehydrogenase Cis-1,2-dihydrobenzene-1,2-diol + NAD(+) = catechol + NADH. Dihydrothymine dehydrogenase Dihydropyrimidine dehydrogenase (NADP(+)) Dihydrouracil dehydrogenase (NADP+) 5,6-dihydrouracil + NADP(+) = uracil + NADPH. Also acts on dihydrothymine. http://purl.uniprot.org/mim/274270 Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase Trans-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol + NADPH. 7-dehydrocholesterol reductase Sterol Delta(7)-reductase 7-DHC reductase http://purl.uniprot.org/mim/270400 http://purl.uniprot.org/mim/268670 Cholesterol + NADP(+) = cholesta-5,7-dien-3-beta-ol + NADPH. Cholestenone 5-alpha-reductase 5-alpha-cholestan-3-one + NADP(+) = cholest-4-en-3-one + NADPH. Biliverdin reductase Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H. 3,5-cyclohexadiene-1,2-diol-1-carboxylate dehydrogenase Cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase 2-hydro-1,2-dihydroxybenzoate dehydrogenase 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid dehydrogenase 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase Dihydrodihydroxybenzoate dehydrogenase DHB dehydrogenase Cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate:NAD(+) oxidoreductase DHBDH (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD(+) = catechol + CO(2) + NADH. Dihydrodipicolinate reductase 2,3,4,5-tetrahydrodipicolinate + NAD(P)(+) = 2,3-dihydrodipicolinate + NAD(P)H. 2-hexadecenal reductase 2-alkenal reductase Hexadecanal + NADP(+) = 2-trans-hexadecenal + NADPH. Specific for long chain 2-trans-and 2-cis-alkenals, with chain length optimum around 14 to 16 carbon atoms. 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase 2,3-DHB dehydrogenase 2,3-dihydro-2,3-dihydroxybenzoate + NAD(+) = 2,3-dihydroxybenzoate + NADH. Cis-dihydrodiol naphthalene dehydrogenase Cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase Cis-naphthalene dihydrodiol dehydrogenase Cis-1,2-dihydronaphthalene-1,2-diol + NAD(+) = naphthalene-1,2-diol + NADH. Also acts, at half the rate, on cis-anthracene dihydrodiol and cis-phenanthrene dihydrodiol. Delta(4)-3-ketosteroid 5-beta-reductase Delta(4)-hydrogenase 3-oxo-Delta(4)-steroid 5-beta-reductase 5-beta-reductase Delta(4)-5-beta-reductase Cholestenone 5-beta-reductase Testosterone 5-beta-reductase Androstenedione 5-beta-reductase Cortisone 5-beta-reductase Steroid 5-beta-reductase Cortisone beta-reductase Delta(4)-3-oxosteroid 5-beta-reductase Cortisone Delta(4)-5-beta-reductase http://purl.uniprot.org/mim/235555 The bile acid intermediates 7-alpha,12-alpha-dihydroxy-4-cholesten-3-one and 7-alpha-hydroxy-4-cholesten-3-one can also act as substrates. (2) 17,21-dihydroxy-5-beta-pregnane-3,11,20-trione + NADP(+) = cortisone + NADPH. (1) 5-beta-cholestan-3-one + NADP(+) = cholest-4-en-3-one + NADPH. The enzyme from human efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites; it can also act on aldosterone, corticosterone and cortisol, but to a lesser extent. Steroid 5-alpha-reductase Progesterone 5-alpha-reductase 5-alpha-pregnan-3,20-dione + NADP(+) = progesterone + NADPH. Testosterone and 20-alpha-hydroxy-4-pregn-3-one can act in place of progesterone. Enoate reductase 2-enoate reductase Acts, in the reverse direction, on a wide range of alkyl and aryl alpha-beta-unsaturated carboxylate ions; 2-butenoate was the best substrate tested. Iron-sulfur FAD Butanoate + NAD(+) = 2-butenoate + NADH. Maleolylacetate reductase Maleylacetate reductase 3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H. Protochlorophyllide oxidoreductase Protochlorophyllide reductase NADPH-protochlorophyllide oxidoreductase Catalyzes a light-dependent trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration. Chlorophyllide a + NADP(+) = protochlorophyllide + NADPH. 2,4-dienoyl-CoA reductase (NADPH) 4-enoyl-CoA reductase (NADPH) Trans-2,3-didehydroacyl-CoA + NADP(+) = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH. http://purl.uniprot.org/mim/222745 Best substrates for reduction contain a 2,4-diene structure with chain length C(8) or C(10). Phosphatidylcholine desaturase Linoleate synthase Oleate desaturase Oleoyl-CoA desaturase 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + NAD(+) = 1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + NADH. Also desaturates phosphatidylcholine containing the oleoyl group on O-2 of the glycerol residue. Geissoschizine dehydrogenase Involved in the interconversion of heteroyohimbine alkaloids in Catharanthus roseus. Geissoschizine + NADP(+) = 4,21-dehydrogeissoschizine + NADPH. Cis-2-enoyl-CoA reductase (NADPH) Acyl-CoA + NADP(+) = cis-2,3-dehydroacyl-CoA + NADPH. Not identical with EC 1.3.1.38 (cf. EC 1.3.1.8). Trans-2-enoyl-CoA reductase (NADPH) Acyl-CoA + NADP(+) = trans-2,3-dehydroacyl-CoA + NADPH. Not identical with EC 1.3.1.37 (cf. EC 1.3.1.8). Enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) Acyl-ACP dehydrogenase The liver enzyme is A-specific with respect to NADP(+) (cf. EC 1.3.1.10). Acyl-[acyl-carrier-protein] + NADP(+) = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH. Cortisone alpha-reductase 4,5-alpha-dihydrocortisone + NADP(+) = cortisone + NADPH. 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate reductase Broad specificity; reduces a number of compounds produced by Pseudomonas from aromatic hydrocarbons by ring fission. 2,6-dioxo-6-phenylhexanoate + NADP(+) = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + NADPH. Xanthommatin reductase 5,12-dihydroxanthommatin + NAD(+) = xanthommatin + NADH. From Drosophila melanogaster. 12-oxophytodienoate reductase Involved in the conversion of linolenate into jasmonate in Zea mays. 8-((1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl)octanoate + NADP(+) = (15Z)-12-oxophyto-10,15-dienoate + NADPH. Cyclohexadienyl dehydrogenase Arogenic dehydrogenase Arogenate dehydrogenase Pretyrosine dehydrogenase L-arogenate:NAD(+) oxidoreductase See also EC 1.3.1.12, EC 1.3.1.78 and EC 1.3.1.79. L-arogenate + NAD(+) = L-tyrosine + NADH + CO(2). Trans-2-enoyl-CoA reductase (NAD(+)) Acyl-CoA + NAD(+) = trans-didehydroacyl-CoA + NADH. The enzyme from Euglena gracilis acts on crotonoyl-CoA and, more slowly, on trans-hex-2-enoyl-CoA and trans-oct-2-enoyl-CoA. 2'-hydroxyisoflavone reductase Vestitone + NADP(+) = 2'-hydroxyformononetin + NADPH. Involved in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain. In the reverse reaction, a 2'-hydroxyisoflavone is reduced to an isoflavanone; 2'-hydroxypseudobaptigenin also acts. Biochanin-A reductase Dihydrobiochanin A + NADP(+) = biochanin A + NADPH. Some other isoflavones are reduced to the corresponding isoflavanones. Alpha-santonin 1,2-reductase 1,2-dihydrosantonin + NAD(P)(+) = alpha-santonin + NAD(P)H. 15-oxoprostaglandin 13-oxidase (5Z)-(15S)-11-alpha-hydroxy-9,15-dioxoprostanoate + NAD(P)(+) = (5Z)-(15S)-11-alpha-hydroxy-9,15-dioxoprosta-13-enoate + NAD(P)H. The enzyme from placenta is specific for NAD(+). Reduces 15-oxoprostaglandins to 13,14-dihydro derivatives. Cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase (+)-cis-3,4-dihydrophenanthrene-3,4-diol + NAD(+) = phenanthrene-3,4-diol + NADH. Cucurbitacin Delta(23)-reductase Manganese 23,24-dihydrocucurbitacin + NAD(P)(+) = cucurbitacin + NAD(P)H. Iron or zinc can replace manganese to some extent. Cucurbitacin is a plant triterpenoid. HDR NADPH:2'-hydroxydaidzein oxidoreductase 2'-hydroxydihydrodaidzein:NADP(+) 2'-oxidoreductase 2'-hydroxydaidzein reductase Also acts on 2'-hydroxyformononetin and to a small extent on 2'-hydroxygenistein. In the reverse reaction, the 2'-hydroxyisoflavone (2'-hydroxydaidzein) is reduced to an isoflavanone. 2'-hydroxy-2,3-dihydrodaidzein + NADP(+) = 2'-hydroxydaidzein + NADPH. The isoflavones biochanin A, daidzein and genestein as well as the flavonoids apigenin, kaempferol and quercetin do not act as substrates. Involved in the biosynthesis of the phytoalexin glyceollin. 2-methyl-branched-chain-enoyl-CoA reductase FAD From Ascaris suum. The reaction proceeds only in the presence of another flavoprotein ('electron-transferring flavoprotein'). 2-methylbutanoyl-CoA + NAD(+) = 2-methylcrotonoyl-CoA + NADH. (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase Dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase Iron (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate + NAD(+) = 3,4-dihydroxybenzoate + CO(2) + NADH. Precorrin-6X reductase Precorrin-6Y:NADP(+) oxidoreductase Precorrin-6A reductase Precorrin-6B + NADP(+) = precorrin-6A + NADPH. Biphenyl-2,3-dihydro-2,3-diol dehydrogenase 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase Catalyzes the second step in the biphenyl degradation pathway in bacteria. Cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD(+) = biphenyl-2,3-diol + NADH. Phloroglucinol reductase Involved in the gallate anaerobic degradation pathway in bacteria. Dihydrophloroglucinol + NADP(+) = phloroglucinol + NADPH. 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase Biphenyl-2,3-dihydro-2,3-diol dehydrogenase Involved in the p-cymene and p-cumate degradation pathways in Pseudomonas putida. Cis-5,6-dihydroxy-4-isopropylcyclohexa-1,3-dienecarboxylate + NAD(+) = 2,3-dihydroxy-p-cumate + NADH. Fumarate reductase (NADH) NADH-dependent fumarate reductase Succinate + NAD(+) = fumarate + NADH. Dibenzothiophene dihydrodiol dehydrogenase Involved in the dibenzothiophene degradation pathway in bacteria. Cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene + NAD(+) = 1,2-dihydroxydibenzothiophene + NADH. Terephthalate 1,2-cis-dihydrodiol dehydrogenase Cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate + NAD(+) = 3,4-dihydroxybenzoate + CO(2) + NADH. Involved in the terephthalate degradation pathway in bacteria. Pimeloyl-CoA dehydrogenase Pimeloyl-CoA + NAD(+) = 6-carboxyhex-2-enoyl-CoA + NADH. Involved in the benzoate degradation (anaerobic) pathway in bacteria. 2,4-dichlorobenzoyl-CoA reductase 4-chlorobenzoyl-CoA + NADP(+) + HCl = 2,4-dichlorobenzoyl-CoA + NADPH. Acts in the reverse direction to form part of the 2,4-dichlorobenzoate degradation pathway in bacteria. Phthalate 4,5-cis-dihydrodiol dehydrogenase Involved in the phthalate degradation pathway in bacteria. Cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD(+) = 4,5-dihydroxyphthalate + NADH. 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline dehydrogenase Acts in the reverse direction to form part of the 3-methylquinoline degradation pathway in bacteria. 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline + NAD(+) = 5,6-dihydroxy-3-methyl-2-oxo-1,2-dihydroquinoline + NADH. Cis-dihydroethylcatechol dehydrogenase Cis-1,2-dihydro-3-ethylcatechol + NAD(+) = 3-ethylcatechol + NADH. Involved in the ethylbenzene degradation pathway in bacteria. Cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate dehydrogenase Cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate + NAD(P)(+) = 4-methylcatechol + NAD(P)H + CO(2). Involved in the p-xylene degradation pathway in bacteria. 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate dehydrogenase Involved in the o-xylene degradation pathway in bacteria. 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate + NAD(+) = 3-methylcatechol + NADH + CO(2). Zeatin reductase Dihydrozeatin + NADP(+) = zeatin + NADPH. Previously classified erroneously as EC 1.1.1.242. Meso-tartrate dehydrogenase Meso-tartrate + NAD(+) = dihydroxyfumarate + NADH. C-14 sterol reductase Sterol C14-reductase Delta(14)-sterol reductase 4,4-dimethyl-5-alpha-cholesta-8,24-dien-3-beta-ol + NADP(+) = 4,4-dimethyl-5-alpha-cholesta-8,14,24-trien-3-beta-ol + NADPH. http://purl.uniprot.org/mim/215140 Acts on a range of steroids with a 14(15)-double bond. Delta(24(24(1)))-sterol reductase C-24(28) sterol reductase Sterol Delta(24(28))-reductase Sterol Delta(24(28))-methylene reductase Ergosterol + NADP(+) = ergosta-5,7,22,24(24(1))-tetraen-3-beta-ol + NADPH. Acts on a range of steroids with a 24(24(1))-double bond. Delta(24)-sterol reductase Lanosterol Delta(24)-reductase 5-alpha-cholest-7-en-3-beta-ol + NADP(+) = 5-alpha-cholesta-7,24-dien-3-beta-ol + NADPH. Acts on a range of steroids with a 24(25)-double bond, including lanosterol, desmosterol and zymosterol. 1,2-dihydrovomilenine reductase 17-O-acetylnorajmaline + NADP(+) = 1,2-dihydrovomilenine + NADPH. Forms part of the ajmaline biosynthesis pathway. 2-alkenal reductase NAD(P)H-dependent alkenal/one oxidoreductase NADPH:2-alkenal alpha,beta-hydrogenase Exhibits high activities also for 2-alkenones such as but-3-en-2-one and pent-3-en-2-one. Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid. Highly specific for 4-hydroxy-non-2-enal and non-2-enal. Involved in the detoxification of alpha,beta-unsaturated aldehydes and ketones. 2-alkenals of shorter chain have lower affinities. n-alkanal + NAD(P)(+) = alk-2-enal + NAD(P)H. [4-vinyl]chlorophyllide a reductase 4VCR Divinyl chlorophyllide a 8-vinyl-reductase Chlorophyllide a + NADP(+) = divinyl chlorophyllide a + NADPH. Also reduces divinyl protochlorophyllide to protochlorophyllide in some species, providing an alternative pathway. Precorrin-2 dehydrogenase Precorrin-2 oxidase Catalyzes the second of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107) and the third step involves the chelation of ferrous iron to sirohydrochlorin to form siroheme (EC 4.99.1.4). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirC being responsible for the above reaction. Precorrin-2 + NAD(+) = sirohydrochlorin + NADH. ANR Anthocyanidin reductase Forms 2,3-cis-flavan-3-ols. Also, while the substrate preference of MtANR is cyanidin>pelargonidin>delphinidin, the reverse preference is found with AtANR. While the enzyme from the legume Medicago truncatula (MtANR) uses both NADPH and NADH as reductant, that from the crucifer Arabidopsis thaliana (AtANR) uses only NADPH. A flavan-3-ol + 2 NAD(P)(+) = an anthocyanidin + 2 NAD(P)H. The isomeric 2,3-trans-flavan-3-ols are formed from flavan-3,4-diols by EC 1.17.1.3. TyrAAT1 TyrAAT2 Pretyrosine dehydrogenase TyrA(a) Arogenate dehydrogenase (NADP(+)) Arogenic dehydrogenase The enzyme from Synechocystis sp. PCC 6803 and the isoform TyrAAT1 cannot use prephenate as a substrate, while the isoform TyrAAT2 can use it only very poorly. L-arogenate + NADP(+) = L-tyrosine + NADPH + CO(2). Unlike EC 1.3.1.43 and EC 1.3.1.79, this enzyme has a strict requirement for NADP(+). Arogenic dehydrogenase Cyclohexadienyl dehydrogenase Pretyrosine dehydrogenase Arogenate dehydrogenase (NAD(P)(+)) See also EC 1.3.1.12, EC 1.3.1.43 and EC 1.3.1.78. L-arogenate + NAD(P)(+) = L-tyrosine + NAD(P)H + CO(2). Enoyl coenzyme A reductase 2-enoyl-CoA reductase Acyl-CoA dehydrogenase (NADP(+)) The liver enzyme acts on enoyl-CoA derivatives of carbon chain length 4 to 16, with optimum activity on 2-hexenoyl-CoA. Acyl-CoA + NADP(+) = 2,3-dehydroacyl-CoA + NADPH. In Escherichia coli, cis-specific and trans-specific enzymes exist (cf. EC 1.3.1.37 and EC 1.3.1.38). NADH-specific enoyl-ACP reductase Enoyl-ACP reductase NADH-enoyl acyl carrier protein reductase Enoyl-[acyl-carrier-protein] reductase (NADH) Acyl-[acyl-carrier-protein] + NAD(+) = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH. Catalyzes the reduction of enoyl-acyl-[acyl-carrier-protein] derivatives of carbon chain length from 4 to 16. With a cytochrome as acceptor GLDHase L-galactono-gamma-lactone dehydrogenase Galactonolactone dehydrogenase L-galactonolactone dehydrogenase GLDase Very specific for its substrate L-galactono-1,4-lactone as D-galactono-gamma-lactone, D-gulono-gamma-lactone, L-gulono-gamma-lactone, D-erythronic-gamma-lactone, D-xylonic-gamma-lactone, L-mannono-gamma-lactone, D-galactonate, D-glucuronate and D-gluconate are not substrates. (2) L-ascorbate + 2 ferricytochrome c = L-dehydroascorbate + 2 ferrocytochrome c + 2 H(+). (1) L-galactono-1,4-lactone + 2 ferricytochrome c = L-ascorbate + 2 ferrocytochrome c + 2 H(+). FAD, NAD(+), NADP(+) and O(2) (cf. EC 1.3.3.12) cannot act as electron acceptor. Catalyzes the final step in the biosynthesis of L-ascorbic acid in higher plants and in nearly all higher animals with the exception of primates and some birds. With oxygen as acceptor Dihydoorotic acid dehydrogenase DHOdehase Dihydroorotate oxidase Dihydroorotate dehydrogenase FMN Ferricyanide can act as acceptor. (S)-dihydroorotate + O(2) = orotate + H(2)O(2). FAD L-tryptophan 2',3'-oxidase Tryptophan alpha,beta-oxidase L-tryptophan alpha,beta-dehydrogenase L-tryptophan + O(2) = alpha,beta-didehydrotryptophan + H(2)O(2). Heme The product of the reaction can hydrolyze spontaneously to form indolepyruvate. Also catalyzes the alpha,beta dehydrogenation of L-tryptophan side chains in peptides. The enzyme from Chromobacterium violaceum is specific for tryptophan derivatives possessing its carboxyl group free or as an amide or ester, and an unsubstituted indole ring. Pyrroloquinoline-quinone synthase So far only a single turnover of the enzyme has been observed, and the pyrroloquinoline quinone remains bound to it; it is not yet known what releases the product in the bacterium. 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinoline-2,4-dicarboxylate + 3 O(2) = 4,5-dioxo-3a,4,5,6,7,8,9,9b-octahydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + 2 H(2)O(2) + 2 H(2)O. L-galactonolactone oxidase L-xylono-1,4-lactone oxidase L-galactono-1,4-lactone + O(2) = L-ascorbate + H(2)O(2). Acts on the 1,4-lactones of L-galactonic, D-altronic, L-fuconic, D-arabinic and D-threonic acids. Not identical with EC 1.1.3.8 (cf. EC 1.3.2.3). FAD Coproporphyrinogenase Coproporphyrinogen oxidase Coprogen oxidase Coproporphyrinogen-III oxidase http://purl.uniprot.org/mim/121300 Coproporphyrinogen-III + O(2) + 2 H(+) = protoporphyrinogen-IX + 2 CO(2) + 2 H(2)O. Iron Protoporphyrinogen oxidase Protoporphyrinogenase Protoporphyrinogen-IX oxidase Also slowly oxidizes mesoporphyrinogen-IX. FAD Protoporphyrinogen-IX + 1.5 O(2) = protoporphyrin-IX + 3 H(2)O. http://purl.uniprot.org/mim/176200 Bilirubin oxidase 2 bilirubin + O(2) = 2 biliverdin + 2 H(2)O. Acyl-CoA oxidase Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + H(2)O(2). Acts on CoA derivatives of fatty acids with chain length from C(8) to C(18). http://purl.uniprot.org/mim/264470 FAD Dihydrouracil oxidase FMN 5,6-dihydrouracil + O(2) = uracil + H(2)O(2). Also oxidizes dihydrothymine to thymine. THB oxidase Tetrahydroberberine oxidase Flavoprotein (S)-tetrahydroberberine + 2 O(2) = berberine + 2 H(2)O(2). (R)-tetrahydroberberines are not oxidized. Secologanin synthase Loganin + NADPH + O(2) = secologanin + NADP(+) + 2 H(2)O. Heme-thiolate Secologanin is the precursor of the monoterpenoid indole alkaloids and ipecac alkaloids. With a quinone or related compound as acceptor Succinic dehydrogenase Succinate dehydrogenase (ubiquinone) FAD Iron-sulfur http://purl.uniprot.org/mim/256000 Succinate + ubiquinone = fumarate + ubiquinol. http://purl.uniprot.org/mim/171300 The complex, present in mitochondria, can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone. http://purl.uniprot.org/mim/252011 http://purl.uniprot.org/mim/115310 With an iron-sulfur protein as acceptor 6-hydroxynicotinate reductase 6-oxotetrahydro-nicotinate dehydrogenase HNA reductase 6-hydroxynicotinic reductase Other enzymes involved in this pathway are EC 1.17.5.1, EC 3.5.2.18, EC 1.1.1.291, EC 5.4.99.4, EC 5.3.3.6, EC 4.2.1.85 and EC 4.1.3.32. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. 6-oxo-1,4,5,6-tetrahydronicotinate + oxidized ferredoxin = 6-hydroxynicotinate + reduced ferredoxin. 15,16-dihydrobiliverdin:ferredoxin oxidoreductase Catalyzes the two-electron reduction of biliverdin IX-alpha at the C15 methine bridge. It has been proposed that this enzyme and EC 1.3.7.3 function as a dual enzyme complex in the conversion of biliverdin IX-alpha into phycoerythrobilin. 15,16-dihydrobiliverdin + oxidized ferredoxin = biliverdin IX-alpha + reduced ferredoxin. Phycoerythrobilin:ferredoxin oxidoreductase Catalyzes the two-electron reduction of the C2 and C3(1) diene system of 15,16-dihydrobiliverdin. It has been proposed that this enzyme and EC 1.3.7.2 function as a dual enzyme complex in the conversion of biliverdin IX-alpha into phycoerythrobilin. (3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin. Specific for 15,16-dihydrobiliverdin. Phytochromobilin:ferredoxin oxidoreductase Phytochromobilin synthase PFB synthase P-Phi-B synthase Can use 2Fe-2S ferredoxins from a number of sources as acceptor but not the 4Fe-4S ferredoxin from Clostridium pasteurianum. The isomerization of (3Z)-phytochromobilin to (3E)-phytochromobilin is thought to occur prior to covalent attachment to apophytochrome in the plant cell cytoplasm. Flavodoxins can be used instead of ferredoxin. Catalyzes the two-electron reduction of biliverdin IX-alpha. (3Z)-phytochromobilin + oxidized ferredoxin = biliverdin IX-alpha + reduced ferredoxin. Phycocyanobilin:ferredoxin oxidoreductase Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings). Reaction proceeds via an isolatable 2-electron intermediate, 18(1),18(2)-dihydrobiliverdin. Flavodoxins can be used instead of ferredoxin. The direct conversion of biliverdin IX-alpha (BV) to (3Z)-phycocyanobilin (PCB) in the cyanobacteria Synechocystis sp. PCC 6803, Anabaena sp. PCC7120 and Nostoc punctiforme is in contrast to the proposed pathways of PCB biosynthesis in the red alga Cyanidium caldarium, which involves (3Z)-phycoerythrobilin (PEB) as an intermediate and in the green alga Mesotaenium caldariorum, in which PCB is an isolable intermediate. (3Z)-phycocyanobilin + oxidized ferredoxin = biliverdin IX-alpha + reduced ferredoxin. With other acceptors Fumarate reductase Fumarate dehydrogenase Fumaric hydrogenase Succinic dehydrogenase Succinate dehydrogenase FAD Succinate + acceptor = fumarate + reduced acceptor. Isovaleryl-CoA dehydrogenase 3-methylbutanoyl-CoA + acceptor = 3-methylbut-2-enoyl-CoA + reduced acceptor. Forms with another flavoprotein ('electron-transferring flavoprotein') and EC 1.5.5.1 a system reducing ubiquinone and other acceptors. FAD http://purl.uniprot.org/mim/243500 Not identical with EC 1.3.99.2, EC 1.3.99.3 or EC 1.3.99.12. n-pentanoate can act as donor. Dihydroorotate dehydrogenase Iron Zinc (S)-dihydroorotate + acceptor = orotate + reduced acceptor. Oxygen can act as acceptor, but much more slowly than 2,6-dichloroindophenol or 1,10-phenanthroline. 2-methylacyl-CoA dehydrogenase Branched-chain acyl-CoA dehydrogenase FAD Also oxidizes 2-methylpropanoyl-CoA. Not identical with EC 1.3.99.2, EC 1.3.99.3, EC 1.3.99.10 or EC 1.3.99.13. 2-methylbutanoyl-CoA + acceptor = 2-methylbut-2-enoyl-CoA + reduced acceptor. Long-chain-acyl-CoA dehydrogenase http://purl.uniprot.org/mim/201460 Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor. FAD Forms with another flavoprotein ('electron-transferring flavoprotein') and EC 1.5.5.1 a system reducing ubiquinone and other acceptors. Not identical with EC 1.3.99.2, EC 1.3.99.3, EC 1.3.99.10 or EC 1.3.99.12. Cyclohexanone dehydrogenase 2,6-dichloroindophenol can act as acceptor. The corresponding ketones of cyclopentane and cycloheptane cannot act as donors. Cyclohexanone + acceptor = cyclohex-2-enone + reduced acceptor. Benzoyl-CoA reductase Benzoyl-CoA reductase (dearomatizing) Benzoyl-CoA + reduced acceptor + 2 ATP = cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2 ADP + 2 phosphate. Manganese or magnesium Reduced methyl viologen can act as electron donor. Inactive toward aromatic acids that are not CoA esters but will also catalyze the reaction: NH(3) + acceptor + 2 ADP + 2 phosphate + H(2)O = hydroxylamine + reduced acceptor + 2 ATP. In the presence of reduced acceptor, but in the absence of oxidizable substrate, the enzyme catalyzes the hydrolysis of ATP to ADP plus phosphate. Isoquinoline 1-oxidoreductase Electron acceptors include 1,2-benzoquinone, cytochrome c, ferricyanide, iodonitrotetrazolium chloride (INT), nitroblue tetrazolium (NBT), Meldola blue and phenazine methosulfate. The enzyme from Pseudomonas diminuta is specific toward N-containing N-heterocyclic substrates, including isoquinoline, isoquinolin-5-ol, phthalazine and quinazoline. Isoquinoline + acceptor + H(2)O = isoquinolin-1(2H)-one + reduced acceptor. Quinoline 2-oxidoreductase FAD In addition to quinoline, quinolin-2-ol, quinolin-7-ol, quinolin-8-ol, 3-, 4-and 8-methylquinolines and 8-chloroquinoline are substrates. Quinoline + acceptor + H(2)O = isoquinolin-1(2H)-one + reduced acceptor. Iron-sulfur Molybdenum Iodonitrotetrazolium chloride (INT) can act as an electron acceptor. Quinaldate 4-oxidoreductase Quinaldic acid 4-oxidoreductase Quinaldate + acceptor + H(2)O = kynurenate + reduced acceptor. 2,4,6-trinitrobenzene sulfonate acid, 1,4-benzoquinone, 1,2-naphthoquinone, nitroblue tetrazolium (NBT), thionine and menadione will serve as an electron acceptor for the former enzyme and ferricyanide for the latter; Meldola blue, iodonitrotetrazolium chloride (INT), phenazine methosulfate (PMS), 2,6-dichlorophenolindophenol (DCPIP) and cytochrome c will act as electron acceptors for both. The enzyme from Pseudomonas sp. AK2 also acts on quinoline-8-carboxylate, whereas that from Serratia marcescens 2CC-1 will oxidize nicotinate; quinaldate is a substrate for both of these enzymes. Quinoline-4-carboxylic acid 2-oxidoreductase Quinoline-4-carboxylate 2-oxidoreductase Quinaldic acid 4-oxidoreductase Quinoline-4-carboxylate + acceptor + H(2)O = 2-oxo-1,2-dihydroquinoline-4-carboxylate + reduced acceptor. Iodonitrotetrazolium chloride, thionine, menadione and 2,6-dichlorophenolindophenol can act as electron acceptors. Molybdopterin cytosine dinucleotide Iron-sulfur Quinoline, 4-methylquinoline and 4-chloroquinoline can also serve as substrates for the enzyme from Agrobacterium sp. 1B. Flavin Butyryl-CoA dehydrogenase Short-chain-acyl-CoA dehydrogenase Butyryl dehydrogenase Unsaturated acyl-CoA reductase Butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor. Forms with another flavoprotein ('electron-transferring flavoprotein') and EC 1.5.5.1 a system reducing ubiquinone and other acceptors. http://purl.uniprot.org/mim/201470 FAD 4-hydroxybenzoyl-CoA reductase 4-hydroxybenzoyl-CoA reductase (dehydroxylating) Flavin Involved in the anaerobic pathway of phenol metabolism in bacteria. Benzoyl-CoA + acceptor = 4-hydroxybenzoyl-CoA + reduced acceptor. A ferredoxin with two [4Fe-4S] clusters functions as the natural electron donor. Iron-sulfur Molybdenum (R)-benzylsuccinyl-CoA dehydrogenase Forms the third step in the anaerobic toluene metabolic pathway in Thauera aromatica. (R)-2-benzylsuccinyl-CoA + 2 electron-transferring flavoprotein = (E)-2-benzylidenesuccinyl-CoA + 2 reduced electron-transferring flavoprotein. Uses the ferricenium ion as the preferred artificial electron acceptor. FAD The enzyme is highly specific for (R)-benzylsuccinyl-CoA and is inhibited by (S)-benzylsuccinyl-CoA. Unlike other acyl-CoA dehydrogenases, this enzyme exhibits high substrate-and enantiomer specificity. Coproporphyrinogen III oxidase Coproporphyrinogen dehydrogenase Oxygen-independent coproporphyrinogen-III oxidase Radical SAM enzyme This conversion, -.CH-CH(2)-COO--> -CH=CH(2) + CO(2) + e(-) replaces the electron initially used. Occurs mainly in bacteria, whereas eukaryotes use the oxygen-dependent oxidase. Coproporphyrinogen-III + 2 S-adenosyl-L-methionine = protoporphyrinogen-IX + 2 CO(2) + 2 L-methionine + 2 5'-deoxyadenosine. Iron-sulfur The reaction starts by using an electron from the reduced form of the enzyme's [4Fe-4S] cluster to split AdoMet into methionine and the radical 5'-deoxyadenosin-5'-yl; this radical initiates attack on the 2-carboxyethyl groups, leading to their conversion into vinyl groups. Differs from EC 1.3.3.3 by using S-adenosyl-L-methionine (AdoMet) instead of oxygen as oxidant. Retinol saturase All-trans-13,14-dihydroretinol:acceptor 13,14-oxidoreductase RetSat All-trans-retinol 13,14-reductase (13,14)-all-trans-retinol saturase All-trans-13,14-dihydroretinol + acceptor = all-trans-retinol + reduced acceptor. May play a role in the metabolism of vitamin A. The reaction is only known to occur in the opposite direction to that given above, with the enzyme being specific for all-trans-retinol as substrate. Neither all-trans-retinoic acid nor 9-cis, 11-cis or 13-cis-retinol isomers are substrates. Acyl-CoA dehydrogenase Medium-chain acyl-CoA dehydrogenase Acyl dehydrogenase FAD http://purl.uniprot.org/mim/201450 Forms with another flavoprotein ('electron-transferring flavoprotein') and EC 1.5.5.1 a system reducing ubiquinone and other acceptors. Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor. 3-oxosteroid 1-dehydrogenase A 3-oxosteroid + acceptor = a 3-oxo-Delta(1)-steroid + reduced acceptor. Steroid 5-alpha-reductase 3-oxo-5-alpha-steroid 4-dehydrogenase http://purl.uniprot.org/mim/264600 A 3-oxo-5-alpha-steroid + acceptor = a 3-oxo-Delta(4)-steroid + reduced acceptor. Delta(4)-3-ketosteroid 5-beta-reductase 3-oxo-5-beta-steroid 4-dehydrogenase A 3-oxo-5-beta-steroid + acceptor = a 3-oxo-Delta(4)-steroid + reduced acceptor. Glutaryl-CoA dehydrogenase FAD http://purl.uniprot.org/mim/231670 Glutaryl-CoA + acceptor = crotonoyl-CoA + CO(2) + reduced acceptor. 2-furoyl-CoA dehydrogenase Furoyl-CoA hydroxylase 2-furoyl-CoA + H(2)O + acceptor = S-(5-hydroxy-2-furoyl)-CoA + reduced acceptor. Copper Methylene blue, nitro blue tetrazolium and a membrane fraction from Pseudomonas putida can act as acceptors. The actual oxidative step is probably dehydrogenation of a hydrated form -CHOH-CH(2)-to -C(OH)=CH-, which tautomerizes non-enzymically to -CO-CH(2)-, giving (5-oxo-4,5-dihydro-2-furoyl)-CoA. The oxygen atom of the -OH produced is derived from water, not O(2). Acting on the CH-NH(2) group of donors With NAD(+) or NADP(+) as acceptor Alanine dehydrogenase L-alanine + H(2)O + NAD(+) = pyruvate + NH(3) + NADH. Glycine dehydrogenase Glycine + H(2)O + NAD(+) = glyoxylate + NH(3) + NADH. L-erythro-3,5-diaminohexanoate dehydrogenase L-erythro-3,5-diaminohexanoate + H(2)O + NAD(+) = (S)-5-amino-3-oxohexanoate + NH(3) + NADH. 2,4-diaminopentanoate dehydrogenase Also acts, more slowly, on 2,5-diaminohexanoate forming 2-amino-5-oxohexanoate, which then cyclizes non-enzymically to 1-pyrroline-2-methyl-5-carboxylate. 2,4-diaminopentanoate + H(2)O + NAD(P)(+) = 2-amino-4-oxopentanoate + NH(3) + NAD(P)H. Glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP) Glutamate synthetase (NADP) Glutamate synthase (NADPH) L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing Glutamine-ketoglutaric aminotransferase NADPH-glutamate synthase NADPH-dependent glutamate synthase GOGAT L-glutamate synthase Glutamate (reduced nicotinamide adenine dinucleotide phosphate) synthase L-glutamate synthetase FMN 2 L-glutamate + NADP(+) = L-glutamine + 2-oxoglutarate + NADPH. Iron-sulfur FAD NADH-dependent glutamate synthase NADH-glutamate synthase L-glutamate synthase Glutamate synthase (NADH) L-glutamate synthetase FMN 2 L-glutamate + NAD(+) = L-glutamine + 2-oxoglutarate + NADH. Lysine dehydrogenase L-lysine + NAD(+) = 1,2-didehydropiperidine-2-carboxylate + NH(3) + NADH. Meso-diaminopimelate D-dehydrogenase Diaminopimelate dehydrogenase Meso-2,6-diaminoheptanedioate + H(2)O + NADP(+) = L-2-amino-6-oxoheptanedioate + NH(3) + NADPH. N-methylalanine dehydrogenase N-methyl-L-alanine + H(2)O + NADP(+) = pyruvate + methylamine + NADPH. Lysine 6-dehydrogenase LysDH L-lysine epsilon-dehydrogenase L-lysine 6-dehydrogenase L-lysine + NAD(+) = (S)-2,3,4,5-tetrahydropiperidine-2-carboxylate + NADH + NH(3). While the enzyme from Agrobacterium tumefaciens can use only NAD(+), that from the thermophilic bacterium Geobacillus stearothermophilus can also use NADP(+), but more slowly. Highly specific for L-lysine as substrate, although (S)-(beta-aminoethyl)-L-cysteine can act as a substrate, but more slowly. TrpDH L-Trp-dehydrogenase L-tryptophan dehydrogenase Tryptophan dehydrogenase Calcium L-tryptophan + NAD(P)(+) = (indol-3-yl)pyruvate + NH(3) + NAD(P)H. Glutamic dehydrogenase Glutamate dehydrogenase L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate + NH(3) + NADH. Phenylalanine dehydrogenase L-phenylalanine dehydrogenase PheDH L-phenylalanine + H(2)O + NAD(+) = phenylpyruvate + NH(3) + NADH. The enzymes from Bacillus badius and Sporosarcina ureae are highly specific for L-phenylalanine; that from Bacillus sphaericus also acts on L-tyrosine. Aspartate dehydrogenase NAD-dependent aspartate dehydrogenase NADH(2)-dependent aspartate dehydrogenase NADP(+)-dependent aspartate dehydrogenase Catalyzes the first step in NAD biosynthesis from aspartate. Strictly specific for L-aspartate as substrate. Has a higher affinity for NAD(+) than NADP(+). L-aspartate + H(2)O + NAD(P)(+) = oxaloacetate + NH(3) + NAD(P)H. Glutamic dehydrogenase Glutamate dehydrogenase (NAD(P)(+)) L-glutamate + H(2)O + NAD(P)(+) = 2-oxoglutarate + NH(3) + NAD(P)H. http://purl.uniprot.org/mim/606762 Glutamate dehydrogenase (NADP(+)) Glutamic dehydrogenase L-glutamate + H(2)O + NADP(+) = 2-oxoglutarate + NH(3) + NADPH. L-amino-acid dehydrogenase Acts on aliphatic amino acids. An L-amino acid + H(2)O + NAD(+) = a 2-oxo acid + NH(3) + NADH. L-serine:NAD oxidoreductase (deaminating) Serine dehydrogenase Serine 2-dehydrogenase L-serine + H(2)O + NAD(+) = 3-hydroxypyruvate + NH(3) + NADH. Valine dehydrogenase (NADP(+)) L-valine + H(2)O + NADP(+) = 3-methyl-2-oxobutanoate + NH(3) + NADPH. Leucine dehydrogenase LeuDH Also acts on isoleucine, valine, norvaline and norleucine. L-leucine + H(2)O + NAD(+) = 4-methyl-2-oxopentanoate + NH(3) + NADH. With a cytochrome as acceptor Glycine-cytochrome c reductase Glycine dehydrogenase (cytochrome) Glycine + H(2)O + 2 ferricytochrome c = glyoxylate + NH(3) + 2 ferrocytochrome c + 2 H(+). With oxygen as acceptor Aspartic oxidase D-aspartate oxidase FAD D-aspartate + H(2)O + O(2) = oxaloacetate + NH(3) + H(2)O(2). Putrescine oxidase 4-aminobutanal condenses non-enzymically to 1-pyrroline. FAD Putrescine + O(2) + H(2)O = 4-aminobutanal + NH(3) + H(2)O(2). L-glutamate oxidase FAD The enzyme from Azotobacter previously listed under this number, which did not produce H(2)O(2), was a crude cell-free extract which probably contained catalase. L-glutamate + O(2) + H(2)O = 2-oxoglutarate + NH(3) + H(2)O(2). Cyclohexylamine oxidase Cyclohexylamine + O(2) + H(2)O = cyclohexanone + NH(3) + H(2)O(2). Some other cyclic amines can act instead of cyclohexylamine, but not simple aliphatic and aromatic amides. FAD Lysyl oxidase Protein-lysine 6-oxidase Also acts on protein 5-hydroxylysine. These reactions play an important role for the development, elasticity and extensibility of connective tissue. Peptidyl-L-lysyl-peptide + O(2) + H(2)O = peptidyl-allysyl-peptide + NH(3) + H(2)O(2). Catalyzes the final known enzymic step required for collagen and elastin cross-linking in the biosynthesis of normal mature extracellular matrices. Also active on free amines, such as cadaverine or benzylamine. L-lysine oxidase L-lysine + O(2) + H(2)O = 6-amino-2-oxohexanoate + NH(3) + H(2)O(2). FAD Also acts, more slowly, on L-ornithine, L-phenylalanine, L-arginine and L-histidine. D-glutamate(D-aspartate) oxidase D-glutamate and D-aspartate are oxidized at the same rate. FAD Other D-monoaminodicarboxylates, and other D-and L-amino acids, are not oxidized. D-glutamate + H(2)O + O(2) = 2-oxoglutarate + NH(3) + H(2)O(2). L-aspartate oxidase A component of the bacterial quinolinate synthase system. L-aspartate + H(2)O + O(2) = oxaloacetate + NH(3) + H(2)O(2). FAD Glycine oxidase (1) Glycine + H(2)O + O(2) = glyoxylate + NH(3) + H(2)O(2). FAD (3) Sarcosine + H(2)O + O(2) = glyoxylate + methylamine + H(2)O(2). The enzyme from Bacillus subtilis is active with glycine, sarcosine, N-ethylglycine, D-alanine, D-alpha-aminobutyrate, D-proline, D-pipecolate and N-methyl-D-alanine. (2) D-alanine + H(2)O + O(2) = pyruvate + NH(3) + H(2)O(2). It differs from EC 1.4.3.3 due to its activity on sarcosine and D-pipecolate. (4) N-ethylglycine + H(2)O + O(2) = glyoxylate + ethylamine + H(2)O(2). L-amino-acid oxidase Ophio-amino-acid oxidase An L-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2). FAD Marinocine L-lysine-epsilon-oxidase Lod L-lysine 6-oxidase The amines cadaverine and putrescine are not substrates. L-lysine + O(2) + H(2)O = 2-aminoadipate 6-semialdehyde + H(2)O(2) + NH(3). Differs from EC 1.4.3.13 by using free L-lysine rather than the protein-bound form. Also acts on L-ornithine, D-lysine and 4-hydroxy-L-lysine, but more slowly. N(2)-acetyl-L-lysine is also a substrate, but N(6)-acetyl-L-lysine, which has an acetyl group at position 6, is not. D-amino-acid oxidase FAD Wide specificity for D-amino acids. Also acts on glycine. A D-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2). Tyraminase Amine oxidase Tyramine oxidase Amine oxidase (flavin-containing) Monoamine oxidase Adrenaline oxidase RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2). FAD Acts on primary amines, and usually also on secondary and tertiary amines. http://purl.uniprot.org/mim/300615 Pyridoxal 5'-phosphate synthase Pyridoxamine 5'-phosphate oxidase PMP oxidase Pyridoxamine phosphate oxidase Pyridoxamine-phosphate oxidase Pyridoxine (pyridoxamine) 5'-phosphate oxidase Pyridoxine (pyridoxamine)phosphate oxidase In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72, EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5. FMN (1) Pyridoxamine 5'-phosphate + H(2)O + O(2) = pyridoxal 5'-phosphate + NH(3) + H(2)O(2). http://purl.uniprot.org/mim/610090 (2) Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'-phosphate + H(2)O(2). DAO Histaminase Diamine oxidase Diamino oxhydrase Amine oxidase (copper-containing) Copper A group of enzymes including those oxidizing primary amines, diamines and histamine. Topaquinone One form of EC 1.3.1.15 from rat kidney also catalyzes this reaction. RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2). D-glutamate oxidase D-glutamic oxidase D-glutamate + H(2)O + O(2) = 2-oxoglutarate + NH(3) + H(2)O(2). Ethanolamine oxidase Cobalt Ethanolamine + H(2)O + O(2) = glycolaldehyde + NH(3) + H(2)O(2). With a disulfide as acceptor Glycine decarboxylase Glycine cleavage system P-protein Glycine-cleavage complex P-protein Glycine dehydrogenase (decarboxylating) The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. Pyridoxal-phosphate A component, with EC 2.1.2.10 and EC 1.8.1.4, of the glycine cleavage system, previously known as glycine synthase. http://purl.uniprot.org/mim/605899 Glycine + H-protein-lipoyllysine = H-protein-S-aminomethyldihydrolipoyllysine + CO(2). With an iron-sulfur protein as acceptor Glutamate synthase (ferredoxin) Ferredoxin-dependent glutamate synthase Flavoprotein 2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H(+). Iron-sulfur With other acceptors D-amino-acid dehydrogenase FAD A D-amino acid + H(2)O + acceptor = a 2-oxo acid + NH(3) + reduced acceptor. Acts to some extent on all D-amino acids except D-aspartate and D-glutamate. Taurine dehydrogenase Taurine + H(2)O + acceptor = sulfoacetaldehyde + NH(3) + reduced acceptor. Primary-amine dehydrogenase MADH Methylamine dehydrogenase Amine dehydrogenase RCH(2)NH(2) + H(2)O + acceptor = RCHO + NH(3) + reduced acceptor. Tryptophan tryptophylquinone (TTQ) Aromatic amine dehydrogenase Aralkylamine dehydrogenase Acts on aromatic amines and, more slowly, on some long-chain aliphatic amines, but not on methylamine or ethylamine (cf. EC 1.4.99.3). Phenazine methosulfate can act as acceptor. RCH(2)NH(2) + H(2)O + acceptor = RCHO + NH(3) + reduced acceptor. Glycine dehydrogenase (cyanide-forming) Hydrogen cyanide synthase HCN synthase The enzyme is membrane-bound, and the 2-electron acceptor is a component of the respiratory chain. The enzyme can act with various artificial electron acceptors, including phenazine methosulfate. Glycine + 2 A = HCN + CO(2) + 2 AH(2). FAD Acting on the CH-NH group of donors With NAD(+) or NADP(+) as acceptor Pyrroline-2-carboxylate reductase Reduces 1-pyrroline-2-carboxylate to L-proline and also 1,2-didehydropiperidine-2-carboxylate to L-pipecolate. L-proline + NAD(P)(+) = 1-pyrroline-2-carboxylate + NAD(P)H. Aminoadipic semialdehyde-glutamic reductase Aminoadipic semialdehyde-glutamate reductase Aminoadipate semialdehyde-glutamate reductase Saccharopine reductase Saccharopine dehydrogenase (NADP(+), L-glutamate-forming) N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP(+) + H(2)O = L-glutamate + L-2-aminoadipate 6-semialdehyde + NADPH. D-octopine synthase Octopine dehydrogenase ODH D-octopine dehydrogenase N(2)-(D-1-carboxyethyl)-L-arginine + NAD(+) + H(2)O = L-arginine + pyruvate + NADH. Also acts, in the reverse direction, on L-ornithine, L-lysine and L-histidine. 1-pyrroline-5-carboxylate dehydrogenase Oxidizes other 1-pyrrolines, e.g. 3-hydroxy-1-pyrroline-5-carboxylate forms 4-hydroxyglutamate. http://purl.uniprot.org/mim/239510 1-pyrroline-5-carboxylate + NAD(+) + H(2)O = L-glutamate + NADH. Methylenetetrahydrofolate dehydrogenase (NAD(+)) 5,10-methylenetetrahydrofolate + NAD(+) = 5,10-methenyltetrahydrofolate + NADH. D-lysopine dehydrogenase Lysopine dehydrogenase D-lysopine synthase In the reverse reaction, a number of L-amino acids can act instead of L-lysine, and 2-oxobutanoate and, to a lesser extent, glyoxylate can act instead of pyruvate. N(2)-(D-1-carboxyethyl)-L-lysine + NADP(+) + H(2)O = L-lysine + pyruvate + NADPH. Alanopine dehydrogenase 2,2'-iminodipropanoate + NAD(+) + H(2)O = L-alanine + pyruvate + NADH. In the reverse reaction, L-alanine can be replaced by L-cysteine, L-serine, or L-threonine; glycine acts very slowly (cf. EC 1.5.1.22). Ephedrine dehydrogenase Acts on a number of related compounds including (-)-sympatol, (+)-pseudoephedrine and (+)-norephedrine. The product immediately hydrolyzes to methylamine and 1-hydroxy-1-phenylpropan-2-one. (-)-ephedrine + NAD(+) = (R)-2-methylimino-1-phenylpropan-1-ol + NADH. Nopaline dehydrogenase D-nopaline dehydrogenase D-nopaline synthase NOS Nopaline synthase N(2)-(D-1,3-dicarboxypropyl)-L-arginine + NADP(+) + H(2)O = L-arginine + 2-oxoglutarate + NADPH. In the reverse direction, forms D-nopaline from L-arginine and D-ornaline from L-ornithine. P5CR Pyrroline-5-carboxylate reductase L-proline + NAD(P)(+) = 1-pyrroline-5-carboxylate + NAD(P)H. Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to L-hydroxyproline. 5,10-methylenetetrahydropteroylglutamate reductase 5-methyltetrahydrofolate:(acceptor) oxidoreductase Methylenetetrahydrofolic acid reductase 5-methyltetrahydrofolate:NAD(+) oxidoreductase Methylenetetrahydrofolate reductase (NADPH(2)) Methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide) reductase 5-methyltetrahydrofolate:NAD oxidoreductase 5,10-methylenetetrahydrofolate reductase 5,10-methylenetetrahydrofolic acid reductase Methylenetetrahydrofolate reductase (NADPH) 5,10-methylenetetrahydrofolate reductase (NADPH) Methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotide phosphate) reductase N(5,10)-methylenetetrahydrofolate reductase N(5),N(10)-methylenetetrahydrofolate reductase MTHFR 5,10-CH(2)-H(4)folate reductase 5-methyltetrahydrofolate:NADP(+) oxidoreductase 5,10-methylenetetrahydrofolate reductase (FADH(2)) Methylenetetrahydrofolate reductase Methylenetetrahydrofolate reductase (NAD(P)H) http://purl.uniprot.org/mim/236250 5-methyltetrahydrofolate + NAD(P)(+) = 5,10-methylenetetrahydrofolate + NAD(P)H. Menadione can also serve as an electron acceptor. FAD Delta(1)-piperideine-2-carboxylate reductase L-pipecolate + NADP(+) = Delta(1)-piperideine-2-carboxylate + NADPH. Strombine dehydrogenase N-(carboxymethyl)-D-alanine + NAD(+) + H(2)O = glycine + pyruvate + NADH. Catalyzes the reaction of EC 1.5.1.17, more slowly. Does not act on L-strombine. Tauropine dehydrogenase In the reverse reaction, alanine can act instead of taurine, more slowly, and 2-oxobutanoate and 2-oxopentanoate can act instead of pyruvate. Tauropine + NAD(+) + H(2)O = taurine + pyruvate + NADH. N(5)-(carboxyethyl)ornithine synthase N(5)-(L-1-carboxyethyl)-L-ornithine + NADP(+) + H(2)O = L-ornithine + pyruvate + NADPH. In the reverse direction L-lysine can act instead of L-ornithine, more slowly. Acts on the amino group (cf. EC 1.5.1.16). Ketimine reductase Thiomorpholine-carboxylate dehydrogenase In the reverse direction, a number of other cyclic unsaturated compounds can act as substrates, more slowly. The product is the cyclic imine of the 2-oxoacid corresponding to S-(2-aminoethyl)cysteine. Thiomorpholine 3-carboxylate + NAD(P)(+) = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H. Beta-alanopine dehydrogenase Beta-alanopine + NAD(+) + H(2)O = beta-alanine + pyruvate + NADH. 1,2-dehydroreticulinium reductase (NADPH) 1,2-dehydroreticulinium ion reductase (R)-reticuline + NADP(+) = 1,2-dehydroreticulinium + NADPH. The enzyme does not catalyze the reverse reaction to any significant extent under physiological conditions. Reduces the 1,2-dehydroreticulinium ion to (R)-reticuline, which is a direct precursor of morphinan alkaloids in the poppy plant. Opine dehydrogenase In the reverse direction, the enzyme acts also on neutral amino acids as an amino donor. Dehydrogenation forms an imine, which dissociates to the amino acid and pyruvate. In the forward direction, the enzyme from Arthrobacter sp. acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. The amino acceptors include 2-oxoacids such as pyruvate, oxaloacetate, glyoxylate and 2-oxobutyrate. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine. (2S)-2-((1-(R)-carboxyethyl)amino)pentanoate + NAD(+) + H(2)O = L-2-aminopentanoic acid + pyruvate + NADH. FMN reductase NAD(P)H:FMN oxidoreductase Flavine mononucleotide reductase NAD(P)H-dependent FMN reductase NAD(P)H:flavin oxidoreductase NAD(P)H(2) dehydrogenase (FMN) NAD(P)H-FMN reductase Riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide (phosphate)) reductase Riboflavin mononucleotide reductase NAD(P)H dehydrogenase (FMN) Flavin mononucleotide reductase Riboflavine mononucleotide reductase NAD(P)H(2):FMN oxidoreductase The enzyme from luminescent bacteria and the SsuE enzyme from Escherichia coli also reduce riboflavin and FAD, but more slowly. FMNH(2) + NAD(P)(+) = FMN + NAD(P)H. In E.coli, this enzyme, in conjunction with EC 1.14.14.5, forms a two-component alkanesulfonate monooxygenase, which allows for utilization of alkanesulfonates as sulfur sources under conditions of sulfate and cysteine starvation. Dihydrofolate reductase Tetrahydrofolate dehydrogenase The enzyme from animals and some micro-organisms also slowly reduces folate to 5,6,7,8-tetrahydrofolate. http://purl.uniprot.org/mim/126060 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH. NADPH-flavin reductase NADPH dehydrogenase (flavin) Riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide phosphate) reductase NADPH-dependent FMN reductase NADPH-FMN reductase Flavine mononucleotide reductase NADPH:flavin oxidoreductase NADPH:riboflavin oxidoreductase Riboflavin mononucleotide reductase Flavin mononucleotide reductase Riboflavine mononucleotide reductase NADPH-specific FMN reductase FMN reductase (NADPH) Flavin reductase Reduced riboflavin + NADP(+) = riboflavin + NADPH. NADH is oxidized more slowly than NADPH. The enzyme from Entamoeba histolytica reduces riboflavin and galactoflavin, and, more slowly, FMN and FAD. Berberine reductase (R)-canadine synthase (R)-canadine + 2 NADP(+) = berberine + 2 NADPH. Also acts on 7,8-dihydroberberine. Involved in alkaloid biosynthesis in Corydalis cava to give (R)-canadine with the opposite configuration to the precursor of berberine (see EC 1.3.3.8). Vomilenine reductase 1,2-dihydrovomilenine + NADP(+) = vomilenine + NADPH. Forms part of the ajmaline biosynthesis pathway. Pteridine reductase Pteridine reductase 1 PTR1 5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = biopterin + 2 NADPH. The enzyme is specific for NADPH; no activity has been detected with NADH. It also catalyzes the reduction of 7,8-dihydropterins and 7,8-dihydrofolate to their tetrahydro forms. It also differs from EC 1.5.1.3 in being specific for the B side of NADPH. In contrast to EC 1.5.1.3 and EC 1.5.1.34, pteridine reductase will not catalyze the reduction of the quinonoid form of dihydrobiopterin. The enzyme from Leishmania (both amastigote and promastigote forms) catalyzes the NADPH-dependent reduction of folate and a wide variety of unconjugated pterins, including biopterin, to their tetrahydro forms. NADPH-dihydropteridine reductase NAD(P)H(2):6,7-dihydropteridine oxidoreductase 6,7-dihydropteridine reductase Dihydropteridine reductase (NADH) Dihydropteridine reductase 6,7-dihydropteridine:NAD(P)H oxidoreductase Dihydropteridine (reduced nicotinamide adenine dinucleotide) reductase DHPR NADH-dihydropteridine reductase NADPH-specific dihydropteridine reductase Not identical with EC 1.5.1.3. The substrate is the quinonoid form of dihydropteridine. A 5,6,7,8-tetrahydropteridine + NAD(P)(+) = a 6,7-dihydropteridine + NAD(P)H. http://purl.uniprot.org/mim/261630 Transferred to EC 1.2.1.19 Methylenetetrahydrofolate dehydrogenase (NADP(+)) http://purl.uniprot.org/mim/172460 5,10-methylenetetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH. Formyltetrahydrofolate dehydrogenase 10-formyltetrahydrofolate dehydrogenase 10-formyltetrahydrofolate + NADP(+) + H(2)O = tetrahydrofolate + CO(2) + NADPH. Lysine-2-oxoglutarate reductase Saccharopine dehydrogenase (NAD(+), L-lysine-forming) N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD(+) + H(2)O = L-lysine + 2-oxoglutarate + NADH. Lysine-ketoglutarate reductase Lysine-2-oxoglutarate reductase Saccharopine dehydrogenase (NADP(+), L-lysine-forming) http://purl.uniprot.org/mim/268700 N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP(+) + H(2)O = L-lysine + 2-oxoglutarate + NADPH. Saccharopin dehydrogenase Saccharopine dehydrogenase (NAD(+), L-glutamate-forming) Aminoadipic semialdehyde synthase N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD(+) + H(2)O = L-glutamate + 2-aminoadipate 6-semialdehyde + NADH. http://purl.uniprot.org/mim/238700 With oxygen as acceptor Sarcosine oxidase The flavin is both covalently and non-covalently bound in a molar ratio of 1:1. Sarcosine + H(2)O + O(2) = glycine + formaldehyde + H(2)O(2). FAD Dimethylglycine oxidase Does not oxidize sarcosine. FAD N,N-dimethylglycine + H(2)O + O(2) = sarcosine + formaldehyde + H(2)O(2). Polyamine oxidase Also acts on N(1)-acetylspermidine and N(1),N(12)-diacetylspermine. FAD N(1)-acetylspermine + O(2) + H(2)O = N(1)-acetylspermidine + 3-aminopropanal + H(2)O(2). Iron Dihydrobenzophenanthridine oxidase Found in higher plants. Produces oxidized forms of the benzophenanthridine alkaloids. (1) Dihydrosanguinarine + O(2) = sanguinarine + H(2)O(2). (3) Dihydromacarpine + O(2) = macarpine + H(2)O(2). Copper (2) Dihydrochelirubine + O(2) = chelirubine + H(2)O(2). N-methyl-L-amino-acid oxidase Flavoprotein An N-methyl-L-amino acid + H(2)O + O(2) = an L-amino acid + formaldehyde + H(2)O(2). Epsilon-alkyllysinase N(6)-methyllysine oxidase N(6)-methyl-lysine oxidase Epsilon-N-methyllysine demethylase N(6)-methyl-L-lysine + H(2)O + O(2) = L-lysine + formaldehyde + H(2)O(2). (S)-6-hydroxynicotine oxidase (S)-6-hydroxynicotine + H(2)O + O(2) = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H(2)O(2). FAD (R)-6-hydroxynicotine oxidase FAD (R)-6-hydroxynicotine + H(2)O + O(2) = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H(2)O(2). L-pipecolate oxidase The product reacts with water to form 2-aminoadipate 6-semialdehyde, i.e. 2-amino-6-oxohexanoate. L-pipecolate + O(2) = 2,3,4,5-tetrahydropyridine-2-carboxylate + H(2)O(2). With a disulfide as acceptor Pyrimidodiazepine synthase Involved in the formation of the eye pigment drosopterin in Drosophila melanogaster. A pyrimidodiazepine + glutathione disulfide + H(2)O = 6-pyruvoyl-tetrahydropterin + 2 glutathione. In the reverse direction of reaction, the reduction of 6-pyruvoyl-tetrahydropterin is accompanied by the opening of the 6-membered pyrazine ring and the formation of the 7-membered diazepine ring. The pyrimidodiazepine involved is an acetyldihydro derivative. With a quinone or similar compound as acceptor Electron-transferring-flavoprotein dehydrogenase ETF-QO ETF-ubiquinone oxidoreductase Electron transfer flavoprotein-ubiquinone oxidoreductase ETF dehydrogenase Iron-sulfur Forms part of the mitochondrial electron-transfer system. http://purl.uniprot.org/mim/231680 Reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol. FAD With an iron-sulfur protein as acceptor 5,10-methylenetetrahydrofolate reductase Methylenetetrahydrofolate reductase (ferredoxin) The enzyme from Clostridium formicoaceticum catalyzes the reduction of methylene blue, menadione, benzyl viologen, rubredoxin or FAD with 5-methyltetrahydrofolate and the oxidation of reduced ferredoxin or FADH(2) with 5,10-methylenetetrahydrofolate. Flavoprotein 5-methyltetrahydrofolate + 2 oxidized ferredoxin = 5,10-methylenetetrahydrofolate + 2 reduced ferredoxin + 2 H(+). However, unlike EC 1.5.1.20, there is no activity with NAD(P)H. Iron-sulfur Zinc With a flavin as acceptor Dimethylamine dehydrogenase DMADh Dimethylamine + H(2)O + electron-transferring flavoprotein = methylamine + formaldehyde + reduced electron-transferring flavoprotein. FAD Iron-sulfur Trimethylamine dehydrogenase TMADh Phenazine methosulfate and 2,6-dichloroindophenol can act as electron acceptors. FMN Iron-sulfur A number of alkyl-substituted derivatives of trimethylamine can also act as electron donors. Trimethylamine + H(2)O + electron-transferring flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein. With other acceptors Sarcosine dehydrogenase http://purl.uniprot.org/mim/268900 Sarcosine + acceptor + H(2)O = glycine + formaldehyde + reduced acceptor. FMN 5,10-methylenetetrahydromethanopterin reductase N(5),N(10)-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase 5,10-methylenetetrahydromethanopterin cyclohydrolase Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase Methylene-H(4)MPT reductase N(5),N(10)-methylenetetrahydromethanopterin reductase 5-methyltetrahydromethanopterin + coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420. Catalyzes an intermediate step in methanogenesis from CO(2) and H(2) in archaea. Cytokinin dehydrogenase Cytokinin oxidase N(6)-dimethylallyladenine + acceptor + H(2)O = adenine + 3-methylbut-2-enal + reduced acceptor. FAD Although this activity was previously thought to be catalyzed by a hydrogen-peroxide-forming oxidase, this enzyme does not require oxygen for activity and does not form hydrogen peroxide. Converts zeatin and related cytokinins. Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is a dimethylallyl or other prenyl group. 2,6-dichloroindophenol, methylene blue, nitroblue tetrazolium, phenazine methosulfate and Cu(2+) in the presence of imidazole can act as acceptors. Dimethylglycine dehydrogenase N,N-dimethylglycine + acceptor + H(2)O = sarcosine + formaldehyde + reduced acceptor. FAD http://purl.uniprot.org/mim/605850 L-pipecolate dehydrogenase The product reacts with water to form 2-aminoadipate 6-semialdehyde, i.e. 2-amino-6-oxohexanoate. L-pipecolate + acceptor = 2,3,4,5-tetrahydropyridine-2-carboxylate + reduced acceptor. Nicotine dehydrogenase Nicotine + acceptor + H(2)O = (S)-6-hydroxynicotine + reduced acceptor. Acts on both (R)-and (S)-isomers. FMN Methylglutamate dehydrogenase N-methyl-L-glutamate + acceptor + H(2)O = L-glutamate + formaldehyde + reduced acceptor. A number of N-methyl-substituted amino acids can act as donors. 2,6-dichloroindophenol is the best acceptor. Spermidine dehydrogenase 4-aminobutanal condenses non-enzymically to 1-pyrroline. FAD Heme Ferricyanide, 2,6-dichloroindophenol and cytochrome c can act as acceptor. Spermidine + acceptor + H(2)O = 1,3-diaminopropane + 4-aminobutanal + reduced acceptor. Proline dehydrogenase L-proline + acceptor + H(2)O = (S)-1-pyrroline-5-carboxylate + reduced acceptor. http://purl.uniprot.org/mim/181500 FAD http://purl.uniprot.org/mim/239500 5,10-methylenetetrahydromethanopterin dehydrogenase N(5),N(10)-methylenetetrahydromethanopterin dehydrogenase Methylenetetrahydromethanopterin dehydrogenase Coenzyme F420 is a 7,8-didemethyl-8-hydroxy-5-deazariboflavin derivative; methanopterin is a pterin analog. The enzyme is involved in the formation of methane from CO(2) in Methanobacterium thermoautotrophicum. 5,10-methylenetetrahydromethanopterin + coenzyme F420 = 5,10-methenyltetrahydromethanopterin + reduced coenzyme F420. Acting on NADH or NADPH With NAD(+) or NADP(+) as acceptor Nicotinamide nucleotide transhydrogenase NAD(P)(+) transhydrogenase (B-specific) Pyridine nucleotide transhydrogenase NADPH + NAD(+) = NADP(+) + NADH. FAD B-specific with respect to both NAD(+) and NADP(+). Also acts with deamino coenzymes. NAD(P)(+) transhydrogenase (AB-specific) Pyridine nucleotide transhydrogenase Transhydrogenase The enzyme from heart mitochondria is A-specific with respect to NAD(+) and B-specific with respect to NADP(+) (cf. EC 1.6.1.1.). NADPH + NAD(+) = NADP(+) + NADH. With a heme protein as acceptor Cytochrome-b5 reductase FAD NADH + 2 ferricytochrome b5 = NAD(+) + H(+) + 2 ferrocytochrome b5. http://purl.uniprot.org/mim/250800 CPR TPNH(2) cytochrome c reductase NADPH:P450 reductase Aldehyde reductase (NADPH-dependent) Reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase NADPH--cytochrome P450 oxidoreductase NADPH:ferrihemoprotein oxidoreductase NADPH--hemoprotein reductase TPNH-cytochrome c reductase NADPH--cytochrome c reductase NADPH--cytochrome c oxidoreductase Ferrihemoprotein P-450 reductase NADPH--cytochrome P450 reductase NADP--cytochrome c reductase NADPH--ferrihemoprotein reductase Reductase, cytochrome c (reduced nicotinamide adenine dinucleotide phosphate) NADPH--ferricytochrome c oxidoreductase Dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c reductase NADP--cytochrome reductase NADPH-dependent cytochrome c reductase Cytochrome P450 reductase FAD-cytochrome c reductase Cytochrome c reductase (reduced nicotinamide adenine dinucleotide phosphate, NADPH, NADPH-dependent) The enzyme catalyzes the reduction of the heme-thiolate-dependent monooxygenases, such as EC 1.14.14.1, and reduction of EC 1.14.99.3. The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction. FMN NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein. It also reduces cytochrome b5 and cytochrome c. It is part of the microsomal hydroxylating system. http://purl.uniprot.org/mim/207410 http://purl.uniprot.org/mim/201750 FAD NADPH--cytochrome-c2 reductase NADPH + 2 ferricytochrome c2 = NADP(+) + H(+) + 2 ferrocytochrome c2. FAD Leghemoglobin reductase NAD(P)H + 2 ferrileghemoglobin = NAD(P)(+) + 2 ferroleghemoglobin. With a oxygen as acceptor Thyroid oxidase 2 THOX2 Dual oxidase ThOX Thyroid oxidase Thyroid NADPH oxidase NAD(P)H oxidase NAD(P)H + O(2) = NAD(P)(+) + H(2)O(2). http://purl.uniprot.org/mim/607200 FAD Heme Calcium This flavoprotein is expressed at the apical membrane of thyrocytes, and provides H(2)O(2) for the thyroid peroxidase-catalyzed biosynthesis of thyroid hormones. The electron bridge within the enzyme contains one molecule of FAD and probably two heme groups. When calcium is present, this transmembrane glycoprotein generates H(2)O(2) by transfering electrons from intracellular NAD(P)H to extracellular molecular oxygen. With a quinone or similar compound as acceptor DT-diaphorase Reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase Flavoprotein NAD(P)H-quinone reductase p-benzoquinone reductase Naphthoquinone reductase Phylloquinone reductase NADH-menadione reductase Quinone reductase Reduced NAD(P)H dehydrogenase Viologen accepting pyridine nucleotide oxidoreductase Azoreductase Vitamin K reductase NAD(P)H-quinone oxidoreductase Dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone) NAD(P)H-quinone dehydrogenase NAD(P)H: menadione oxidoreductase Vitamin-K reductase Menadione reductase Diaphorase NAD(P)H(2) dehydrogenase (quinone) Menadione oxidoreductase NAD(P)H:(quinone-acceptor)oxidoreductase NAD(P)H menadione reductase NAD(P)H dehydrogenase (quinone) NAD(P)H dehydrogenase FAD The enzyme catalyzes a two-electron reduction and has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone. The animal, but not the plant, form of the enzyme is inhibited by dicoumarol. NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone. NADH-Q6 oxidoreductase Reduced nicotinamide adenine dinucleotide-coenzyme Q reductase Coenzyme Q reductase Mitochondrial electron transport complex 1 Type 1 dehydrogenase NADH-CoQ oxidoreductase NADH-ubiquinone-1 reductase Complex 1 dehydrogenase Complex I (mitochondrial electron transport) Complex I (electron transport chain) NADH coenzyme Q1 reductase NADH-ubiquinone oxidoreductase Electron transfer complex I DPNH-ubiquinone reductase NADH-ubiquinone reductase Mitochondrial electron transport complex I Ubiquinone reductase NADH:ubiquinone oxidoreductase complex NADH-CoQ reductase Complex I (NADH:Q1 oxidoreductase) NADH-coenzyme Q oxidoreductase NADH-coenzyme Q reductase Dihydronicotinamide adenine dinucleotide-coenzyme Q reductase NADH dehydrogenase (ubiquinone) DPNH-coenzyme Q reductase http://purl.uniprot.org/mim/256000 The complex, present in mitochondria, can be degraded to form EC 1.6.99.3. http://purl.uniprot.org/mim/502500 http://purl.uniprot.org/mim/535000 http://purl.uniprot.org/mim/540000 FAD http://purl.uniprot.org/mim/252010 http://purl.uniprot.org/mim/500001 NADH + ubiquinone = NAD(+) + ubiquinol. Iron-sulfur Monodehydroascorbate reductase (NADH) NADH + 2 monodehydroascorbate = NAD(+) + 2 ascorbate. NADPH:quinone reductase Zeta-crystallin Quinone oxidoreductase Zinc Specific for NADPH. NADPH + quinone = NADP(+) + semiquinone. Catalyzes the one-electron reduction of certain quinones; orthoquinones are the best substrates. Abundant in the lens of the eye of some mammalian species. Dicoumarol (cf. EC 1.6.5.2) and nitrofurantoin are competitive inhibitors with respect to the quinone substrate. p-benzoquinone reductase (NADPH) Involved in the 4-nitrophenol degradation pathway in bacteria. NADPH + p-benzoquinone = NADP(+) + hydroquinone. 2-hydroxy-1,4-benzoquinone reductase Hydroxybenzoquinone reductase The enzyme differs in substrate speificity from other quinone reductases. The enzyme in Burkholderia cepacia is inducible by 2,4,5-trichlorophenoxyacetate. FMN 2-hydroxy-1,4-benzoquinone + NADH = 1,2,4-trihydroxybenzene + NAD(+). With a nitrogenous group as acceptor Trimethylamine-N-oxide reductase Trimethylamine oxidase NADH + trimethylamine N-oxide = NAD(+) + trimethylamine + H(2)O. With other acceptors NADPH dehydrogenase NADPH diaphorase NADPH + acceptor = NADP(+) + reduced acceptor. FMN or FAD FMN in yeasts; FAD in plants. NADH:cytochrome c oxidoreductase Dihydrocodehydrogenase I dehydrogenase NADH diaphorase NADH dehydrogenase NADH oxidoreductase Reduced diphosphopyridine nucleotide diaphorase Dihydronicotinamide adenine dinucleotide dehydrogenase Diphosphopyrinase NADH-menadione oxidoreductase NADH hydrogenase Diaphorase Cytochrome c reductase Type I dehydrogenase Type 1 dehydrogenase DPNH diaphorase Beta-NADH dehydrogenase dinucleotide Flavoprotein Iron-sulfur Under normal conditions, two protons are extruded from the cytoplasm or the intramitochondrial or stromal compartment. NADH + acceptor = NAD(+) + reduced acceptor. Present in a mitochondrial complex as EC 1.6.5.3. After preparations have been subjected to certain treatments cytochrome c may act as acceptor. NADH dehydrogenase (quinone) Inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. NADH + acceptor = NAD(+) + reduced acceptor. Menaquinone or other quinones can act as acceptor. NADPH dehydrogenase (quinone) NADPH + acceptor = NADP(+) + reduced acceptor. Menaquinone can act as acceptor. Flavoprotein Inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol. Acting on other nitrogenous compounds as donors With NAD(+) or NADP(+) as acceptor Nitrate reductase (NADH(2)) Assimilatory nitrate reductase NADH-nitrate reductase Nitrate reductase (NADH) NADH-dependent nitrate reductase Assimilatory NADH:nitrate reductase NADH:nitrate oxidoreductase Heme Molybdenum Nitrite + NAD(+) + H(2)O = nitrate + NADH. FAD or FMN Ammonium dehydrogenase Hydroxylamine reductase (NADH) NADH:hydroxylamine oxidoreductase NADH-hydroxylamine reductase N-hydroxy amine reductase Hydroxylamine reductase NH(3) + NAD(+) + H(2)O = hydroxylamine + NADH. Also acts on some hydroxamates. 4-(dimethylamino)phenylazoxybenzene reductase Dimethylaminoazobenzene N-oxide reductase N,N-dimethyl-p-aminoazobenzene oxide reductase NADPH:4-(dimethylamino)phenylazoxybenzene oxidoreductase NADPH-dependent DMAB N-oxide reductase 4-(dimethylamino)phenylazobenzene + NADP(+) = 4-(dimethylamino)phenylazoxybenzene + NADPH. N-hydroxy-2-acetylaminofluorene reductase N-hydroxy-2-acetamidofluorene reductase NAD(P)H:N-hydroxy-2-acetamidofluorene N-oxidoreductase 2-acetamidofluorene + NAD(P)(+) + H(2)O = N-hydroxy-2-acetamidofluorene + NAD(P)H. Also acts, more slowly, on N-hydroxy-4-acetamidobiphenyl. PreQ(1) synthase 7-cyano-7-deazaguanine reductase PreQ(0) oxidoreductase PreQ(0) reductase Queosine is found in the wobble position of tRNA(GUN) in eukaryotes and bacteria and is thought to be involved in translational modulation. This enzyme catalyzes one of the early steps in the synthesis of queosine (Q-tRNA), and is followed by the action of EC 2.4.2.29. The reaction occurs in the reverse direction. 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-carbaguanine + 2 NADPH. NAD(P)H bispecific nitrate reductase Assimilatory nitrate reductase NAD(P)H-nitrate reductase Nitrate reductase NAD(P)H Nitrate reductase (reduced nicotinamide adenine dinucleotide (phosphate)) NAD(P)H:nitrate oxidoreductase Assimilatory NAD(P)H-nitrate reductase Nitrate reductase (NAD(P)H) FAD or FMN Molybdenum Heme Nitrite + NAD(P)(+) + H(2)O = nitrate + NAD(P)H. Nitrate reductase (NADPH) Assimilatory NADPH-nitrate reductase Nitrate reductase (NADPH(2)) NADPH:nitrate reductase NADPH:nitrate oxidoreductase NADPH-nitrate reductase Assimilatory nitrate reductase Assimilatory reduced nicotinamide adenine dinucleotide phosphate-nitrate reductase Triphosphopyridine nucleotide-nitrate reductase FAD Nitrite + NADP(+) + H(2)O = nitrate + NADPH. Iron-sulfur Molybdenum Heme Nitrite reductase (NAD(P)H) Nitrite reductase (reduced nicotinamide adenine dinucleotide (phosphate)) Assimilatory nitrite reductase NADH-nitrite oxidoreductase NADPH-nitrite reductase NAD(P)H:nitrite oxidoreductase Iron FAD Iron-sulfur Ammonium hydroxide + 3 NAD(P)(+) + H(2)O = nitrite + 3 NAD(P)H. Siroheme NADH:hyponitrite oxidoreductase Hyponitrite reductase Metal ions 2 hydroxylamine + 2 NAD(+) = hyponitrous acid + 2 NADH. p-aminoazobenzene reductase Orange II azoreductase Dimethylaminobenzene reductase N,N-dimethyl-4-phenylazoaniline azoreductase Orange I azoreductase Dibromopropylaminophenylazobenzoic azoreductase Azo reductase NADPH:4-(dimethylamino)azobenzene oxidoreductase Nicotinamide adenine dinucleotide (phosphate) azoreductase NADPH-dependent azoreductase Methyl red azoreductase NAD(P)H:1-(4'-sulfophenylazo)-2-naphthol oxidoreductase New coccine (NC)-reductase p-dimethylaminoazobenzene azoreductase Azo-dye reductase Azoreductase Azobenzene reductase NC-reductase N,N-dimethyl-1,4-phenylenediamine + aniline + NADP(+) = 4-(dimethylamino)azobenzene + NADPH. Guanosine 5'-monophosphate oxidoreductase Guanosine monophosphate reductase Guanosine 5'-monophosphate reductase Guanosine 5'-phosphate reductase GMP reductase NADPH:GMP oxidoreductase (deaminating) NADPH:guanosine-5'-phosphate oxidoreductase (deaminating) Guanylate reductase Inosine 5'-phosphate + NH(3) + NADP(+) = guanosine 5'-phosphate + NADPH. NAD(P)H:4-nitroquinoline-N-oxide oxidoreductase 4NQO reductase 4-nitroquinoline 1-oxide reductase Nitroquinoline-N-oxide reductase 4-(hydroxyamino)quinoline N-oxide + 2 NAD(P)(+) + H(2)O = 4-nitroquinoline N-oxide + 2 NAD(P)H. With a cytochrome as acceptor Hydroxylamine (acceptor) reductase Cytochrome cd1 Nitrite reductase (cytochrome) Nitrite reductase cd-cytochrome nitrite reductase Methyl viologen-nitrite reductase Nitrite reductase (NO-forming) Cytochrome cd Nitrite reductase (cytochrome; NO-forming) Cytochrome c-551:O(2), NO(2)(+) oxidoreductase Pseudomonas cytochrome oxidase One type comprises proteins containing multiple copper centers, the other a heme protein, cytochrome cd1. FAD Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+). Cytochrome cd1 also has oxidase and hydroxylamine reductase activities. The reaction is catalyzed by two types of enzymes, found in the perimplasm of denitrifying bacteria. Acceptors include c-type cytochromes such as cytochrome c-550 or cytochrome c-551 from Paracoccus denitrificans or Pseudomonas aeruginosa, and small blue copper proteins such as azurin and pseudoazurin. May also catalyze the reaction of EC 1.7.99.1 since this is a well-known activity of cytochrome cd1. Copper or iron Cytochrome c nitrite reductase Cytochrome c552 Multiheme nitrite reductase Nitrite reductase (cytochrome; ammonia-forming) Heme The enzyme also reduces nitric oxide and hydroxylamine to ammonia, and sulfite to sulfide. NH(3) + 2 H(2)O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H(+). Calcium TMAO reductase Trimethylamine-N-oxide reductase (cytochrome c) TOR The cytochrome c involved in photosynthetic bacteria is a pentaheme protein. Trimethylamine + 2 (ferricytochrome c)-subunit + H(2)O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H(+). The reductant is a membrane-bound multiheme cytochrome c. Also reduces dimethyl sulfoxide to dimethyl sulfide. Bis(molybdopterin guanine dinucleotide)molybdenum cofactor With oxygen as acceptor NAO Nitroalkane oxidase Nitroethane oxidase Nitroethane reductase A nitroalkane + H(2)O + O(2) = an aldehyde + nitrite + H(2)O(2). While nitroethane may be the physiological substrate, the enzyme also acts on several other nitroalkanes, including 1-nitropropane, 2-nitropropane, 1-nitrobutane, 1-nitropentane, 1-nitrohexane, nitrocyclohexane and some nitroalkanols. Differs from EC 1.13.11.32 in that the preferred substrates are neutral nitroalkanes rather than anionic nitronates. FAD Acetylindoxyl oxidase N-acetylindoxyl + O(2) = N-acetylisatin + H(2)O. Uric acid oxidase Urate oxidase Uricase II Uricase The 5-hydroxyisourate formed decomposes spontaneously to form allantoin and CO(2), although there is an enzyme-catalyzed pathway in which EC 3.5.2.17 catalyzes the first step. Was previously thought to be a copper protein, but it is now known that the enzymes from soybean (Glycine max), the mold Aspergillus flavus and Bacillus subtilis contains no copper nor any other transition-metal ion. Urate + O(2) + H(2)O = 5-hydroxyisourate + H(2)O(2). Hydroxylamine oxidase Heme Hydroxylamine + O(2) = nitrite + H(2)O. Hemoprotein with 7 c-type hemes and one P-460-type heme per subunit. 3-aci-nitropropanoate oxidase 3-aci-nitropropanoate + O(2) = 3-oxopropanoate + nitrite + H(2)O(2). FMN The primary products of the enzymatic reaction are probably the nitropropanoate free radical and superoxide. Also acts, more slowly, on 4-aci-nitrobutanoate. With an iron-sulfur protein as acceptor Ferredoxin--nitrite reductase Iron-sulfur Siroheme NH(3) + 2 H(2)O + 6 oxidized ferredoxin = nitrite + 6 reduced ferredoxin + 7 H(+). Assimilatory nitrate reductase Ferredoxin--nitrate reductase Iron-sulfur Nitrite + H(2)O + 2 oxidized ferredoxin = nitrate + 2 reduced ferredoxin + 2 H(+). Molybdenum With other acceptors Hydroxylamine reductase Hydroxylamine (acceptor) reductase May be identical to EC 1.7.2.1. Reduced pyocyanine, methylene blue and flavins act as donors for the reduction of hydroxylamine. NH(3) + H(2)O + acceptor = hydroxylamine + reduced acceptor. Flavoprotein Nitrate reductase Respiratory nitrate reductase Nitrite + acceptor = nitrate + reduced acceptor. Reduced benzyl viologen and other dyes bring about the reduction of nitrate. The Pseudomonas enzyme is a cytochrome, but the enzyme from Micrococcus halodenitrificans is an iron protein containing molybdenum. Nitrous-oxide reductase Copper Reduced viologens or methylene blue act as donors for the reduction of nitrous oxide. N(2) + H(2)O + acceptor = N(2)O + reduced acceptor. Nitric-oxide reductase Nitrous oxide + acceptor + H(2)O = 2 nitric oxide + reduced acceptor. Phenazine methosulfate can act as acceptor. A heterodimer of cytochromes b and c. Hydroxylamine oxidoreductase (1) Hydroxylamine + NH(3) = hydrazine + H(2)O. Ferricyanide, phenazine methosulfate and methylthiazolyltetrazolium bromide can act as acceptors in this 4-electron transfer reaction. The enzyme from anammox bacteria is inhibited by phosphate, oxygen and high nitrite concentrations and is also capable of reducing NO to N(2)O. (2) Hydrazine + acceptor = N(2) + reduced acceptor. Acting on a sulfur group of donors With NAD(+) or NADP(+) as acceptor CoA-glutathione reductase Coenzyme A glutathione disulfide reductase NADPH:CoA-glutathione oxidoreductase CoA-glutathione reductase (NADPH) Coenzyme A disulfide-glutathione reductase NADPH-dependent coenzyme A-SS-glutathione reductase Flavoprotein The substrate is a mixed disulfide. CoA + glutathione + NADP(+) = CoA-glutathione + NADPH. May be identical to EC 1.8.1.9. Asparagusic dehydrogenase NADH:asparagusate oxidoreductase Asparagusate reductase (NADH) Asparagusate reductase Asparagusate dehydrogenase Also acts on lipoate. 3-mercapto-2-mercaptomethylpropanoate + NAD(+) = asparagusate + NADH. Trypanothione reductase NADPH:trypanothione oxidoreductase N(1),N(8)-bis(glutathionyl)spermidine reductase Trypanothione-disulfide reductase Trypanothione + NADP(+) = trypanothione disulfide + NADPH. The activity is dependent on a redox-active cystine at the active center (cf. EC 1.8.1.7). FAD Trypanothione disulfide is the oxidized form of N(1),N(8)-bis(glutathionyl)-spermidine from the insect-parasitic trypanosomatid Crithidia fasciculata. Bis-gamma-glutamylcystine reductase NADPH:bis-gamma-glutamylcysteine oxidoreductase Bis-gamma-glutamylcystine reductase (NADPH) Highly specific. 2 gamma-glutamylcysteine + NADP(+) = bis-gamma-glutamylcystine + NADPH. Not identical with EC 1.8.1.7 or EC 1.8.1.14. CoADR Coenzyme A disulfide reductase CoA-disulfide reductase CoA-disulfide reductase (NAD(P)H) NADH:CoA-disulfide oxidoreductase FAD Not identical with EC 1.8.1.6, EC 1.8.1.7, or EC 1.8.1.13. 2 CoA + NAD(P)(+) = CoA-disulfide + NAD(P)H. While the enzyme from Staphylococcus aureus has a strong preference for NADPH, that from the thermophilic archaea Pyrococcus horikoshii can use both NADH and NADPH efficiently. Mycothione reductase Mycothiol-disulfide reductase No activity with glutathione, trypanothione or coenzyme A as substrate. 2 mycothiol + NAD(P)(+) = mycothione + NAD(P)H. FAD Sulfite reductase (NADPH) FMN Heme FAD H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH. Hypotaurine dehydrogenase Molybdenum Heme Hypotaurine + H(2)O + NAD(+) = taurine + NADH. Diaphorase L-protein Lipoamide reductase (NADH) Dehydrolipoate dehydrogenase Lipoic acid dehydrogenase Dihydrothioctic dehydrogenase Dihydrolipoic dehydrogenase E3 component of alpha-ketoacid dehydrogenase complexes LDP-Glc Lipoyl dehydrogenase Lipoamide reductase Lipoamide oxidoreductase (NADH) Lipoamide dehydrogenase (NADH) LDP-Val Lipoate dehydrogenase Glycine-cleavage system L-protein Dihydrolipoyl dehydrogenase Dihydrolipoamide dehydrogenase A component of the multienzyme 2-oxo-acid dehydrogenase complexes. Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH. http://purl.uniprot.org/mim/248600 It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine. Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. FAD In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups. It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. 2-KPCC NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase 2-oxopropyl-CoM reductase (carboxylating) NADPH:2-(2-ketopropylthio)ethanesulfonate oxidoreductase/carboxylase Also acts on thioethers longer in chain length on the oxo side, e.g. 2-oxobutyl-CoM, but this portion must be attached to CoM (2-mercaptoethanesulfonate); no CoM analogs will substitute. 2-mercaptoethanesulfonate + acetoacetate + NADP(+) = 2-(2-oxopropylthio)ethanesulfonate + CO(2) + NADPH. Forms component II of a four-component enzyme system (comprising EC 4.4.1.23 (component I), EC 1.8.1.5 (component II), EC 1.1.1.268 (component III) and EC 1.1.1.269 (component IV)) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2. Cystine reductase NADH:L-cystine oxidoreductase NADH-dependent cystine reductase Cystine reductase (NADH) 2 L-cysteine + NAD(+) = L-cystine + NADH. GSH reductase Glutathione-disulfide reductase NADPH:oxidized-glutathione oxidoreductase Glutathione reductase NADPH-GSSG reductase NADPH-glutathione reductase GSSG reductase Glutathione reductase (NADPH) Glutathione S-reductase Activity is dependent on a redox-active disulfide in each of the active centers. http://purl.uniprot.org/mim/138300 2 glutathione + NADP(+) = glutathione disulfide + NADPH. FAD Protein-disulfide reductase Protein disulfide reductase Disulfide reductase NAD(P)H:protein-disulfide oxidoreductase Insulin-glutathione transhydrogenase Protein dithiol + NAD(P)(+) = protein disulfide + NAD(P)H. NADPH--thioredoxin reductase Thioredoxin reductase (NADPH) NADPH:oxidized thioredoxin oxidoreductase Thioredoxin-disulfide reductase NADP--thioredoxin reductase May be identical to EC 1.8.1.10. Thioredoxin + NADP(+) = thioredoxin disulfide + NADPH. With a cytochrome as acceptor Sulfite dehydrogenase Associated with cytochrome c-551. Sulfite + 2 ferricytochrome c + H(2)O = sulfate + 2 ferrocytochrome c + 2 H(+). Thiosulfate dehydrogenase Tetrathionate synthase 2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2 ferrocytochrome c. With oxygen as acceptor Sulfite oxidase Heme http://purl.uniprot.org/mim/272300 Sulfite + O(2) + H(2)O = sulfate + H(2)O(2). Molybdenum Thiol oxidase Sulfhydryl oxidase 4 R'C(R)SH + O(2) = 2 R'C(R)S-S(R)CR' + 2 H(2)O. The enzyme is not specific for R'. R may be =S or =O, or a variety of other groups. Glutathione oxidase Also acts, more slowly, on L-cysteine and several other thiols. FAD 2 glutathione + O(2) = glutathione disulfide + H(2)O(2). Methanethiol oxidase Methylmercaptan oxidase Methanethiol + O(2) + H(2)O = formaldehyde + H(2)S + H(2)O(2). Prenylcysteine lyase Prenylcysteine oxidase An S-prenyl-L-cysteine + O(2) + H(2)O = a prenal + L-cysteine + H(2)O(2). FAD Originally thought to be a simple lyase, EC 4.4.1.18. May represent the final step in the degradation of prenylated proteins in mammalian tissues. N-acetyl-prenylcysteine and prenylcysteinyl peptides are not substrates. Cleaves the thioether bond of S-prenyl-L-cysteines, such as S-farnesylcysteine and S-geranylgeranylcysteine. With a disulfide as acceptor Glutathione--homocystine transhydrogenase 2 glutathione + homocystine = glutathione disulfide + 2 homocysteine. The reactions catalyzed by this enzyme and by others in this subclass may be similar to those catalyzed by EC 2.5.1.18. Adenylyl-sulfate reductase (thioredoxin) Thioredoxin-dependent 5'-adenylylsulfate reductase AMP + sulfite + thioredoxin disulfide = 5'-adenylyl sulfate + thioredoxin. Uses thioredoxin as electron donor, not glutathione or other donors, distinguishing it from EC 1.8.4.9 and EC 1.8.99.2. Uses adenylyl sulfate, not phosphoadenylyl sulfate, distinguishing this enzyme from EC 1.8.4.8. Methionine sulfoxide reductase Peptide methionine sulfoxide reductase Methionine S-oxide reductase (S-form oxidizing) Peptide-methionine-(S)-S-oxide reductase Methionine S-oxide reductase Peptide Met(O) reductase Methionine sulfoxide reductase A Methionine sulphoxide reductase A (1) Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. The reaction proceeds via a sulfenic-acid intermediate. On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly. Plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. (2) L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S-oxide + thioredoxin. Exhibits high specificity for the reduction of the S-form of L-methionine S-oxide, acting faster on the residue in a peptide than on the free amino acid. The reaction occurs in the reverse direction to that shown above. Methionine sulfoxide reductase Methionine sulfoxide reductase B Methionine S-oxide reductase (R-form oxidizing) Methionine S-oxide reductase Selenoprotein R Peptide-methionine (R)-S-oxide reductase The reaction occurs in the reverse direction to that shown above. For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well. Exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide. Plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. Selenium Zinc The reaction proceeds via a sulfenic-acid intermediate. While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater. Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin. Acetylmethionine sulfoxide reductase Methionine sulfoxide reductase Methionine-S-oxide reductase Methyl sulfoxide reductase I and II L-methionine-(S)-S-oxide reductase FSMsr Free-methionine (S)-S-oxide reductase Dithiothreitol can replace reduced thioredoxin. NADPH The reaction occurs in the opposite direction to that given above. L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S-oxide + thioredoxin. L-methionine (R)-S-oxide is not a substrate (see EC 1.8.4.14). Free met-R-(o) reductase FRMsr L-methionine-(R)-S-oxide reductase Free-methionine (R)-S-oxide reductase L-methionine + thioredoxin disulfide + H(2)O = L-methionine (R)-S-oxide + thioredoxin. Unlike EC 1.8.4.12 this enzyme cannot use peptide-bound methionine (R)-S-oxide as a substrate. Differs from EC 1.8.4.13, in that L-methionine (S)-S-oxide is not a substrate. NADPH Insulin reductase Protein-disulfide reductase (glutathione) Glutathione--insulin transhydrogenase Reduces insulin and some other proteins. 2 glutathione + protein-disulfide = glutathione disulfide + protein-dithiol. Glutathione--CoA-glutathione transhydrogenase CoA + glutathione disulfide = CoA-glutathione + glutathione. Glutathione--cystine transhydrogenase 2 glutathione + cystine = oxidized glutathione + 2 cysteine. Glutathione-dependent thiol:disulfide oxidoreductase Enzyme-thiol transhydrogenase (oxidized-glutathione) [Xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase Thiol:disulfide oxidoreductase Enzyme-thiol transhydrogenase (glutathione-disulfide) Also reduces the disulfide bond of ricin. Not inhibited by Cu(2+) or thiol reagents. [Xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] + 2 glutathione. Converts EC 1.17.1.4 into EC 1.17.3.2 in the presence of glutathione disulfide. 3'-phosphoadenylylsulfate reductase Phosphoadenosine-phosphosulfate reductase Thioredoxin:3'-phospho-adenylylsulfate reductase PAdoPS reductase Phosphoadenylyl-sulfate reductase (thioredoxin) Thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase PAPS sulfotransferase PAPS reductase PAPS reductase, thioredoxin-dependent Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin. Specific for PAPS. The enzyme from Escherichia coli will use thioredoxins from other species. Adenylyl-sulfate reductase (glutathione) AMP,sulfite:oxidized-glutathione oxidoreductase (adenosine-5'-phosphosulfate-forming) 5'-adenylylsulfate reductase Plant-type 5'-adenylylsulfate reductase AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione. Glutathione can be replaced by gamma-glutamylcysteine or dithiothreitol, but not by thioredoxin, glutaredoxin or mercaptoethanol. The enzyme from Arabidopsis thaliana contains a glutaredoxin-like domain. Also found in other photosynthetic eukaryotes, e.g., the Madagascar periwinkle, Catharanthus roseus and the hollow green seaweed, Enteromorpha intestinalis. Differs from EC 1.8.99.2, in using glutathione as the reductant. With a quinone or similar compound as acceptor Glutathione dehydrogenase (ascorbate) 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate. Thiosulfate:quinone oxidoreductase Thiosulfate dehydrogenase (quinone) TQO Thiosulfate oxidoreductase, tetrathionate-forming Unlike EC 1.8.2.2, this enzyme cannot utilize cytochrome c as an acceptor. The reaction can also proceed with ferricyanide as the electron acceptor, but more slowly. 2 thiosulfate + 2 6-decylubiquinone = tetrathionate + 2 6-decylubiquinol. With an iron-sulfur protein as acceptor Sulfite reductase (ferredoxin) Iron H(2)S + 3 oxidized ferredoxin + 6 H(2)O = sulfite + 6 reduced ferredoxin + 6 H(+). With other, known, acceptors CoB--CoM heterodisulfide reductase Soluble heterodisulfide reductase Heterodisulfide reductase Coenzyme B + coenzyme M + methanophenazine = N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-phospho-L-threonine + dihydromethanophenazine. Found in methanogenic archaea, particularly Methanosarcina species, and regenerates coenzyme M and coenzyme B after the action of EC 2.8.4.1. Highly specific for both coenzyme M and coenzyme B. Reacts with various phenazine derivatives, including 2-hydroxyphenazine and 2-bromophenazine. Heme Iron-sulfur Peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase Sulfiredoxin Occasionally the S-hydroxycysteine residue is further oxidized to the sulfinic acid S-hydroxy-S-oxocysteine, thereby inactivating the enzyme. Peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R. Attack by a thiol splits this bond, leaving the peroxiredoxin as the sulfenic acid and the reductase as the thiol. The reductase provides a mechanism for regenerating the active form of peroxiredoxin, i.e. the peroxiredoxin-(S-hydroxycysteine) form. In the course of the reaction of EC 1.11.1.15, its cysteine residue is alternately oxidized to the sulfenic acid, S-hydroxycysteine, and reduced back to cysteine. Apparently the reductase first catalyzes the phosphorylation of the -S(O)-OH group by ATP to give -S(O)-O-P, which is attached to the peroxiredoxin by a cysteine residue, forming an -S(O)-S-link between the two enzymes. With other acceptors Sulfite reductase Iron H(2)S + acceptor + 3 H(2)O = SO(3)(2-) + reduced acceptor. A stoichiometry of six molecules of reduced methyl viologen per molecule of sulfide formed was found. Adenylyl-sulfate reductase Methyl viologen can act as acceptor. Iron FAD AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor. Desulfoviridin Desulforubidin Desulfofuscidin Hydrogensulfite reductase Bisulfite reductase Dissimilatory sulfite reductase Iron-sulfur (O(3)S.S.SO(3))(2-) + acceptor + 2 H(2)O + OH(-) = 3 HSO(3)(-) + reduced acceptor. Methyl viologen can act as acceptor. Siroheme A group of sirohemoproteins containing iron-sulfur centers (P-582). Acting on a heme group of donors With oxygen as acceptor Cytochrome-c oxidase Warburg's respiratory enzyme Cytochrome oxidase Cytochrome aa3 Complex IV (mitochondrial electron transport) Cytochrome a3 Copper The reduction of O(2) to water is accompanied by the extrusion of four protons from the intramitochondrial compartment. Several bacteria appear to contain analogous oxidases. http://purl.uniprot.org/mim/535000 4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O. http://purl.uniprot.org/mim/220110 With a nitrogenous group as acceptor Nitrate reductase (cytochrome) 2 ferrocytochrome + nitrate + 2 H(+) = 2 ferricytochrome + nitrite. With other acceptors Iron--cytochrome-c reductase Iron Ferrocytochrome c + Fe(3+) = ferricytochrome c + Fe(2+). Other oxidoreductases Sole sub-subclass for oxidoreductases that do not belong in the other subclasses Chlorate reductase AH(2) + chlorate = A + H(2)O + chlorite. Flavins or benzylviologen can act as acceptor. Type II iodothyronine deiodinase L-thyroxine iodohydrolase (reducing) Iodothyronine 5'-deiodinase Diiodothyronine 5'-deiodinase Thyroxine 5-deiodinase Iodothyronine outer ring monodeiodinase Thyroxine 5'-deiodinase Type I iodothyronine deiodinase The enzyme consists of type I and type II enzymes, both containing selenocysteine, but with different kinetics. The enzyme activity has only been demonstrated in the direction of 5'-deiodination, which renders the thyroid hormone more active. For the type I enzyme the first reaction is a reductive deiodination converting the -Se-H group of the enzyme into an -Se-I group; the reductant then reconverts this into -Se-H, releasing iodide. 3,5,3'-triiodo-L-thyronine + iodide + A + H(+) = L-thyroxine + AH(2). http://purl.uniprot.org/mim/147892 Iodothyronine 5-deiodinase Thyroxine 5-deiodinase Type III iodothyronine deiodinase Iodothyronine inner ring monodeiodinase Diiodothyronine 5'-deiodinase This removal of the 5-iodine, i.e. from the inner ring, largely inactivates the hormone thyroxine. 3,3',5'-triiodo-L-thyronine + iodide + A + H(+) = L-thyroxine + AH(2). The enzyme activity has only been demonstrated in the direction of 5-deiodination. Pyrogallol hydroxytransferase Transhydroxylase Pyrogallol hydroxyltransferase 1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene = 1,3,5-trihydroxybenzene + 1,2,3,5-tetrahydroxybenzene. 1,2,3,5-tetrahydroxybenzene acts as a cosubstrate for the conversion of pyrogallol into phloroglucinol, and for a number of similar isomerizations. Molybdenum The enzyme is provisionally listed here, but might be considered as the basis for a new class in the transferases, analogous to the aminotransferases. Sulfur reductase Reduction of elemental sulfur or polysulfide to H(2)S. Sulfur can be reduced with hydrogen as donor in the presence of hydrogenase, or by photochemical reduction in the presence of phenosafranin. Formate acetyltransferase-glycine dihydroflavodoxin:S-adenosyl-L-methionine oxidoreductase (S-adenosyl-L-methionine cleaving) Formate acetyltransferase activating enzyme [Formate-C-acetyltransferase]-activating enzyme [Pyruvate formate-lyase]-activating enzyme PFL activase PFL-glycine:S-adenosyl-L-methionine H transferase (flavodoxin-oxidizing, S-adenosyl-L-methionine-cleaving) Iron-sulfur S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical. A single glycine residue in EC 2.3.1.54 is oxidized to the corresponding radical by transfer of H from its CH(2) to AdoMet with concomitant cleavage of the latter. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue. Tetrachloroethene reductase Tetrachloroethene reductive dehalogenase Although the physiological reductant is unknown, the supply of reductant in some organisms is via reduced menaquinone, itself formed from molecular hydrogen, via EC 1.12.99.3. The reaction occurs in the reverse direction. Trichloroethene + chloride + acceptor = tetrachloroethene + reduced acceptor. This enzyme allows the common pollutant tetrachloroethene to support bacterial growth and is responsible for disposal of a number of chlorinated hydrocarbons by this organism. The enzyme also reduces trichloroethene to dichloroethene. Methyl viologen can act as electron donor. Iron-sulfur Selenate reductase A number of compounds, including acetate, lactate, pyruvate, and certain sugars, amino acids, fatty acids, di-and tricarboxylic acids, and benzoate can serve as electron donors. Molybdenum Heme Selenite + H(2)O + acceptor = selenate + reduced acceptor. Nitrate, nitrite, chlorate and sulfate are not substrates. Iron-sulfur The periplasmic enzyme from Thauera selenatis is a complex comprising three heterologous subunits (alpha, beta and gamma). Transferases Transferring one-carbon groups Methyltransferases Nicotinamide N-methyltransferase S-adenosyl-L-methionine + nicotinamide = S-adenosyl-L-homocysteine + 1-methylnicotinamide. Homocysteine S-methyltransferase The bacterial enzyme uses S-methylmethionine as donor more actively than S-adenosyl-L-methionine. S-adenosyl-L-methionine + L-homocysteine = S-adenosyl-L-homocysteine + L-methionine. Protein-S-isoprenylcysteine O-methyltransferase Isoprenylcysteine carboxylmethyltransferase Prenylcysteine carboxyl methyltransferase Prenylated protein carboxyl methyltransferase C-terminal S-geranylgeranylcysteine and S-geranylcysteine residues are also methylated, more slowly. S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine = S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester. Macrocin O-methyltransferase The 3-hydroxyl group of a 2-O-methyl-6-deoxy-D-allose residue in the macrolide antibiotic macrocin acts as methyl acceptor; also converts lactenosin into desmyocin. S-adenosyl-L-methionine + macrocin = S-adenosyl-L-homocysteine + tylosin. Not identical with EC 2.1.1.102. Demethylmacrocin O-methyltransferase The 2-hydroxyl group of a 6-deoxy-D-allose residue in demethylmacrocin acts as methyl acceptor. Not identical with EC 2.1.1.101. S-adenosyl-L-methionine + demethylmacrocin = S-adenosyl-L-homocysteine + macrocin. Phosphoethanolamine N-methyltransferase S-adenosyl-L-methionine + ethanolamine phosphate = S-adenosyl-L-homocysteine + N-methylethanolamine phosphate. The enzyme may catalyze the transfer of two further methyl groups to the product. Caffeoyl-CoA O-methyltransferase Trans-caffeoyl-CoA 3-O-methyltransferase S-adenosyl-L-methionine + caffeoyl-CoA = S-adenosyl-L-homocysteine + feruloyl-CoA. N-benzoyl-4-hydroxyanthranilate 4-O-methyltransferase S-adenosyl-L-methionine + N-benzoyl-4-hydroxyanthranilate = S-adenosyl-L-homocysteine + N-benzoyl-4-methoxyanthranilate. Involved in the biosynthesis of phytoalexins. Tryptophan 2-C-methyltransferase D-tryptophan and (indol-3-yl)pyruvate can also act as acceptors, but more slowly. S-adenosyl-L-methionine + L-tryptophan = S-adenosyl-L-homocysteine + L-2-methyltryptophan. Uroporphyrinogen-III C-methyltransferase Uroporphyrin-III C-methyltransferase SUMT S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase Uroporphyrinogen-III methylase Uroporphyrinogen III methylase Uroporphyrinogen methyltransferase Adenosylmethionine-uroporphyrinogen III methyltransferase Urogen III methylase Uroporphyrinogen-III methyltransferase Also involved in the biosynthesis of cobalamin. This enzyme catalyzes two sequential methylation reactions, the first forming precorrin-1 and the second leading to the formation of precorrin-2. (2) S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. (1) S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirA being responsible for the above reaction. The second step involves an NAD(+)-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76) and the third step involves the chelation of Fe(2+) to sirohydrochlorin to form siroheme (EC 4.99.1.4). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. It is the first of three steps leading to the formation of siroheme from uroporphyrinogen III. 6-hydroxymellein O-methyltransferase 6-methoxymellein is a phytoalexin produced by carrot tissue. S-adenosyl-L-methionine + 6-hydroxymellein = S-adenosyl-L-homocysteine + 6-methoxymellein. 3,4-dehydro-6-hydroxymellein can also act as acceptor. Demethylsterigmatocystin 6-O-methyltransferase S-adenosyl-L-methionine + 6-demethylsterigmatocystin = S-adenosyl-L-homocysteine + sterigmatocystin. Involved in the biosynthesis of aflatoxins in fungi. Dihydrodemethylsterigmatocystin can also act as acceptor. Magnesium protoporphyrin IX methyltransferase Mg-protoporphyrin IX methyltransferase S-adenosyl-L-methionine:magnesium-protoporphyrin O-methyltransferase S-adenosyl-L-methionine:Mg protoporphyrin methyltransferase S-adenosylmethionine-magnesium protoporphyrin methyltransferase Magnesium-protoporphyrin O-methyltransferase (-)-S-adenosyl-L-methionine:magnesium-protoporphyrin IX methyltransferase S-adenosylmethioninemagnesium protoporphyrin methyltransferase S-adenosyl-L-methionine + magnesium protoporphyrin IX = S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester. Sterigmatocystin 7-O-methyltransferase Sterigmatocystin 8-O-methyltransferase O-methyltransferase II S-adenosyl-L-methionine:sterigmatocystin 7-O-methyltransferase Sterigmatocystin methyltransferase S-adenosyl-L-methionine + sterigmatocystin = S-adenosyl-L-homocysteine + 8-O-methylsterigmatocystin. Involved in the biosynthesis of aflatoxins in fungi. Dihydrosterigmatocystin can also act as acceptor. Anthranilate N-methyltransferase S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine + N-methylanthranilate. Involved in the biosynthesis of acridine alkaloids in plant tissues. Glucuronoxylan 4-O-methyltransferase S-adenosyl-L-methionine + glucuronoxylan D-glucuronate = S-adenosyl-L-homocysteine + glucuronoxylan 4-O-methyl-D-glucuronate. Restriction-modification system Modification methylase N(4)-cytosine-specific DNA methylase Site-specific DNA-methyltransferase (cytosine-N(4)-specific) This is a large group of enzymes, the majority of which, with enzymes of similar site specificity listed as EC 3.1.21.3, EC 3.1.21.4 and EC 3.1.21.5, form so-called restriction-modification systems. See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/ S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine + DNA N(4)-methylcytosine. Hexaprenyldihydroxybenzoate methyltransferase DHHB-Mt DHHB methyltransferase 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase Dihydroxyhexaprenylbenzoate methyltransferase S-adenosyl-L-methionine + 3-hexaprenyl-4,5-dihydroxybenzoate = S-adenosyl-L-homocysteine + 3-hexaprenyl-4-hydroxy-5-methoxybenzoate. Involved in the pathway of ubiquinone synthesis. (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase (RS)-tetrahydrobenzylisoquinoline N-methyltransferase Norreticuline N-methyltransferase The physiological substrate is likely to be coclaurine. Broad substrate specificity for (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinolines; including coclaurine, norcoclaurine, isococlaurine, norarmepavine, norreticuline and tetrahydropapaverine. Participates in the pathway leading to benzylisoquinoline alkaloid synthesis in plants. Both R-and S-enantiomers are methylated. However, norreticuline has not been found to occur in nature and that rdfs:label does not reflect the broad specificity of the enzyme for (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinolines. Was earlier termed norreticuline N-methyltransferase. S-adenosyl-L-methionine + (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline = S-adenosyl-L-homocysteine + N-methyl-(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline. 3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase S-adenosyl-L-methionine + 3'-hydroxy-N-methyl-(S)-coclaurine = S-adenosyl-L-homocysteine + (S)-reticuline. Has also been shown to catalyze the methylation of (RS)-laudanosoline, (S)-3'-hydroxycoclaurine and (RS)-7-O-methylnoraudanosoline. Involved in isoquinoline alkaloid metabolism in plants. (S)-scoulerine 9-O-methyltransferase The product of this reaction is a precursor for protoberberine alkaloids in plants. S-adenosyl-L-methionine + (S)-scoulerine = S-adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine. Columbamine O-methyltransferase Distinct in specificity from EC 2.1.1.88. S-adenosyl-L-methionine + columbamine = S-adenosyl-L-homocysteine + palmatine. The product of this reaction is a protoberberine alkaloid that is widely distributed in the plant kingdom. 10-hydroxydihydrosanguinarine 10-O-methyltransferase S-adenosyl-L-methionine + 10-hydroxydihydrosanguinarine = S-adenosyl-L-homocysteine + dihydrochelirubine. Part of the pathway for synthesis of benzophenanthridine alkaloids in plants. Methionine S-methyltransferase Zinc or manganese S-adenosyl-L-methionine + L-methionine = S-adenosyl-L-homocysteine + S-methyl-L-methionine. 12-hydroxydihydrochelirubine 12-O-methyltransferase S-adenosyl-L-methionine + 12-hydroxydihydrochelirubine = S-adenosyl-L-homocysteine + dihydromacarpine. Part of the pathway for synthesis of benzophenanthridine alkaloid macarpine in plants. 6-O-methylnorlaudanosoline 5'-O-methyltransferase Nororientaline is a precursor of the alkaloid papaverine. S-adenosyl-L-methionine + 6-O-methylnorlaudanosoline = S-adenosyl-L-homocysteine + nororientaline. Tetrahydroprotoberberine cis-N-methyltransferase (S)-tetrahydroprotoberberine N-methyltransferase Involved in the biosynthesis of isoquinoline alkaloids in plants. S-adenosyl-L-methionine + (S)-7,8,13,14-tetrahydroprotoberberine = S-adenosyl-L-homocysteine + cis-N-methyl-(S)-7,8,13,14-tetrahydroprotoberberine. [Cytochrome c]-methionine S-methyltransferase S-adenosyl-L-methionine + [cytochrome c]-methionine = S-adenosyl-L-homocysteine + [cytochrome c]-S-methyl-methionine. [Cytochrome c]-arginine N-methyltransferase S-adenosyl-L-methionine + [cytochrome c]-arginine = S-adenosyl-L-homocysteine + [cytochrome c]-N(omega)-methyl-arginine. Histone-arginine N-methyltransferase Protein-arginine N-methyltransferase Histone protein methylase Protein methylase I The rdfs:label protein methylase I is misleading since it has been used for a number of enzymes with different specificities. S-adenosyl-L-methionine + histone-arginine = S-adenosyl-L-homocysteine + histone-N(omega)-methyl-arginine. Forms the N(omega)-monomethyl-and N(omega),N(omega')-dimethyl, but not the N(omega),N(omega)-dimethyl-arginine derivatives. Protein methylase I Protein-arginine N-methyltransferase Myelin basic protein methylase [Myelin basic protein]-arginine N-methyltransferase S-adenosyl-L-methionine + [myelin basic protein]-arginine = S-adenosyl-L-homocysteine + [myelin basic protein]-N(omega)-methyl-arginine. Forms the N(omega)-monomethyl-, N(omega),N(omega)-dimethyl-and N(omega),N(omega')-dimethyl-arginine derivatives. The rdfs:label protein methylase I is misleading since it has been used for a number of enzymes with different specificities. RuBisCO LSMT [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase Ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase RuBisCO methyltransferase The enzyme methylates Lys-14 in the large subunits of hexadecameric higher plant EC 4.1.1.39. S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine = S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N(6)-methyl-L-lysine. (RS)-norcoclaurine 6-O-methyltransferase The enzyme will also catalyze the 6-O-methylation of (RS)-norlaudanosoline to form 6-O-methyl-norlaudanosoline, but this alkaloid has not been found to occur in plants. Norcoclaurine is 6,7-dihydroxy-1-((4-hydroxyphenyl)methyl)-1,2,3,4-tetrahydroisoquinoline. S-adenosyl-L-methionine + (RS)-norcoclaurine = S-adenosyl-L-homocysteine + (RS)-coclaurine. Myo-inositol 4-O-methyltransferase Myo-inositol 6-O-methyltransferase S-adenosyl-L-methionine:myo-inositol 4-O-methyltransferase Inositol 4-methyltransferase The enzyme also methylates 1L-1,2,4/3,5-cyclohexanepentol, 2,4,6/3,5-pentahydroxycyclohexanone, D,L-2,3,4,6/5-pentacyclohexanone and 2,2'-anhydro-2-C-hydroxymethyl-myo-inositol, but at lower rates than that of myo-inositol. The enzyme from Vigna umbellata is highly specific for S-adenosyl-L-methionine. S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + 1D-4-O-methyl-myo-inositol. Methyltetrahydrofolate--homocysteine vitamin B12 methyltransferase 5-methyltetrahydrofolate--homocysteine transmethylase Methionine synthase Tetrahydrofolate methyltransferase Methionine synthase (cobalamin-dependent) N(5)-methyltetrahydrofolate methyltransferase 5-methyltetrahydrofolate--homocysteine S-methyltransferase N(5)-methyltetrahydrofolate--homocysteine cobalamin methyltransferase Tetrahydropteroylglutamate methyltransferase Vitamin B12 methyltransferase N-methyltetrahydrofolate:L-homocysteine methyltransferase Cobalamin-dependent methionine synthase Methionine synthetase Tetrahydropteroylglutamic methyltransferase N(5)-methyltetrahydrofolic--homocysteine vitamin B12 transmethylase B12 N(5)-methyltetrahydrofolate homocysteine methyltransferase In bacteria, the reducing agent is flavodoxin, and no further catalyst is needed (the flavodoxin is kept in the reduced state by NADPH and EC 1.18.1.2). For the mammalian enzyme, the reducing system involves NADPH and EC 1.16.1.8. Reactivation by reductive methylation is catalyzed by the enzyme itself, with S-adenosyl-L-methionine as the methyl donor and a reducing system. Zinc 5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine. The enzyme becomes inactivated occasionally during its cycle by oxidation of Co(I) to Co(II). Cobalamin http://purl.uniprot.org/mim/250940 Acts on the monoglutamate as well as the triglutamate folate, in contrast with EC 2.1.1.14, which acts only on the triglutamate. Precorrin-2 C20-methyltransferase S-adenosyl-L-methionine--precorrin-2 methyltransferase Precorrin-2 C(20)-methyltransferase S-adenosyl-L-methionine + precorrin-2 = S-adenosyl-L-homocysteine + precorrin-3A. Precorrin-3 methyltransferase Precorrin-3 methylase Precorrin-3B C17-methyltransferase Precorrin-3B C(17)-methyltransferase The first of the four steps is carried out by EC 1.14.13.83 (CobG), yielding precorrin-3B as the product. S-adenosyl-L-methionine + precorrin-3B = S-adenosyl-L-homocysteine + precorrin-4. This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin-4, precorrin-5 and precorrin-6A, respectively. In the aerobic cobalamin biosythesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A. Precorrin-6Y C(5,15)-methyltransferase (decarboxylating) Precorrin-6Y C5,15-methyltransferase (decarboxylating) Precorrin-6 methyltransferase Precorrin-6Y methylase 2 S-adenosyl-L-methionine + precorrin-6Y = 2 S-adenosyl-L-homocysteine + precorrin-8X + CO(2). The enzyme from Pseudomonas denitrificans has S-adenosyl-L-methionine-dependent methyltransferase and decarboxylase activities. Precorrin-4 C11-methyltransferase Precorrin-4 C(11)-methyltransferase Precorrin-3 methylase S-adenosyl-L-methionine + precorrin-4 = S-adenosyl-L-homocysteine + precorrin-5. The first of the four steps is carried out by EC 1.14.13.83 (CobG), yielding precorrin-3B as the product. In the aerobic cobalamin biosythesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A. This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin-4, precorrin-5 and precorrin-6A, respectively. Trichlorophenol O-methyltransferase Chlorophenol O-methyltransferase Halogenated phenol O-methyltransferase S-adenosyl-L-methionine + trichlorophenol = S-adenosyl-L-homocysteine + trichloroanisole. The enzyme from Trichoderma virgatum, when cultured in the presence of halogenated phenol, also acts on a range of mono-, di-and trichlorophenols. S-adenosyl-L-methionine:arsenic(III) methyltransferase Arsenite methyltransferase Methylarsonite methyltransferase S-adenosyl-L-methionine:methylarsonite As-methyltransferase (1) S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate. (2) S-adenosyl-L-methionine + methylarsonite = S-adenosyl-L-homocysteine + dimethylarsinate. An enzyme of the biotransformation pathway that forms dimethylarsinate from inorganic arsenite and arsenate. It methylates arsenite to form methylarsonate, Me-AsO(3)H(2), which is reduced by EC 1.20.4.2 to methylarsonite, Me-As(OH)(2). Methylarsonite is also a substrate for this enzyme which converts it into the much less toxic compound dimethylarsinate (cacodylate), Me(2)As(O)-OH. 3'-demethylstaurosporine O-methyltransferase Staurosporine synthase 3'-demethoxy-3'-hydroxystaurosporine O-methyltransferase Catalyzes the final step in the biosynthesis of staurosporine, an alkaloidal antibiotic that is a potent inhibitor of protein kinases, especially protein kinase C. S-adenosyl-L-methionine + 3'-demethylstaurosporine = S-adenosyl-L-homocysteine + staurosporine. Methionine synthase (cobalamin-independent) Tetrahydropteroylglutamate-homocysteine transmethylase Homocysteine methylase Cobalamin-independent methionine synthase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase Methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase Unlike EC 2.1.1.13 this enzyme does not contain cobalamin. The enzyme from Escherichia coli also requires a reducing system. 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. Zinc Requires phosphate. (S)-coclaurine-N-methyltransferase Norcoclaurine can also act as an acceptor. The enzyme is specific for the (S)-isomer of coclaurine. S-adenosyl-L-methionine + (S)-coclaurine = S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine. Jasmonic acid carboxyl methyltransferase Jasmonate O-methyltransferase 9,10-dihydrojasmonic acid is a poor substrate for the enzyme. Enzyme activity is inhibited by the presence of divalent cations, e.g., Ca(2+), Cu(2+), Mg(2+) and Zn(2+). The enzyme does not convert 12-oxo-phytodienoic acid (a precursor of jasmonic acid), salicylic acid, benzoic acid, linolenic acid or cinnamic acid into their corresponding methyl esters. S-adenosyl-L-methionine + jasmonate = S-adenosyl-L-homocysteine + methyl jasmonate. Cycloartenol 24-C-methyltransferase Sterol C-methyltransferase S-adenosyl-L-methionine + cycloartenol = S-adenosyl-L-homocysteine + (24R)-24-methylcycloart-25-en-3-beta-ol. S-adenosyl-L-methionine methylates the Si face of the 24(25)-double bond with elimination of a hydrogen atom from the pro-Z methyl group at C-25. 24-methylenesterol C-methyltransferase 24-methylenelophenol C-24(1)-methyltransferase SMT(2) S-adenosyl-L-methionine + 24-methylenelophenol = S-adenosyl-L-homocysteine + (Z)-24-ethylidenelophenol. This is the second methylation step of plant sterol biosynthesis (cf. EC 2.1.1.142). Trans-aconitate 2-methyltransferase Also catalyzes the formation of the methyl monoester of cis-aconitate, isocitrate and citrate, but more slowly. While the enzyme from Escherichia coli forms (E)-3-(methoxycarbonyl)-pent-2-enedioate as the product, that from Saccharomyces cerevisiae forms (E)-2-(methoxycarbonylmethyl)butenedioate and is therefore classified as a separate enzyme (cf. EC 2.1.1.145). S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + (E)-3-(methoxycarbonyl)pent-2-enedioate. Trans-aconitate 3-methyltransferase Also catalyzes the formation of the methyl monoester of cis-aconitate, isocitrate and citrate, but more slowly. S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate. While the enzyme from Saccharomyces cerevisiae forms (E)-2-(methoxycarbonylmethyl)butenedioate as the product, that from Escherichia coli forms (E)-3-(methoxycarbonyl)-pent-2-enedioate and is therefore classified as a separate enzyme (cf. EC 2.1.1.144). (Iso)eugenol O-methyltransferase S-adenosyl-L-methionine + isoeugenol = S-adenosyl-L-homocysteine + isomethyleugenol. Acts on eugenol and chavicol as well as isoeugenol. Corydaline synthase Also acts on 7,8-dihydropalmatine. S-adenosyl-L-methionine + palmatine + 2 NADPH = S-adenosyl-L-homocysteine + corydaline + 2 NADP(+). FDTS Thymidylate synthase (FAD) Flavin dependent thymidylate synthase 5,10-methylenetetrahydrofolate + dUMP + FADH(2) = dTMP + tetrahydrofolate + FAD. The reaction shown is distinct from that of the classical thymidylate synthase, EC 2.1.1.45. FMN can replace FAD. Flavonoid 3',5'-O-dimethyltransferase Myricetin O-methyltransferase CrCOMT2 The enzyme from Catharanthus roseus (Madagascar periwinkle) is unusual as it carries out two methylations of the same substrate. Also catalyzes the methylation of dihydromyricetin. 2 S-adenosyl-L-methionine + myricetin = 2 S-adenosyl-L-homocysteine + syringetin. Fatty-acid O-methyltransferase S-adenosyl-L-methionine + a fatty acid = S-adenosyl-L-homocysteine + a fatty acid methyl ester. Oleic acid is the most effective fatty acid acceptor. Isoflavone 7-O-methyltransferase S-adenosyl-L-methionine + a 7-hydroxyisoflavone = S-adenosyl-L-homocysteine + a 7-methoxyisoflavone. The enzyme from alfalfa can methylate daidzein, genistein and 6,7,4'-trihydroxyisoflavone but not flavones or flavanones. Cobalt-factor II C(20)-methyltransferase Cobalt-precorrin-2 C(20)-methyltransferase S-adenosyl-L-methionine + cobalt-factor II = S-adenosyl-L-homocysteine + cobalt-factor III. Involved in the anaerobic biosynthesis of vitamin B12. Precorrin-6A synthase (deacetylating) Precorrin-6X synthase (deacetylating) This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin-4, precorrin-5 and precorrin-6A, respectively. The first of the four steps is carried out by EC 1.14.13.83 (CobG), yielding precorrin-3B as the product. In the aerobic cobalamin biosythesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A. S-adenosyl-L-methionine + precorrin-5 + H(2)O = S-adenosyl-L-homocysteine + precorrin-6A + acetate. Vitexin 2''-O-rhamnoside 7-O-methyltransferase The flavonoids vitexin and isovitexin 2''-O-arabinoside do not act as substrates for the enzyme from oats (Avena sativa). S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside = S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside. Isoliquiritigenin 2'-O-methyltransferase Chalcone OMT CHMT Not identical to EC 2.1.1.65. While EC 2.1.1.154 can use licodione as a substrate, EC 2.1.1.65 cannot use isoliquiritigenin as a substrate. S-adenosyl-L-methionine + isoliquiritigenin = S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin. S-adenosyl-L-methionine:flavonoid 4'-O-methyltransferase F 4'-OMT Kaempferol 4'-O-methyltransferase Kaempferol, apigenin and kaempferol triglucoside are substrates, as is genistein, which reacts more slowly. Compounds with an hydroxy group in the 3' and 4' positions, such as quercetin and eriodictyol, do not act as substrates. The enzyme acts on the hydroxy group in the 4'-position of some flavones, flavanones and isoflavones. Similar to EC 2.1.1.75 and EC 2.1.1.83. S-adenosyl-L-methionine + kaempferol = S-adenosyl-L-homocysteine + kaempferide. Glycine-sarcosine methyltransferase GMT Glycine sarcosine N-methyltransferase Glycine/sarcosine N-methyltransferase GSMT Cells of the oxygen-evolving halotolerant cyanobacterium Aphanocthece halophytica synthesize betaine from glycine by a three-step methylation process. Acetate, dimethylglycine and S-adenosyl-L-homocysteine can inhibit the reaction. (2) S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine. Differs from EC 2.1.1.20, as it can further methylate the product of the first reaction. This is the first enzyme and it leads to the formation of either sarcosine or N,N-dimethylglycine, which is further methylated to yield betaine (N,N,N-trimethylglycine) by the action of EC 2.1.1.157. (1) S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine. SDMT Sarcosine dimethylglycine N-methyltransferase Sarcosine-dimethylglycine methyltransferase Sarcosine/dimethylglycine N-methyltransferase ApDMT The first enzyme, EC 2.1.1.156, leads to the formation of either sarcosine or N,N-dimethylglycine, which is further methylated to yield betaine (N,N,N-trimethylglycine) by the action of this enzyme. (2) S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + betaine. Cells of the oxygen-evolving halotolerant cyanobacterium Aphanocthece halophytica synthesize betaine from glycine by a three-step methylation process. Both of these enzymes can catalyze the formation of N,N-dimethylglycine from sarcosine. (1) S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine. The reactions are strongly inhibited by S-adenosyl-L-homocysteine. Xanthosine methyltransferase 7-methylxanthosine synthase XMT XRS1 The enzyme is specific for xanthosine, as XMP and xanthine cannot act as substrates. S-adenosyl-L-methionine + xanthosine = S-adenosyl-L-homocysteine + 7-methylxanthosine. This is the first methylation step in the production of caffeine. The enzyme does not have N(1)-or N(3)-methylation activity. MXMT Monomethylxanthine methyltransferase Theobromine synthase S-adenosyl-L-methionine + 7-methylxanthine = S-adenosyl-L-homocysteine + 3,7-dimethylxanthine. This is the third enzyme in the caffeine-biosynthesis pathway. Can also catalyze the conversion of paraxanthine into caffeine, although the paraxanthine pathway is considered to be a minor pathway for caffeine biosynthesis. Unsaturated-phospholipid methyltransferase Methylene-fatty-acyl-phospholipid synthase Cyclopropane synthetase S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid methylene fatty acid. The enzyme transfers a methyl group to the 10-position of a Delta(9)-olefinic acyl chain in phosphatidylglycerol, phosphatidylinositol, or, more slowly, phosphatidylethanolamine; subsequent proton transfer produces a 10-methylene group (cf. EC 2.1.1.79). 3N-methyltransferase Dimethylxanthine methyltransferase Caffeine synthase (1) S-adenosyl-L-methionine + 3,7-dimethylxanthine = S-adenosyl-L-homocysteine + 1,3,7-trimethylxanthine. (3) S-adenosyl-L-methionine + 7-dimethylxanthine = S-adenosyl-L-homocysteine + 3,7-dimethylxanthine. Paraxanthine is the best substrate for this enzyme but the paraxanthine pathway is considered to be a minor pathway for caffeine biosynthesis. (2) S-adenosyl-L-methionine + 1,7-dimethylxanthine = S-adenosyl-L-homocysteine + 1,3,7-trimethylxanthine. Phosphatidylethanolamine N-methyltransferase S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine. Polysaccharide O-methyltransferase S-adenosyl-L-methionine + 1,4-alpha-D-glucooligosaccharide = S-adenosyl-L-homocysteine + oligosaccharide containing 6-methyl-D-glucose units. Trimethylsulfonium--tetrahydrofolate N-methyltransferase Trimethylsulfonium + tetrahydrofolate = dimethylsulfide + 5-methyltetrahydrofolate. Guanidinoacetate N-methyltransferase S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine. http://purl.uniprot.org/mim/601240 Glycine methyltransferase Glycine N-methyltransferase S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine. Inhibited by 5-methyltetrahydrofolate pentaglutamate. http://purl.uniprot.org/mim/606664 Sarcosine, which has no physiological role, is converted back into glycine by the action of EC 1.5.99.1. Thought to play an important role in the regulation of methyl group metabolism in the liver and pancreas by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine. N-methylglutamate synthase Methylamine--glutamate N-methyltransferase Methylamine + L-glutamate = NH(3) + N-methyl-L-glutamate. Carnosine N-methyltransferase S-adenosyl-L-methionine + carnosine = S-adenosyl-L-homocysteine + anserine. Phenol O-methyltransferase S-adenosyl-L-methionine + phenol = S-adenosyl-L-homocysteine + anisole. Acts on a wide variety of simple alkyl-, methoxy-and halo-phenols. Iodophenol O-methyltransferase S-adenosyl-L-methionine + 2-iodophenol = S-adenosyl-L-homocysteine + 2-iodophenol methyl ether. Tyramine N-methyltransferase S-adenosyl-L-methionine + tyramine = S-adenosyl-L-homocysteine + N-methyltyramine. Has some activity on phenylethylamine analogs. Noradrenaline N-methyltransferase Phenylethanolamine N-methyltransferase S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L-homocysteine + N-methylphenylethanolamine. Acts on various phenylethanolamines; converts noradrenaline into adrenaline. tRNA (cytosine-5-)-methyltransferase S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 5-methylcytosine. Thetin--homocysteine S-methyltransferase Dimethylsulfonioacetate + L-homocysteine = S-methylthioglycolate + L-methionine. tRNA (guanine-N(1)-)-methyltransferase S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N(1)-methylguanine. N(2),N(2)-dimethylguanine tRNA methyltransferase tRNA 2,2-dimethylguanosine-26 methyltransferase tRNA(m(2,2)G26)dimethyltransferase tRNA (guanine-N(2)-)-methyltransferase tRNA(guanine-26,N(2)-N(2)) methyltransferase In eukaryotic tRNAs, two N(2)-guanine methylations occur, at the N(2)-methylguanine at position 10 and the N(2)-methylguanine at position 29. S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N(2)-methylguanine. tRNA (guanine-N(7)-)-methyltransferase S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N(7)-methylguanine. S-adenosyl-L-methionine:tRNA (guanosine-2'-O-)-methyltransferase Transfer ribonucleate guanosine 2'-methyltransferase tRNA (Gm18) 2'-O-methyltransferase tRNA (Gm18) methyltransferase tRNA guanosine-2'-O-methyltransferase tRNA (guanosine 2')-methyltransferase tRNA (guanosine-2'-O-)-methyltransferase tRNA guanosine 2'-methyltransferase Yeast tRNA(Phe) is one of the best substrate tRNAs. S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 2'-O-methylguanosine. Methylates the 2'-hydroxy group of a guanosine present in a GG sequence at position 18. tRNA:m(5)U54-methyltransferase M5U-methyltransferase tRNA uracil 5-methyltransferase Transfer RNA uracil methylase Ribothymidyl synthase Transfer RNA uracil 5-methyltransferase RUMT tRNA (uracil-5-)-methyltransferase One almost universal post-translational modification is the conversion of U(54) into ribothymidine in the T-Psi-C loop, and this modification is found in most species studied to date. Unlike this enzyme, EC 2.1.1.74 uses 5,10-methylenetetrahydrofolate and FADH(2) to supply the atoms for methylation of U(54). Up to 25% of the bases in mature tRNA are post-translationally modified or hypermodified. S-adenosyl-L-methionine + tRNA containing uridine at position 54 = S-adenosyl-L-homocysteine + tRNA containing ribothymidine at position 54. tRNA (adenine-N(1)-)-methyltransferase The enzymes from different sources are specific for different adenine residues in tRNA. S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N(1)-methyladenine. Cytosine DNA methyltransferase Methylphosphotriester-DNA methyltransferase Deoxyribonucleate methyltransferase DNA methylase DNA cytosine C(5) methylase Deoxyribonucleic acid (cytosine-5-)-methyltransferase Deoxyribonucleate methylase DNA 5-cytosine methylase Site-specific DNA-methyltransferase (cytosine-specific) DNA cytosine methylase Type II DNA methylase Cytosine DNA methylase Cytosine-specific DNA methyltransferase DNA methyltransferase DNA (cytosine-5-)-methyltransferase Deoxyribonucleic acid methylase Restriction-modification system DNA-cytosine methyltransferase Deoxyribonucleic methylase Deoxyribonucleic acid methyltransferase DNA-cytosine 5-methylase Deoxyribonucleic acid modification methylase Cytosine 5-methyltransferase Modification methylase DNA transmethylase Deoxyribonucleic (cytosine-5-)-methyltransferase S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine. http://purl.uniprot.org/mim/242860 See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/ O-demethylpuromycin O-methyltransferase S-adenosyl-L-methionine + O-demethylpuromycin = S-adenosyl-L-homocysteine + puromycin. Puromycin is the antibiotic derived from N(6)-dimethyladenosine by replacing the 3'-hydroxy group with an amino group and acylating this with 4-O-methyltyrosine. Inositol L-1-methyltransferase Myo-inositol 1-methyltransferase Inositol 3-methyltransferase Myo-inositol 1-O-methyltransferase S-adenosyl-L-methionine:myo-inositol 1-O-methyltransferase S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + 1D-3-O-methyl-myo-inositol. Acetylserotonin O-methyltransferase Hydroxyindole O-methyltransferase Some other hydroxyindoles also act as acceptor, more slowly. S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine. Inositol D-1-methyltransferase Myo-inositol 3-O-methyltransferase Inositol 1-methyltransferase Inositol 3-O-methyltransferase S-adenosylmethionine:myo-inositol 3-methyltransferase S-adenosyl-L-methionine:myo-inositol 3-O-methyltransferase S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + 1D-1-O-methyl-myo-inositol. S-adenosyl-L-methionine:Delta(24(23))-sterol methyltransferase S-adenosyl-4-methionine:sterol Delta(24)-methyltransferase Delta(24)-methyltransferase Zymosterol-24-methyltransferase Sterol 24-C-methyltransferase SMT1 Delta(24)-sterol methyltransferase Phytosterol methyltransferase 24-sterol C-methyltransferase S-adenosyl-L-methionine + 5-alpha-cholesta-8,24-dien-3-beta-ol = S-adenosyl-L-homocysteine + 24-methylene-5-alpha-cholest-8-en-3-beta-ol. While zymosterol is the preferred substrate it also acts on desmosterol, 5-alpha-cholesta-7,24-dien-3-beta-ol, 5-alpha-cholesta-5,7,24-trien-3-beta-ol, 4-alpha-methylzymosterol and others. Glutathione Acts on a range of sterols with a 24(25)-double bond in the side chain. S-adenosyl-L-methionine attacks the Si face of the 24(25) double bond and the C-24 hydrogen is transferred to C-25 on the Re face of the double bond. o-dihydric phenol methyltransferase Luteolin O-methyltransferase S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone = S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone. Also acts on luteolin 7-O-beta-D-glucoside. Protein methyltransferase II Histone-lysine N-methyltransferase Protein-lysine N-methyltransferase Protein methylase 3 Protein methylase III http://purl.uniprot.org/mim/130650 http://purl.uniprot.org/mim/194190 S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine. http://purl.uniprot.org/mim/277590 http://purl.uniprot.org/mim/610253 http://purl.uniprot.org/mim/117550 Dimethylhistidine N-methyltransferase S-adenosyl-L-methionine + N(alpha),N(alpha)-dimethyl-L-histidine = S-adenosyl-L-homocysteine + N(alpha),N(alpha),N(alpha)-trimethyl-L-histidine. Methylhistidine and histidine can also act as methyl acceptors, with trimethylhistidine being formed in both cases. Thymidylate synthase 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. Isoflavone 4'-O-methyltransferase S-adenosyl-L-methionine + an isoflavone = S-adenosyl-L-homocysteine + a 4'-O-methylisoflavone. Indolepyruvate C-methyltransferase Indolepyruvate 3-methyltransferase Indolepyruvate methyltransferase Indolepyruvic acid methyltransferase S-adenosyl-L-methionine + (indol-3-yl)pyruvate = S-adenosyl-L-homocysteine + (3S)-3-(indol-3-yl)-3-oxobutanoate. rRNA (adenine-N(6)-)-methyltransferase Ribosomal ribonucleate adenine 6-methyltransferase Ribonucleic acid-adenine (N(6)) methylase S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing N(6)-methyladenine. Also methylates 2-aminoadenosine to 2-methylaminoadenosine. Amine N-methyltransferase Nicotine N-methyltransferase Tryptamine N-methyltransferase Arylamine N-methyltransferase S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine. A wide range of primary, secondary, and tertiary amines can act as acceptors, including tryptamine, aniline, nicotine and a variety of drugs and other xenobiotics. Betaine--homocysteine S-methyltransferase Trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine. Zinc Loganate O-methyltransferase Methylates the 11-carboxy group of the monoterpenoid loganate. S-adenosyl-L-methionine + loganate = S-adenosyl-L-homocysteine + loganin. Also acts on secologanate. rRNA (guanine-N(1)-)-methyltransferase S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing N(1)-methylguanine. rRNA (guanine-N(2)-)-methyltransferase S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing N(2)-methylguanine. Putrescine N-methyltransferase S-adenosyl-L-methionine + putrescine = S-adenosyl-L-homocysteine + N-methylputrescine. Deoxycytidylate C-methyltransferase 5,10-methylenetetrahydrofolate + dCMP = dihydrofolate + deoxy-5-methylcytidylate. dCMP is methylated by formaldehyde in the presence of tetrahydrofolate. CMP, dCTP and CTP can act as acceptor, more slowly. tRNA (adenine-N(6)-)-methyltransferase S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N(6)-methyladenine. Messenger RNA guanine 7-methyltransferase Messenger ribonucleate guanine 7-methyltransferase Guanine-7-methyltransferase mRNA (guanine-N(7)-)-methyltransferase R may be guanosine or adenosine. Adds an N(7)-methylguanine cap to mRNA. S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. mRNA (nucleoside-2'-O-)-methyltransferase mRNA (adenosine-2'-O-)-methyltransferase R may be guanosine or adenosine. Adds an 2'-O-methylpurine cap to mRNA. S-adenosyl-L-methionine + m(7)G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(7)G(5')pppRm-RNA. Cytochrome c (lysine) methyltransferase Cytochrome c methyltransferase Cytochrome c-specific protein methylase III Cytochrome c-specific protein-lysine methyltransferase [Cytochrome c]-lysine N-methyltransferase S-adenosyl-L-methionine + [cytochrome c]-L-lysine = S-adenosyl-L-homocysteine + [cytochrome c]-N(6)-methyl-L-lysine. Catechol O-methyltransferase http://purl.uniprot.org/mim/116790 S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol. The mammalian enzymes act more rapidly on catecholamines such as adrenaline or noradrenaline than on catechols. Calmodulin-lysine N-methyltransferase S-adenosyl-L-methionine + calmodulin L-lysine = S-adenosyl-L-homocysteine + calmodulin N(6)-methyl-L-lysine. tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase http://purl.uniprot.org/mim/580000 Specific for the terminal methyl group of 5-methylaminomethyl-2-thiouridylate. S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate. mRNA (2'-O-methyladenosine-N(6)-)-methyltransferase mRNA containing an N(6),2'-O-dimethyladenosine cap. S-adenosyl-L-methionine + m(7)G(5')pppAm = S-adenosyl-L-homocysteine + m(7)G(5')pppm(6)Am. Methylated-DNA--[protein]-cysteine S-methyltransferase 6-O-methylguanine-DNA methyltransferase O-6-methylguanine-DNA-alkyltransferase This enzyme catalyzes only one turnover and therefore is not strictly catalytic. This protein is involved in the repair of alkylated DNA. DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine. It acts only on the alkylated DNA (cf. EC 3.2.2.20 and EC 3.2.2.21). 3-demethylubiquinone-9 3-O-methyltransferase S-adenosyl-L-methionine + 3-demethylubiquinone-9 = S-adenosyl-L-homocysteine + ubiquinone-9. Licodione 2'-O-methyltransferase S-adenosyl-L-methionine + licodione = S-adenosyl-L-homocysteine + 2'-O-methyllicodione. As well as licodione (1-(2,4-dihydroxyphenyl)-3-(4-hydroxyphenyl)-1,3-propanedione), the 2''-hydroxy-derivative and isoliquiritigenin can act as acceptors, more slowly. Thiostrepton-resistance methylase rRNA (adenosine-2'-O-)-methyltransferase RNA-pentose methylase S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing a single residue of 2'-O-methyladenosine. Thiopurine S-methyltransferase http://purl.uniprot.org/mim/610460 S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether. Not identical with EC 2.1.1.9. Also acts, more slowly, on thiopyrimidines and aromatic thiols. Caffeate O-methyltransferase 3,4-dihydroxybenzaldehyde and catechol can act as acceptor, more slowly. S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate. Bergaptol O-methyltransferase Furanocoumarin 5-methyltransferase 5-hydroxyfuranocoumarin 5-O-methyltransferase BMT Bergaptol methyltransferase Bergaptol 5-O-methyltransferase Furanocoumarin 5-O-methyltransferase Converts bergaptol into bergapten, which has therapeutic potential in the treatment of psoriasis as it has photosensitizing and antiproliferative activities. Methylates the 5-hydroxy group of some hydroxy-and methylcoumarins, but has little activity on non-coumarin phenols; caffeate, 5-hydroxyferulate and daphnetin are not substrates. (1) S-adenosyl-L-methionine + a 5-hydroxyfurocoumarin = S-adenosyl-L-homocysteine + a 5-methoxyfurocoumarin. See also EC 2.1.1.70. Cu(2+), Zn(2+) and Co(2+) cause enzyme inhibition. (2) S-adenosyl-L-methionine + bergaptol = S-adenosyl-L-homocysteine + bergapten. Nicotinate N-methyltransferase S-adenosyl-L-methionine + nicotinate = S-adenosyl-L-homocysteine + N-methylnicotinate. XMT 8-hydroxyfuranocoumarin 8-O-methyltransferase Furanocoumarin 8-O-methyl-transferase Xanthotoxol 8-O-methyltransferase Furanocoumarin 8-methyltransferase Methylates the 8-hydroxy group of some hydroxy-and methylcoumarins, but has little activity on non-coumarin phenols. See also EC 2.1.1.69. (2) S-adenosyl-L-methionine + xanthotoxol = S-adenosyl-L-homocysteine + xanthotoxin. (1) S-adenosyl-L-methionine + an 8-hydroxyfurocoumarin = S-adenosyl-L-homocysteine + an 8-methoxyfurocoumarin. Converts xanthotoxol into xanthotoxin, which has therapeutic potential in the treatment of psoriasis as it has photosensitizing and antiproliferative activities. Phosphatidyl-N-methylethanolamine N-methyltransferase S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine. Also catalyzes the transfer of a further methylgroup, producing phosphatidylcholine. Restriction-modification system N-6 adenine-specific DNA methylase Modification methylase Site-specific DNA-methyltransferase (adenine-specific) See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/ This is a large group of enzymes, the majority of which, with enzymes of similar site specificity listed as EC 3.1.21.3, EC 3.1.21.4 and EC 3.1.21.5, form so-called restriction-modification systems. S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine. Folate-dependent ribothymidyl synthase Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase (FADH(2)-oxidizing) 5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH(2) = tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD. Unlike this enzyme, which uses 5,10-methylenetetrahydrofolate and FADH(2) to supply the atoms for methylation of U(54), EC 2.1.1.35 uses S-adenosyl-L-methionine. Up to 25% of the bases in mature tRNA are post-translationally modified or hypermodified. One almost universal post-translational modification is the conversion of U(54) (in the T-Psi-C loop) into ribothymidine (5-methyluridine), and this modification is found in most species studied to date. Flavonoid O-methyltransferase Apigenin 4'-O-methyltransferase Converts apigenin into acacetin. S-adenosyl-L-methionine + 5,7,4'-trihydroxyflavone = S-adenosyl-L-homocysteine + 4'-methoxy-5,7-dihydroxyflavone. Naringenin (5,7,4'-trihydroxyflavonone) can also act as acceptor, more slowly. Flavonol 3-O-methyltransferase Quercetin 3-O-methyltransferase Related enzymes bring about the 3-O-methylation of other flavonols, such as galangin and kaempferol. Specific for quercetin. S-adenosyl-L-methionine + 3,5,7,3',4'-pentahydroxyflavone = S-adenosyl-L-homocysteine + 3-methoxy-5,7,3',4'-tetrahydroxyflavone. Protein beta-aspartate O-methyltransferase Protein D-aspartate methyltransferase Protein-L-isoaspartate(D-aspartate) O-methyltransferase L-isoaspartyl protein carboxyl methyltransferase Protein L-isoaspartyl methyltransferase D-aspartate (but not L-aspartate) residues in proteins can also act as acceptors. S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester. Isoorientin 3'-O-methyltransferase Involved in the biosynthesis of flavones. S-adenosyl-L-methionine + isoorientin = S-adenosyl-L-homocysteine + isoscoparin. Also acts on isoorientin 2''-O-rhamnoside. Cyclopropane fatty acid synthase Unsaturated-phospholipid methyltransferase Cyclopropane-fatty-acyl-phospholipid synthase CFA synthase Cyclopropane synthetase S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid. Adds a methylene group across the 9,10 position of a Delta(9)-olefinic acyl chain in phosphatidylethanolamine or, more slowly, phosphatidylglycerol or phosphatidylinositol forming a cyclopropane derivative (cf. EC 2.1.1.16). Histamine N-methyltransferase S-adenosyl-L-methionine + histamine = S-adenosyl-L-homocysteine + N(tau)-methylhistamine. Protein-glutamate O-methyltransferase Methyl-accepting chemotaxis protein O-methyltransferase S-adenosyl-L-methionine + protein L-glutamate = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester. Forms ester groups with L-glutamate residues in a number of membrane proteins. 3-methylquercitin 7-O-methyltransferase 7-OMT 3-methylquercetin 7-O-methyltransferase Flavonol 7-O-methyltransferase Flavonol 7-methyltransferase Involved with EC 2.1.1.76 and EC 2.1.1.83 in the methylation of quercetin to 3,7,4'-trimethylquercetin in Chrysosplenium americanum. Does not act on flavones, dihydroflavonols, or their glucosides. S-adenosyl-L-methionine + 3',4',5,7-tetrahydroxy-3-methoxyflavone = S-adenosyl-L-homocysteine + 3',4',5-trihydroxy-3,7-dimethoxy-flavone. 4'-OMT 3,7-dimethylquercitin 4'-O-methyltransferase Flavonol 4'-methyltransferase Flavonol 4'-O-methyltransferase 3,7-dimethylquercetin 4'-O-methyltransferase Involved with EC 2.1.1.76 and EC 2.1.1.82 in the methylation of quercetin to 3,7,4'-trimethylquercetin in Chrysosplenium americanum. S-adenosyl-L-methionine + 3',4',5-trihydroxy-3,7-dimethoxyflavone = S-adenosyl-L-homocysteine + 3',5-dihydroxy-3,4',7-trimethoxy-flavone. 3,7-dimethylquercetagetin can also act as acceptor. Does not act on flavones, dihydroflavonols, or their glucosides. Methylquercetagetin 6-O-methyltransferase Flavonol 6-O-methyltransferase S-adenosyl-L-methionine + 3',4',5,6-tetrahydroxy-3,7-dimethoxyflavone = S-adenosyl-L-homocysteine + 3',4',5-trihydroxy-3,6,7-trimethoxyflavone. Does not act on flavones, dihydroflavonols, or their glucosides. The enzymes from Chrysosplenium americanum also methylates 3,7,3'-trimethylquercetagetin at the 6-position. Protein-histidine N-methyltransferase Protein methylase IV S-adenosyl-L-methionine + protein L-histidine = S-adenosyl-L-homocysteine + protein N(tau)-methyl-L-histidine. Highly specific for histidine residues, for example, in actin. N(5)-methyltetrahydromethanopterin--coenzyme M methyltransferase Tetrahydromethanopterin methyltransferase Tetrahydromethanopterin S-methyltransferase Involved in the formation of methane from CO in methanogenic archaea. 5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate = 5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate. Pyridine N-methyltransferase S-adenosyl-L-methionine + pyridine = S-adenosyl-L-homocysteine + N-methylpyridinium. Flavonol 8-O-methyltransferase 8-hydroxyquercetin 8-O-methyltransferase Also acts on 8-hydroxykaempferol, but not on the glycosides of 8-hydroxyflavonols. S-adenosyl-L-methionine + 3,3',4',5,7,8-hexahydroxyflavone = S-adenosyl-L-homocysteine + 3,3',4',5,7-pentahydroxy-8-methoxy-flavone. An enzyme from the flower buds of Lotus corniculatus. Tetrahydrocolumbamine 2-O-methyltransferase Involved in the biosynthesis of the berberine alkaloids. S-adenosyl-L-methionine + 5,8,13,13a-tetrahydrocolumbamine = S-adenosyl-L-homocysteine + tetrahydropalmatine. Thiol S-methyltransferase S-adenosyl-L-methionine + a thiol = S-adenosyl-L-homocysteine + a thioether. H(2)S and a variety of alkyl, aryl and heterocyclic thiols and hydroxy thiols can act as acceptors. Methanol--5-hydroxybenzimidazolylcobamide Co-methyltransferase Methanol + 5-hydroxybenzimidazolylcobamide = Co-methyl-Co-5-hydroxybenzimidazolylcob(I)amide + H(2)O. Inactivated by oxygen and other oxidizing agents, and reactivated by catalytic amounts of ATP and hydrogen. The enzyme from Methanosarcina barkeri contains 3-4 molecules of bound 5-hydroxybenzimidazolylcobamide which act as methyl acceptor. Aldoxime methyltransferase Isobutyraldoxime O-methyltransferase S-adenosyl-L-methionine + 2-methylpropanal oxime = S-adenosyl-L-homocysteine + 2-methylpropanal O-methyloxime. Oximes of C(4) to C(6) aldehydes can act as acceptors. The most active substrate is 2-methylbutyraldoxime. Bergaptol O-methyltransferase S-adenosyl-L-methionine + bergaptol = S-adenosyl-L-homocysteine + O-methylbergaptol. Xanthotoxol O-methyltransferase S-adenosyl-L-methionine + xanthotoxol = S-adenosyl-L-homocysteine + O-methylxanthotoxol. Also acts on 5-hydroxyxanthotoxin, forming isopimpinellin. 11-O-demethyl-17-O-deacetylvindoline O-methyltransferase S-adenosyl-L-methionine:11-O-demethyl-17-O-deacetylvindoline 11-O-methyltransferase 11-demethyl-17-deacetylvindoline 11-methyltransferase Tabersonine 16-O-methyltransferase S-adenosyl-L-methionine + 16-hydroxytabersonine = S-adenosyl-L-homocysteine + 16-methoxytabersonine. Involved in the biosynthesis of vindoline from tabersonine in the Madagascar periwinkle, Catharanthus roseus. Tocopherol O-methyltransferase S-adenosyl-L-methionine + gamma-tocopherol = S-adenosyl-L-homocysteine + alpha-tocopherol. Thioether S-methyltransferase S-adenosyl-L-methionine + dimethyl sulfide = S-adenosyl-L-homocysteine + trimethylsulfonium. Also acts on dimethyl selenide, dimethyl telluride, diethyl sulfide, 1,4-dithiane and many other thioethers. 3-hydroxyanthranilate 4-C-methyltransferase Involved in the biosynthesis of the antibiotic actinomycin in Streptomyces antibioticus. S-adenosyl-L-methionine + 3-hydroxyanthranilate = S-adenosyl-L-homocysteine + 3-hydroxy-4-methylanthranilate. Diphthine synthase S-adenosyl-L-methionine + 2-(3-carboxy-3-aminopropyl)-L-histidine = S-adenosyl-L-homocysteine + 2-(3-carboxy-3-(methylammonio)propyl)-L-histidine. 2-(3-carboxy-3-(methylammonio)propyl)-L-histidine and the corresponding dimethyl compound can also act as acceptors. The trimethylated product, diphthine, is converted into diphthamide by EC 6.3.2.22. NMT 3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase 16-methoxy-2,3-dihydro-3-hydroxytabersonine methyltransferase 16-methoxy-2,3-dihydro-3-hydroxytabersonine N-methyltransferase S-adenosyl-L-methionine:16-methoxy-2,3-dihydro-3-hydroxytabersonine N-methyltransferase Involved in the biosynthesis of vindoline from tabersonine in the Madagascar periwinkle Catharanthus roseus. S-adenosyl-L-methionine + 3-hydroxy-16-methoxy-2,3-dihydrotabersonine = S-adenosyl-L-homocysteine + deacetoxyvindoline. Hydroxymethyl-, formyl- and related transferases Serine hydroxymethyltransferase Threonine aldolase Serine aldolase Serine hydroxymethylase Glycine hydroxymethyltransferase Pyridoxal-phosphate 5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine. Also catalyzes the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine. Aminomethyltransferase Tetrahydrofolate aminomethyltransferase Glycine synthase Glycine-cleavage system T-protein The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. http://purl.uniprot.org/mim/605899 A component, with EC 1.4.4.2 and EC 1.8.1.4, of the glycine cleavage system, formerly known as glycine synthase. [Protein]-S(8)-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH(3). Ketopantoate hydroxymethyltransferase Alpha-ketoisovalerate hydroxymethyltransferase 3-methyl-2-oxobutanoate hydroxymethyltransferase Dehydropantoate hydroxymethyltransferase 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H(2)O = tetrahydrofolate + 2-dehydropantoate. GAR formyltransferase 5'-phosphoribosylglycinamide transformylase 5,10-methenyltetrahydrofolate:2-amino-N-ribosylacetamide ribonucleotide transformylase Phosphoribosylglycinamide formyltransferase 2-amino-N-ribosylacetamide 5'-phosphate transformylase GAR TFase GART GAR transformylase Glycinamide ribonucleotide transformylase 10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide. 5-amino-4-imidazolecarboxamide ribotide transformylase Aminoimidazolecarboxamide ribonucleotide transformylase AICAR transformylase 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase Phosphoribosylaminoimidazolecarboxamide formyltransferase 5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase 5-amino-4-imidazolecarboxamide ribonucleotide transformylase AICAR formyltransferase 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. http://purl.uniprot.org/mim/608688 FIG formiminotransferase Glycine formiminotransferase Glycine formimidoyltransferase Formiminoglycine formiminotransferase 5-formimidoyltetrahydrofolate + glycine = tetrahydrofolate + N-formimidoylglycine. Formiminoglutamic acid transferase Glutamate formyltransferase Formiminoglutamic formiminotransferase Glutamate formiminotransferase Glutamate formimidoyltransferase Pyridoxal-phosphate http://purl.uniprot.org/mim/229100 (1) 5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate. In eukaryotes occurs as a bifunctional enzyme also having EC 4.3.1.4 activity. (2) 5-formyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formyl-L-glutamate. D-alanine hydroxymethyltransferase D-alanine 2-hydroxymethyltransferase 2-methylserine hydroxymethyltransferase 5,10-methylenetetrahydrofolate + D-alanine + H(2)O = tetrahydrofolate + 2-methylserine. Also acts on 2-hydroxymethylserine. Deoxycytidylate hydroxymethylase dCMP hydroxymethylase Deoxycytidylate 5-hydroxymethyltransferase Deoxycytidylate hydroxymethyltransferase 5,10-methylenetetrahydrofolate + H(2)O + deoxycytidylate = tetrahydrofolate + 5-hydroxymethyldeoxycytidylate. Formylmethionyl-transfer ribonucleic synthetase Methionyl-tRNA Met formyltransferase Methionyl-transfer ribonucleic transformylase Methionyl-tRNA formyltransferase Methionyl ribonucleic formyltransferase Methionyl-transfer ribonucleate methyltransferase Methionyl-transfer RNA transformylase Methionyl-tRNA transformylase N(10)-formyltetrahydrofolic-methionyl-transfer ribonucleic transformylase 10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) + H(2)O = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). Carboxyl- and carbamoyltransferases Methylmalonyl-CoA carboxyltransferase Transcarboxylase Methylmalonyl-CoA carboxytransferase Zinc Biotin Cobalt (S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate. ATCase Carbamylaspartotranskinase Aspartate carbamoyltransferase Aspartate transcarbamylase Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate. OTCase OTC Citrulline phosphorylase Ornithine carbamoyltransferase Ornithine transcarbamylase http://purl.uniprot.org/mim/311250 The plant enzyme also catalyzes the reactions of EC 2.1.3.6, EC 2.7.2.2 and EC 3.5.3.12, thus acting as putrescine synthase, converting agmatine and ornithine into putrescine and citrulline respectively. Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline. Oxamic transcarbamylase Oxamate carbamoyltransferase Carbamoyl phosphate + oxamate = phosphate + oxalureate. Putrescine carbamoyltransferase Carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine. The plant enzyme also catalyzes the reactions of EC 2.1.3.3, EC 2.7.2.2 and EC 3.5.3.12, thus acting as putrescine synthase, converting agmatine and ornithine into putrescine and citrulline respectively. 3-hydroxymethylcephem carbamoyltransferase Activated by ATP. Carbamoyl phosphate + a 3-hydroxymethylceph-3-em-4-carboxylate = phosphate + a 3-carbamoyloxymethylcephem. Acts on a wide range of 3-hydroxymethylcephems (a subclass of the cephalosporin antibiotics). Lysine transcarbamylase Lysine carbamoyltransferase Not identical with EC 2.1.3.3. Carbamoyl phosphate + L-lysine = phosphate + L-homocitrulline. N-acetylornithine carbamoyltransferase AOTC N-acetylornithine transcarbamylase Acetylornithine transcarbamylase Carbamoyl phosphate + N(2)-acetyl-L-ornithine = phosphate + N-acetyl-L-citrulline. Differs from EC 2.1.3.3. This enzyme replaces EC 2.1.3.3 in the canonic arginine biosynthetic pathway of several eubacteria and has no catalytic activity with L-ornithine as substrate. Amidinotransferases L-arginine:glycine amidinotransferase Glycine amidinotransferase http://purl.uniprot.org/mim/602360 Canavanine can act instead of arginine. L-arginine + glycine = L-ornithine + guanidinoacetate. L-arginine:inosamine-P-amidinotransferase L-arginine:inosamine phosphate amidinotransferase Inosamine-phosphate amidinotransferase Scyllo-inosamine-4-phosphate amidinotransferase Inosamine-P amidinotransferase 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol 6-phosphate, streptamine phosphate and 2-deoxystreptamine phosphate can also act as acceptors. L-arginine + 1-amino-1-deoxy-scyllo-inositol 4-phosphate = L-ornithine + 1-guanidino-1-deoxy-scyllo-inositol 4-phosphate. Canavanine can act as donor. Transferring aldehyde or ketone residues Transketolases and transaldolases Transketolase Glycoaldehyde transferase Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO(2) and R-CHOH-CO-CH(2)OH. Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate. Thiamine diphosphate http://purl.uniprot.org/mim/277730 Transketolase from Alcaligenes faecalis shows high activity with D-erythrose as acceptor. Dihydroxyacetone transferase Transaldolase Glycerone transferase Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. http://purl.uniprot.org/mim/606003 Glycerone synthase Formaldehyde transketolase DHAS Dihydroxyacetone synthase Also converts hydroxypyruvate and formaldehyde into glycerone and CO(2). Thiamine diphosphate D-xylulose 5-phosphate + formaldehyde = glyceraldehyde 3-phosphate + glycerone. Not identical with EC 2.2.1.1. Acetoin--ribose-5-phosphate transaldolase 1-deoxy-D-altro-heptulose-7-phosphate synthetase 3-hydroxybutan-2-one + D-ribose 5-phosphate = acetaldehyde + 1-deoxy-D-altro-heptulose 7-phosphate. Thiamine diphosphate 2-hydroxy-3-oxoadipate glyoxylate-lyase (carboxylating) 2-hydroxy-3-oxoadipate synthase Oxoglutarate: glyoxylate carboligase Alpha-ketoglutaric-glyoxylic carboligase 2-hydroxy-3-oxoadipate synthetase 2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO(2). The product decarboxylates to 5-hydroxy-4-oxopentanoate. The enzyme can decarboxylate 2-oxoglutarate. Acetaldehyde can replace glyoxylate. Thiamine diphosphate Acetohydroxy acid synthetase Alpha-acetohydroxy acid synthetase Acetolactate synthase Acetolactic synthetase Acetohydroxyacid synthase Alpha-acetohydroxyacid synthase Alpha-acetolactate synthase Acetolactate pyruvate-lyase (carboxylating) Alpha-acetolactate synthetase The enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine. The reaction shown is in the pathway of biosynthesis of valine. 2 pyruvate = 2-acetolactate + CO(2). Thiamine diphosphate DXP-synthase 1-deoxy-D-xylulose-5-phosphate pyruvate-lyase (carboxylating) 1-deoxyxylulose-5-phosphate synthase 1-deoxy-D-xylulose-5-phosphate synthase Thiamine diphosphate The enzyme forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO(2). Fluorothreonine transaldolase Unlike EC 2.1.2.1 does not use glycine as a substrate. Can also convert chloroacetaldehyde into 4-chloro-L-threonine. L-threonine + fluoroacetaldehyde = acetaldehyde + 4-fluoro-L-threonine. Pyridoxal-phosphate Acyltransferases Transferring groups other than amino-acyl groups N-acetylglutamate synthase Amino-acid N-acetyltransferase Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. Also acts with L-aspartate and, more slowly, with some other amino acids. http://purl.uniprot.org/mim/237310 Hydrogen-sulfide S-acetyltransferase Acetyl-CoA + H(2)S = CoA + thioacetate. [Myelin-proteolipid] O-palmitoyltransferase Acyl-protein synthase Myelin PLP acyltransferase Palmitoyl-CoA + [myelin proteolipid] = CoA + O-palmitoyl-[myelin proteolipid]. The enzyme in brain transfers long-chain acyl residues to the endogenous myelin proteolipid. Formylmethanofuran--tetrahydromethanopterin N-formyltransferase Methanofuran is a complex 4-substituted furfurylamine and is involved in the formation of methane from CO(2) in Methanobacterium thermoautotrophicum. Formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin. N(6)-hydroxylysine O-acetyltransferase N(6)-hydroxylysine acetylase Involved in the synthesis of aerobactin from lysine in a strain of Escherichia coli. Acetyl-CoA + N(6)-hydroxy-L-lysine = CoA + N(6)-acetyl-N(6)-hydroxy-L-lysine. Sinapoylglucose--sinapoylglucose O-sinapoyltransferase 2 1-O-sinapoyl beta-D-glucoside = D-glucose + 1,2-bis-O-sinapoyl beta-D-glucoside. 1-alkenylglycerophosphocholine O-acyltransferase Acyl-CoA + 1-alkenylglycerophosphocholine = CoA + 1-alkenyl-2-acylglycerophosphocholine. Not identical with EC 2.3.1.121. Alkylglycerophosphate 2-O-acetyltransferase Involved in the biosynthesis of thrombocyte activating factor in animal tissues. Acetyl-CoA + 1-alkyl-sn-glycero-3-phosphate = CoA + 1-alkyl-2-acetyl-sn-glycero-3-phosphate. Tartronate sinapoyltransferase Hydroxycinnamoyl-coenzyme-A:tartronate hydroxycinnamoyltransferase Tartronate O-hydroxycinnamoyltransferase 4-coumaroyl-CoA (4-hydroxycinnamoyl-CoA), caffeoyl-CoA (3,4-dihydroxycinnamoyl-CoA) and feruloyl-CoA (4-hydroxy-3-methoxycinnamoyl-CoA) can also act as donors for the enzyme from the mung bean (Vigna radiata). Sinapoyl-CoA + 2-hydroxymalonate = CoA + sinapoyltartronate. Acetyl-CoA-17-O-deacetylvindoline 17-O-acetyltransferase Acetylcoenzyme A:deacetylvindoline 4-O-acetyltransferase Acetylcoenzyme A-deacetylvindoline 4-O-acetyltransferase DAT Deacetylvindoline acetyltransferase 17-O-deacetylvindoline O-acetyltransferase Acetylcoenzyme A:deacetylvindoline O-acetyltransferase Deacetylvindoline O-acetyltransferase Acetyl-CoA:17-O-deacetylvindoline 17-O-acetyltransferase 17-O-deacetylvindoline-17-O-acetyltransferase Acetyl-CoA + deacetylvindoline = CoA + vindoline. Catalyzes the final step in the biosynthesis of vindoline from tabersonine in the Madagascar periwinkle, Catharanthus roseus. TAT Alpha-tubulin acetylase Tubulin N-acetyltransferase Alpha-tubulin N-acetyltransferase Alpha-tubulin acetyltransferase Tubulin acetyltransferase The enzyme from Chlamydomonas flagella also acetylates mammalian brain alpha-tubulin. Acetyl-CoA + [alpha-tubulin]-L-lysine = CoA + [alpha-tubulin]-N(6)-acetyl-L-lysine. Arginine succinyltransferase AST Arginine and ornithine N(2)-succinyltransferase AOST Arginine N-succinyltransferase This is the first enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine. Also acts on L-ornithine. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. Succinyl-CoA + L-arginine = CoA + N(2)-succinyl-L-arginine. The five enzymes involved in this pathway are EC 2.3.1.109, EC 3.5.3.23, EC 2.6.1.81, EC 1.2.1.71 and EC 3.5.1.96. Thioethanolamine acetyltransferase Thioltransacetylase B Thioethanolamine S-acetyltransferase Acetyl-CoA + 2-aminoethanethiol = CoA + S-(2-aminoethyl)thioacetate. 2-sulfanylethanol (2-mercaptoethanol) can act as a substrate. Tyramine N-feruloyltransferase Feruloyl-CoA + tyramine = CoA + N-feruloyltyramine. Cinnamoyl-CoA, 4-coumaroyl-CoA and sinapoyl-CoA can also act as donors. Some aromatic amines can act as acceptors. Mycocerosate synthase Elongates CoA esters of fatty acids from C(6) to C(20) by incorporation of methylmalonyl, but not malonyl, residues, to form multimethyl-branched fatty-acyl-CoA such as 2,4,6,8-tetramethyl-octosanoyl-CoA. Acyl-CoA + n methylmalonyl-CoA + 2n NADPH = multi-methyl-branched acyl-CoA + n CoA + n CO(2) + 2n NADP(+). D-tryptophan N-malonyltransferase 1-aminocyclopropane-1-carboxylate can act instead of malonyl-CoA. Malonyl-CoA + D-tryptophan = CoA + N(2)-malonyl-D-tryptophan. Anthranilate N-malonyltransferase Malonyl-CoA + anthranilate = CoA + N-malonylanthranilate. 3,4-dichloroaniline N-malonyltransferase Malonyl-CoA + 3,4-dichloroaniline = CoA + N-(3,4-dichlorophenyl)-malonamate. Flavone/flavonol 7-O-beta-D-glucoside malonyltransferase Isoflavone-7-O-beta-glucoside 6''-O-malonyltransferase The 6-position of the glucose residue of formononetin can also act as acceptor; some other 7-O-glucosides of isoflavones, flavones and flavonols can also act, but more slowly. Malonyl-CoA + biochanin A 7-O-beta-D-glucoside = CoA + biochanin A 7-O-(6-O-malonyl-beta-D-glucoside). Flavonol-3-O-beta-glucoside O-malonyltransferase Malonyl-CoA + flavonol 3-O-beta-D-glucoside = CoA + flavonol 3-O-(6-O-malonyl-beta-D-glucoside). Tetrahydrodipicolinate N-succinyltransferase Succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase Tetrahydrodipicolinate succinylase Tetrahydrodipicolinate succinyltransferase 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate. Involved in the biosynthesis of lysine in bacteria, cyanobacteria and higher plants. Earlier erroneously called 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase. N-hydroxyarylamine O-acetyltransferase Arylamine N-acetyltransferase Arylhydroxamate N,O-acetyltransferase Acetyl-CoA + an N-hydroxyarylamine = CoA + an N-acetoxyarylamine. The enzyme from liver, but not that from bacteria, can also catalyze N-acetylation of arylamines and N,O-acetylation of arylhydroxamates. Acyl-CoA elongase Icosanoyl-CoA synthase Stearoyl-CoA + malonyl-CoA + 2 NAD(P)H = icosanoyl-CoA + CO(2) + 2 NAD(P)(+). Icosanoyl-CoA can act in place of stearoyl-CoA. The membrane enzyme brings about the elongation of these long-chain fatty-acyl-CoAs. Lipoic transacetylase Lipoic acetyltransferase Acetyl-CoA:dihydrolipoamide S-acetyltransferase Dihydrolipoic transacetylase Lipoylacetyltransferase Dihydrolipoate acetyltransferase Dihydrolipoyl acetyltransferase Transacetylase X Thioltransacetylase A Dihydrolipoyllysine-residue acetyltransferase Lipoate acetyltransferase Lipoic acid acetyltransferase Lipoate transacetylase Dihydrolipoamide S-acetyltransferase A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1 and EC 1.8.1.4. The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalyzed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A. Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. 1-alkenylglycerophosphoethanolamine O-acyltransferase Not identical with EC 2.3.1.104. Acyl-CoA + 1-alkenylglycerophosphoethanolamine = CoA + 1-alkenyl-2-acylglycerophosphoethanolamine. Long-chain unsaturated acyl-CoAs are the best substrates. Trehalose O-mycolyltransferase Trehalose 6-palmitate can also act as donor. 2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose + alpha,alpha'-trehalose 6,6'-bismycolate. Catalyzes the exchange of mycolic acid between trehalose, trehalose mycolate and trehalose bismycolate. Dolichol O-acyltransferase Alpha-saturated dolichols are acylated more rapidly than the alpha-unsaturated analogs. Palmitoyl-CoA + dolichol = CoA + dolichyl palmitate. Other acyl-CoAs can act, more slowly. 1-hexadecyl-2-acetylglycerol acyltransferase 1-alkyl-2-acetylglycerol O-acyltransferase A number of acyl-CoAs can act as acyl donor; maximum activity is obtained with linoleoyl-CoA. Acyl-CoA + 1-O-alkyl-2-acetyl-sn-glycerol = CoA + 1-O-alkyl-2-acetyl-3-acyl-sn-glycerol. Not identical with EC 2.3.1.20. Isocitrate O-dihydroxycinnamoyltransferase Feruloyl-CoA and 4-coumaroyl-CoA can also act as donors. Caffeoyl-CoA + isocitrate = CoA + 2-caffeoylisocitrate. Ornithine N-benzoyltransferase 2 benzoyl-CoA + L-ornithine = 2 CoA + N(2),N(5)-dibenzoyl-L-ornithine. Ribosomal-protein-alanine N-acetyltransferase A groups of enzymes in Escherichia coli that acetylate the N-terminal alanine residues of specific ribosomal proteins (cf. EC 2.3.1.88). Acetyl-CoA + ribosomal-protein L-alanine = CoA + ribosomal-protein N-acetyl-L-alanine. UDP-N-acetylglucosamine acyltransferase Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase Acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase Involved with EC 2.4.1.182 and EC 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Escherichia coli. (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetylglucosamine = [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine. Glycine N-acyltransferase Not identical with EC 2.3.1.68 or EC 2.3.1.71. Acyl-CoA + glycine = CoA + N-acylglycine. The CoA derivatives of a number of aliphatic and aromatic acids, but not phenylacetyl-CoA or (indol-3-yl)acetyl-CoA, can act as donor. Galactarate O-hydroxycinnamoyltransferase Feruloyl-CoA + galactarate = CoA + O-feruloylgalactarate. Sinapoyl-CoA and 4-coumaroyl-CoA can also act as donors. Glucarate O-hydroxycinnamoyltransferase 4-coumaroyl-CoA, feruloyl-CoA and caffeoyl-CoA can also act as donors, more slowly. Sinapoyl-CoA + glucarate = CoA + O-sinapoylglucarate. Glucarolactone O-hydroxycinnamoyltransferase Sinapoyl-CoA + glucarolactone = CoA + O-sinapoylglucarolactone. 4-coumaroyl-CoA, feruloyl-CoA and caffeoyl-CoA can also act as donors, more slowly. Shikimate O-hydroxycinnamoyltransferase Caffeoyl-CoA, feruloyl-CoA and sinapoyl-CoA can also act as donors, more slowly. 4-coumaroyl-CoA + shikimate = CoA + 4-coumaroylshikimate. Galactolipid:galactolipid acyltransferase Galactolipid O-acyltransferase 2 mono-beta-D-galactosyldiacylglycerol = acylmono-beta-D-galactosyldiacylglycerol + mono-beta-D-galactosylacylglycerol. Di-D-galactosyldiacylglycerol can also act as acceptor. Phosphatidylcholine--retinol O-acyltransferase Lecithin--retinol acyltransferase http://purl.uniprot.org/mim/604863 Specific for transfer of the sn-1-acyl residue of phosphatidylcholine. Phosphatidylcholine + retinol--[cellular-retinol-binding-protein] = 2-acylglycerophosphocholine + retinyl-ester--[cellular-retinol-binding-protein]. Polysialic-acid O-acetyltransferase Catalyzes the modification of capsular polysaccharides in some strains of Escherichia coli. Acts only on substrates containing more than 14 sialosyl residues. Acetyl-CoA + an alpha-2,8-linked polymer of sialic acid = CoA + polysialic acid acetylated at O-7 or O-9. Carnitine O-octanoyltransferase Octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine. Cf. EC 2.3.1.7 and EC 2.3.1.21. Acts on a range of acyl-CoAs, with optimal activity with C(6) or C(8) acyl groups. Putrescine N-hydroxycinnamoyltransferase Caffeoyl-CoA + putrescine = CoA + N-caffeoylputrescine. Feruloyl-CoA, cinnamoyl-CoA and sinapoyl-CoA can also act as donors, more slowly. Ecdysone O-acyltransferase Palmitoyl-CoA + ecdysone = CoA + ecdysone palmitate. Glutamine N-phenylacetyltransferase Phenylacetyl-CoA + L-glutamine = CoA + alpha-N-phenylacetyl-L-glutamine. Rosmarinate synthase Involved with EC 1.1.1.237 in the biosynthesis of rosmarinic acid. Caffeoyl-CoA + 3-(3,4-dihydroxyphenyl)lactate = CoA + rosmarinate. Galactosylacylglycerol O-acyltransferase Transfers long-chain acyl groups to the sn-1 position of the glycerol residues. Acyl-[acyl-carrier-protein] + sn-3-D-galactosyl-sn-2-acylglycerol = [acyl-carrier-protein] + D-galactosyldiacylglycerol. Glycoprotein O-fatty-acyltransferase Palmitoyl-CoA + mucus glycoprotein = CoA + O-palmitoylglycoprotein. Beta-glucogallin--tetrakisgalloylglucose O-galloyltransferase 1-O-galloyl-beta-D-glucose + 1,2,3,6-tetrakis-O-galloyl-beta-D-glucose = D-glucose + 1,2,3,4,6-pentakis-O-galloyl-beta-D-glucose. Anthranilate N-benzoyltransferase Involved in the biosynthesis of phytoalexins. Benzoyl-CoA + anthranilate = CoA + N-benzoylanthranilate. Cinnamoyl-CoA, 4-coumaroyl-CoA and salicyloyl-CoA can act as donors, more slowly. Piperidine N-piperoyltransferase (E,E)-piperoyl-CoA + piperidine = CoA + N-((E,E)-piperoyl)-piperidine. Pyrrolidine and 3-pyrroline can also act as acceptors, more slowly. Stilbene synthase Pinosylvin synthase 3 malonyl-CoA + cinnamoyl-CoA = 4 CoA + pinosylvin + 4 CO(2). Not identical with EC 2.3.1.74 or EC 2.3.1.95. Glycerophospholipid arachidonoyl-transferase (CoA-independent) The organyl group on sn-1 of the donor or acceptor molecule can be alkyl, acyl or alk-1-enyl. 1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine = 1-organyl-2-arachidonoyl-sn-glycero-3-phosphoethanolamine + 1-organyl-2-lyso-sn-glycero-3-phosphocholine. Catalyzes the transfer of arachidonate and other polyenoic fatty acids from intact choline or ethanolamine-containing glycerophospholipids to the sn-2 position of a lyso-glycerophospholipid. Differs from EC 2.3.1.148 in not requiring CoA and in its specificity for poly-unsaturated acyl groups. The term 'radyl' has sometimes been used to refer to such substituting groups. Glycerophospholipid acyltransferase (CoA-dependent) Catalyzes the transfer of fatty acids from intact choline-or ethanolamine-containing glycerophospholipids to the sn-2 position of a lyso-glycerophospholipid. 1-organyl-2-acyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine = 1-organyl-2-acyl-sn-glycero-3-phosphoethanolamine + 1-organyl-2-lyso-sn-glycero-3-phosphocholine. The term 'radyl' has sometimes been used to refer to such substituting groups. The organyl group on sn-1 of the donor or acceptor molecule can be alkyl, acyl or alk-1-enyl. Coenzyme-A Differs from EC 2.3.1.147 in requiring CoA and not favoring the transfer of polyunsaturated acyl groups. PAF acetyltransferase Platelet-activating factor acetyltransferase 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phospholipid = 1-organyl-2-lyso-sn-glycero-3-phosphocholine + 1-alkyl-2-acetyl-sn-glycero-3-phospholipid. Catalyzes the transfer of the acetyl group from 1-alkyl-2-acyl-sn-glycero-3-phosphocholine (platelet-activating factor) to the sn-2 position of lyso-glycerophospholipids containing ethanolamine, choline, serine, inositol or phosphate groups at the sn-3 position as well as to sphingosine and long-chain fatty alcohols. The organyl group can be alkyl, acyl or alk-1-enyl (sometimes also collectively referred to as 'radyl'). Glycerol-3-phosphate O-acyltransferase Acyl-[acyl-carrier-protein] can also act as acyl donor. Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate. Acts only with derivatives of fatty acids of chain length above C(10). Salutaridinol 7-O-acetyltransferase From the opium poppy plant, Papaver somniferum. Acetyl-CoA + salutaridinol = CoA + 7-O-acetylsalutaridinol. At higher pH values the product, 7-O-acetylsalutaridinol, spontaneously closes the 4->5 oxide bridge by allylic elimination to form the morphine precursor thebaine. Benzophenone synthase 3 malonyl-CoA + 3-hydroxybenzoyl-CoA = 4 CoA + 2,3',4,6-tetrahydroxybenzophenone + 3 CO(2). Involved in the biosynthesis of plant xanthomes. Benzoyl-CoA can replace 3-hydroxybenzoyl-CoA. Alcohol O-cinnamoyltransferase Acceptor alcohols (ROH) include methanol, ethanol and propanol. No cofactors are required as 1-O-trans-cinnamoyl-beta-D-glucopyranose itself is an 'energy-rich' (activated) acyl-donor, comparable to CoA-thioesters. 1-O-trans-cinnamoyl-beta-D-gentobiose can also act as the acyl donor, but with much less affinity. 1-O-trans-cinnamoyl-beta-D-glucopyranose + ROH = alkyl cinnamate + glucose. Anthocyanin 5-aromatic acyltransferase Hydroxycinnamoyl-CoA + anthocyanidin-3,5-diglucoside = CoA + anthocyanidin 3-glucoside-5-hydroxycinnamoylglucoside. Malonyl-CoA cannot act as a donor. Transfers the hydroxycinnamoyl group only to the C-5 glucoside of anthocyanin. 3-oxopristanoyl-CoA hydrolase 3-oxopristanoyl-CoA thiolase Propionyl-CoA C(2)-trimethyltridecanoyltransferase It also acts on 3-oxopalmitoyl-CoA as a substrate but differs from EC 2.3.1.16 which has little activity toward the 3-oxoacyl-CoA esters of 2-methyl-branched chain fatty acids such as 3-oxopristanoyl-CoA. 4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = 3-oxopristanoyl-CoA + CoA. The peroxisomal protein sterol carrier protein X (SCPx) combines this thiolase activity with its carrier function, and is involved in branched chain fatty acid beta-oxidation in peroxisomes. 3-oxopalmitoyl-CoA-CoA acetyltransferase Acetyl-CoA C-myristoyltransferase Myristoyl-CoA C-acetyltransferase 3-oxopalmitoyl-CoA hydrolase A peroxisomal enzyme involved in branched chain fatty acid beta-oxidation in peroxisomes. It differs from EC 2.3.1.154 in not being active toward 3-oxopristanoyl-CoA. Myristoyl-CoA + acetyl-CoA = 3-oxopalmitoyl-CoA + CoA. Valerophenone synthase 3-methyl-1-(trihydroxyphenyl)butan-1-one synthase Phloroisovalerophenone synthase The product, 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one, is phloroisovalerophenone. Also acts on isobutyryl-CoA as substrate to give phlorisobutyrophenone. Isovaleryl-CoA + 3 malonyl-CoA = 4 CoASH + 3 CO(2) + 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one. The products are intermediates in the biosynthesis of the bitter (alpha) acids in hops (Humulus lupulus). Closely related to EC 2.3.1.74. Glucosamine-1-phosphate N-acetyltransferase Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. The enzyme from several bacteria has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23. Phospholipid:diacylglycerol acyltransferase PDAT Phospholipid + 1,2-diacylglycerol = lysophospholipid + triacylglycerol. The enzyme from the yeast Saccharomyces cerevisiae specifically transfers acyl groups from the sn-2 position of the phospholipid to diacylglycerol, thus forming an sn-1-lysophospholipid. This enzyme differs from EC 2.3.1.20 by synthesising triacylglycerol using an acyl-CoA-independent mechanism. The specificity of the enzyme for the acyl group in the phospholipid varies with species, e.g., the enzyme from castor bean (Ricinus communis) preferentially incorporates vernoloyl (12,13-epoxyoctadec-9-enoyl) groups into triacylglycerol, whereas that from the hawk's beard (Crepis palaestina) incorporates both ricinoleoyl (12-hydroxyoctadec-9-enoyl) and vernoloyl groups. Acridone synthase 3 malonyl-CoA + N-methylanthraniloyl-CoA = 4 CoA + 1,3-dihydroxy-N-methylacridone + 3 CO(2). Beta-ketothiolase 3-ketoacyl-CoA thiolase Acetyl-CoA C-acyltransferase Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. http://purl.uniprot.org/mim/609015 Vinorine synthase Generates the ajmalan skeleton, which forms part of the route to ajmaline. This alcohol is then acetylated. Also acts on gardneral (11-methoxy-16-epivellosimine). Acetyl-CoA + 16-epivellosimine = CoA + vinorine. The reaction proceeds in two stages. The indole nitrogen of 16-epivellosimine interacts with its aldehyde group giving an hydroxy-substituted new ring. Lovastatin nonaketide synthase Acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine = dihydromonacolin L + 9 CoA + 8 CO(2) + 11 NADP(+) + S-adenosyl-L-homocysteine + 6 H(2)O. The microbial enzyme is a multi-functional protein catalyzing many of the chain building reactions of EC 2.3.1.85 as well as a reductive methylation and a Diels-Alder reaction. Taxadien-5-alpha-ol O-acetyltransferase Taxadienol acetyltransferase Acetyl coenzyme A:taxa-4(20),11(12)-dien-5-alpha-ol O-acetyl transferase Taxa-4(20),11(12)-dien-5alpha-ol-O-acetyltransferase Acetyl-CoA + taxa-4(20),11-dien-5-alpha-ol = CoA + taxa-4(20),11-dien-5-alpha-yl acetate. Acetyl coenzyme A:10-hydroxytaxane O-acetyltransferase 10-hydroxytaxane O-acetyltransferase Acetyl-CoA + 10-desacetyltaxuyunnanin C = CoA + taxuyunnanin C. May be identical to EC 2.3.1.167. Acts on a number of related taxane diterpenoids with a free 10-beta-hydroxy group. Isopenicillin N:acyl-CoA acyltransferase Isopenicillin-N N-acyltransferase Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase Acyl-coenzyme A:isopenicillin N acyltransferase Different from EC 3.5.1.11. Proceeds by a two stage mechanism via 6-aminopenicillanic acid. Phenylacetyl-CoA + isopenicillin N + H(2)O = CoA + penicillin G + L-2-aminohexanedioate. 6-methylsalicylic acid synthase 6-MSAS MSAS A multienzyme complex with a 4'-phosphopantetheine prosthetic group on the acyl carrier protein. Acetyl-CoA + 3 malonyl-CoA + NADPH = 6-methylsalicylate + 4 CoA + 3 CO(2) + NADP(+). It has a similar sequence to vertebrate type I fatty acid synthase. Acetoacetyl-CoA can also act as a starter molecule. 2-alpha-hydroxytaxane 2-O-benzoyltransferase 2-debenzoyl-7,13-diacetylbaccatin III-2-O-benzoyl transferase Benzoyl-CoA:taxane 2-alpha-O-benzoyltransferase It will not acylate the hydroxy group at 1-beta, 7-beta, 10-beta or 13-alpha of 10-deacetylbaccatin III, or at 2-alpha or 5-alpha of taxa-4(20),11-diene-2-alpha,5-alpha-diol. Benzoyl-CoA + 10-deacetyl-2-debenzoylbaccatin III = CoA + 10-deacetylbaccatin III. The enzyme was studied using the semisynthetic substrate 2-debenzoyl-7,13-diacetylbaccatin III. 10-deacetylbaccatin III 10-O-acetyltransferase May be identical to EC 2.3.1.163. Acetyl-CoA + 10-deacetylbaccatin III = CoA + baccatin III. The enzyme will not acylate the hydroxy group at 1-beta, 7-beta, 13-alpha of 10-deacetylbaccatin III, or at 5-alpha of taxa-4(20), 11-dien-5-alpha-ol. Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase Dihydrolipoyl transacylase In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine. A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4 and EC 1.8.1.4. http://purl.uniprot.org/mim/248600 The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalyzed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A. 2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine. CO-methylating acetyl-CoA synthase ACS Also catalyzes exchange reactions of carbon between C-1 of acetyl-CoA and CO, and between C-2 of acetyl-CoA and methyl corrinoid protein. To follow its stoichiometry, the reaction can be written as: CH(3)-CO-S-CoA + protein Co(+) + H(+) = CO + protein Co(2+)-CH(3) + HS-CoA. Acetyl-CoA + corrinoid protein = CO + methylcorrinoid protein + CoA. Involved, together with EC 1.2.7.4, in the synthesis of acetyl-CoA from CO(2) and H(2). Iron-sulfur Nickel Aspartate N-acetyltransferase Acetyl-CoA + L-aspartate = CoA + N-acetyl-L-aspartate. 6'-deoxychalcone synthase Isoliquiritigenin is the precursor of liquiritigenin, a 5-deoxyflavanone. 3 malonyl-CoA + 4-coumaroyl-CoA + NADPH = 4 CoA + isoliquiritigenin + 3 CO(2) + NADP(+) + H(2)O. Malonyl-coenzymeA:anthocyanidin-3-O-beta-D-glucoside 6''-O-malonyltransferase Anthocyanin 6''-O-malonyltransferase 3MaT Acts on pelargonidin 3-O-glucoside in dahlia (Dahlia variabilis), delphinidin 3-O-glucoside, and on cyanidin 3-O-glucoside in transgenic petunia (Petunia hybrida). Malonyl-CoA + an anthocyanidin 3-O-beta-D-glucoside = CoA + an anthocyanidin 3-O-(6-O-malonyl-beta-D-glucoside). Anthocyanin 5-O-glucoside 6'''-O-malonyltransferase Ss5MaT1 Malonyl-CoA + pelargonidin 3-O-(6-caffeoyl-beta-D-glucoside) 5-O-beta-D-glucoside = CoA + 4'''-demalonylsalvianin. Specific for the penultimate step in salvianin biosynthesis. The enzyme also catalyzes the malonylation of shisonin to malonylshisonin (cyanidin 3-O-(6''-O-p-coumaryl-beta-D-glucoside)-5-(6'''-O-malonyl-beta-D-glucoside)). The compounds 4'''-demalonylsalvianin, salvianin, pelargonidin 3,5-diglucoside and delphinidin 3,5-diglucoside cannot act as substrates. Flavonol-3-O-triglucoside O-coumaroyltransferase Acylates kaempferol 3-O-triglucoside on the terminal glucosyl unit, almost certainly at C-6. 4-coumaroyl-CoA + a flavonol 3-O-(beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside) = CoA + a flavonol 3-O-(6-(4-coumaroyl)-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside). 3-oxoadipyl-CoA thiolase Succinyl-CoA + acetyl-CoA = CoA + 3-oxoadipyl-CoA. CPC acetylhydrolase Acetyl-CoA:DAC acetyltransferase Acetyl coenzyme A:DAC acetyltransferase DAC-AT DAC acetyltransferase Deacetylcephalosporin-C acetyltransferase Deacetylcephalosporin C acetyltransferase Acetyl-CoA + deacetylcephalosporin C = CoA + cephalosporin C. This enzyme catalyzes the final step in the biosynthesis of cephalosporin C. PTE-2 SCP(chi) SCP-X Sterol carrier protein-X Propanoyl-CoA C-acyltransferase Peroxisomal thiolase 2 Sterol carrier protein-chi 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3-alpha,7-alpha,12-alpha-trihydroxy-24-oxo-5-beta-cholestanoyl-CoA. Catalyzes the penultimate step in the formation of bile acids. Also acts on dihydroxy-5-beta-cholestanoyl-CoA and other branched chain acyl-CoA derivatives. The bile acid moiety is transferred from the acyl-CoA thioester (RCO-SCoA) to either glycine or taurine (NH(2)R') by EC 2.3.1.65. BIS Biphenyl synthase 2-hydroxybenzoyl-CoA can also act as substrate but it leads to the derailment product 2-hydroxybenzoyltriacetic acid lactone. Uses the same starter substrate as EC 2.3.1.151. 3 malonyl-CoA + benzoyl-CoA = 4 CoA + 3,5-dihydroxybiphenyl + 4 CO(2). A polyketide synthase that is involved in the production of the phytoalexin aucuparin. DABA acetyltransferase DABAcT Diaminobutyrate acetyltransferase 2,4-diaminobutanoate acetyltransferase DAB acetyltransferase Diaminobutyric acid acetyltransferase L-2,4-diaminobutyrate acetyltransferase L-2,4-diaminobutanoate acetyltransferase Ornithine, lysine, aspartate, and alpha-, beta-and gamma-aminobutanoate cannot act as substrates. Acetyl-CoA + L-2,4-diaminobutanoate = CoA + N(4)-acetyl-L-2,4-diaminobutanoate. Sodium or potassium Forms part of the ectoine biosynthesis pathway, the other enzymes involved being EC 2.6.1.76 and EC 4.2.1.108. However, acetyl-CoA can be replaced by propanoyl-CoA, although the reaction proceeds more slowly. KASII 3-oxoacyl-acyl carrier protein synthase I Beta-ketoacyl-ACP synthase II KAS II Beta-ketoacyl-acyl-carrier-protein synthase II The fatty-acid composition of Escherichia coli changes as a function of growth temperature, with the proportion of unsaturated fatty acids increasing with lower growth temperature. While the substrate specificity of this enzyme is very similar to that of EC 2.3.1.41, it differs in that palmitoleoyl-ACP is not a good substrate of EC 2.3.1.41 but is an excellent substrate of this enzyme. Controls the temperature-dependent regulation of fatty-acid composition, with mutants lacking this acivity being deficient in the elongation of palmitoleate to cis-vaccenate at low temperatures. (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]. Involved in the dissociated (or type II) fatty acid biosynthesis system that occurs in plants and bacteria. Thiogalactoside acetyltransferase Galactoside O-acetyltransferase Acts on thiogalactosides and phenylgalactoside. Acetyl-CoA + a beta-D-galactoside = CoA + a 6-acetyl-beta-D-galactoside. Beta-ketoacyl-ACP synthase III Beta-ketoacyl-acyl-carrier-protein synthase III Beta-ketoacyl (acyl carrier protein) synthase III 3-ketoacyl-acyl carrier protein synthase III 3-oxoacyl:ACP synthase III Beta-ketoacyl-acyl carrier protein synthase III KAS III KASIII Involved in the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria. Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacyl-[acyl-carrier-protein] + CoA + CO(2). Responsible for initiating both straight-and branched-chain fatty-acid biosynthesis, with the substrate specificity in an organism reflecting the fatty-acid composition found in that organism. In contrast to EC 2.3.1.41 and EC 2.3.1.179, this enzyme specifically uses CoA thioesters rather than acyl-ACP as the primer. For example, Streptococcus pneumoniae, a Gram-positive bacterium, is able to use both straight-and branched-chain (C4--C6) acyl-CoA primers whereas Escherichia coli, a Gram-negative organism, uses primarily short straight-chain acyl CoAs, with a preference for acetyl-CoA. In addition to the above reaction, the enzyme can also catalyze the reaction of EC 2.3.1.38, but to a much lesser extent. Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase Lipoyltransferase Lipoyl (octanoyl)-[acyl-carrier-protein]-protein N-lipoyltransferase Lipoyl(octanoyl) transferase Lipoate/octanoate transferase Lipoyl(octanoyl)transferase An alternative lipoylation pathway involves EC 2.7.7.63, which can lipoylate apoproteins using exogenous lipoic acid (or its analogs). The lipoyl cofactor is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. The first committed step in the biosynthesis of lipoyl cofactor. The other enzyme involved in the biosynthesis of lipoyl cofactor is EC 2.8.1.8. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the true substrate. Examples of such lipoylated proteins include pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein). Octanoyl-[acyl-carrier-protein] + protein = protein N(6)-(octanoyl)lysine + acyl carrier protein. Phosphate butyryltransferase Phosphotransbutyrylase Butanoyl-CoA + phosphate = CoA + butanoylphosphate. Imidazole N-acetyltransferase Imidazole acetylase Acetyl-CoA + imidazole = CoA + N-acetylimidazole. Also acts with propanoyl-CoA. Diacylglycerol O-acyltransferase Diglyceride acyltransferase Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors. Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol. Carnitine O-palmitoyltransferase http://purl.uniprot.org/mim/255120 http://purl.uniprot.org/mim/255110 http://purl.uniprot.org/mim/600649 Palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine. http://purl.uniprot.org/mim/608836 Broad specificity to acyl group, over the range C(8) to C(18); optimal activity with palmitoyl-CoA (cf. EC 2.3.1.7 and EC 2.3.1.137). Acylglycerol palmitoyltransferase Monoglyceride acyltransferase 2-acylglycerol O-acyltransferase Various 2-acylglycerols can act as acceptor. Acyl-CoA + 2-acylglycerol = CoA + diacylglycerol. The sn-1 position and the sn-3 position are both acylated, at about the same rate. Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors. 1-acylglycerophosphocholine O-acyltransferase Lysolecithin acyltransferase Acts preferentially with unsaturated acyl-CoA derivatives. 1-acyl-sn-glycero-3-phosphoinositol can also act as acceptor. Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine. Sphingosine N-acyltransferase Acts on sphingosine or its 2-epimer. Acyl-CoA + sphingosine = CoA + N-acylsphingosine. Plasmalogen synthase Acyl-CoA + 1-O-alk-1-enyl-glycero-3-phosphocholine = CoA + plasmenylcholine. Sterol O-acyltransferase Cholesterol acyltransferase Sterol-ester synthase The animal enzyme is highly specific for transfer of acyl groups with a single cis double bond 9 carbon atoms distant from the carboxy group. Acyl-CoA + cholesterol = CoA + cholesterol ester. Cortisol O-acetyltransferase Acetyl-CoA + cortisol = CoA + cortisol 21-acetate. Chloramphenicol O-acetyltransferase Chloramphenicol is an antibiotic. Acetyl-CoA + chloramphenicol = CoA + chloramphenicol 3-acetate. Glycine C-acetyltransferase 2-amino-3-ketobutyrate coenzyme A ligase Pyridoxal-phosphate Acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate. Glucosamine N-acetyltransferase Glucosamine acetylase Acetyl-CoA + D-glucosamine = CoA + N-acetyl-D-glucosamine. Serine O-acetyltransferase Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine. Homoserine O-acetyltransferase Homoserine O-trans-acetylase Homoserine transacetylase Acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine. Lysine acetyltransferase Lysine N-acetyltransferase Lysine N(6)-acetyltransferase LAT Acetyl phosphate + L-lysine = phosphate + N(6)-acetyl-L-lysine. Histidine N-acetyltransferase Acetyl-CoA + L-histidine = CoA + N-acetyl-L-histidine. D-tryptophan N-acetyltransferase Acetyl-CoA + D-tryptophan = CoA + N-acetyl-D-tryptophan. Acetylglutamic-acetylornithine transacetylase N-acetylglutamate synthase Acetylornithinase Glutamate acetyltransferase Ornithine acetyltransferase Acetylornithine glutamate acetyltransferase N-acetyl-L-glutamate synthetase N-acetylglutamate synthetase Acetylglutamate synthetase Acetylglutamate-acetylornithine transacetylase Acetylglutamic synthetase Glutamate N-acetyltransferase Ornithine transacetylase Also has some hydrolytic activity on acetyl-L-ornithine, but the rate is 1% of that of transferase activity. N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate. D-amino-acid N-acetyltransferase Acetyl-CoA + a D-amino acid = CoA + an N-acetyl-D-amino acid. ALAS 5-aminolevulinic acid synthase Delta-ALA synthetase 5-aminolevulinate synthase Delta-aminolevulinate synthase Pyridoxal-phosphate http://purl.uniprot.org/mim/301300 Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO(2). ACAT [Acyl-carrier-protein] S-acetyltransferase Acyl-carrier-protein acetyltransferase Acetyl coenzyme A-acyl-carrier-protein transacylase ACP acetyltransferase Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein]. Essential, along with EC 2.3.1.39, for the initiation of fatty-acid biosynthesis in bacteria. This is one of the activities associated with EC 2.3.1.180. The substrate acetyl-CoA protects the enzyme against inhibition by N-ethylmaleimide or iodoacetamide. Malonyl coenzyme A-acyl carrier protein transacylase Acyl carrier protein malonyltransferase [Acyl-carrier-protein] S-malonyltransferase Malonyl transferase MCAT Malonyl transacylase Malonyl-CoA-acyl carrier protein transacylase The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis. Also provides the malonyl groups for polyketide biosynthesis. In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7) is the preferred substrate. Essential, along with EC 2.3.1.38, for the initiation of fatty-acid biosynthesis in bacteria. Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein]. Glucosamine-6-phosphate acetylase N-acetylglucosamine-6-phosphate synthase Glucosamine 6-phosphate N-acetyltransferase Aminodeoxyglucosephosphate acetyltransferase Glucosamine-phosphate N-acetyltransferase D-glucosamine-6-P N-acetyltransferase Glucosamine 6-phosphate acetylase Phosphoglucosamine acetylase Phosphoglucosamine transacetylase Phosphoglucosamine N-acetylase Acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate. Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase Acyl-[acyl-carrier-protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = [acyl-carrier-protein] + O-(1-beta-acyl-2-acyl-sn-glycero-3-phospho)ethanolamine. Fatty acid condensing enzyme Acyl-malonyl(acyl-carrier-protein)-condensing enzyme Acyl-malonyl acyl carrier protein-condensing enzyme Beta-ketoacyl-[acyl carrier protein] synthase Beta-ketoacyl synthetase KAS I Beta-ketoacyl-acyl-carrier-protein synthase I Beta-ketoacyl acyl carrier protein synthase Beta-ketoacylsynthase 3-oxoacyl-[acyl-carrier-protein] synthase Condensing enzyme Beta-ketoacyl-ACP synthetase 3-ketoacyl-acyl carrier protein synthase Beta-ketoacyl-ACP synthase I Beta-ketoacyl-acyl carrier protein synthetase The substrate specificity is very similar to that of EC 2.3.1.179 with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C(16)-Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature. Can use fatty acyl thioesters of ACP (C(2) to C(16)) as substrates, as well as fatty acyl thioesters of Co-A (C(4) to C(16)). Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]. Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. Responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. Glycerone-phosphate O-acyltransferase Dihydroxyacetone phosphate acyltransferase http://purl.uniprot.org/mim/222765 Acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate. Uses CoA derivatives of palmitate, stearate, and oleate, with highest activity on palmitoyl-CoA. Phospholipid--cholesterol acyltransferase Lecithin--cholesterol acyltransferase LCAT Phosphatidylcholine--sterol O-acyltransferase The bacterial enzyme also catalyzes the reactions of EC 3.1.1.4 and EC 3.1.1.5. http://purl.uniprot.org/mim/136120 http://purl.uniprot.org/mim/245900 Palmitoyl, oleoyl, and linoleoyl can be transferred; a number of sterols, including cholesterol, can act as acceptors. Phosphatidylcholine + a sterol = 1-acylglycerophosphocholine + a sterol ester. N-acetylneuraminate 4-O-acetyltransferase Acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-4-O-acetylneuraminate. Both free and glycosidically bound N-acetyl-and N-glycolyl-neuraminates can act as O-acetyl acceptors. N-acetylneuraminate 7-O(or 9-O)-acetyltransferase Acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-7-O(or 9-O)-acetylneuraminate. Both free and glycosidically bound N-acetyl-and N-glycolylneuraminates can act as O-acetyl acceptors. Homoserine O-succinyltransferase Homoserine O-transsuccinylase Succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine. 8-amino-7-ketopelargonate synthase AONS 8-amino-7-oxononanoate synthase 7-keto-8-amino-pelargonic acid synthetase 7-KAP synthetase 6-carboxyhexanoyl-CoA + L-alanine = 8-amino-7-oxononanoate + CoA + CO(2). Pyridoxal-phosphate Histone acetyltransferase A group of enzymes with differing specificity toward histone acceptors. http://purl.uniprot.org/mim/180849 Acetyl-CoA + histone = CoA + acetylhistone. Deacetyl-[citrate-(pro-3S)-lyase] S-acetyltransferase Both this enzyme and EC 6.2.1.22 acetylate and activate EC 4.1.3.6. S-acetylphosphopantotheine + deacetyl-[citrate-oxaloacetate-lyase((pro-3S)-CH(2)COO(-)->acetate)] = phosphopantotheine + [citrate-oxaloacetate-lyase((pro-3S)-CH(2)COO(-)->acetate)]. Arylamine acetylase Arylamine N-acetyltransferase Acetyl-CoA + an arylamine = CoA + an N-acetylarylamine. http://purl.uniprot.org/mim/243400 Wide specificity for aromatic amines, including serotonin; also catalyzes acetyl-transfer between arylamines without CoA. Serine C-palmitoyltransferase http://purl.uniprot.org/mim/162400 Pyridoxal-phosphate Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO(2). 1-acylglycerol-3-phosphate O-acyltransferase The animal enzyme is specific for the transfer of unsaturated fatty acyl groups. Acyl-[acyl-carrier-protein] can also act as acyl donor. Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate. http://purl.uniprot.org/mim/608594 2-acylglycerol-3-phosphate O-acyltransferase Acyl-CoA + 2-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate. Saturated acyl-CoA thioesters are the most effective acyl donors. Phenylalanine N-acetyltransferase Also acts, more slowly, on L-histidine and L-alanine. Acetyl-CoA + L-phenylalanine = CoA + N-acetyl-L-phenylalanine. Formate C-acetyltransferase Pyruvate formate-lyase Acetyl-CoA + formate = CoA + pyruvate. Aromatic-hydroxylamine O-acetyltransferase N-hydroxy-4-acetylaminobiphenyl + N-hydroxy-4-aminobiphenyl = N-hydroxy-4-aminobiphenyl + N-acetoxy-4-aminobiphenyl. Transfers the N-acetyl group of some aromatic acethydroxamates to the O-position of some aromatic hydroxylamines. Putrescine acetylase Putrescine (diamine)-acetylating enzyme Putrescine N-acetyltransferase Diamine N-acetyltransferase Spermidine acetyltransferase Acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase Putrescine acetyltransferase Spermidine N(1)-acetyltransferase Diamine acetyltransferase Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine. Acts on 1,3-diaminopropane, 1,5-diaminopentane, putrescine, spermidine (forming N(1)-and N(8)-acetylspermidine), spermine, N(1)-acetylspermidine and N(8)-acetylspermidine. Oxalyldiaminopropionate synthase Oxalyldiaminopropionic synthase 2,3-diaminopropionate N-oxalyltransferase ODAP synthase Oxalyl-CoA + L-2,3-diaminopropanoate = CoA + N(3)-oxalyl-L-2,3-diaminopropanoate. Gentamicin 2'-N-acetyltransferase Gentamycin acetyltransferase II Acetyl-CoA + gentamicin C(1a) = CoA + N(2')-acetylgentamicin C(1a). The antibiotics gentamicin A, sisomicin, tobramycin, paromomycin, neomycin B, kanamycin B and kanamycin C can also act as acceptors. Choline O-acetyltransferase Choline acetylase CHOACTase http://purl.uniprot.org/mim/254210 Propanoyl-CoA can act, more slowly, in place of acetyl-CoA. Acetyl-CoA + choline = CoA + O-acetylcholine. http://purl.uniprot.org/mim/254200 Gentamicin acetyltransferase I Gentamicin 3'-N-acetyltransferase Aminoglycoside acetyltransferase AAC(3)-I Acetyl-CoA + gentamicin C = CoA + N(3')-acetylgentamicin C. Also acetylates sisomicin. Dihydrolipoyl transsuccinylase Dihydrolipoamide succinyltransferase Succinyl-CoA:dihydrolipoamide S-succinyltransferase Succinyl-CoA:dihydrolipoate S-succinyltransferase Dihydrolipoic transsuccinylase Dihydrolipoyllysine-residue succinyltransferase Dihydrolipoamide S-succinyltransferase Lipoic transsuccinylase Lipoate succinyltransferase Lipoyl transsuccinylase Dihydrolipolyl transsuccinylase Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine. A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2 and EC 1.8.1.4. The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalyzed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A. 2-acylglycerophosphocholine O-acyltransferase Acyl-CoA + 2-acyl-sn-glycero-3-phosphocholine = CoA + phosphatidylcholine. 1-alkylglycerophosphocholine O-acyltransferase May be identical with EC 2.3.1.23. Acyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acyl-1-alkyl-sn-glycero-3-phosphocholine. Agmatine coumaroyltransferase p-coumaroyl-CoA-agmatine N-p-coumaroyltransferase Agmatine N(4)-coumaroyltransferase 4-coumaroyl-CoA + agmatine = CoA + N-(4-guanidinobutyl)-4-hydroxycinnamamide. BAT Cholyl-CoA:taurine N-acyltransferase BACAT Glycine N-choloyltransferase Glycine--taurine N-acyltransferase Cholyl-CoA glycine-taurine N-acyltransferase Bile acid-CoA:amino acid N-acyltransferase Amino acid N-choloyltransferase Taurine and 2-fluoro-beta-alanine can act as substrates, but more slowly. Can also conjugate fatty acids to glycine and can act as a very-long-chain acyl-CoA thioesterase. Also acts on CoA derivatives of other bile acids. Choloyl-CoA + glycine = CoA + glycocholate. http://purl.uniprot.org/mim/607748 This is the second enzyme in a two-step process leading to the conjugation of bile acids with amino acids; the first step is the conversion of bile acids into their acyl-CoA thioesters, which is catalyzed by EC 6.2.1.7. Bile-acid--amino-acid conjugates serve as detergents in the gastrointestinal tract, solubilizing long chain fatty acids, mono-and diglycerides, fat-soluble vitamins and cholesterol. Leucine N-acetyltransferase L-arginine, L-valine, L-phenylalanine and peptides containing L-leucine can act as acceptor. Acetyl-CoA + L-leucine = CoA + N-acetyl-L-leucine. Propanoyl-CoA can act, more slowly, as donor. Acetyl-CoA:lyso-PAF acetyltransferase Lyso-GPC:acetyl CoA acetyltransferase Platelet-activating factor-synthesizing enzyme Lyso-platelet-activating factor:acetyl-CoA acetyltransferase Lyso-platelet activating factor:acetyl-CoA acetyltransferase PAF acetyltransferase 1-alkyl-2-lysolecithin acetyltransferase Acyl-CoA:1-alkyl-sn-glycero-3-phosphocholine acyltransferase Platelet-activating factor acylhydrolase LysoPAF:acetyl CoA acetyltransferase 1-alkyl-2-lyso-sn-glycero-3-phosphocholine acetyltransferase Blood platelet-activating factor acetyltransferase 1-alkylglycerophosphocholine O-acetyltransferase Acetyl-CoA:1-alkyl-2-lyso-sn-glycero-3-phosphocholine 2-O-acetyltransferase Acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine. Glutamine N-acyltransferase Not identical with EC 2.3.1.13 or EC 2.3.1.71. Acyl-CoA + L-glutamine = CoA + N-acyl-L-glutamine. Phenylacetyl-CoA and (indol-3-yl)acetyl-CoA, but not benzoyl-CoA, can act as acyl donor. Monoterpenol O-acetyltransferase Menthol transacetylase Acetyl-CoA + a monoterpenol = CoA + a monoterpenol acetate ester. (-)-menthol, (+)-neomenthol, borneol, cyclohexanol and N-decanol can be acetylated. Carnitine acetylase Carnitine O-acetyltransferase Also acts on propanoyl-CoA and butanoyl-CoA (cf. EC 2.3.1.21 and EC 2.3.1.137). Acetyl-CoA + carnitine = CoA + O-acetylcarnitine. CDP-acylglycerol O-arachidonoyltransferase Arachidonoyl-CoA + CDP-acylglycerol = CoA + CDP-diacylglycerol. Highly specific for both donor and acceptor. Glycine N-benzoyltransferase Benzoyl-CoA + glycine = CoA + N-benzoylglycine. Not identical with EC 2.3.1.13 or EC 2.3.1.68. Indoleacetylglucose--inositol O-acyltransferase The position of acylation is indeterminate because of the ease of acyl transfer between hydroxy groups. 1-O-(indol-3-yl)acetyl-beta-D-glucose + myo-inositol = D-glucose + O-(indol-3-yl)acetyl-myo-inositol. Diacylglycerol--sterol O-acyltransferase Transfers a number of long-chain fatty acyl groups. Cholesterol, sitosterol, campesterol and diacylglycerol can act as acceptors. 1,2-diacyl-sn-glycerol + a sterol = monoacylglycerol + a sterol ester. Naringenin-chalcone synthase Flavonone synthase Chalcone synthase 6'-deoxychalcone synthase In the presence of NADH and a reductase, 6'-deoxychalcone is produced. 3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO(2). Wax synthase Long-chain-alcohol O-fatty-acyltransferase Transfers saturated or unsaturated acyl residues of chain length C(18) to C(20) to long-chain alcohols, forming waxes. Acyl-CoA + a long-chain alcohol = CoA + a long-chain ester. The best acceptor is cis-icos-11-en-1-ol. Retinol O-fatty-acyltransferase Acyl-CoA + retinol = CoA + retinyl ester. Acts on palmitoyl-CoA and other long-chain fatty-acyl derivatives of CoA. Triacylglycerol--sterol O-acyltransferase Tripalmitoylglycerol can act as donor, and, more slowly, other triacylglycerols containing C(6) to C(22) fatty acids. The best acceptors are 3-beta-hydroxysterols with a planar ring system. Triacylglycerol + a 3-beta-hydroxysterol = diacylglycerol + a 3-beta-hydroxysterol ester. Heparan-alpha-glucosaminide N-acetyltransferase Not identical with EC 2.3.1.3 or EC 2.3.1.4. Acetyl-CoA + heparan sulfate alpha-D-glucosaminide = CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide. Also acts on heparin. Brings about the acetylation of glucosamine groups of heparan sulfate and heparin from which the sulfate has been removed. http://purl.uniprot.org/mim/252930 Maltose O-acetyltransferase Acetyl-CoA + maltose = CoA + acetyl-maltose. Not identical with EC 2.3.1.18. Phosphoacylase Phosphate acetyltransferase Phosphotransacetylase Also acts with other short-chain acyl-CoAs. Acetyl-CoA + phosphate = CoA + acetyl phosphate. Cysteine-S-conjugate N-acetyltransferase S-benzyl-L-cysteine can act as acceptor, and, in decreasing order of activity, S-butyl-L-cysteine, S-propyl-L-cysteine, O-benzyl-L-serine and S-ethyl-L-cysteine. Acetyl-CoA + an S-substituted L-cysteine = CoA + an S-substituted N-acetyl-L-cysteine. Gentamicin-(3)-N-acetyltransferase Aminoglycoside N(3')-acetyltransferase A wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptor, including gentamicin, kanamycin, tobramycin, neomycin and apramycin. Acetyl-CoA + a 2-deoxystreptamine antibiotic = CoA + N(3')-acetyl-2-deoxystreptamine antibiotic. Different from EC 2.3.1.60. 6'-aminoglycoside-N-acetyltransferase AAC(6') Kanamycin 6'-N-acetyltransferase Aminoglycoside N(6')-acetyltransferase Acetyl-CoA + kanamycin-B = CoA + N(6')-acetylkanamycin-B. The antibiotics kanamycin A, kanamycin B, neomycin, gentamicin C(1a), gentamicin C(2), sisomicin and tobramycin are substrates. The antibiotic paromomycin is not a substrate. The 6-amino group of the purpurosamine ring is acetylated. Phosphatidylcholine--dolichol O-acyltransferase 3-sn-phosphatidylcholine + dolichol = 1-acyl-sn-glycero-3-phosphocholine + acyldolichol. AATASE Alcohol O-acetyltransferase Acetyl-CoA + an alcohol = CoA + an acetyl ester. Acts on a range of short-chain aliphatic alcohols, including methanol and ethanol. Fatty-acid synthase Acetyl-CoA + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + (n+1) CoA + n CO(2) + 2n NADP(+). The animal enzyme is a multifunctional protein catalyzing the reactions of EC 2.3.1.38, EC 2.3.1.39, EC 2.3.1.41, EC 1.1.1.100, EC 4.2.1.61, EC 1.3.1.10 and EC 3.1.2.14. Fatty-acyl-CoA synthase Yeast fatty acid synthase The Saccharomyces cerevisiae enzyme is a multi-functional protein catalyzing the reactions of EC 2.3.1.38, EC 2.3.1.39, EC 2.3.1.41, EC 1.1.1.100, EC 1.1.1.279, EC 4.2.1.61 and EC 1.3.1.9. Acetyl-CoA + n malonyl-CoA + 2n NADH + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO(2) + 2n NAD(+) + 2n NADP(+). Arylalkylamine N-acetyltransferase Melatonin rhythm enzyme AANAT Serotonin N-acetyltransferase Serotonin acetylase Serotonin acetyltransferase Aralkylamine N-acetyltransferase Narrow specificity toward 2-arylethylamines, including serotonin (5-hydroxytryptamine), tryptamine, 5-methoxytryptamine and phenylethylamine. Differs from EC 2.3.1.5. Acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine. http://purl.uniprot.org/mim/600950 This is the penultimate enzyme in the production of melatonin (5-methoxy-N-acetyltryptamine) and controls its synthesis (cf. EC 2.1.1.4). Amino-terminal amino acid-acetylating enzyme Peptide acetyltransferase Peptide alpha-N-acetyltransferase Beta-endorphin acetyltransferase Protein N-terminal acetyltransferase NAT N(alpha)-acetyltransferase Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA. Acetylates N-terminal alanine, serine, methionine and glutamate residues in a number of peptides and proteins, including beta-endorphin, corticotropins and melanotropin (cf. EC 2.3.1.108). Tetrahydrodipicolinate N-acetyltransferase Tetrahydrodipicolinate acetylase Acetyl-CoA + (S)-2,3,4,5-tetrahydrodipicolinate-2,6-dicarboxylate + H(2)O = CoA + L-2-acetamido-6-oxoheptanedioate. Acetyl-CoA C-acetyltransferase Acetoacetyl-CoA thiolase http://purl.uniprot.org/mim/203750 http://purl.uniprot.org/mim/100678 2 acetyl-CoA = CoA + acetoacetyl-CoA. Beta-glucogallin O-galloyltransferase 2 1-O-galloyl-beta-D-glucose = D-glucose + 1-O,6-O-digalloyl-beta-D-glucose. Digalloylglucose can also act as acceptor, with the formation of 1-O,2-O,6-O-trigalloylglucose. Beta-glucogallin can act as donor and as acceptor. Sinapoylglucose--choline O-sinapoyltransferase Sinapine synthase 1-O-sinapoyl-beta-D-glucose + choline = D-glucose + sinapoylcholine. Sinapoylglucose--malate O-sinapoyltransferase 1-O-sinapoyl-beta-D-glucose + (S)-malate = D-glucose + sinapoyl-(S)-malate. 13-hydroxylupinine O-tigloyltransferase Involved in the synthesis of lupinine alkaloids. (E)-2-methylcrotonoyl-CoA + 13-hydroxylupinine = CoA + 13-(2-methylcrotonoyl)oxylupinine. Benzoyl-CoA and, more slowly, pentanoyl-CoA, 3-methylbutanoyl-CoA and butanoyl-CoA can act as acyl donors. Erythronolide condensing enzyme Erythronolide synthase The product, which contains a 14-membered lactone ring, is an intermediate in the biosynthesis of erythromycin antibiotics (cf. EC 2.3.1.74). 6 malonyl-CoA + propionyl-CoA = 7 CoA + 6-deoxyerythronolide B. Stilbene synthase Trihydroxystilbene synthase Resveratrol synthase 3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + 3,4',5-trihydroxystilbene + 4 CO(2). Not identical with EC 2.3.1.74 or EC 2.3.1.146. Glycoprotein N-palmitoyltransferase Palmitoyl-CoA + glycoprotein = CoA + N-palmitoylglycoprotein. Activated by 1,4-dithiothreitol. Acts on glycoprotein from mucus. Peptide N-myristoyltransferase Peptide N-tetradecanoyltransferase Glycylpeptide N-tetradecanoyltransferase The enzyme from mammalian heart transfers acyl groups to a specific acceptor protein of 51 kDa. Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide. The enzyme from Saccharomyces cerevisiae is highly specific for tetradecanoyl-CoA, and for N-terminal glycine in oligopeptides containing serine in the 5-position. Chlorogenate--glucarate O-hydroxycinnamoyltransferase Galactarate can act as acceptor, more slowly. Chlorogenate + glucarate = quinate + 2-O-caffeoylglucarate. Involved with EC 2.3.1.99 in the formation of caffeoylglucarate in tomato. Hydroxycinnamoyl coenzyme A-quinate transferase Quinate O-hydroxycinnamoyltransferase Involved in the biosynthesis of chlorogenic acid in sweet potato and, with EC 2.3.1.98 in the formation of caffeoyl-CoA in tomato. Caffeoyl-CoA and 4-coumaroyl-CoA can also act as donors, more slowly. Feruloyl-CoA + quinate = CoA + O-feruloylquinate. Aminoacyltransferases D-glutamyltransferase D-glutamyl transpeptidase L(or D)-glutamine + D-glutamyl-peptide = NH(3) + 5-glutamyl-D-glutamyl-peptide. Alanyl-transfer ribonucleate-uridine diphosphoacetylmuramoylpentapeptide transferase Uridine diphosphoacetylmuramoylpentapeptide lysine N(6)-alanyltransferase UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase UDP-N-acetylmuramoylpentapeptide lysine N(6)-alanyltransferase Also acts on L-seryl-tRNA. L-alanyl-tRNA + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine = tRNA + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N(6)-(L-alanyl)-L-lysyl-D-alanyl-D-alanine. Alanylphosphatidylglycerol synthase L-alanyl-tRNA + phosphatidylglycerol = tRNA + 3-O-L-alanyl-1-O-phosphatidylglycerol. Peptidyltransferase Peptidyl-tRNA(1) + aminoacyl-tRNA(2) = tRNA(1) + peptidyl(aminoacyl-tRNA(2)). An enzyme in ribosomes. Glutaminylpeptide gamma-glutamyltransferase Fibrinoligase TGase Protein-glutamine gamma-glutamyltransferase Transglutaminase Polyamine transglutaminase http://purl.uniprot.org/mim/242300 Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH(3). http://purl.uniprot.org/mim/609796 The gamma-carboxymide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein-and peptide-bound lysine residues act as acceptors, to give intra-and inter-molecular N(6)-(5-glutamyl)lysine crosslinks. http://purl.uniprot.org/mim/242100 http://purl.uniprot.org/mim/134570 Calcium D-alanine gamma-glutamyltransferase Also catalyzes some of the reactions of EC 2.3.2.2. L-glutamine + D-alanine = NH(3) + gamma-L-glutamyl-D-alanine. D-phenylalanine and D-2-aminobutyrate can also act as acceptors, more slowly. Glutathione gamma-glutamylcysteinyltransferase Phytochelatin synthase Glutathione + (Glu(-Cys))(n)-Gly = Gly + (Glu(-Cys))(n+1)-Gly. Gamma-glutamyltransferase Gamma-glutamyl transpeptidase Glutamyl transpeptidase (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid. http://purl.uniprot.org/mim/231950 Lysyltransferase L-lysyl-tRNA + phosphatidylglycerol = tRNA + 3-phosphatidyl-1'-(O(3')-L-lysyl)glycerol. Gamma-glutamylcyclotransferase (5-L-glutamyl)-L-amino acid = 5-oxoproline + L-amino acid. Acts on derivatives of L-glutamate, L-2-aminobutanoate, L-alanine and glycine. Glutaminyl-peptide cyclotransferase Glutaminyl-tRNA cyclotransferase Glutaminyl cyclase Involved in the formation of thyrotropin-releasing hormone and other biologically active peptides containing N-terminal pyroglutamyl residues. L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH(3). The enzyme from papaya also acts on glutaminyl-tRNA. L/F transferase Leucyl/phenylalanyl-tRNA--protein transferase Leucyl-tRNA--protein transferase Leucyltransferase L-leucyl-tRNA + protein = tRNA + L-leucyl-protein. Peptides and proteins containing an N-terminal arginine, lysine or histidine residue can act as acceptors. Monovalent cation Also transfers phenylalanyl groups. Aspartyltransferase L-asparagine + hydroxylamine = NH(3) + L-aspartylhydroxamate. Arginyl-tRNA--protein transferase Arginyltransferase Requires mercaptoethanol and a univalent cation. L-arginyl-tRNA + protein = tRNA + L-arginyl-protein. Peptides and proteins containing an N-terminal glutamate, aspartate or cystine residue can act as acceptors. Agaritine gamma-glutamyltransferase 4-hydroxyaniline, cyclohexylamine, 1-naphthylhydrazine and similar compounds can act as acceptors. Agaritine + acceptor = 4-hydroxymethylphenylhydrazine + gamma-L-glutamyl-acceptor. Also catalyzes the hydrolysis of agaritine. Acyl groups converted into alkyl on transfer Citrate synthase Citrate oxaloacetate-lyase ((pro-3S)-CH(2)COO(-)->acetyl-CoA) Citrogenase (R)-citric synthase Citrate (Si)-synthase Citrate synthetase Citrate condensing enzyme Oxaloacetate transacetase Oxalacetic transacetase Citrate oxaloacetate-lyase, CoA-acetylating Citric synthase Citric-condensing enzyme Condensing enzyme The stereospecificity of this enzyme is opposite to that of EC 2.3.3.3, which is found in some anaerobes. Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA. 3-hydroxy-3-methylglutaryl-coenzyme A synthase 3-hydroxy-3-methylglutaryl CoA synthetase 3-hydroxy-3-methylglutaryl coenzyme A synthase Hydroxymethylglutaryl coenzyme alpha-condensing enzyme Hydroxymethylglutaryl coenzyme A synthase HMG-CoA synthase Hydroxymethylglutaryl-CoA synthase (S)-3-hydroxy-3-methylglutaryl-CoA acetoacetyl-CoA-lyase (CoA-acetylating) Beta-hydroxy-beta-methylglutaryl-CoA synthase 3-hydroxy-3-methylglutaryl coenzyme A synthetase Acetoacetyl coenzyme A transacetase 3-hydroxy-3-methylglutaryl-CoA synthase Acetyl-CoA + H(2)O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA. 2-hydroxyglutarate glyoxylate-lyase (CoA-propanoylating) 2-hydroxyglutaratic synthetase 2-hydroxyglutaric synthetase Alpha-hydroxyglutarate synthase Hydroxyglutarate synthase 2-hydroxyglutarate synthase Propanoyl-CoA + H(2)O + glyoxylate = 2-hydroxyglutarate + CoA. n-propylmalate synthase 3-(n-propyl)-malate synthase 3-propylmalate glyoxylate-lyase (CoA-pentanoylating) Beta-n-propylmalate synthase 3-propylmalate synthase Pentanoyl-CoA + H(2)O + glyoxylate = 3-propylmalate + CoA. Alpha-IPM synthetase Isopropylmalate synthase Alpha-isopropylmalic synthetase Alpha-isopropylmalate synthase Alpha-isopropylmalate synthetase 3-carboxy-3-hydroxy-4-methylpentanoate 3-methyl-2-oxobutanoate-lyase (CoA-acetylating) Isopropylmalate synthetase 2-isopropylmalate synthase Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O = (2S)-2-isopropylmalate + CoA. Potassium Acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase Homocitrate synthase 2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acetylating) Homocitrate synthetase Also acts with oxaloacetate as substrate, but more slowly. Belongs in the alpha-aminoadipate pathway of lysine synthesis, along with EC 4.2.1.36. Acetyl-CoA + H(2)O + 2-oxoglutarate = (R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA. Sulfoacetaldehyde acetyltransferase Magnesium Thiamine diphosphate Acetyl phosphate + sulfite = 2-sulfoacetaldehyde + phosphate. 2-decylcitrate synthase (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate oxaloacetate-lyase (CoA-acylating) Decylcitrate synthase Lauroyl-CoA + H(2)O + oxaloacetate = (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate + CoA. Citrate oxaloacetate-lyase ((pro-3R)-CH(2)COO(-)->acetyl-CoA) (R)-citrate synthase Citrate (Re)-synthase Re-citrate-synthase Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA. This enzyme is inactivated by oxygen and is found in some anaerobes. Its stereospecificity is opposite to that of EC 2.3.3.1. 2-decylhomocitrate synthase Decylhomocitrate synthase 3-hydroxytetradecane-1,3,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acylating) Dodecanoyl-CoA + H(2)O + 2-oxoglutarate = (3S,4S)-3-hydroxytetradecane-1,3,4-tricarboxylate + CoA. Decanoyl-CoA can act instead of dodecanoyl-CoA, but 2-oxoglutarate cannot be replaced by oxaloacetate or pyruvate. MCS Methylcitrate synthetase 2-methylcitrate synthase 2-methylcitrate oxaloacetate-lyase Methylcitrate synthase Oxaloacetate cannot be replaced by glyoxylate, pyruvate or 2-oxoglutarate. The relative rate of condensation of acetyl-CoA and oxaloacetate is 140% of that of propanoyl-CoA and oxaloacetate, but the enzyme has been separated from EC 2.3.3.1. Propanoyl-CoA + H(2)O + oxaloacetate = (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA. The enzyme acts on acetyl-CoA, propanoyl-CoA, butanoyl-CoA and pentanoyl-CoA. Propylmalic synthase Propylmalate synthase (R)-2-ethylmalate 2-oxobutanoyl-lyase (CoA-acetylating) 2-ethylmalate-3-hydroxybutanedioate synthase 2-ethylmalate synthase Also acts on (R)-2-(n-propyl)-malate. Acetyl-CoA + H(2)O + 2-oxobutanoate = (R)-2-ethylmalate + CoA. 3-ethylmalate glyoxylate-lyase (CoA-butanoylating) 2-ethyl-3-hydroxybutanedioate synthase 3-ethylmalate synthase Butanoyl-CoA + H(2)O + glyoxylate = 3-ethylmalate + CoA. Adenosine triphosphate citrate lyase ATP-citrate (pro-S-)-lyase Citrate-ATP lyase Acetyl-CoA:oxaloacetate acetyltransferase (isomerizing; ADP-phosphorylating) ATP-citric lyase Citrate cleavage enzyme ATP citrate (pro-S)-lyase ATP:citrate oxaloacetate-lyase ((pro-S)-CH(2)COO(-)->acetyl-CoA) (ATP-dephosphorylating) Citric cleavage enzyme ATP citrate synthase The enzyme can be dissociated into components, two of which are identical with EC 4.1.3.34 and EC 6.2.1.18. ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA. Malate synthetase Malic-condensing enzyme Glyoxylic transacetase Malate condensing enzyme Malate synthase Malic synthetase Glyoxylate transacetase Glyoxylate transacetylase L-malate glyoxylate-lyase (CoA-acetylating) Acetyl-CoA + H(2)O + glyoxylate = (S)-malate + CoA. Glycosyltransferases Hexosyltransferases Amylophosphorylase Muscle phosphorylase a and b Polyphosphorylase Phosphorylase http://purl.uniprot.org/mim/232700 http://purl.uniprot.org/mim/232600 The description (official rdfs:label) should be qualified in each instance by adding the rdfs:label of the natural substance, e.g. maltodextrin phosphorylase, starch phosphorylase, glycogen phosphorylase. (1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate. Levansucrase Sucrose 6-fructosyl transferase Sucrose + (2,6-beta-D-fructosyl)(n) = glucose + (2,6-beta-D-fructosyl)(n+1). Some other sugars can act as D-fructosyl acceptors. 1,2-beta-D-fructan 1(F)-fructosyltransferase Fructan:fructan fructosyl transferase 1,2-beta-fructan 1(F)-fructosyltransferase 1,2-beta-D-fructan:1,2-beta-D-fructan 1(F)-beta-D-fructosyltransferase 2,1-fructan:2,1-fructan 1-fructosyltransferase FFT (Beta-D-fructosyl-(2->1)-)(m) + (beta-D-fructosyl-(2->1)-)(n) = (beta-D-fructosyl-(2->1)-)(m-1) + (beta-D-fructosyl-(2->1)-)(n+1). N-acetylglucosaminyltransferase I Uridine diphosphoacetylglucosamine-alpha-1,3-mannosylglycoprotein beta-1,2-N-acetylglucosaminyltransferase Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase UDP-N-acetylglucosaminyl:alpha-1,3-D-mannoside-beta-1,2-N-acetylglucosaminyltransferase I GnTI UDP-N-acetylglucosaminyl:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 3-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R. R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor. Note that this enzyme acts before N-acetylglucosaminyltransferases II (EC 2.4.1.143), III (EC 2.4.1.144), IV (EC 2.4.1.145), V (EC 2.4.1.155) and VI (EC 2.4.1.201). O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase Beta(6)-N-acetylglucosaminyltransferase Cf. EC 2.4.1.146, EC 2.4.1.147, and EC 2.4.1.148. UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R = UDP + beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R. Alizarin 2-beta-glucosyltransferase Acts on other hydroxy-and dihydroxy-derivatives of 9,10-anthraquinone. UDP-glucose + alizarin = UDP + 1-hydroxy-2-(beta-D-glucosyloxy)-9,10-anthraquinone. o-dihydroxycoumarin 7-O-glucosyltransferase Converts the aglycone daphetin into daphnin and, more slowly, esculetin into cichoriin, umbelliferone into skimmin, hydrangetin into hydrangin and scopoletin into scopolin. UDP-glucose + 7,8-dihydroxycoumarin = UDP + daphnin. Vitexin beta-glucosyltransferase Vitexin is a flavonoid from Cannabis sativa (hemp) and some populations of Silene alba. UDP-glucose + vitexin = UDP + vitexin 2''-O-beta-D-glucoside. Isovitexin beta-glucosyltransferase Isovitexin is a flavonoid from petals of Silene alba. UDP-glucose + isovitexin = UDP + isovitexin 2''-O-beta-D-glucoside. Dolichyl-phosphate-mannose--protein mannosyltransferase Transfers mannosyl residues to the hydroxy of serine or threonine residues, producing cell-wall mannoproteins. http://purl.uniprot.org/mim/609308 http://purl.uniprot.org/mim/236670 Acts only on long-chain alpha-dihydropolyprenyl derivatives, larger than C(35). Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein. Glycogen (starch) synthase UDP-glucose-glycogen glucosyltransferase The enzyme requires glucosylated glycogenin as a primer; this is the reaction product of EC 2.4.1.186. Glycogen synthase from animal tissues is a complex of a catalytic subunit and the protein glycogenin. A similar enzyme utilizes ADP-glucose (cf. EC 2.4.1.21). The description (official rdfs:label) varies according to the source of the enzyme and the nature of its synthetic product. UDP-glucose + (1,4-alpha-D-glucosyl)(n) = UDP + (1,4-alpha-D-glucosyl)(n+1). http://purl.uniprot.org/mim/240600 tRNA-queuosine beta-mannosyltransferase GDP-mannose + tRNA(Asp)-queuosine = GDP + tRNA(Asp)-O-5''-beta-D-mannosylqueuosine. Coniferyl-alcohol glucosyltransferase UDP-glucose + coniferyl alcohol = UDP + coniferin. Sinapyl alcohol can also act as acceptor. Alpha-1,4-glucan-protein synthase (ADP-forming) ADP-glucose + protein = ADP + alpha-D-glucosyl-protein. Builds up alpha-1,4-glucan chains covalently bound to protein, thus acting as an initiator of glycogen synthesis. 2-coumarate O-beta-glucosyltransferase UDP-glucose + trans-2-hydroxycinnamate = UDP + trans-beta-D-glucosyl-2-hydroxycinnamate. Coumarinate (cis-2-hydroxycinnamate) does not act as acceptor. 3-GT UDP-glucose:anthocyanidin/flavonol 3-O-glucosyltransferase Anthocyanidin 3-O-glucosyltransferase UDP-glucose:anthocyanidin 3-O-D-glucosyltransferase UDP-glucose:cyanidin-3-O-glucosyltransferase Uridine diphosphoglucose-anthocyanidin 3-O-glucosyltransferase It may act on the pseudobase precursor of the anthocyanidin rather than on the anthocyanidin itself. The anthocyanidin compounds cyanidin, delphinidin, peonidin and to a lesser extent pelargonidin can act as substrates. Does not catalyze glucosylation of the 5-position of cyanidin and does not act on flavanols such as quercetin and kaempferol (cf. EC 2.4.1.91). UDP-D-glucose + an anthocyanidin = UDP + an anthocyanidin-3-O-beta-D-glucoside. In conjunction with EC 1.14.11.19, it is involved in the conversion of leucoanthocyanidin into anthocyanidin 3-glucoside. Uridine diphosphoglucose-cyanidin 3-rhamnosylglucoside 5-O-glucosyltransferase Cyanidin-3-rhamnosylglucoside 5-O-glucosyltransferase Cyanidin-3-O-rutinoside 5-O-glucosyltransferase Also acts on pelargonidin-3-rutinoside. Does not catalyze the glucosylation of the 5-hydroxy group of cyanidin-3-glucoside. UDP-glucose + cyanidin 3-O-rutinoside = UDP + cyanidin 3-O-rutinoside 5-O-beta-D-glucoside. Dolichyl-phosphate beta-glucosyltransferase Solanesyl phosphate and ficaprenyl phosphate can act as acceptors, more slowly. UDP-glucose + dolichyl phosphate = UDP + dolichyl beta-D-glucosyl phosphate. Cytokinin 7-beta-glucosyltransferase Uridine diphosphoglucose-zeatin 7-glucosyltransferase Cytokinin 7-glucosyltransferase UDP-glucose-zeatin 7-glucosyltransferase Acts on a range of N(6)-substituted adenines, including zeatin and N(6)-benzylaminopurine, but not N(6)-benzyladenine. With some acceptors, 9-beta-D-glucosides are also formed. UDP-glucose + N(6)-alkylaminopurine = UDP + N(6)-alkylaminopurine-7-beta-D-glucoside. Dolichyl-diphosphooligosaccharide--protein glycotransferase Transfers the glucosyl-mannosyl-glucosamine polysaccharide side-chains of glycoproteins to an asparagine residue in a sequence Asn-Xaa-Ser/Thr in the nascent polypeptide chains of the protein moiety. Dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine. UDP-glucose--beta-glucan glucosyltransferase UDP-glucose-beta-D-glucan glucosyltransferase Cellulose synthase (UDP-forming) UDP-glucose-cellulose glucosyltransferase A similar enzyme utilizes GDP-glucose (cf. EC 2.4.1.29). UDP-glucose + (1,4-beta-D-glucosyl)(n) = UDP + (1,4-beta-D-glucosyl)(n+1). Involved in the synthesis of cellulose. Sinapate 1-glucosyltransferase Some other hydroxycinnamates, including 4-coumarate, ferulate and caffeate, can also act as acceptors, more slowly. UDP-glucose + sinapate = UDP + 1-sinapoyl-D-glucose. Only glucose esters, not glucosides, are formed (cf. EC 2.4.1.126). Indole-3-acetate beta-glucosyltransferase IAA-Glu synthetase UDP-glucose + (indol-3-yl)acetate = UDP + 1-O-(indol-3-yl)acetyl-beta-D-glucose. Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase UDP-galactose + glycoprotein N-acetyl-D-galactosamine = UDP + glycoprotein D-galactosyl-1,3-N-acetyl-D-galactosamine. The non-reducing O-serine-linked N-acetylgalactosamine residues in mucin glycoproteins can act as acceptors. UDP-galactose:myo-inositol 3-alpha-D-galactosyltransferase Galactinol synthase Inositol 3-alpha-galactosyltransferase Inositol 1-alpha-galactosyltransferase UDP-galactose + myo-inositol = UDP + O-alpha-D-galactosyl-(1->3)-1D-myo-inositol. An enzyme from plants involved in the formation of raffinose and stachyose (cf. EC 2.4.1.67 and EC 2.4.1.82). Water-soluble-glucan synthase Sucrose--1,6-alpha-glucan 3(6)-alpha-glucosyltransferase Also transfers glucosyl residues to the 3-position on glucose residues in glucans, producing a highly-branched 1,6-alpha-D-glucan. Sucrose + (1,6-alpha-D-glucosyl)(n) = D-fructose + (1,6-alpha-D-glucosyl)(n+1). Hydroxycinnamate 4-beta-glucosyltransferase UDP-glucose + trans-4-hydroxycinnamate = UDP + 4-O-beta-D-glucosyl-4-hydroxycinnamate. Acts on 4-coumarate, ferulate, caffeate and sinapate, forming a mixture of 4-glucosides and glucose esters (cf. EC 2.4.1.120). Monoterpenol beta-glucosyltransferase UDP-glucose + (-)-menthol = UDP + (-)-menthyl O-beta-D-glucoside. (+)-neomenthol can also act as acceptor. Scopoletin glucosyltransferase UDP-glucose + scopoletin = UDP + scopolin. PG-II Bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase Penicillin binding protein (3 or 1B) Peptidoglycan transglycosylase Peptidoglycan TGase Peptidoglycan glycosyltransferase The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-center, as it is in Gram-negative and some Gram-positive organisms. (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate. Involved in the synthesis of cell-wall peptidoglycan. The undecaprenol involved is ditrans,octacis-undecaprenol. Sucrose-UDP glucosyltransferase Sucrose synthetase Sucrose synthase Sucrose-uridine diphosphate glucosyltransferase Uridine diphosphoglucose-fructose glucosyltransferase UDP-glucose-fructose glucosyltransferase NDP-glucose + D-fructose = NDP + sucrose. Although UDP is generally considered to be the preferred nucleoside diphosphate for sucrose synthase, numerous studies have shown that ADP serves as an effective acceptor molecule to produce ADP-glucose. Sucrose synthase has a dual role in producing both UDP-glucose (necessary for cell wall and glycoprotein biosynthesis) and ADP-glucose (necessary for starch biosynthesis). Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase Four of the nine mannosyl residues in the main membrane lipid-linked oligosaccharide of the structure Glc(3)Man(9)GlcNAc(2) are produced by the action of this enzyme. Transfers an alpha-D-mannosyl residue from dolichyl-phosphate D-mannose into membrane lipid-linked oligosaccharide. Glycolipid 2-alpha-mannosyltransferase Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-1,2-D-mannosyl-D-mannose linkage. The two 1,2-linked mannosyl residues in the mammalian lipid-linked oligosaccharide of the structure Glc(3)Man(9)GlcNAc(2) are produced by the action of this enzyme. Glycolipid 3-alpha-mannosyltransferase Mannosyltransferase II The 1,3-linked mannosyl residue in the mammalian lipid-linked oligosaccharide of the structure Glc(3)Man(9)GlcNAc(2) is produced by this enzyme. Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-1,3-D-mannosyl-D-mannose linkage. Galactosyltransferase I Xylosylprotein 4-beta-galactosyltransferase UDP-D-galactose:D-xylose galactosyltransferase Uridine diphosphogalactose-xylose galactosyltransferase UDP-D-galactose:xylose galactosyltransferase UDP-galactose + O-beta-D-xylosylprotein = UDP + 4-beta-D-galactosyl-O-beta-D-xylosylprotein. http://purl.uniprot.org/mim/130070 Manganese Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Galactosylxylosylprotein 3-beta-galactosyltransferase Galactosyltransferase II Uridine diphosphogalactose-galactosylxylose galactosyltransferase Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). UDP-galactose + 4-beta-D-galactosyl-O-beta-D-xylosylprotein = UDP + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein. Manganese Uridine diphosphate glucuronic acid:acceptor glucuronosyltransferase Glucuronosyltransferase I Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein = UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein. Manganese Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). UDP-glucose--vanillate 1-glucosyltransferase Gallate 1-beta-glucosyltransferase Vanillin is the best acceptor investigated. A number of substituted benzoic acids and, more slowly, cinnamic acids, can act as acceptors. UDP-glucose + gallate = UDP + 1-galloyl-beta-D-glucose. Floridoside-phosphate synthase sn-glycerol-3-phosphate 2-alpha-galactosyltransferase UDP-galactose + sn-glycerol 3-phosphate = UDP + 2-(alpha-D-galactosyl)-sn-glycerol 3-phosphate. The product is hydrolyzed by a phosphatase to floridoside (cf. EC 2.4.1.96). Mannotetraose 2-alpha-N-acetylglucosaminyltransferase Alpha-N-acetylglucosaminyltransferase UDP-N-acetyl-D-glucosamine + 1,3-alpha-D-mannosyl-1,2-alpha-D-mannosyl-1,2-alpha-D-mannosyl-D-mannose = UDP + 1,3-alpha-D-mannosyl-1,2-(N-acetyl-alpha-D-glucosaminyl-alpha-D-mannosyl)-1,2-alpha-D-mannosyl-D-mannose. Maltose synthase Neither free phosphate nor maltose 1-phosphate is an intermediate in the reaction. 2 alpha-D-glucose 1-phosphate + H(2)O = maltose + 2 phosphate. Sucrose-phosphate synthase UDP-glucose-fructose-phosphate glucosyltransferase Sucrosephosphate-UDP glucosyltransferase UDP-glucose + D-fructose 6-phosphate = UDP + sucrose 6-phosphate. Sucrose:1,6-, 1,3-alpha-D-glucan 3-alpha- and 6-alpha-D-glucosyltransferase Sucrose-1,6(3)-alpha-glucan 6(3)-alpha-glucosyltransferase Alternansucrase Transfers alternately an alpha-D-glucosyl residue from sucrose to the 6-position and the 3-position of the non-reducing terminal residue of an alpha-D-glucan, thus producing a glucan having alternating alpha-1,6- and alpha-1,3-linkages. The product, which has quite different properties from other dextrans, has been called alternan. N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-diphosphodolichol = UDP + N,N'-diacetylchitobiosyl-diphosphodolichol. Chitobiosyldiphosphodolichol beta-mannosyltransferase GDP-mannose-dolichol diphosphochitobiose mannosyltransferase Guanosine diphosphomannose-dolichol diphosphochitobiose mannosyltransferase http://purl.uniprot.org/mim/608540 GDP-mannose + chitobiosyldiphosphodolichol = GDP + beta-1,4-D-mannosylchitobiosyldiphosphodolichol. Uridine diphosphoacetylglucosamine-alpha-D-mannoside beta-1-2-acetylglucosaminyltransferase Acetylglucosaminyltransferase II Uridine diphosphoacetylglucosamine-alpha-1,6-mannosylglycoprotein beta-1-2-N-acetylglucosaminyltransferase N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase Alpha-1,6-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase UDP-GlcNAc:mannoside alpha-1-6 acetylglucosaminyltransferase N-acetylglucosaminyltransferase II Uridine diphosphoacetylglucosamine-mannoside alpha-1->6-acetylglucosaminyltransferase GnTII http://purl.uniprot.org/mim/212066 Note that this enzyme acts after N-acetylglucosaminyltransferase I (EC 2.4.1.101) but before N-acetylglucosaminyltransferases III (EC 2.4.1.144), IV (EC 2.4.1.145), V (EC 2.4.1.155) and VI (EC 2.4.1.201). R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor. UDP-N-acetyl-D-glucosamine + 6-(alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 6-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R. N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III Beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase N-acetylglucosaminyltransferase III Uridine diphosphoacetylglucosamine-glycopeptide beta-4-acetylglucosaminyltransferase III GnTIII Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor. The action of this enzyme probably prevents further attachment of N-acetylglucosamine residues to the growing carbohydrate chain. UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R = UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R. Uridine diphosphoacetylglucosamine-glycopeptide beta-4-acetylglucosaminyltransferase IV GnTIV N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IV N-acetylglucosaminyltransferase IV Beta-acetylglucosaminyltransferase IV Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase Alpha-1,3-mannosylglycoprotein beta-1,4-N-acetylglucosaminyltransferase The best acceptor for this enzyme is probably the same as that favored by EC 2.4.1.144. UDP-N-acetyl-D-glucosamine + 3-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 3-(2,4-bis(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R. R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor. O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase Elongation 3-beta-GalNAc-transferase Cf. EC 2.4.1.102, EC 2.4.1.147, and EC 2.4.1.148. UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,3-(N-acetyl-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R. O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III Core 3-beta-GlcNAc-transferase Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-galactosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-D-galactosaminyl-R. Cf. EC 2.4.1.102, EC 2.4.1.146, and EC 2.4.1.148. Core 6-beta-GalNAc-transferase B Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IV Cf. EC 2.4.1.102, EC 2.4.1.146, and EC 2.4.1.147. UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-D-galactosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,3)-N-acetyl-D-galactosaminyl-R. GnTE Poly-N-acetyllactosamine extension enzyme N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R. Acts on beta-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-alpha(1)-acid glycoprotein and other glycoproteins and oligosaccharides. Trehalose 6-phosphate synthase Transglucosylase Alpha,alpha-trehalose-phosphate synthase (UDP-forming) Trehalosephosphate-UDP glucosyltransferase Trehalose phosphate synthetase Trehalose phosphate synthase UDP-glucose--glucose-phosphate glucosyltransferase Trehalose 6-phosphate synthetase See also EC 2.4.1.36. UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate. N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase N-acetylglucosaminyltransferase Acts on beta-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-alpha(1)-acid glycoprotein. UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R. 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase Lewis-negative alpha-3-fucosyltransferase GDP-L-fucose:1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-L-fucosyltransferase Plasma alpha-3-fucosyltransferase Galactoside 3-fucosyltransferase Guanosine diphosphofucose-glucoside alpha-1->3-fucosyltransferase This enzyme fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4, unlike EC 2.4.1.65, which fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3. Normally acts on a glycoconjugate where R (see CA line) is a glycoprotein or glycolipid. GDP-beta-L-fucose + 1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R = GDP + 1,4-beta-D-galactosyl-(alpha-1,3-L-fucosyl)-N-acetyl-D-glucosaminyl-R. Dolichyl-phosphate acetylglucosaminyltransferase Dolichyl-phosphate alpha-N-acetylglucosaminyltransferase Dolichyl-phosphate N-acetylglucosaminyltransferase UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UDP + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate. Alpha-1,3(6)-mannosylglycoprotein beta-1,6-N-acetylglucosaminyltransferase Alpha-1,6-mannosyl-glycoprotein 6-beta-N-acetylglucosaminyltransferase Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase UDP-N-acetylglucosamine:alpha-mannoside-beta-1,6 N-acetylglucosaminyltransferase Uridine diphosphoacetylglucosamine-alpha-mannoside beta-1->6-acetylglucosaminyltransferase GnTV N-acetylglucosaminyltransferase V UDP-N-acetyl-D-glucosamine + 6-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 6-(2,6-bis(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R. R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor. Uridine diphosphogalactose-indolylacetylinositol galactosyltransferase Indolylacetyl-myo-inositol galactosyltransferase Indol-3-ylacetyl-myo-inositol galactoside synthase UDP-galactose + (indol-3-yl)acetyl-myo-inositol = UDP + 5-O-(indol-3-yl)acetyl-myo-inositol D-galactoside. 1,2-diacylglycerol 3-glucosyltransferase UDP-glucose-diacylglycerol glucosyltransferase UDP-glucose + 1,2-diacylglycerol = UDP + 3-D-glucosyl-1,2-diacylglycerol. Many diacylglycerols with long-chain acyl groups can act as acceptors. UDP-glucose-13-hydroxydocosanoate glucosyltransferase 13-glucosyloxydocosanoate 2'-beta-glucosyltransferase 13-hydroxydocosanoate 13-beta-glucosyltransferase 13-beta-D-glucosyloxydocosanoate can also act as acceptor, leading to the formation by Candida bogoriensis of the extracellular glycolipid, hydroxydocosanoate sophoroside diacetate. UDP-glucose + 13-hydroxydocosanoate = UDP + 13-beta-D-glucosyloxydocosanoate. Uridine diphosphorhamnose-flavonol 3-O-glucoside rhamnosyltransferase UDP-rhamnose:flavonol 3-O-glucoside rhamnosyltransferase Flavonol-3-O-glucoside L-rhamnosyltransferase Converts flavonol 3-O-glucosides to 3-O-rutinosides. UDP-L-rhamnose + a flavonol 3-O-D-glucoside = UDP + a flavonol 3-O-(beta-L-rhamnosyl-(1->6)-beta-D-glucoside). Also acts, more slowly, on rutin, quercetin 3-O-galactoside and flavonol 3-O-rhamnosides. Chitin-UDP acetyl-glucosaminyl transferase Chitin synthase Converts UDP-N-acetyl-D-glucosamine into chitin and UDP. UDP-N-acetyl-D-glucosamine + (1,4-(N-acetyl-beta-D-glucosaminyl))(n) = UDP + (1,4-(N-acetyl-beta-D-glucosaminyl))(n+1). UDP-glucose-pyridoxine glucosyltransferase Pyridoxine 5'-O-beta-D-glucosyltransferase UDP-glucose + pyridoxine = UDP + 5'-O-beta-D-glucosylpyridoxine. 4'-deoxypyridoxine and pyridoxamine can also act as acceptors, more slowly. Oligosaccharide 4-alpha-D-glucosyltransferase Amylase III Transfers the non-reducing terminal alpha-D-glucose residue from a 1,4-alpha-D-glucan to the 4-position of an alpha-D-glucan, thus bringing about the hydrolysis of oligosaccharides. Acts on amylose, amylopectin, glycogen and maltooligosaccharides, but not on maltose. No detectable free glucose is formed. Aldose beta-D-fructosyltransferase Alpha-D-aldosyl(1) beta-D-fructoside + D-aldose(2) = D-aldose(1) + alpha-D-aldosyl(2) beta-D-fructoside. Poly-N-acetyllactosamine extension enzyme Beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3-acetylglucosaminyltransferase UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide = UDP + N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide. Manganese Galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,6-N-acetylglucosaminyltransferase UDP-N-acetyl-D-glucosamine + D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide = UDP + N-acetyl-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide. Manganese N-acetylneuraminylgalactosylglucosylceramide beta-1,4-N-acetylgalactosaminyltransferase Only substances containing sialic acid residues can act as acceptors; bovine fetuin is the best acceptor tested. Manganese UDP-N-acetyl-D-galactosamine + N-acetylneuraminyl-2,3-alpha-D-galactosyl-1,4-beta-D-glucosylceramide = UDP + N-acetyl-D-galactosaminyl-1,4-beta-N-acetylneuraminyl-2,3-alpha-D-galactosyl-1,4-beta-D-glucosylceramide. Raffinose--raffinose alpha-galactosyltransferase Involved in the accumulation of the tetrasaccharides lychnose and isolychnose in the leaves of Cerastium arvense and other plants of the family Caryophyllaceae during late autumn. The 3(F) position of raffinose can also act as galactosyl acceptor. 2 raffinose = 1(F)-alpha-D-galactosylraffinose + sucrose. Sucrose 6(F)-alpha-galactosyltransferase Involved in the synthesis of the trisaccharide planteose and higher analogs in the seeds of Plantago and Sesamum species. UDP-galactose + sucrose = UDP + 6(F)-alpha-D-galactosylsucrose. Xyloglucan 4-glucosyltransferase Not identical with EC 2.4.1.12. Transfers a beta-D-glucosyl residue from UDP-glucose on to a glucose residue in xyloglucan, forming a beta-1,4-D-glucosyl-D-glucose linkage. Concurrent transfers of glucose and xylose are essential for this synthesis. In association with EC 2.4.2.39, brings about the synthesis of xyloglucan. UDP glucuronyltransferase Uridine diphosphoglucuronosyltransferase Uridine diphosphoglucuronate-estriol 16-alpha-glucuronosyltransferase UDPGT UDPglucuronate beta-D-glucuronosyltransferase (acceptor-unspecific) PNP-UDPGT UDP glucuronate-estriol glucuronosyltransferase UDP glucuronate-estradiol-glucuronosyltransferase Glucuronosyltransferase 1-naphthol glucuronyltransferase UDP glucuronic acid transferase Uridine diphosphoglucuronate-bilirubin glucuronosyltransferase 3-OH androgenic UDPGT 17-OH steroid UDPGT Uridine diphosphoglucuronate-1,2-diacylglycerol glucuronosyltransferase UDPGA-glucuronyltransferase GT 17-beta-hydroxysteroid UDP-glucuronosyltransferase UDP-glucuronosyltransferase Uridine diphosphate glucuronyltransferase Morphine glucuronyltransferase 4-nitrophenol UDP-glucuronyltransferase Uridine 5'-diphosphoglucuronyltransferase UDP-glucuronate-4-hydroxybiphenyl glucuronosyltransferase UDP-glucuronyltransferase 3-alpha-hydroxysteroid UDP-glucuronosyltransferase Uridine diphosphoglucuronate-estradiol glucuronosyltransferase Estriol UDPglucuronosyltransferase Phenyl-UDP-glucuronosyltransferase Ciramadol UDP-glucuronyltransferase UDPGA transferase p-phenylphenol glucuronyltransferase Bilirubin uridine diphosphoglucuronyltransferase 4-methylumbelliferone UDP-glucuronosyltransferase Bilirubin monoglucuronide glucuronyltransferase p-nitrophenol UDP-glucuronyltransferase Uridine diphosphoglucuronate-estriol glucuronosyltransferase Estrone UDPglucuronosyltransferase Bilirubin UDP-glucuronosyltransferase Uridine diphosphoglucuronate-4-hydroxybiphenyl glucuronosyltransferase Uridine diphosphoglucuronate-bilirubin glucuronoside glucuronosyltransferase Uridine diphosphoglucuronyltransferase Bilirubin UDPGT p-nitrophenylglucuronosyltransferase 1-naphthol-UDP-glucuronosyltransferase p-hydroxybiphenyl UDP glucuronyltransferase p-nitrophenol UDP-glucuronosyltransferase 4-nitrophenol UDPGT UDP-glucuronate-bilirubin glucuronyltransferase Bilirubin glucuronyltransferase 4-hydroxybiphenyl UDP-glucuronosyltransferase http://purl.uniprot.org/mim/606785 http://purl.uniprot.org/mim/143500 A temporary nomenclature for the various forms whose delineation is in a state of flux. http://purl.uniprot.org/mim/218800 Some of the activities catalyzed were previously listed separately as EC 2.4.1.42, EC 2.4.1.59, EC 2.4.1.61, EC 2.4.1.76, EC 2.4.1.77, EC 2.4.1.84, EC 2.4.1.107 and EC 2.4.1.108. UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside. Family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines and fatty acids. http://purl.uniprot.org/mim/237900 Isoflavone 7-O-glucosyltransferase The enzyme does not act on isoflavanones, flavones, flavanones, flavanols or coumarins. UDP-glucose + an isoflavone = UDP + an isoflavone 7-O-beta-D-glucoside. The 4'-methoxy isoflavones biochanin A and formononetin and, more slowly, the 4'-hydroxy isoflavones genistein and daidzein, can act as acceptors. Methyl-ONN-azoxymethanol beta-D-glucosyltransferase Cycasin synthase Brings about the biosynthesis of the toxic substance cycasin in the leaves of Japanese cycad, Cycas revoluta. UDP-glucose + CH(3)-N(O)=N-CH(2)OH = UDP + cycasin. Salicyl-alcohol beta-D-glucosyltransferase UDP-glucose + salicyl alcohol = UDP + salicin. Sterol 3-beta-glucosyltransferase UDP-glucose + a sterol = UDP + a sterol 3-beta-D-glucoside. Not identical with EC 2.4.1.192 or EC 2.4.1.193. Uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase I N-acetylgalactosaminyltransferase I Glucuronylgalactosylproteoglycan beta-1,4-N-acetylgalactosaminyltransferase Glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase Involved in the biosynthesis of chondroitin sulfate. UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-D-galactosyl-proteoglycan = UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronyl-1,3-beta-D-galactosylproteoglycan. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core. N-acetylgalactosaminyltransferase II Glucuronyl-N-acetylgalactosaminylproteoglycan beta-1,4-N-acetylgalactosaminyltransferase Chondroitin synthase Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase Uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase II UDP-N-acetyl-D-galactosamine:D-glucuronyl-N-acetyl-1,3-beta-D-galactosaminylproteoglycan beta-1,4-N-acetylgalactosaminyltransferase Involved in the biosynthesis of chondroitin sulfate. Similar chondroitin synthase 'copolymerases' can be found in Pasteurella multocida and Escherichia coli. The human form of this enzyme is a bifunctional glycosyltransferase, which also has the EC 2.4.1.226 activity required for the synthesis of the chondroitin sulfate disaccharide repeats. UDP-N-acetyl-D-galactosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-proteoglycan = UDP + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-proteoglycan. Gibberellin beta-D-glucosyltransferase Acts on the plant hormone gibberellin GA(3) and related compounds. UDP-glucose + gibberellin = UDP + gibberellin 2-O-beta-D-glucoside. Cinnamate beta-D-glucosyltransferase UDP-glucose + trans-cinnamate = UDP + trans-cinnamoyl beta-D-glucoside. Involved in the biosynthesis of chlorogenic acid in the root of the sweet potato. 4-coumarate, 2-coumarate, benzoate, feruloate and caffeate can also act as acceptors, more slowly. Hydroxymandelonitrile glucosyltransferase Cyanohydrin glucosyltransferase UDP-glucose + 4-hydroxymandelonitrile = UDP + taxiphyllin. 3,4-dihydroxymandelonitrile can also act as acceptor. Lactosylceramide beta-1,3-galactosyltransferase UDP-galactose + D-galactosyl-1,4-beta-D-glucosyl-R = UDP + D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosyl-R. R may be an oligosaccharide or a glycolipid. Involved in the elongation of oligosaccharide chains, especially in glycolipids. Lactose can also act as acceptor, more slowly. Amylo-(1,4 to 1,6)transglucosidase Branching enzyme 1,4-alpha-glucan branching enzyme Glycogen branching enzyme Amylo-(1,4->1,6)-transglycosylase The description (official rdfs:label) requires a qualification depending on the product, glycogen or amylopectin, e.g. glycogen branching enzyme, amylopectin branching enzyme. Converts amylose into amylopectin. http://purl.uniprot.org/mim/232500 http://purl.uniprot.org/mim/263570 Transfers a segment of a 1,4-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain. The latter has frequently been termed Q-enzyme. Lipopolysaccharide N-acetylmannosaminouronosyltransferase UDP-N-acetyl-beta-D-mannosaminouronate + lipopolysaccharide = UDP + N-acetyl-beta-D-mannosaminouronosyl-1,4-lipopolysaccharide. Involved in the biosynthesis of common antigen in Enterobacteriaceae. Hydroxyanthraquinone glucosyltransferase A range of anthraquinones and some flavones can act as acceptors; best substrates are emodin, anthrapurpurin, quinizarin, 2,6-dihydroxyanthraquinone and 1,8-dihydroxyanthraquinone. UDP-glucose + an hydroxyanthraquinone = UDP + a glucosyloxyanthraquinone. Lipid-A-disaccharide synthase Involved with EC 2.3.1.129 and EC 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Escherichia coli. UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate = UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate. Alpha-1,3-glucan synthase UDP-glucose + (alpha-D-glucosyl-(1-3))(n) = UDP + (alpha-D-glucosyl-(1-3))(n+1). A glucan primer is needed to begin the reaction, which brings about elongation of the glucan chains. Galactolipid:galactolipid galactosyltransferase Digalactosyldiacylglycerol synthase Galactolipid galactosyltransferase GGGT Interlipid galactosyltransferase Galactolipid-galactolipid galactosyltransferase DGDG synthase By further transfers of galactosyl residues to the digalactosyldiacylglycerol, trigalactosyldiacylglycerol and tetragalactosyldiacylglycerol are also formed. Its activity is localized to chloroplast envelope membranes, but it does not contribute to net galactolipid synthesis in plants. 2 3-(beta-D-galactosyl)-1,2-diacyl-sn-glycerol = 3-(alpha-D-galactosyl-(1->6)-beta-D-galactosyl)-1,2-diacyl-sn-glycerol + 1,2-diacyl-sn-glycerol. Was originally thought to be the major enzyme involved in the production of digalactosyldiacylglycerol in plants as it masked the effect of the true enzyme (EC 2.4.1.241). Flavanone 7-O-beta-glucosyltransferase No action on flavones or flavonols. UDP-glucose + a flavanone = UDP + a flavanone 7-O-beta-D-glucoside. Naringenin and hesperetin can act as acceptors. Glycogenin glucosyltransferase Priming glucosyltransferase Glycogenin It continues to glucosylate an existing glucosyl group until a length of about 5-13 residues has been formed. Manganese Further lengthening of the glycogen chain is then carried out by EC 2.4.1.11. UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin. Thus primate liver contains glycogenin-2, of molecular mass 66 kDa, whereas the more widespread form is glycogenin-1, with a molecular mass of 38 kDa. Various forms of the enzyme exist, and different forms predominate in different organs. Not highly specific for the donor, using UDP-xylose in addition to UDP-glucose (although not glucosylating or xylosylating a xylosyl group so added). It can also use CDP-glucose and TDP-glucose, but not ADP-glucose or GDP-glucose. The first reaction of this enzyme is to catalyze its own glucosylation, normally at a specific Tyr of the protein if this group is free; when the Tyr is replaced by Thr or Phe, the enzyme's self-glucosylation activity is lost but its intermolecular transglucosylation ability remains. Similarly it is not highly specific for the acceptor, using water (i.e. hydrolyzing UDP-glucose) among others. N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase Involved in the biosynthesis of teichoic acid linkage units in bacterial cell walls. UDP-N-acetyl-D-mannosamine + N-acetyl-D-glucosaminyldiphosphoundecaprenol = UDP + N-acetyl-beta-D-mannosaminyl-1,4-N-acetyl-D-glucosaminyldiphosphoundecaprenol. N-acetylglucosaminyldiphosphoundecaprenol glucosyltransferase UDP-glucose + N-acetyl-D-glucosaminyldiphosphoundecaprenol = UDP + beta-D-glucosyl-1,4-N-acetyl-D-glucosaminyldiphosphoundecaprenol. Luteolin 7-O-glucuronosyltransferase UDP-glucuronate + luteolin = UDP + luteolin 7-O-beta-D-glucuronide. Cyclodextrin glucanotransferase Cyclomaltodextrin glucanotransferase Cyclodextrin glycosyltransferase Bacillus macerans amylase Cyclizes part of a 1,4-alpha-D-glucan chain by formation of a 1,4-alpha-D-glucosidic bond. Also disproportionates linear maltodextrins without cyclizing (cf. EC 2.4.1.25). Cyclomaltodextrins (Schardinger dextrins) of various sizes (6, 7, 8, etc. glucose units) are formed reversibly from starch and similar substrates. LMT Uridine diphosphoglucuronate-luteolin 7-O-glucuronide glucuronosyltransferase Luteolin-7-O-glucuronide 2''-O-glucuronosyltransferase UDP-glucuronate + luteolin 7-O-beta-D-glucuronide = UDP + luteolin 7-O-(beta-D-glucuronosyl-(1->2)-beta-D-glucuronide). Luteolin-7-O-diglucuronide 4'-O-glucuronosyltransferase UDP-glucuronate + luteolin 7-O-beta-D-diglucuronide = UDP + luteolin 7-O-(beta-D-glucuronosyl-(1->2)-beta-D-glucuronide)-4'-O-beta-D-glucuronide. Nuatigenin 3-beta-glucosyltransferase Involved in the biosynthesis of plant saponins. UDP-glucose + (20S,22S,25S)-22,25-epoxyfurost-5-ene-3-beta,26-diol = UDP + (20S,22S,25S)-22,25-epoxyfurost-5-ene-3-beta,26-diol 3-O-beta-D-glucoside. Not identical with EC 2.4.1.173 or EC 2.4.1.193. Some other sapogenins can act as glucosyl acceptors. Sarsapogenin 3-beta-glucosyltransferase Not identical with EC 2.4.1.173 or EC 2.4.1.192. Specific to 5-beta-spirostanols. UDP-glucose + (25S)-5-beta-spirostan-3-beta-ol = UDP + (25S)-5-beta-spirostan-3-beta-ol 3-O-beta-D-glucoside. Involved in the biosynthesis of plant saponins. 4-hydroxybenzoate 4-O-beta-D-glucosyltransferase UDP-glucose + 4-hydroxybenzoate = UDP + 4-(beta-D-glucosyloxy)benzoate. Thiohydroximate S-glucosyltransferase N-hydroxythioamide S-beta-glucosyltransferase Thiohydroximate beta-D-glucosyltransferase Thiohydroximate glucosyltransferase Desulfoglucosinolate-uridine diphosphate glucosyltransferase Uridine diphosphoglucose-thiohydroximate glucosyltransferase UDP-glucose + N-hydroxy-2-phenylethanethioamide = UDP + desulfoglucotropeolin. Involved with EC 2.8.2.24 in the biosynthesis of thioglucosides in cruciferous plants. Nicotinate glucosyltransferase UDP-glucose + nicotinate = UDP + N-glucosylnicotinate. High-mannose-oligosaccharide beta-1,4-N-acetylglucosaminyltransferase Transfers an N-acetyl-D-glucosamine residue from UDP-N-acetyl-D-glucosamine to the 4-position of a mannose linked alpha-1,6 to the core mannose of high-mannose oligosaccharides produced by Dictyostelium discoideum. The activity of the intersecting mannose residue as acceptor is dependent on two other mannose residues attached by alpha-1,3 and alpha-1,6 links. Phosphatidylinositol N-acetylglucosaminyltransferase Uridine diphosphoacetylglucosamine alpha-1,6-acetyl-D-glucosaminyltransferase UDP-N-acetyl-D-glucosamine:phosphatidylinositol N-acetyl-D-glucosaminyltransferase In mammalian cells, the enzyme is composed of at least five subunits (PIG-A, PIG-H, PIG-C, GPI1 and PIG-P). PIG-A subunit is the catalytic subunit. Involved in the first step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. In some species, the long-chain acyl groups of the phosphatidyl group are partly replaced by long-chain alkyl or alk-1-enyl groups. UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol. http://purl.uniprot.org/mim/311770 Beta-mannosylphosphodecaprenol--mannooligosaccharide 6-mannosyltransferase Involved in the formation of mannooligosaccharides in the membrane of Mycobacterium smegmatis. Beta-D-mannosylphosphodecaprenol + 1,6-alpha-D-mannosyloligosaccharide = decaprenol phosphate + 1,6-alpha-D-mannosyl-1,6-alpha-D-mannosyl-oligosaccharide. Dextrin 6-glucosyltransferase Dextrin dextranase (1,4-alpha-D-glucosyl)(n) + (1,6-alpha-D-glucosyl)(m) = (1,4-alpha-D-glucosyl)(n-1) + (1,6-alpha-D-glucosyl)(m+1). Cellobiose phosphorylase Cellobiose + phosphate = alpha-D-glucose 1-phosphate + D-glucose. N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase VI GnTVI Uridine diphosphoacetylglucosamine-glycopeptide beta-1->4-acetylglucosaminyltransferase VI N-acetylglucosaminyltransferase VI Mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase Alpha-1,6-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase UDP-N-acetyl-D-glucosamine + 2,6-bis(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl-R = UDP + 2,4,6-tris(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl-R. R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor. 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase UDP-glucose + 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one = UDP + 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucoside. Zeatin O-beta-D-glucosyltransferase Uridine diphosphoglucose-zeatin O-glucosyltransferase Trans-zeatin O-beta-D-glucosyltransferase Zeatin O-glucosyltransferase UDP-glucose + trans-zeatin = UDP + O-beta-D-glucosyl-trans-zeatin. Unlike EC 2.4.1.215, UDP-xylose can also act as donor (cf. EC 2.4.2.40). Galactogen 6-beta-galactosyltransferase 1,6-D-galactosyltransferase Galactogen from Helix pomatia is the most effective acceptor. UDP-galactose + galactogen = UDP + 1,6-beta-D-galactosylgalactogen. Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase UDP-N-acetyl-D-glucosamine + D-galactosyl-1,4-beta-D-glucosylceramide = UDP + N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide. Xyloglucan:xyloglucosyl transferase Xyloglucan endotransglycosylase Endo-xyloglucan transferase Breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan. Does not use cello-oligosaccharides as either donor or acceptor. Monoglucosyl diacylglycerol (1->2) glucosyltransferase MGlcDAG (1->2) glucosyltransferase DGlcDAG synthase Diglucosyl diacylglycerol synthase Magnesium UDP-glucose + 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol = 1,2-diacyl-3-O-(alpha-D-glucopyranosyl(1->2)-O-alpha-D-glucopyranosyl)-sn-glycerol + UDP. Cis-p-coumarate glucosyltransferase The corresponding trans-isomers are not substrates. UDP-glucose + cis-p-coumarate = 4'-O-beta-D-glucosyl-cis-p-coumarate + UDP. Cis-caffeic acid also serves as a glucosyl acceptor with the enzyme from Sphagnum fallax kinggr. Glycogen synthase ADP-glucose--starch glucosyltransferase Starch synthase Starch (bacterial glycogen) synthase The description (official rdfs:label) various according to the source of the enzyme and the nature of its synthetic product, e.g. starch synthase, bacterial glycogen synthase. A similar enzyme utilizes UDP-glucose (cf. EC 2.4.1.11). ADP-glucose + (1,4-alpha-D-glucosyl)(n) = ADP + (1,4-alpha-D-glucosyl)(n+1). Limonoid UDP-glucosyltransferase Limonoid glucosyltransferase LGTase UDP-glucose + limonin = glucosyl-limonin + UDP. The enzyme purified from navel orange albedo tissue also acts on the related tetranortriterpenoid nomilin. 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase Beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine + phosphate = alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine. Reaction also occurs with beta-D-galactopyranosyl-(1->3)-N-acetyl-D-galactosamine as the substrate, giving N-acetyl-D-galactosamine as the product. HAS Hyaluronan synthase Adds GlcNAc to nascent hyaluronan when the non-reducing end is GlcA, but it adds GlcA when the non-reducing end is GlcNAc. Magnesium (1) UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-(nascent hyaluronan) = UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-(nascent hyaluronan). Highly specific for UDP-GlcNAc and UDP-GlcA; no copolymerization is observed if either is replaced by UDP-Glc, UDP-Gal, UDP-GalNAc or UDP-GalA. (2) UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-(nascent hyaluronan) = UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-(nascent hyaluronan). Glucosylglycerol-phosphate synthase Glucosyl-glycerol-phosphate synthase GGPS GG-phosphate synthase ADP-glucose + sn-glycerol 3-phosphate = 2-(beta-D-glucosyl)-sn-glycerol 3-phosphate + ADP. Acts with EC 3.1.3.69 to form glucosylglycerol, an osmolyte that endows cyanobacteria with resistance to salt. GDP-L-Fuc:Asn-linked GlcNAc alpha-1,3-fucosyltransferase GDP-fucose:beta-N-acetylglucosamine (Fuc to (Fuc-alpha-1->6-GlcNAc)-Asn-peptide) alpha-1->3-fucosyltransferase Glycoprotein 3-alpha-L-fucosyltransferase GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha-1,3-fucosyltransferase The N-glycan products of this enzyme are present in plants, insects and some other invertebrates (e.g., Schistosoma, Haemonchus, Lymnaea). Manganese This enzyme catalyzes a reaction similar to that of EC 2.4.1.68, but transferring the L-fucosyl group from GDP-beta-L-fucose to form an alpha-1,3-linkage rather than an alpha-1,6-linkage. GDP-L-fucose + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)asparagine = GDP + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-(alpha-L-fucosyl-(1->3))-N-acetyl-beta-D-glucosaminyl)asparagine. The enzyme transfers to N-linked oligosaccharide structures (N-glycans), generally with a specificity for N-glycans with one unsubstituted non-reducing terminal GlcNAc residue. Cis-zeatin O-beta-D-glucosyltransferase Unlike EC 2.4.1.203 UDP-xylose cannot act as a donor. UDP-glucose + cis-zeatin = UDP + O-beta-D-glucosyl-cis-zeatin. The enzyme from maize can use cis-zeatin and UDPglucose as substrates, but not cis-ribosylzeatin, trans-zeatin or trans-ribosylzeatin. Trehalose 6-phosphate phosphorylase Trehalose 6-phosphate + phosphate = glucose 6-phosphate + beta-D-glucose 1-phosphate. The enzyme from Lactococcus lactis is specific for trehalose 6-phosphate. Differs from EC 2.4.1.64 in that trehalose is not a substrate. Mannosyl-3-phosphoglycerate synthase MPG synthase GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate. Magnesium The enzyme is absolutely specific for GDP-mannose and 3-phosphoglycerate, and transfers the mannosyl group with retention of configuration. In the hyperthermophilic archaeon Pyrococcus horikoshii, the mannosyl-3-phosphoglycerate formed is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70, producing mannosylglycerate. Arbutin synthase Hydroquinone glucosyltransferase Hydroquinone:O-glucosyltransferase Hydroquinone is the most effective acceptor, but over 40 phenolic compounds are also glucosylated, but at lower rates. UDP-glucose + hydroquinone = UDP + hydroquinone-O-beta-D-glucopyranoside. Vomilenine glucosyltransferase UDPG:vomilenine 21-beta-D-glucosyltransferase The indole alkaloid raucaffricine accumulates during the culture of Rauvolfia cell suspensions. UDP-glucose + vomilenine = UDP + raucaffricine. N-acetyllactosamine synthase Lactose synthase UDP-galactose--glucose galactosyltransferase The enzyme is a complex of 2 proteins A and B. In the absence of the B protein (alpha-lactalbumin) the enzyme catalyzes the transfer of galactose from UDP-galactose to N-acetylglucosamine (cf. EC 2.4.1.90). UDP-galactose + D-glucose = UDP + lactose. Indoxyl-UDPG-glucosyltransferase Indoxyl-UDPG glucosyltransferase Also acts to a limited extent on 4-, 5-, 6-and 7-hydroxyindole. UDP-glucose + indoxyl = UDP + indican. After enzymic or chemical hydrolysis, indican forms indoxyl, which, in turn, is converted in the presence of oxygen to the dye indigo. Peptide-O-fucosyltransferase GDP-fucose:polypeptide fucosyltransferase GDP-fucose protein O-fucosyltransferase GDP-L-fucose:polypeptide fucosyltransferase Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor. The attachment of O-linked fucose to serine or threonine occurs on EGF domains within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys. Involved in the biosynthesis of O-fucosylated epidermal growth factor (EGF) and thrombospondin type 1 repeats. O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase O-fucosylpeptide beta-1,3-N-acetylglucosaminyltransferase O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferases are the products of fringe genes. http://purl.uniprot.org/mim/609813 O-linked fucose is an unusual form of glycosylation where the fucose is attached directly to proteins through the hydroxy groups of Ser or Thr residues. Transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor. Glucuronosylgalactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase Alpha-N-acetylglucosaminyltransferase I Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase Alpha-1,4-N-acetylglucosaminyltransferase Enzyme involved in the initiation of heparin and heparan sulfate synthesis, transferring GlcNAc to the (GlcA-Gal-Gal-Xyl-)Ser core. UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan = UDP + alpha-N-acetyl-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan. Apparently products of both the human EXTL2 and EXTL3 genes can catalyze this reaction. In Caenorhabditis elegans, the product of the rib-2 gene displays this activity as well as that of EC 2.4.1.224. Glucuronyl-N-acetylglucosaminylproteoglycan alpha-1,4-N-acetylglucosaminyltransferase Alpha-N-acetylglucosaminyltransferase II Glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase Other human forms of this enzyme (e.g. the product of the EXTL1 gene) have only the 4-alpha-N-acetylglucosaminyltransferase activity. Involved in the biosynthesis of heparin and heparan sulfate. http://purl.uniprot.org/mim/133701 UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan = UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan. http://purl.uniprot.org/mim/133700 In Caenorhabditis elegans, the product of the rib-2 gene displays the activities of this enzyme as well as EC 2.4.1.223. http://purl.uniprot.org/mim/215300 Some forms of the enzyme from human (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the EC 2.4.1.225 activity required for the synthesis of the heparan sulfate disaccharide repeats. http://purl.uniprot.org/mim/150230 http://purl.uniprot.org/mim/601224 N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase N-acetylglucosaminylproteoglycan beta-1,4-glucuronyltransferase Heparan glucuronyltransferase II http://purl.uniprot.org/mim/150230 http://purl.uniprot.org/mim/601224 Some forms of the human enzyme (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the EC 2.4.1.244 activity required for the synthesis of the heparan sulfate disaccharide repeats. UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan. http://purl.uniprot.org/mim/133700 http://purl.uniprot.org/mim/133701 Involved in the biosynthesis of heparin and heparan sulfate. N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase Chondroitin glucuronyltransferase II The human chondroitin synthetase is a bifunctional glycosyltransferase, which also has the EC 2.4.1.175 activity required for the synthesis of the chondroitin sulfate disaccharide repeats. UDP-alpha-D-glucuronate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan. There is also another human protein with apparently only the 3-beta-glucuronosyltransferase activity. Similar chondroitin synthase 'copolymerases' can be found in Pasteurella multocida and Escherichia coli. Involved in the biosynthesis of chondroitin and dermatan sulfate. Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase MurG transferase Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase The undecaprenol involved is ditrans,octacis-undecaprenol. UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-center, as it is in Gram-negative and some Gram-positive organisms. Histo-blood group P(k) UDP-galactose Lactosylceramide 4-alpha-galactosyltransferase Globotriaosylceramide/CD77 synthase Gal-beta-1-4Glc-beta-1-Cer alpha-1,4-galactosyltransferase UDP-galactose + beta-D-galactosyl-(1->4)-D-glucosylceramide = UDP + alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-D-glucosylceramide. UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase UDP-GlcNAc:hydroxyproline polypeptide GlcNAc-transferase [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase Skp1-HyPro GlcNAc-transferase UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase The fucose residue is probably in the alpha configuration. This enzyme commences the building up of a pentasaccharide (Gal-alpha-1-6Gal-alpha-1-L-Fuc-alpha-1-2Gal-beta-1-3GlcNAc) on Hyp-143 of the Dictyostelium protein Skp1, which is required for the ubiquitination of cell-cycle regulatory proteins and transcription factors. Requires dithiothreitol and a divalent cation for activity. The specificity of the enzyme for Skp1-Hyp-143 and its high affinity for this substrate suggests that it is the GlcNAc-transferase that modifies Skp1 in vivo. UDP-N-acetylglucosamine + [Skp1-protein]-hydroxyproline = UDP + [Skp1-protein]-O-(N-acetyl-D-glucosaminyl)hydroxyproline. Sphingosine beta-galactosyltransferase Psychosine--UDP galactosyltransferase UDP-galactose + sphingosine = UDP + psychosine. Kojibiose phosphorylase The enzyme is inactive when dissaccharides with linkages other than alpha-1,2 linkages, such as sophorose, trehalose, neotrehalose, nigerose, laminaribiose, maltose, cellobiose, isomaltose, gentiobiose, sucrose and lactose, are used as substrates. The enzyme from Thermoanaerobacter brockii can act with alpha-1,2-oligoglucans, such as selaginose, as substrate, but more slowly. 2-alpha-D-glucosyl-D-glucose + phosphate = D-glucose + beta-D-glucose 1-phosphate. Trehalose phosphorylase Alpha,alpha-trehalose phosphorylase (configuration-retaining) Alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate. Unlike EC 2.4.1.64, this enzyme retains its anomeric configuration. Vanadate is a strong competitive inhibitor of this reversible reaction. GDP-mannose:oligosaccharide 1,6-alpha-D-mannosyltransferase Initiation-specific alpha-1,6-mannosyltransferase Alpha-1,6-mannosyltransferase GDP-mannose:glycolipid 1,6-alpha-D-mannosyltransferase Glycolipid 6-alpha-mannosyltransferase Manganese Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-1,6-D-mannosyl-D-mannose linkage. Man(8)GlcNAc and Man(9)GlcNAc are equally good substrates. In Saccharomyces cerevisiae, this enzyme catalyzes an essential step in the outer chain elongation of N-linked oligosaccharides. F3GalTase Kaempferol 3-O-galactosyltransferase UDP-galactose + kaempferol = UDP + kaempferol 3-O-beta-D-galactoside. The reaction can occur equally well in both directions. Acts on the endogenous flavonols kaempferol and quercetin, to a lesser extent on myricetin and fisetin, and weakly on galangin and isorhamnetin. 1->2 UDP-rhamnosyltransferase UDP-rhamnose:flavanone-7-O-glucoside-2''-O-rhamnosyltransferase Flavanone 7-O-glucoside 2''-O-beta-L-rhamnosyltransferase Acts on the 7-O-glucoside of naringenin and hesperetin, also the flavone 7-O-glucosides of luteolin and apigenin. UDP-L-rhamnose + a flavanone 7-O-glucoside = UDP + a flavanone 7-O-(beta-L-rhamnosyl-(1->2)-beta-D-glucoside). UDP-glucose:flavonol 7-O-glucosyltransferase Flavonol 7-O-beta-glucosyltransferase Acts on the flavonols gossypetin (8-hydroxyquercetin) and to a lesser extent on quercetin, kaempferol and myricetin. UDP-glucose + a flavonol = UDP + a flavonol 7-O-beta-D-glucoside. UDP-glucose:anthocyanin 3'-O-glucosyltransferase 3'GT Anthocyanin 3'-O-beta-glucosyltransferase Acts on delphinidin 3,5-di-O-glucoside in gentian (Gentiana triflora). This enzyme specifically glucosylates the 3'-hydroxy group of delphinidin-3-O-glucosyl-5-O-(6-O-caffeoylglucosyl)-3'-O-(6-O-caffeoylglucoside)-type anthocyanins containing glucose groups at the 3 and 5 positions. UDP-glucose + an anthocyanin = UDP + an anthocyanin 3'-O-beta-D-glucoside. Flavonol-3-O-glucoside glucosyltransferase One of three specific glucosyltransferases in pea (Pisum sativum) that successively add a beta-D-glucosyl group first to O-3 of kaempferol, and then to O-2 of the previously added glucosyl group giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see also EC 2.4.1.91 and EC 2.4.1.240). TDP-glucose can replace UDP-glucose as the glucose donor but the reaction proceeds more slowly. UDP-glucose + a flavonol 3-O-beta-D-glucoside = UDP + a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside. Oligoglucan-branching glycosyltransferase 1,4-alpha-glucan 6-alpha-glucosyltransferase Transfers an alpha-D-glucosyl residue in a 1,4-alpha-D-glucan to the primary hydroxy group of glucose, free or combined in a 1,4-alpha-D-glucan. Flavonol-3-O-glycoside glucosyltransferase One of three specific glucosyltransferases in pea (Pisum sativum) that successively add a beta-D-glucosyl group first to O-3 of kaempferol, and then to O-2 of the previously added glucosyl group giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see also EC 2.4.1.91 and EC 2.4.1.239). UDP-glucose + a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside = UDP + a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside. DGDG synthase UDP-galactose-dependent DGDG synthase UDP-galactose:MGDG galactosyltransferase UDP-galactose-dependent digalactosyldiacylglycerol synthase Digalactosyldiacylglycerol synthase Magnesium Diacylglycerol cannot serve as an acceptor molecule for galactosylation as in the reaction catalyzed by EC 2.4.1.46. The enzyme has been localized to the outer side of chloroplast envelope membranes. UDP-galactose + 3-(beta-D-galactosyl)-1,2-diacyl-sn-glycerol = UDP + 3-(alpha-D-galactosyl-(1->6)-beta-D-galactosyl)-1,2-diacyl-sn-glycerol. DGD2 is responsible for the synthesis of DGDG molecular species that are rich in C16 fatty acids at sn-1 of diacylglycerol whereas DGD1 leads to molecular species rich in C18 fatty acids. While both DGD1 and DGD2 are increased under phosphate-limiting conditions, DGD2 does not contribute significantly under optimal growth conditions. When phosphate is limiting, phospholipids in plant membranes are reduced but these are replaced, at least in part, by the glycolipids digalactosyldiacylglycerol (DGDG) and sulfoquinovosyldiacylglycerol. Granule-bound starch synthase II Granule-bound starch synthase I Starch synthase II NDPglucose-starch glucosyltransferase GBSSII GBSSI NDP-glucose--starch glucosyltransferase Waxy protein Starch granule-bound nucleoside diphosphate glucose-starch glucosyltransferase GBSS Granule-bound starch synthase NDP-glucose + (1,4-alpha-D-glucosyl)(n) = NDP + (1,4-alpha-D-glucosyl)(n+1). Mutants that lack the Wx (waxy) allele cannot produce this enzyme, which plays an important role in the normal synthesis of amylose. Unlike EC 2.4.1.11 and EC 2.4.1.21 which use UDP-glucose and ADP-glucose, respectively, this enzyme can use either UDP-or ADP-glucose. In such mutants, only amylopectin is produced in the endosperm or pollen. 6(G)-FFT 6(G)-fructotransferase 6(G)-FT 6(G)-fructosyltransferase Fructan:fructan 6(G)-fructosyltransferase Sucrose cannot be a donor substrate in the reaction (i.e. m cannot be zero) and inulin cannot act as an acceptor. This enzyme catalyzes the transfer of the terminal (2->1)-linked beta-D-fructosyl group of a mono-or oligosaccharide substituent on O-1 of the fructose residue of sucrose onto O-6 of its glucose residue. For example, if 1-kestose (1(F)-(beta-D-fructofuranosyl)sucrose) is both the donor and recipient in the reaction shown above, i.e., if m = 1 and n = 1, then the products will be sucrose and 6(G)-di-beta-D-fructofuranosylsucrose. Side reactions catalyzed are transfer of a beta-D-fructosyl group between compounds of the structure 1(F)-(1-beta-D-fructofuranosyl)(m)-6(G)-(1-beta-D-fructofuranosyl)(n) sucrose, where m >= 0 and n = 1 for the donor, and m >= 0 and n >= 0 for the acceptor. (1-beta-D-fructofuranosyl-(2->1)-)(m+1) alpha-D-glucopyranoside + (1-beta-D-fructofuranosyl-(2->1)-)(n+1) alpha-D-glucopyranoside = (1-beta-D-fructofuranosyl-(2->1)-)(m) alpha-D-glucopyranoside + (1-beta-D-fructofuranosyl-(2->1)-)(n+1) beta-D-fructofuranosyl-(2->6)-alpha-D-glucopyranoside (m > 0; n >= 0). In this notation, the superscripts F and G are used to specify whether the fructose or glucose residue of the sucrose carries the substituent; alternatively, this may be indicated by the presence and/or absence of primes. Beta-1,4-N-acetylgalactosaminyltransferase Beta-4GalNAc-T3 N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase Beta-4GalNAc-T4 The N-acetyl-beta-D-glucosaminyl group is normally on a core oligosaccharide although benzyl glycosides have been used in enzyme-characterization experiments. The enzyme from human can transfer N-acetyl-D-galactosamine (GalNAc) to N-glycan and O-glycan substrates that have N-acetyl-D-glucosamine (GlcNAc) but not D-glucuronic acid (GlcUA) at their non-reducing end. UDP-N-acetyl-D-galactosamine + N-acetyl-beta-D-glucosaminyl group = UDP + N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl group. Some glycohormones, e.g. lutropin and thyrotropin contain the N-glycan structure containing the N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl group. D-enzyme Dextrin glycosyltransferase Disproportionating enzyme 4-alpha-glucanotransferase Oligo-1,4-1,4-glucantransferase An enzymic activity of this nature forms part of the mammalian and Saccharomyces cerevisiae glycogen branching system (see EC 3.2.1.33). Transfers a segment of a 1,4-alpha-D-glucan to a new position in an acceptor, which may be glucose or a 1,4-alpha-D-glucan. http://purl.uniprot.org/mim/232400 DNA alpha-glucosyltransferase Transfers an alpha-D-glucosyl residue from UDP-glucose to an hydroxymethylcytosine residue in DNA. DNA beta-glucosyltransferase Transfers a beta-D-glucosyl residue from UDP-glucose to an hydroxymethylcytosine residue in DNA. Glucosyl-DNA beta-glucosyltransferase Transfers a beta-D-glucosyl residue from UDP-glucose to a glucosylhydroxymethylcytosine residue in DNA. GDP-glucose-cellulose glucosyltransferase Cellulose synthase (GDP-forming) GDP-glucose-beta-D-glucan glucosyltransferase A similar enzyme utilizes UDP-glucose (cf. EC 2.4.1.12). GDP-glucose + (1,4-beta-D-glucosyl)(n) = GDP + (1,4-beta-D-glucosyl)(n+1). Involved in the synthesis of cellulose. 1,3-beta-oligoglucan phosphorylase Beta-1,3-oligoglucan:orthophosphate glucosyltransferase II (1,3-beta-D-glucosyl)(n) + phosphate = (1,3-beta-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate. Does not act on laminarin. Differs in specificity from EC 2.4.1.31 and EC 2.4.1.97. Laminaribiose phosphorylase Also acts on 1,3-beta-D-oligoglucans. 3-beta-D-glucosyl-D-glucose + phosphate = D-glucose + alpha-D-glucose 1-phosphate. Differs in specificity from EC 2.4.1.30 and EC 2.4.1.97. Glucomannan 4-beta-mannosyltransferase Glucomannan-synthase GDP-mannose + (glucomannan)(n) = GDP + (glucomannan)(n+1). Alginate synthase Mannuronosyl transferase GDP-D-mannuronate + (alginate)(n) = GDP + (alginate)(n+1). UDP-glucose--3-beta-D-glucan glucosyltransferase 1,3-beta-D-glucan-UDP glucosyltransferase Callose synthase UDP-glucose-1,3-beta-D-glucan glucosyltransferase Callose synthetase 1,3-beta-glucan synthase 1,3-beta-D-glucan--UDP glucosyltransferase UDP-glucose + (1,3-beta-D-glucosyl)(n) = UDP + (1,3-beta-D-glucosyl)(n+1). UDP-glucosyltransferase Phenol beta-glucosyltransferase Acts on a wide range of phenols. UDP-glucose + a phenol = UDP + an aryl beta-D-glucoside. Alpha,alpha-trehalose-phosphate synthase (GDP-forming) GDP-glucose-glucosephosphate glucosyltransferase Trehalose phosphate synthase (GDP-forming) GDP-glucose + glucose 6-phosphate = GDP + alpha,alpha-trehalose 6-phosphate. See also EC 2.4.1.15. B transferase [Blood group substance] alpha-galactosyltransferase Blood-group substance B-dependent galactosyltransferase UDPgalactose:O-alpha-L-fucosyl(1->2)D-galactose alpha-D-galactosyltransferase Glycoprotein-fucosylgalactoside alpha-galactosyltransferase Histo-blood substance beta-dependent galactosyltransferase Fucosylgalactoside 3-alpha-galactosyltransferase Histo-blood group B transferase Fucosylglycoprotein 3-alpha-galactosyltransferase UDPgalactose:glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose 3-alpha-D-galactosyltransferase Blood-group substance beta-dependent galactosyltransferase UDP-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R = UDP + alpha-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->2))-D-galactosyl-R. Acts on blood group substance, and can use a number of 2-fucosyl-galactosides as acceptors. GalT Glycoprotein 4-beta-galactosyltransferase UDP-galactose--glycoprotein galactosyltransferase Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase Thyroid galactosyltransferase Terminal N-acetyl-beta-D-glucosaminyl residues in polysaccharides, glycoproteins and glycopeptides can act as acceptor. High activity is shown toward such residues in branched-chain polysaccharides when these are linked by beta-1,6 links to galactose residues; lower activity toward residues linked to galactose by beta-1,3 links. UDP-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminylglycopeptide. A component of EC 2.4.1.22. Sucrose-glucan glucosyltransferase Steroid N-acetylglucosaminyltransferase UDP-N-acetyl-D-glucosamine + estradiol-17-alpha 3-D-glucuronoside = UDP + 17-alpha-(N-acetyl-D-glucosaminyl)-estradiol 3-D-glucuronoside. Amylosucrase Sucrose--glucan glucosyltransferase Sucrose + (1,4-alpha-D-glucosyl)(n) = D-fructose + (1,4-alpha-D-glucosyl)(n+1). Histo-blood group A acetylgalactosaminyltransferase Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase A transferase Fucosylgalactose alpha-N-acetylgalactosaminyltransferase Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase Histo-blood group A transferase Can use a number of 2-fucosyl-galactosides as acceptors. UDP-N-acetyl-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose = UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1,3)-(alpha-L-fucosyl-(1,2))-D-galactose. Acts on blood group substance H. http://purl.uniprot.org/mim/110300 Polypeptide N-acetylgalactosaminyltransferase Protein-UDP acetylgalactosaminyltransferase http://purl.uniprot.org/mim/610233 http://purl.uniprot.org/mim/211900 The glycosyl residue is transferred to threonine or serine hydroxy groups on the polypeptide core of submaxillary mucin, kappa-casein, apofetuin and some other acceptors of high molecular mass. UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. Calcium Manganese Polygalacturonate 4-alpha-galacturonosyltransferase UDP-D-galacturonate + (1,4-alpha-D-galacturonosyl)(n) = UDP + (1,4-alpha-D-galacturonosyl)(n+1). UDP-galactose:lipopolysaccharide alpha,3-galactosyltransferase Lipopolysaccharide 1,3-galactosyltransferase Uridine diphosphate galactose:lipopolysaccharide alpha-3-galactosyltransferase UDP-galactose:polysaccharide galactosyltransferase Uridine diphosphogalactose-lipopolysaccharide alpha,3-galactosyltransferase Lipopolysaccharide galactosyltransferase Lipopolysaccharide 3-alpha-galactosyltransferase Transfers D-galactosyl residues to D-glucose in the partially completed core of lipopolysaccharide (cf. EC 2.4.1.56, EC 2.4.1.58, and EC 2.4.1.73). UDP-galactose + lipopolysaccharide = UDP + 3-alpha-D-galactosyl-[lipopolysaccharide glucose]. 2-hydroxyacylsphingosine 1-beta-galactosyltransferase UDP-galactose-ceramide galactosyltransferase Cerebroside synthase Highly specific. UDP-galactose + 2-(2-hydroxyacyl)sphingosine = UDP + 1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine. 1,2-diacylglycerol 3-beta-galactosyltransferase Uridine diphosphogalactose-1,2-diacylglycerol galactosyltransferase Monogalactosyldiacylglycerol synthase UDP-galactose:diacylglycerol galactosyltransferase UDP-galactose-diacylglyceride galactosyltransferase MGDG synthase UDPgalactose:1,2-diacylglycerol 3-beta-D-galactosyltransferase 1-beta-MGDG UDP galactose-1,2-diacylglycerol galactosyltransferase There are three isoforms in Arabidopsis that can be divided into two types, A-type (MGD1) and B-type (MGD2 and MGD3). UDP-galactose + 1,2-diacyl-sn-glycerol = UDP + 3-beta-D-galactosyl-1,2-diacyl-sn-glycerol. MGD1 is the isoform responsible for the bulk of monogalactosyldiacylglycerol (MGDG) synthesis in Arabidopsis. This enzyme adds only one galactosyl group to the diacylglycerol; EC 2.4.1.241 adds a galactosyl group to the product of the above reaction. N-acylsphingosine galactosyltransferase UDP-galactose + N-acylsphingosine = UDP + D-galactosylceramide. Heteroglycan alpha-mannosyltransferase The acceptor is a heteroglycan primer containing mannose, galactose and xylose. GDP-mannose + heteroglycan = GDP + 2(or 3)-(alpha-D-mannosyl)heteroglycan. 1,2-and 1,3-mannosyl bonds are formed. Cellodextrin phosphorylase (1,4-beta-D-glucosyl)(n) + phosphate = (1,4-beta-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate. Sucrose 6-glucosyltransferase Dextransucrase Sucrose + (1,6-alpha-D-glucosyl)(n) = D-fructose + (1,6-alpha-D-glucosyl)(n+1). Hydroxylysine galactosyltransferase Procollagen galactosyltransferase Probably involved in the synthesis of carbohydrate units in complement (cf. EC 2.4.1.66). UDP-galactose + procollagen 5-hydroxy-L-lysine = UDP + procollagen 5-(D-galactosyloxy)-L-lysine. Poly(glycerol-phosphate) alpha-glucosyltransferase UDP-glucose + poly(glycerol phosphate) = UDP + O-(alpha-D-glucosyl)poly(glycerol phosphate). Poly(ribitol-phosphate) beta-glucosyltransferase UDP-glucose + poly(ribitol phosphate) = UDP + (beta-D-glucosyl)poly(ribitol phosphate). Undecaprenyl-phosphate mannosyltransferase GDP-mannose + undecaprenyl phosphate = GDP + D-mannosyl-1-phosphoundecaprenol. Requires phosphatidylglycerol. Lipopolysaccharide N-acetylglucosaminyltransferase UDP-N-acetyl-D-glucosamine + lipopolysaccharide = UDP + N-acetyl-D-glucosaminyllipopolysaccharide. Transfers N-acetylglucosaminyl residues to a D-galactose residue in the partially completed lipopolysaccharide core (cf. EC 2.4.1.44, EC 2.4.1.58, and EC 2.4.1.73). Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase GDP mannose-phosphatidyl-myo-inositol alpha-mannosyltransferase Phosphatidyl-myo-inositol alpha-mannosyltransferase Phosphatidylinositol alpha-mannosyltransferase GDPmannose:1-phosphatidyl-myo-inositol alpha-D-mannosyltransferase Transfers one or more alpha-D-mannose residues from GDP-mannose to positions 2,6 and others in 1-phosphatidyl-myo-inositol. Lipopolysaccharide glucosyltransferase I Transfers glucosyl residues to the backbone portion of lipopolysaccharide (cf. EC 2.4.1.44, EC 2.4.1.56, and EC 2.4.1.73). UDP-glucose + lipopolysaccharide = UDP + D-glucosyl-lipopolysaccharide. Abequosyltransferase CDP-abequose + D-mannosyl-L-rhamnosyl-D-galactose-1-diphospholipid = CDP + D-abequosyl-D-mannosyl-rhamnosyl-D-galactose-1-diphospholipid. Ganglioside galactosyltransferase The substrate is also known as G(M2). UDP-galactose + N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-1,4-beta-D-glucosyl-N-acylsphingosine = UDP + D-galactosyl-1,3-beta-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-N-acylsphingosine. Linamarin synthase UDP-glucose + 2-hydroxy-2-methylpropanenitrile = UDP + linamarin. Glucosylates the cyanohydrins of butanone and pentan-3-one as well as that of acetone. Alpha,alpha-trehalose phosphorylase Alpha,alpha-trehalose + phosphate = D-glucose + beta-D-glucose 1-phosphate. Alpha-(1->4)-L-fucosyltransferase Lewis blood group alpha-(1->3/4)-fucosyltransferase Lewis(Le) blood group gene-dependent alpha-(1->3/4)-L-fucosyltransferase Lewis FT Lewis alpha-(1->3/4)-fucosyltransferase FucT-II Guanosine diphosphofucose-beta-acetylglucosaminylsaccharide 4-alpha-L-fucosyltransferase Blood-group substance Le(a)-dependent fucosyltransferase Guanosine diphosphofucose-glycoprotein 4-alpha-fucosyltransferase Alpha-(1,3/1,4) fucosyltransferase III Galactoside 3(4)-L-fucosyltransferase 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase Guanosine diphosphofucose-glycoprotein 4-alpha-L-fucosyltransferase Beta-acetylglucosaminylsaccharide fucosyltransferase Blood group Lewis alpha-4-fucosyltransferase (Le(a))-dependent (alpha-3/4)-fucosyltransferase Alpha-4-L-fucosyltransferase In addition, the fucTa gene of Helicobacter strain UA948 encodes a fucosyltransferase with both 3-alpha-and 4-alpha-fucosyltransferase activities. http://purl.uniprot.org/mim/136836 Product of the Lewis blood group gene. Although it is a 4-fucosyltransferase, it has a persistent 3-fucosyltransferase activity toward the glucose residue in free lactose. http://purl.uniprot.org/mim/111100 GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-R = GDP + beta-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->4))-N-acetyl-beta-D-glucosaminyl-R. Fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3, unlike EC 2.4.1.152 which fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4. Enzymes catalyzing the 4-alpha-fucosylation of the GlcNAc in beta-D-Gal-(1->3)-beta-GlcNAc sequences (with some activity also as 3-alpha-fucosyltransferases) are present in plants, where the function in vivo is the modification of N-glycans. Normally acts on a glycoconjugate where R (see CA line) is a glycoprotein or glycolipid. Procollagen glucosyltransferase Galactosylhydroxylysine-glucosyltransferase Probably involved in the synthesis of carbohydrate units in complement (cf. EC 2.4.1.50). http://purl.uniprot.org/mim/131880 UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen = UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen. Galactinol-raffinose galactosyltransferase Galactinol--raffinose galactosyltransferase Stachyose synthetase See also EC 2.4.1.82. Alpha-D-galactosyl-(1->3)-1D-myo-inositol + raffinose = myo-inositol + stachyose. This enzyme also catalyzes galactosyl transfer from stachyose to raffinose (shown by labelling). For synthesis of the substrate, see EC 2.4.1.123. Glycoprotein 6-alpha-L-fucosyltransferase Glycoprotein fucosyltransferase GDP-L-fucose-glycoprotein fucosyltransferase GDP-fucose--glycoprotein fucosyltransferase GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha-(1->6)fucosyltransferase Guanosine diphosphofucose-glycoprotein fucosyltransferase GDP-L-fucose + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)asparagine = GDP + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-(alpha-L-fucosyl-(1->6))-N-acetyl-beta-D-glucosaminyl)asparagine. Catalyzes a reaction similar to that of EC 2.4.1.214, but transfers the L-fucosyl group from GDP-beta-L-fucose to form an alpha-1,6-linkage rather than an alpha-1,3-linkage. GDP fucose-lactose fucosyltransferase Guanosine diphospho-L-fucose-lactose fucosyltransferase Guanosine diphosphofucose-glycoprotein 2-alpha-L-fucosyltransferase Secretor-type beta-galactoside alpha-1->2 fucosyltransferase Blood group H alpha-2-fucosyltransferase Galactoside 2-alpha-L-fucosyltransferase Alpha-2-fucosyltransferase Alpha-(1->2)-L-fucosyltransferase Guanosine diphosphofucose-galactosylacetylglucosaminylgalactosyl-glucosylceramide alpha-L-fucosyltransferase Guanosine diphosphofucose-galactoside 2-L-fucosyltransferase GDP-L-fucose:lactose fucosyltransferase Guanosine diphosphofucose-glycoprotein 2-alpha-fucosyltransferase Blood-group substance H-dependent fucosyltransferase Beta-galactoside alpha-1->2 fucosyltransferase H-gene-encoded beta-galactoside alpha-1->2 fucosyltransferase Guanosine diphosphofucose-lactose fucosyltransferase Alpha-2-L-fucosyltransferase Guanosine diphosphofucose-beta-D-galactosyl-alpha-2-L-fucosyltransferase Galactoside 2-L-fucosyltransferase GDP-beta-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R. The action on glycolipid was previously listed as EC 2.4.1.89. Free lactose can act as acceptor. Sucrose phosphorylase Sucrose glucosyltransferase Disaccharide glucosyltransferase In the forward reaction, arsenate may replace phosphate. In the reverse reaction, various ketoses and L-arabinose may replace D-fructose. Sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate. Poly(ribitol-phosphate) N-acetylglucosaminyltransferase UDP-N-acetyl-D-glucosamine + poly(ribitol phosphate) = UDP + (N-acetyl-D-glucosaminyl)poly(ribitol phosphate). Involved in the synthesis of teichoic acids. Arylamine glucosyltransferase UDP glucose-arylamine glucosyltransferase UDP-glucose + an arylamine = UDP + an N-D-glucosylarylamine. Lipopolysaccharide glucosyltransferase II Transfers glucosyl residues to the D-galactosyl-D-glucosyl side-chains in the partially completed core of lipopolysaccharide (cf. EC 2.4.1.44, EC 2.4.1.56, and EC 2.4.1.58). UDP-glucose + lipopolysaccharide = UDP + alpha-D-glucosyl-lipopolysaccharide. Glycosaminoglycan galactosyltransferase Involved in the biosynthesis of galactose-containing glycosaminoglycan of Dictyostelium discoideum. UDP-galactose + glycosaminoglycan = UDP + D-galactosylglycosaminoglycan. Phosphopolyprenol glucosyltransferase UDP-glucose + polyprenyl phosphate = UDP + polyprenylphosphate-glucose. Ficaprenyl phosphate is the best substrate; other polyprenols can also act as substrates, more slowly. Beta-3GalNAc-T1 Globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase Uridine diphosphoacetylgalactosamine-galactosylgalactosylglucosylceramide acetylgalactosaminyltransferase Galactosylgalactosylglucosylceramide beta-D-acetylgalactosaminyltransferase Globoside synthetase Globoside synthase Lactosylceramide, globoside and gangliosides GM3 and GD3 are not substrates. Globoside is a neutral glycosphingolipid in human erythrocytes and has blood-group-P-antigen activity. Manganese UDP-GalNAc is the only sugar donor that is used efficiently by the enzyme: UDP-Gal and UDP-GlcNAc result in very low enzyme activity. UDP-N-acetyl-D-galactosamine + alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-beta-D-glucosylceramide = UDP + beta-N-acetyl-D-galactosaminyl-(1->3)-alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-beta-D-glucosylceramide. Maltose phosphorylase Maltose + phosphate = D-glucose + beta-D-glucose 1-phosphate. Ceramide glucosyltransferase Glucosylceramide synthase UDP-glucose-ceramide glucosyltransferase Sphingosine and dihydrosphingosine can also act as acceptors. UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine. CDP-glucose can act as donor. UDP-glucose-apigenin beta-glucosyltransferase UDP-glucose-luteolin beta-D-glucosyltransferase Flavone 7-O-beta-glucosyltransferase UDP-glucose + 5,7,3',4'-tetrahydroxyflavone = UDP + 7-O-beta-D-glucosyl-5,7,3',4'-tetrahydroxyflavone. Different from EC 2.4.1.91. A number of flavones, flavonones and flavonols can function as acceptors. 1-alpha-D-galactosyl-myo-inositol:sucrose 6-alpha-D-galactosyltransferase Galactinol--sucrose galactosyltransferase Alpha-D-galactosyl-(1->3)-1D-myo-inositol + sucrose = myo-inositol + raffinose. 4-nitrophenyl-alpha-D-galactopyranoside can also act as donor. Also catalyzes an exchange reaction between raffinose and sucrose (cf. EC 2.4.1.123). Dolichyl-phosphate beta-D-mannosyltransferase Dolichol-phosphate mannosyltransferase Dolichol-phosphate mannose synthase Mannosylphosphodolichol synthase Mannosylphosphoryldolichol synthase GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate. Acts only on long-chain polyprenyl phosphates and alpha-dihydropolyprenyl phosphates, larger than C(35). http://purl.uniprot.org/mim/608799 Uridine diphosphoglucose-p-hydroxymandelonitrile glucosyltransferase UDP-glucose:(S)-4-hydroxymandelonitrile beta-D-glucosyltransferase UDP-glucose-p-hydroxymandelonitrile glucosyltransferase Cyanohydrin beta-glucosyltransferase Uridine diphosphoglucose-cyanohydrin glucosyltransferase UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase Uridine diphosphoglucose:aldehyde cyanohydrin beta-glucosyltransferase UGT85B1 Acts on a wide range of substrates in vitro, including cyanohydrins, terpenoids, phenolics, hexanol derivatives and plant hormones, in a regiospecific manner. UDP-D-glucose + (S)-4-hydroxymandelonitrile = UDP + (S)-4-hydroxymandelonitrile beta-D-glucoside. Involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum, along with EC 1.14.13.41 and EC 1.14.13.68. This reaction prevents the disocciation and release of toxic hydrogen cyanide. Paragloboside synthase Glucosaminylgalactosylglucosylceramide beta-galactosyltransferase UDP-galactose + N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-D-glucosylceramide = UDP + 1,3-beta-D-galactosyl-N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-D-glucosylceramide. Uridine diphosphogalactose-acetyllactosamine galactosyltransferase Glucosaminylglycopeptide alpha-1,3-galactosyltransferase N-acetyllactosaminide alpha-1,3-galactosyltransferase Galactosyltransferase UDP-Gal:N-acetyllactosaminide alpha-1,3-D-galactosyltransferase Uridine diphosphogalactose-acetyllactosamine alpha-1->3-galactosyltransferase UDP-Gal:N-acetyllactosaminide alpha-(1,3)-galactosyltransferase UDP-galactose-acetyllactosamine alpha-D-galactosyltransferase UDP-Gal:Gal-beta-1->4GlcNAc-R alpha-1->3-galactosyltransferase Alpha-galactosyltransferase UDPgalactose:beta-D-galactosyl-beta-1,4-N-acetyl-D-glucosaminyl-glycopeptide alpha-1,3-D-galactosyltransferase N-acetyllactosaminide 3-alpha-galactosyltransferase Uridine diphosphogalactose-galactosylacetylglucosaminylgalactosyl-glucosylceramide galactosyltransferase UDP-Gal:beta-D-Gal(1,4)-D-GlcNAc alpha-(1,3)-galactosyltransferase Beta-D-galactosyl-N-acetylglucosaminylglycopeptide alpha-1,3-galactosyltransferase Now includes EC 2.4.1.124 and EC 2.4.1.151. Acts on beta-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-alpha(1)-acid glycoprotein and N-acetyllactosamine (beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine), but not on 2'-fucosylated-N-acetyllactosamine. UDP-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R = UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R. The non-reducing terminal N-acetyllactosamine residues of glycoproteins can also act as acceptor. Forssman synthase Globoside alpha-N-acetylgalactosaminyltransferase UDP-N-acetyl-D-galactosamine + N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide = UDP + N-acetyl-D-galactosaminyl-N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide. Sucrose 1-fructosyl transferase Inulosucrase Some other sugars can act as D-fructosyl acceptors. Converts sucrose into inulin and D-glucose. Sucrose + (2,1-beta-D-fructosyl)(n) = glucose + (2,1-beta-D-fructosyl)(n+1). UDP-galactose-N-acetylglucosamine beta-D-galactosyltransferase N-acetyllactosamine synthase NAL synthetase N-acetylglucosamine (beta-1,4)galactosyltransferase Acetyllactosamine synthetase UDP-galactose--N-acetylglucosamine beta-D-galactosyltransferase The reaction is catalyzed by a component of EC 2.4.1.22, which is identical with EC 2.4.1.38, and by an enzyme from the Golgi apparatus of animal tissues. UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine. Flavonol 3-O-glucosyltransferase UDP-glucose flavonol 3-O-glucosyltransferase UDP-glucose + a flavonol = UDP + a flavonol 3-O-D-glucoside. Acts on a variety of flavonols, including quercetin and quercetin 7-O-glucoside. Different from EC 2.4.1.81. Uridine diphosphoacetylgalactosamine-acetylneuraminylgalactosylglucosylceramide acetylgalactosaminyltransferase UDP-N-acetylgalactosamine GM3 N-acetylgalactosaminyltransferase GM2/GD2-synthase Asialo-GM2 synthase UDP acetylgalactosamine-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide acetylgalactosaminyltransferase GM2 synthase Uridine diphosphoacetylgalactosamine-ganglioside GM3 acetylgalactosaminyltransferase (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase Ganglioside GM3 acetylgalactosaminyltransferase GalNAc-T Ganglioside GM2 synthase Beta-1,4N-aetylgalactosaminyltransferase Uridine diphosphoacetylgalactosamine-hematoside acetylgalactosaminyltransferase Catalyzes the formation of the gangliosides (i.e. sialic-acid-containing glycosphingolipids) GM2, GD2 and SM2 from GM3, GD3 and SM3, respectively. UDP-N-acetyl-D-galactosamine + 1-O-(O-(N-acetyl-alpha-neuraminosyl)-(2->3)-O-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranosyl)-ceramide = UDP + 1-O-(O-2-(acetylamino)-2-deoxy-beta-D-galactopyranosyl-(1->4)-O-(N-acetyl-alpha-neuraminosyl-(2->3))-O-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranosyl)-ceramide. Asialo-GM3 and lactosylceramide are also substrates, but glycoproteins and oligosaccharides are not substrates. Protein N-acetylglucosaminyltransferase N-GlcNAc transferase The acceptor is the asparagine residue in a sequence of the form Asn-Xaa-(Ser/Thr). UDP-N-acetyl-D-glucosamine + protein = UDP + 4-N-(N-acetyl-D-glucosaminyl)-protein. Bilirubin-glucuronoside glucuronosyltransferase Bilirubin monoglucuronide transglucuronidase 2 bilirubin-glucuronoside = bilirubin + bilirubin-bisglucuronoside. Isofloridoside-phosphate synthase sn-glycerol-3-phosphate 1-galactosyltransferase UDP-galactose + sn-glycerol 3-phosphate = UDP + alpha-D-galactosyl-(1,1')-sn-glycerol 3-phosphate. The product is hydrolyzed by a phosphatase to isofloridoside, which is involved in osmoregulation (cf. EC 2.4.1.137). 1,3-beta-D-glucan phosphorylase Laminarin phosphorylase Acts on a range of beta-1,3-oligoglucans, and on glucans of laminarin type. Different from EC 2.4.1.30 and EC 2.4.1.31. (1,3-beta-D-glucosyl)(n) + phosphate = (1,3-beta-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate. Sucrose:sucrose 1-fructosyltransferase Sucrose:sucrose 1(F)-beta-D-fructosyltransferase Sucrose 1(F)-fructosyltransferase Sucrose-sucrose 1-fructosyltransferase SST Sucrose:sucrose fructosyltransferase 2 sucrose = D-glucose + beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl alpha-D-glucopyranoside. Pentosyltransferases PNPase Inosine phosphorylase Purine-nucleoside phosphorylase http://purl.uniprot.org/mim/164050 Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate. Can also catalyze ribosyltransferase reactions of the type catalyzed by EC 2.4.2.5. Specificity not completely determined. Orotate phosphoribosyltransferase Orotidine-5'-phosphate diphosphorylase Orotidine-5'-phosphate pyrophosphorylase OPRT Orotidylic acid phosphorylase The enzyme from higher eukaryotes also catalyzes the reaction listed as EC 4.1.1.23. Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. http://purl.uniprot.org/mim/258900 Nicotinic acid phosphoribosyltransferase Niacin ribonucleotidase Nicotinic acid mononucleotide glycohydrolase Nicotinic acid mononucleotide pyrophosphorylase Nicotinate phosphoribosyltransferase Nicotinate D-ribonucleotide + diphosphate = nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate. Nicotinamide phosphoribosyltransferase NMN diphosphorylase NMN pyrophosphorylase Nicotinamide D-ribonucleotide + diphosphate = nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate. Glutamine phosphoribosylpyrophosphate amidotransferase Phosphoribosyldiphosphate 5-amidotransferase Amidophosphoribosyltransferase 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H(2)O. Guanosine phosphorylase Guanosine + phosphate = guanine + alpha-D-ribose 1-phosphate. Also acts on deoxyguanosine. Urate-ribonucleotide phosphorylase Urate D-ribonucleotide + phosphate = urate + alpha-D-ribose 1-phosphate. Phosphoribosyl-ATP diphosphorylase ATP phosphoribosyltransferase Phosphoribosyl-ATP pyrophosphorylase 1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. Phosphoribosyl-anthranilate diphosphorylase Anthranilate phosphoribosyltransferase Phosphoribosyl-anthranilate pyrophosphorylase In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, and EC 5.3.1.24). N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate. Nicotinate-nucleotide pyrophosphorylase (carboxylating) Quinolinate phosphoribosyltransferase (decarboxylating) Nicotinate-nucleotide diphosphorylase (carboxylating) Nicotinate D-ribonucleotide + diphosphate + CO(2) = pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate. Pyrimidine-nucleoside phosphorylase Py-NPase Both uridine and thymidine are substrates. A pyrimidine nucleoside + phosphate = a pyrimidine base + alpha-D-ribose 1-phosphate. Dioxotetrahydropyrimidine phosphoribosyltransferase Dioxotetrahydropyrimidine-ribonucleotide pyrophosphorylase Dioxotetrahydropyrimidine-ribonucleotide diphosphorylase A 2,4-dioxotetrahydropyrimidine D-ribonucleotide + diphosphate = a 2,4-dioxotetrahydropyrimidine + 5-phospho-alpha-D-ribose 1-diphosphate. Acts, in the reverse direction, on uracil and other pyrimidines and pteridines containing a 2,4-diketo structure. Nicotinate mononucleotide-dimethylbenzimidazole phosphoribosyltransferase Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase N(1)-alpha-phosphoribosyltransferase Beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole = nicotinate + alpha-ribazole 5'-phosphate. Also acts on benzimidazole, and the clostridial enzyme acts on adenine to form 7-alpha-D-ribosyladenine 5'-phosphate. The product of the reaction, alpha-ribazole 5'-phosphate, forms part of the corrin-biosynthesis pathway and is a substrate for EC 2.7.8.2. It can also be dephosphorylated to form alpha-ribazole by the action of EC 3.1.3.73. Xanthine-guanine phosphoribosyltransferase Xanthosine 5'-phosphate pyrophosphorylase Xanthine phosphoribosyltransferase Xan phosphoribosyltransferase Xanthylic pyrophosphorylase Xanthylate pyrophosphorylase XMP pyrophosphorylase XMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + xanthine. Deoxyuridine phosphorylase 2'-deoxyuridine + phosphate = uracil + 2-deoxy-alpha-D-ribose 1-phosphate. 1,4-beta-D-xylan synthase UDP-D-xylose + (1,4-beta-D-xylan)(n) = UDP + (1,4-beta-D-xylan)(n+1). Flavone apiosyltransferase 7-O-beta-D-glucosides of a number of flavonoids and of 4-substituted phenols can act as acceptors. UDP-apiose + 5,7,4'-trihydroxyflavone 7-O-beta-D-glucoside = UDP + 5,7,4'-trihydroxyflavone 7-O-(beta-D-apiosyl-(1->2)-beta-D-glucoside). Uridine diphosphoxylose-protein xylosyltransferase UDP-D-xylose:core protein beta-D-xylosyltransferase Protein xylosyltransferase Uridine diphosphoxylose-core protein beta-xylosyltransferase UDP-D-xylose:proteoglycan core protein beta-D-xylosyltransferase UDP-xylose-core protein beta-D-xylosyltransferase UDP-D-xylose:core protein xylosyltransferase Transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxy group of an acceptor protein substrate. Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). dTDP-dihydrostreptose--streptidine-6-phosphate dihydrostreptosyltransferase dTDP-L-dihydrostreptose + streptidine 6-phosphate = dTDP + O-1,4-alpha-L-dihydrostreptosyl-streptidine 6-phosphate. Methylthioadenosine nucleoside phosphorylase S-methyl-5-thioadenosine phosphorylase Methylthioadenosine phosphorylase 5'-methylthioadenosine phosphorylase MTA phosphorylase MeSAdo/Ado phosphorylase MeSAdo phosphorylase 5'-deoxy-5'-methylthioadenosine phosphorylase MTAPase 5'-methylthioadenosine nucleosidase Also acts on 5'-deoxyadenosine and other analogs having 5'-deoxy groups. S-methyl-5-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate. Queuine tRNA-ribosyltransferase tRNA-guanine transglycosylase Guanine insertion enzyme Also catalyzes the exchange of precursors of queuine and of guanine itself for guanine located in the first position of certain tRNA anticodons. [tRNA]-guanine + queuine = [tRNA]-queuine + guanine. Pyrimidine phosphorylase Uridine phosphorylase UPase UrdPase Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate. NAD(+) ADP-ribosyltransferase Poly(ADP-ribose) synthetase Poly(ADP-ribose)polymerase ADP-ribosyltransferase (polymerizing) Poly(adenosine diphosphate ribose) polymerase NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor. The ADP-D-ribosyl group of NAD(+) is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. NAD(P)(+)--arginine ADP-ribosyltransferase ADP-ribosyltransferase NAD(P)(+)--protein-arginine ADP-ribosyltransferase Mono(ADP-ribosyl)transferase NAD(+):L-arginine ADP-D-ribosyltransferase Free arginine, agmatine ((4-aminobutyl)guanidine), arginine methyl ester and guanidine can also do so. (2) NADP(+) + protein-L-arginine = nicotinamide + N(omega)-((2'-phospho-ADP)-D-ribosyl)-protein-L-arginine. Some bacterial enterotoxins possess similar enzymatic activities (cf. EC 2.4.2.36). Arginine residues in proteins act as acceptors. Catalyzes the NAD(+)-dependent activation of EC 4.6.1.1. (1) NAD(+) + protein-L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-protein-L-arginine. http://purl.uniprot.org/mim/110600 Dolichyl-phosphate D-xylosyltransferase UDP-D-xylose + dolichyl phosphate = UDP + dolichyl D-xylosyl phosphate. Dolichyl-xylosyl-phosphate--protein xylosyltransferase Dolichyl D-xylosyl phosphate + protein = dolichyl phosphate + D-xylosylprotein. Indolylacetylinositol arabinosyltransferase Arabinosylindolylacetylinositol synthase The position of acylation is indeterminate because of the ease of acyl transfer between hydroxy groups. UDP-L-arabinose + (indol-3-yl)acetyl-1D-myo-inositol = UDP + (indol-3-yl)acetyl-myo-inositol 3-L-arabinoside. Flavonol-3-O-glycoside xylosyltransferase UDP-D-xylose + a flavonol 3-O-glycoside = UDP + a flavonol 3-(beta-D-xylosyl-(1->2)-beta-D-glycoside). Flavonol 3-O-glucoside, flavonol 3-O-galactoside and, more slowly, rutin, can act as acceptors. Mono(ADP-ribosyl)transferase ADP-ribosyltransferase NAD(+)--diphthamide ADP-ribosyltransferase Diphtheria toxin and some other bacterial toxins catalyze this reaction. NAD(+) + peptide diphthamide = nicotinamide + peptide N-(ADP-D-ribosyl)diphthamide. The acceptor is a diphthamide residue in elongation factor 2 (cf. EC 2.4.2.31). NAD--azoferredoxin (ADPribose)transferase NAD(+)--dinitrogen-reductase ADP-D-ribosyltransferase NAD--dinitrogen-reductase ADP-D-ribosyltransferase NAD(+) + [dinitrogen reductase] = nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]. Together with EC 3.2.2.24, controls the level of activity of EC 1.18.6.1. Beta-1,2-xylosyltransferase Glycoprotein 2-beta-D-xylosyltransferase Specific for N-linked oligosaccharides (N-glycans). UDP-D-xylose + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)asparagine = UDP + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-(beta-D-xylosyl-(1->2))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)asparagine. Xyloglucan 6-alpha-D-xylosyltransferase Xyloglucan 6-xylosyltransferase Uridine diphosphoxylose-xyloglucan 6-alpha-xylosyltransferase In association with EC 2.4.1.168 this enzyme brings about the synthesis of xyloglucan. Transfers an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan, forming an alpha-1,6-D-xylosyl-D-glucose linkage. Concurrent transfers of glucose and xylose are necessary for this synthesis. Thymidine phosphorylase Pyrimidine phosphorylase Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate. http://purl.uniprot.org/mim/603041 In some tissues also catalyzes deoxyribosyltransferase reactions of the type catalyzed by EC 2.4.2.6. Zeatin O-beta-D-xylosyltransferase Uridine diphosphoxylose-zeatin xylosyltransferase Zeatin O-xylosyltransferase UDP-D-xylose + zeatin = UDP + O-beta-D-xylosylzeatin. Does not act on UDP-glucose (cf. EC 2.4.1.103). Nucleoside ribosyltransferase Base(1) and base(2) represent various purines and pyrimidines. D-ribosyl-base(1) + base(2) = D-ribosyl-base(2) + base(1). Nucleoside deoxyribosyltransferase 2-deoxy-D-ribosyl-base(1) + base(2) = 2-deoxy-D-ribosyl-base(2) + base(1). Base(1) and base(2) represent various purines and pyrimidines. APRT Transphosphoribosidase AMP diphosphorylase AMP pyrophosphorylase Adenine phosphoribosyltransferase http://purl.uniprot.org/mim/102600 AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate. 5-amino-4-imidazolecarboxamide can replace adenine. IMP pyrophosphorylase Transphosphoribosidase HGPRTase Hypoxanthine-guanine phosphoribosyltransferase Hypoxanthine phosphoribosyltransferase IMP diphosphorylase Guanine phosphoribosyltransferase Guanine and 6-mercaptopurine can replace hypoxanthine. IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate. http://purl.uniprot.org/mim/300322 http://purl.uniprot.org/mim/300323 UMP pyrophosphorylase UMP diphosphorylase Uracil phosphoribosyltransferase UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. Transferring other glycosyl groups CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase Beta-galactosamide alpha-2,6-sialyltransferase Beta-galactoside alpha-2,6-sialyltransferase CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine = CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine. The terminal beta-D-galactosyl residue of the oligosaccharide of glycoproteins, as well as lactose, can act as acceptor. Neolactotetraosylceramide alpha-2,3-sialyltransferase Sialyltransferase CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-D-glucosylceramide = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-D-glucosylceramide. Lactosylceramide alpha-2,6-N-sialyltransferase CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide = CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-beta-D-glucosylceramide. Monosialoganglioside sialyltransferase May be identical with EC 2.4.99.4. CMP-N-acetylneuraminate + D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide = CMP + N-acetylneuraminyl-D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide. Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase GalNAc alpha-2,6-sialyltransferase I CMP-N-acetylneuraminate + glycano-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein = CMP + glycano-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein. Alpha-N-acetylgalactosamine linked to threonine or serine is also an acceptor, when substituted at the 3-position. CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase Beta-galactoside alpha-2,3-sialyltransferase May be identical with EC 2.4.99.2. CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R. Lactose can also act as acceptor. The acceptor is Gal-beta-1,3-GalNAc-R, where R is H, a threonine or serine residue in a glycoprotein, or a glycolipid. Galactosyldiacylglycerol alpha-2,3-sialyltransferase CMP-N-acetylneuraminate + 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol = CMP + 1,2-diacyl-3-(3-(alpha-D-N-acetylneuraminyl)-beta-D-galactosyl)-sn-glycerol. The beta-D-galactosyl residue of the oligosaccharide of glycoproteins may also act as acceptor. N-acetyllactosaminide alpha-2,3-sialyltransferase Acts on beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl termini on glycoprotein. CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein. Sialyltransferase 7D Cytidine monophosphoacetylneuraminate-(alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide-alpha-2,6-sialyltransferase Sialyltransferase NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc-alpha-2,6-sialyltransferase (Alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetyl-galactosaminide 6-alpha-sialyltransferase Alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferase ST6GALNAC Sialyltransferase 3C Attaches N-acetylneuraminic acid in alpha-2,6-linkage to N-acetyl-galactosamine only when present in the structure of alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminyl-R, where R may be protein or p-nitrophenol. Not identical with EC 2.4.99.3. CMP-N-acetylneuraminate + N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-D-galactosaminyl-R = CMP + N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-(N-acetyl-alpha-neuraminyl-(2->6))-N-acetyl-D-galactosaminyl-R. Alpha-N-acetylneuraminate alpha-2,8-sialyltransferase Alpha-2,8-sialyltransferase Gangliosides act as acceptors. CMP-N-acetylneuraminate + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-R = CMP + alpha-N-acetylneuraminyl-2,8-alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-R. Ganglioside GM3 synthase Lactosylceramide alpha-2,3-sialyltransferase http://purl.uniprot.org/mim/609056 Lactose cannot act as acceptor. CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide. Transferring alkyl or aryl groups, other than methyl groups Transferring alkyl or aryl groups, other than methyl groups Geranyl-diphosphate synthase Prenyltransferase Dimethylallyltranstransferase Dimethylallyltransferase Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate. Will not accept larger prenyl diphosphates as efficient donors. Farnesyl diphosphate synthetase Geranyltranstransferase Farnesyl pyrophosphate synthetase Farnesyl-diphosphate synthase FPP synthetase Will not accept larger prenyl diphosphates as efficient donors. Geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate. Some forms of this enzyme will also use dimethylallyl diphosphate as a substrate. Solanesyl-diphosphate synthase Trans-octaprenyltranstransferase All-trans-nonaprenyl-diphosphate synthase All-trans-octaprenyl diphosphate + isopentenyl diphosphate = diphosphate + all-trans-nonaprenyl diphosphate. Will also use geranyl diphosphate and all-trans-prenyl diphosphates of intermediate size as donors, but not dimethylallyl diphosphate. Dihydropteroate pyrophosphorylase DHPS Dihydropteroate synthase Dihydropteroate diphosphorylase (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate. Putrescine aminopropyltransferase Aminopropyltransferase Spermidine synthase The mammalian enzyme is highly specific but the bacterial enzyme can use other acceptors and can synthesize spermine. S-adenosylmethioninamine + putrescine = 5'-S-methyl-5'-thioadenosine + spermidine. Not identical with EC 2.5.1.22. Aquacob(I)alamin adenosyltransferase Cob(I)alamin adenosyltransferase ATP:corrinoid adenosyltransferase Cob(I)yrinic acid a,c-diamide adenosyltransferase Aquocob(I)alamin vitamin B12s adenosyltransferase ATP:cob(I)alamin Co-beta-adenosyltransferase The corrinoid adenosylation pathway comprises three steps: (1) Reduction of Co(III) to Co(II) by a one-electron transfer; this can be carried out by EC 1.16.1.3, or non-enzymically in the presence of dihydroflavin nucleotides. (2) Co(II) is reduced to Co(I) in a second single-electron transfer by EC 1.16.1.4. (3) The Co(I) conducts a nucleophilic attack on the adenosyl moiety of ATP to leave the cobalt atom in a Co(III) state (EC 2.5.1.17). In P.denitrificans, the enzyme shows specificity for cobyrinic acid a,c-diamide and the corrinoids that occur later in the biosynthetic pathway whereas CobA seems to have broader specificity. (1) ATP + cob(I)yrinic acid a,c-diamide = triphosphate + adenosylcob(III)yrinic acid a,c-diamide. (2) ATP + cobinamide = triphosphate + adenosylcobinamide. http://purl.uniprot.org/mim/251110 The enzyme responsible for the adenosylation reaction is the product of the gene cobO in the aerobic bacterium Pseudomonas denitrificans and of the gene cobA in the anaerobic bacterium Salmonella typhimurium. While CobA has a preference for ATP and Mn(2+), it is able to transfer a variety of nucleosides to the cobalt, including CTP, UTP and GTP, in decreasing order of preference and to use Mg(2+) instead of Mn(2+). Glutathione S-aryltransferase Glutathione transferase Glutathione S-aralkyltransferase Glutathione S-alkyltransferase S-(hydroxyalkyl)glutathione lyase R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyzes the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange. RX + glutathione = HX + R-S-glutathione. A group of enzymes of broad specificity. 5-enolpyruvylshikimate-3-phosphate synthase EPSP synthase 3-enol-pyruvoylshikimate-5-phosphate synthase 3-phosphoshikimate 1-carboxyvinyltransferase Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. Thiamine pyridinylase Thiamine pyridinolase Thiamine hydrolase Thiaminase I Pyrimidine transferase Thiaminase Thiamine:base 2-methyl-4-aminopyrimidine-5-methenyltransferase Thiamine + pyridine = 1-((4-amino-2-methylpyrimidin-5-yl)methyl)pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole. Various bases and thiol compounds can act instead of pyridine. Rubber transferase Rubber cis-polyprenylcistransferase Rubber allyltransferase Rubber particles act as acceptor. Poly-cis-polyprenyl diphosphate + isopentenyl diphosphate = diphosphate + a poly-cis-polyprenyl diphosphate longer by one C(5) unit. Farnesyltransferase Squalene synthase Squalene synthetase Presqualene-diphosphate synthase Presqualene synthase Farnesyl-diphosphate farnesyltransferase (1) 2 farnesyl diphosphate = diphosphate + presqualene diphosphate. Magnesium or manganese In the absence of NAD(P)H, presqualene diphosphate is accumulated. (2) Presqualene diphosphate + NAD(P)H = squalene + diphosphate + NAD(P)(+). Spermine synthase Spermidine aminopropyltransferase Not identical with EC 2.5.1.16 or EC 2.5.1.23. S-adenosylmethioninamine + spermidine = 5'-methylthioadenosine + spermine. Sym-norspermidine synthase S-adenosylmethioninamine + propane-1,3-diamine = 5'-methylthioadenosine + bis(3-aminopropyl)amine. Not identical with EC 2.5.1.16 or EC 2.5.1.22. Discadenine synthetase Discadenine synthase S-adenosyl-L-methionine + N(6)-(Delta(2)-isopentenyl)-adenine = 5'-methylthioadenosine + discadenine. tRNA-uridine aminocarboxypropyltransferase S-adenosyl-L-methionine + tRNA uridine = 5'-methylthioadenosine + tRNA 3-(3-amino-3-carboxypropyl)-uridine. Alkyl-DHAP synthase Alkyldihydroxyacetonephosphate synthase Alkylglycerone-phosphate synthase The ester-linked fatty acid of the substrate is cleaved and replaced by a long-chain alcohol in an ether linkage. 1-acyl-glycerone 3-phosphate + a long-chain alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid anion. http://purl.uniprot.org/mim/600121 Isopentenyltransferase Cytokinin synthase Adenylate isopentenyltransferase Adenylate dimethylallyltransferase Dimethylallyl diphosphate + AMP = diphosphate + N(6)-(dimethylallyl)adenosine 5'-phosphate. Neryl-diphosphate synthase Dimethylallylcistransferase Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + neryl diphosphate. Will not use larger prenyl diphosphates as efficient donors. Geranylgeranyl-PP synthetase Farnesyltransferase Geranylgeranyl pyrophosphate synthase Geranylgeranyl-diphosphate synthase Geranylgeranyl pyrophosphate synthetase Farnesyltranstransferase Some forms of this enzyme will also use geranyl diphosphate and dimethylallyl diphosphate as donors; it will not use larger prenyl diphosphates as efficient donors. Trans,trans-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate. Thiamine-phosphate pyrophosphorylase TMP diphosphorylase Thiamine-phosphate diphosphorylase TMP pyrophosphorylase Thiamine-phosphate synthase 2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate. All-trans-heptaprenyl-diphosphate synthase Heptaprenyl diphosphate synthase Trans-hexaprenyltranstransferase Heptaprenyl pyrophosphate synthetase All-trans-hexaprenyl diphosphate + isopentenyl diphosphate = diphosphate + all-trans-heptaprenyl diphosphate. Will also use trans-trans-farnesyl diphosphate and all-trans-prenyl diphosphates of intermediate size as donors, but not dimethylallyl diphosphate. Undecaprenyl pyrophosphate synthase Di-trans,poly-cis-decaprenylcistransferase Bactoprenyl-diphosphate synthase Undecaprenyl-diphosphate synthase Di-trans,poly-cis-undecaprenyl-diphosphate synthase UPP synthetase Undecaprenyl pyrophosphate synthetase The two trans-bonds in the substrate and product are those furthest from the diphosphate group. Will also use trans,trans-farnesyl diphosphate and di-trans,poly-cis-prenyl diphosphates of intermediate size as donors. Di-trans,poly-cis-decaprenyl diphosphate + isopentenyl diphosphate = diphosphate + di-trans,poly-cis-undecaprenyl diphosphate. PSase Phytoene synthetase Geranylgeranyl-diphosphate geranylgeranyltransferase Prephytoene-diphosphate synthase Phytoene synthase Manganese (1) 2 geranylgeranyl diphosphate = diphosphate + prephytoene diphosphate. The enzyme appears to be stereospecific, normally producing 15-cis-phytoene. (2) Prephytoene diphosphate = phytoene + diphosphate. However, in Erwinia herbicola, the product is the 15-trans isomer. All-trans-hexaprenyl-diphosphate synthase Trans-pentaprenyltranstransferase Will also use trans,trans-farnesyl diphosphate and all-trans-geranylgeranyl diphosphate as donors. All-trans-pentaprenyl diphosphate + isopentenyl diphosphate = diphosphate + all-trans-hexaprenyl diphosphate. Tryptophan dimethylallyltransferase Dimethylallyl diphosphate + L-tryptophan = diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan. Aspulvinone dimethylallyltransferase Will also use as acceptor aspulvinone G, a hydroxylated derivative of the complex phenolic pigment aspulvinone E. 2 dimethylallyl diphosphate + aspulvinone E = 2 diphosphate + aspulvinone H. Dimethylallylpyrophosphate:trihydroxypterocarpan dimethylallyl transferase Dimethylallyl-diphosphate:(6aS,11aS)-3,6a,9-trihydroxypterocarpan dimethyltransferase Dimethylallylpyrophosphate:3,6a,9-trihydroxypterocarpan dimethylallyltransferase Glyceollin synthase Trihydroxypterocarpan dimethylallyltransferase Part of the glyceollin biosynthesis system in soybean. (1) Dimethylallyl diphosphate + (6aS,11aS)-3,6a,9-trihydroxypterocarpan = diphosphate + 2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan. (2) Dimethylallyl diphosphate + (6aS,11aS)-3,6a,9-trihydroxypterocarpan = diphosphate + 4-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan. Isonocardicin synthase Involved in the biosynthesis of the beta-lactam antibiotic nocardicin A. S-adenosyl-L-methionine + nocardicin E = 5'-methylthioadenosine + isonocardicin A. 4-hydroxybenzoate nonaprenyltransferase Involved in the biosynthesis of ubiquinone. Solanesyl diphosphate + 4-hydroxybenzoate = diphosphate + nonaprenyl-4-hydroxybenzoate. Adenosylmethionine cyclotransferase S-adenosyl-L-methionine = 5'-methylthioadenosine + 2-aminobutan-4-olide. Phosphoglycerol geranylgeranyltransferase Geranylgeranyl diphosphate + sn-glyceryl phosphate = diphosphate + sn-3-O-(geranylgeranyl)glyceryl 1-phosphate. Geranylgeranylglycerol-phosphate geranylgeranyltransferase Geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = diphosphate + 2,3-bis-O-(geranylgeranyl)glycerol 1-phosphate. Nicotianamine synthase 3 S-adenosyl-L-methionine = 3 S-methyl-5'-thioadenosine + nicotianamine. Homospermidine synthase (1) 2 putrescine = sym-homospermidine + NH(3) + H(+). Hence the overall reaction is transfer of a 4-aminobutyl group. The reaction of this enzyme occurs in three steps, with some of the intermediates presumably remaining enzyme-bound: NAD(+)-dependent dehydrogenation of putrescine, transfer of the 4-aminobutylidene group from dehydroputrescine to a second molecule of putrescine and reduction of the imine intermediate to form homospermidine. (2) Putrescine + spermidine = sym-homospermidine + propane 1,3-diamine. Differs from EC 2.5.1.45, which cannot use putrescine as donor of the aminobutyl group. NAD Homospermidine synthase (spermidine-specific) The reaction of this enzyme occurs in three steps: (1) NAD(+)-dependent dehydrogenation of spermidine. (2) Transfer of the 4-aminobutylidene group from dehydrospermidine to a second molecule of putrescine. (3) Reduction of the imine intermediate to form homospermidine. This enzyme is more specific than EC 2.5.1.44 which is found in bacteria, as it cannot use putrescine as donor of the 4-aminobutyl group. Spermidine + putrescine = sym-homospermidine + propane-1,3-diamine. NAD Hence the overall reaction is transfer of a 4-aminobutyl group. Forms part of the biosynthetic pathway of the poisonous pyrrolizidine alkaloids of the ragworts (Senecio). Spermidine dehydrogenase [eIF-5A]-deoxyhypusine synthase Deoxyhypusine synthase (4-aminobutyl)lysine synthase Hypusine is formed from deoxyhypusine by the action of EC 1.14.99.29. [eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine. Catalyzes the first reaction of hypusine formation from one specific lysine residue of the eIF5A precursor. For the plant enzyme, homospermidine can substitute for spermidine and putrescine can substitute for the lysine residue of the eIF5A precursor. Hence the overall reaction is transfer of a 4-aminobutyl group. The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity. NAD The reaction occurs in four steps: NAD(+)-dependent dehydrogenation of spermidine (1a), formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue (1b), transfer of the same 4-aminobutylidene group from the enzyme intermediate to the e1F5A precursor (1c), reduction of the e1F5A-imine intermediate to form a deoxyhypusine residue (1d). O-acetylserine (thiol)-lyase A Cysteine synthetase O-acetylserine (thiol)-lyase O(3)-acetyl-L-serine acetate-lyase (adding hydrogen-sulfide) O-acetyl-L-serine sulfohydrolase OAS sulfhydrylase O-acetyl-L-serine sulfhydrylase Acetylserine sulfhydrylase O-acetylserine sulfhydrylase Cysteine synthase Not identical with EC 2.5.1.51, EC 2.5.1.52 and EC 2.5.1.53. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. O(3)-acetyl-L-serine + H(2)S = L-cysteine + acetate. Pyridoxal-phosphate Cystathionine gamma-synthase O-succinylhomoserine synthetase Homoserine O-transsuccinylase Homoserine transsuccinylase Cystathionine synthase O-succinyl-L-homoserine succinate-lyase (adding cysteine) Cystathionine synthetase O-succinylhomoserine (thiol)-lyase O-succinylhomoserine synthase Also reacts with H(2)S and methanethiol as replacing agents, producing homocysteine and methionine, respectively. In the absence of thiol, can also catalyze beta,gamma-elimination to form 2-oxobutanoate, succinate and ammonia. O(4)-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate. Pyridoxal-phosphate O-acetylhomoserine aminocarboxypropyltransferase O-acetylhomoserine (thiol)-lyase O-acetylhomoserine sulfhydrolase O-acetyl-L-homoserine sulfhydrolase Methionine synthase OAH sulfhydrylase O-acetyl-L-homoserine acetate-lyase (adding methanethiol) The rdfs:label methionine synthase is more commonly applied to EC 2.1.1.13. The enzyme from Saccharomyces cerevisiae also catalyzes the reaction of EC 2.5.1.47, but more slowly. O-acetyl-L-homoserine + methanethiol = L-methionine + acetate. Also reacts with other thiols and H(2)S, producing homocysteine or thioethers. Galactose-6-sulfurylase Galactose-6-sulfatase Porphyran sulfatase Eliminates sulfate from the D-galactose 6-sulfate residues of porphyran, producing 3,6-anhydrogalactose residues. Beta-(9-cytokinin)alanine synthase Beta-(9-cytokinin)-alanine synthase O-acetyl-L-serine acetate-lyase (adding N(6)-substituted adenine) Lupinate synthetase Lupinic acid synthetase Lupinic acid synthase Zeatin 9-aminocarboxyethyltransferase The reaction destroys their cytokinin activity and forms the corresponding 3-(adenin-9-yl)-L-alanine. O-acetyl-L-serine + zeatin = lupinate + acetate. The enzyme acts not only on zeatin but also on other N(6)-substituted adenines. Beta-pyrazolylalanine synthase (acetylserine) Beta-pyrazolylalanine synthase Pyrazolealanine synthase Beta-(1-pyrazolyl)alanine synthase O(3)-acetyl-L-serine acetate-lyase (adding pyrazole) Beta-pyrazolealanine synthase BPA-synthase Pyrazolylalaninase O(3)-acetyl-L-serine + pyrazole = 3-(pyrazol-1-yl)-L-alanine + acetate. Not identical with EC 2.5.1.52. Highly specific for acetylserine and pyrazole. L-mimosine synthase O(3)-acetyl-L-serine acetate-lyase (adding 3,4-dihydroxypyridin-1-yl) Brings about the biosynthesis of L-mimosine in Leucaena sp. and Mimosa. Not identical with EC 2.5.1.51. O(3)-acetyl-L-serine + 3,4-dihydroxypyridine = 3-(3,4-dihydroxypyridin-1-yl)-L-alanine + acetate. Uracilylalanine synthase Isowillardiine synthase Willardiine synthase O(3)-acetyl-L-serine acetate-lyase (adding uracil) O(3)-acetyl-L-serine + uracil = 3-(uracil-1-yl)-L-alanine + acetate. Both L-willardiine and L-isowillardiine are produced in the reaction. Not identical with EC 2.5.1.47. 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating) KDPH synthetase DAHP synthase Phospho-2-keto-3-deoxyheptonate aldolase KDPH synthase 2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase 3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase 7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating) D-erythrose-4-phosphate-lyase Deoxy-D-arabino-heptulosonate-7-phosphate synthetase Phospho-2-oxo-3-deoxyheptonate aldolase Phospho-2-keto-3-deoxyheptanoate aldolase DS-Mn 3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase DHAP synthase 2-dehydro-3-deoxy-phosphoheptonate aldolase Phospho-2-dehydro-3-deoxyheptonate aldolase D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating) 3-deoxy-7-phosphoheptulonate synthase 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase DAH7-P synthase Phospho-2-keto-3-deoxyheptonic aldolase DS-Co Phosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate. 2-keto-3-deoxy-8-phosphooctonic synthetase 3-deoxyoctulosonic 8-phosphate synthetase KDOP synthase 3-deoxy-D-manno-octulosonate-8-phosphate synthase KDO-8-P synthase 3-deoxy-8-phosphooctulonate synthase 2-dehydro-3-deoxy-phosphooctonate aldolase Phospho-2-keto-3-deoxyoctonate aldolase KDO-8-phosphate synthetase 3-deoxy-D-mannooctulosonate-8-phosphate synthetase 2-dehydro-3-deoxy-D-octonate-8-phosphate D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating) 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase Phosphoenolpyruvate + D-arabinose 5-phosphate + H(2)O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate. N-acetylneuraminate pyruvate-lyase (pyruvate-phosphorylating) N-acetylneuraminate synthase NeuAc synthase N-acetylneuraminic acid synthase (NANA)condensing enzyme Phosphoenolpyruvate + N-acetyl-D-mannosamine + H(2)O = phosphate + N-acetylneuraminate. N-acylneuraminate-9-phosphate pyruvate-lyase (pyruvate-phosphorylating) N-acetylneuraminate 9-phosphate lyase N-acetylneuraminate 9-phosphate sialic acid 9-phosphate synthase Sialic acid 9-phosphate synthetase N-acylneuraminate-9-phosphate synthase N-acetylneuraminate 9-phosphate synthetase Acts on N-glycoloyl and N-acetyl-derivatives. Phosphoenolpyruvate + N-acyl-D-mannosamine 6-phosphate + H(2)O = N-acylneuraminate 9-phosphate + phosphate. Protein farnesyltransferase CAAX farnesyltransferase FTase Catalyzes the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA(1)A(2)X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59. Magnesium Zinc Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate. Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, gamma-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction. The enzymes are relaxed in specificity for A(1), but cannot act if A(2) is aromatic. This enzyme, along with EC 2.5.1.59 and EC 2.5.1.60, constitutes the protein prenyltransferase family of enzymes. Protein geranylgeranyltransferase type I Type I protein geranyl-geranyltransferase GGTase-I GGTaseI Catalyzes the formation of a thioether linkage between the C-1 atom of the geranylgeranyl group and a cysteine residue fourth from the C-terminus of the protein. Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate. This enzyme, along with EC 2.5.1.58 and EC 2.5.1.60, constitutes the protein prenyltransferase family of enzymes. Zinc The Zn(2+) is required for peptide, but not for isoprenoid, substrate binding. Known targets of this enzyme include most gamma-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families. These protein acceptors have the C-terminal sequence CA(1)A(2)X, where the terminal residue, X, is preferably leucine; serine, methionine, alanine or glutamine makes the protein a substrate for EC 2.5.1.58. The enzymes are relaxed in specificity for A(1), but cannot act if A(2) is aromatic. Methionine adenosyltransferase S-adenosylmethionine synthetase AdoMet synthetase ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L-methionine. http://purl.uniprot.org/mim/250850 RabGGTase Rab geranylgeranyltransferase Type II protein geranyl-geranyltransferase Protein geranylgeranyltransferase type II GGTaseII Attaches geranylgeranyl groups to two C-terminal cysteines in Ras-related GTPases of a single family, the Rab family (Ypt/Sec4 in lower eukaryotes) that terminate in XXCC, XCXC and CCXX motifs. Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate. Post-translational modification with the geranylgeranyl moiety is essential for Rab GTPases to be able to control the processes of membrane docking and fusion. Reaction is entirely dependent on the Rab substrate being bound to Rab escort protein (REP). This enzyme, along with EC 2.5.1.58 and EC 2.5.1.59, constitutes the protein prenyltransferase family of enzymes. Uroporphyrinogen synthetase Uroporphyrinogen synthase HMB-synthase Hydroxymethylbilane synthase (4-(2-carboxyethyl)-3-(carboxymethyl)pyrrol-2-yl)methyltransferase (hydrolyzing) Uroporphyrinogen I synthetase Uroporphyrinogen I synthase Pre-uroporphyrinogen synthase Porphobilinogen deaminase http://purl.uniprot.org/mim/176000 If EC 4.2.1.75 is absent, the hydroxymethylbilane cyclizes spontaneously to form uroporphyrinogen I. 4 porphobilinogen + H(2)O = hydroxymethylbilane + 4 NH(3). The terminal tetrapyrrole is then hydrolyzed to yield the product, leaving a cysteine-bound dipyrrole on which assembly continues. Dipyrromethane In the presence of a second enzyme, EC 4.2.1.75, which is often called cosynthase, the product is cyclized to form uroporphyrinogen III. The enzyme works by stepwise addition of pyrrolylmethyl groups until a hexapyrrole is present at the active center. Chlorophyll synthase Chlorophyllide a + phytyl diphosphate = chlorophyll a + diphosphate. The enzyme is modified by binding of the first substrate, phytyl diphosphate, before reaction of the modified enzyme with the second substrate, chlorophyllide a, can occur. The reaction also occurs when phytyl diphosphate is replaced by geranylgeranyl diphosphate. Magnesium Fluorinase Adenosyl-fluoride synthase S-adenosyl-L-methionine + fluoride = 5'-deoxy-5'-fluoroadenosine + L-methionine. 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase--alpha-ketoglutarate decarboxylase 6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate synthase SHCHC synthase 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase 2-oxoglutarate + isochorismate = (1S,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate + pyruvate + CO(2). In the first step of the reaction, the oxoglutarate is decarboxylated and an adduct of the succinic semialdhyde is formed with thiamine diphosphate of the enzyme, as in both E1 of the EC 1.2.4.2 complex and in the reaction of EC 4.1.1.71 which liberates free succinic semialdehyde. O-phosphoserine(thiol)-lyase O-phosphoserine sulfhydrylase Pyridoxal-phosphate O-phospho-L-serine + H(2)S = L-cysteine + phosphate. The enzyme from Aeropyrum pernix acts on both O-phospho-L-serine and O(3)-acetyl-L-serine, in contrast with EC 2.5.1.47, which acts only on O(3)-acetyl-L-serine. CEA synthetase N(2)-(2-carboxyethyl)arginine synthetase CEAS N(2)-(2-carboxyethyl)arginine synthase D-glyceraldehyde 3-phosphate + L-arginine = N(2)-(2-carboxyethyl)-L-arginine + phosphate. Requires thiamine diphosphate and catalyzes the first step in the clavulanic-acid biosynthesis pathway. The 2-hydroxy-3-oxo group transferred from glyceraldehyde 3-phosphate is isomerized during transfer to form the 2-carboxyethyl group. CPPase Chrysanthemyl diphosphate synthase Chrysanthemyl diphosphate is a monoterpene with a non-head-to-tail linkage; it is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail. Magnesium or manganese The mechanism of its formation is similar to that of the early steps of squalene and phytoene biosynthesis. 2 dimethylallyl diphosphate = diphosphate + chrysanthemyl diphosphate. Chrysanthemyl diphosphate is the precursor of chrysanthemic acid, the acid half of the pyrethroid insecticides found in chrysanthemums. (Z)-farnesyl diphosphate synthase Z-farnesyl diphosphate synthase The product of this reaction is an intermediate in the synthesis of decaprenyl phosphate, which plays a central role in the biosynthesis of most features of the mycobacterial cell wall, including peptidoglycan, linker unit galactan and arabinan. Neryl diphosphate can also act as substrate. Magnesium or manganese Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2Z,6E)-farnesyl diphosphate. FDS-5 Lavandulyl diphosphate synthase Lavandulyl diphosphate is a monoterpene with a non-head-to-tail linkage; it is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail. When this enzyme is incubated with dimethylallyl diphosphate and isopentenyl diphosphate, it also forms the regular monoterpene geranyl diphosphate. The enzyme from Artemisia tridentata (big sagebrush) forms both lavandulyl diphosphate and chrysanthemyl diphosphate (see EC 2.5.1.67) when dimethylally diphosphate is the sole substrate. 2 dimethylallyl diphosphate = diphosphate + lavandulyl diphosphate. UDP-N-acetylglucosamine enoylpyruvyltransferase Pyruvate-uridine diphospho-N-acetyl-glucosamine transferase Phosphoenolpyruvate:UDP-2-acetamido-2-deoxy-D-glucose 2-enoyl-1-carboxyethyltransferase UDP-N-acetylglucosamine 1-carboxyvinyltransferase Phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine enolpyruvyltransferase MurA transferase Phosphopyruvate-uridine diphosphoacetylglucosamine pyruvatetransferase Pyruvate-uridine diphospho-N-acetylglucosamine transferase Pyruvic-uridine diphospho-N-acetylglucosaminyltransferase Pyruvate-UDP-acetylglucosamine transferase Phosphoenolpyruvate-UDP-acetylglucosamine-3-enolpyruvyltransferase Enoylpyruvate transferase Phosphoenolpyruvate:uridine-5'-diphospho-N-acetyl-2-amino-2-deoxyglucose 3-enolpyruvyltransferase UDP-N-acetylglucosamine 1-carboxyvinyl-transferase Phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine. tRNA isopentenyltransferase IPP transferase Isopentenyl-diphosphate:tRNA isopentenyltransferase Isopentenyl diphosphate + tRNA = diphosphate + tRNA containing 6-isopentenyladenosine. Riboflavin synthase 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine. Transferring nitrogenous groups Transaminases (aminotransferases) Aspartate aminotransferase Aspartate transaminase Glutamic--aspartic transaminase Transaminase A Glutamic--oxaloacetic transaminase L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. This activity can be formed from EC 2.6.1.57 by controlled proteolysis. Pyridoxal-phosphate N(2)-acetylornithine 5-transaminase N-acetylornithine-delta-transaminase Acetylornithine transaminase ACOAT Acetylornithine 5-aminotransferase Acetylornithine aminotransferase Succinylornithine aminotransferase N-acetylornithine aminotransferase Acetylornithine delta-transaminase N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. Pyridoxal-phosphate Also acts on L-ornithine and N(2)-succinyl-L-ornithine. Alanine--oxo-acid aminotransferase Alanine--oxo-acid transaminase L-alanine + a 2-oxo acid = pyruvate + an L-amino acid. Pyridoxal-phosphate Ornithine--keto acid transaminase Ornithine--keto acid aminotransferase Ornithine--ketoglutarate aminotransferase Ornithine transaminase Ornithine--oxo-acid transaminase L-ornithine 5-aminotransferase Ornithine--oxo acid aminotransferase L-ornithine aminotransferase Ornithine--2-oxoacid aminotransferase Ornithine ketoacid aminotransferase Ornithine--alpha-ketoglutarate aminotransferase Ornithine delta-transaminase Ornithine aminotransferase Ornithine 5-aminotransferase L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid. Pyridoxal-phosphate http://purl.uniprot.org/mim/258870 Asparagine--oxo-acid aminotransferase Asparagine--oxo-acid transaminase L-asparagine + a 2-oxo acid = 2-oxosuccinamate + an amino acid. Pyridoxal-phosphate Glutamine--pyruvate aminotransferase Glutaminase II Glutamine transaminase L Glutamine--oxo-acid transaminase Glutamine--pyruvate transaminase Pyridoxal-phosphate L-glutamine + pyruvate = 2-oxoglutaramate + L-alanine. L-methionine can act as donor. Glyoxylate can act as acceptor. GlcN6P synthase Hexosephosphate aminotransferase Glucosamine-6-phosphate synthase D-fructose-6-phosphate amidotransferase L-glutamine-D-fructose-6-phosphate amidotransferase Glucosamine-6-phosphate isomerase (glutamine-forming) Glucosamine--fructose-6-phosphate aminotransferase (isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing) L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate. Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination). Succinyldiaminopimelate transaminase Succinyldiaminopimelate aminotransferase Succinyldiaminopimelate transferase N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-2-L-amino-6-oxoheptanedioate + L-glutamate. Pyridoxal-phosphate Omega-amino acid--pyruvate aminotransferase Beta-alanine--pyruvate aminotransferase Beta-alanine--pyruvate transaminase L-alanine + 3-oxopropanoate = pyruvate + beta-alanine. Pyridoxal-phosphate Gamma-amino-N-butyrate transaminase 4-aminobutyrate aminotransferase 4-aminobutyrate transaminase GABA transaminase Beta-alanine--oxoglutarate aminotransferase http://purl.uniprot.org/mim/137150 Some preparations also act on beta-alanine, 5-aminopentanoate and (R,S)-3-amino-2-methylpropanoate. 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate. Alanine aminotransferase Glutamic--pyruvic transaminase Alanine transaminase Glutamic--alanine transaminase 2-aminobutanoate acts slowly instead of alanine. L-alanine + 2-oxoglutarate = pyruvate + L-glutamate. Pyridoxal-phosphate D-aspartate transaminase D-alanine transaminase D-amino-acid transaminase D-aspartic aminotransferase D-aspartate aminotransferase D-amino acid aminotransferase D-alanine aminotransferase D-amino acid transaminase D-alanine-D-glutamate transaminase D-alanine + 2-oxoglutarate = pyruvate + D-glutamate. The enzyme from thermophilic Bacillus species acts on many D-amino acids with D-alanine and D-2-aminobutyrate as the best amino donors. The enzyme from some other sources has a broader specificity. It can similarly use any of several 2-oxo acids as amino acceptor, with 2-oxoglutarate and 2-oxobutyrate among the best. Pyridoxal-phosphate Beta-aminobutyric transaminase L-3-aminoisobutyrate aminotransferase L-AIBAT (S)-3-amino-2-methylpropionate aminotransferase Beta-aminoisobutyrate-alpha-ketoglutarate transaminase L-3-aminoisobutyrate transaminase (S)-3-amino-2-methylpropionate transaminase L-3-aminoisobutyric aminotransferase Also acts on beta-alanine and other omega-amino acids having carbon chains between 2 and 5. (S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate. The two enantiomers of the 2-methyl-3-oxopropanoate formed by the enzyme interconvert by enolization, so that this enzyme, together with EC 2.6.1.40, provide a route for interconversion of the enantiomers of 3-amino-2-methylpropanoate. 4-hydroxyglutamate aminotransferase 4-hydroxyglutamate transaminase 4-hydroxy-L-glutamate + 2-oxoglutarate = 4-hydroxy-2-oxoglutarate + L-glutamate. Oxaloacetate can replace 2-oxoglutarate. May be identical with EC 2.6.1.1. Diiodotyrosine aminotransferase Diiodotyrosine transaminase Also acts on 3,5-dichloro-, 3,5-dibromo-and 3-iodo-L-tyrosine, thyroxine and triiodothyronine. Pyridoxal-phosphate 3,5-diiodo-L-tyrosine + 2-oxoglutarate = 3,5-diiodo-4-hydroxyphenylpyruvate + L-glutamate. Thyroid-hormone transaminase 3,5-dinitrotyrosine aminotransferase Thyroid-hormone aminotransferase Acts on monoiodotyrosine, diiodotyrosine, triiodothyronine, thyroxine and dinitrotyrosine (unlike EC 2.6.1.24, which does not act on dinitrotyrosine). Pyridoxal-phosphate L-3,5,3'-triiodothyronine + 2-oxoglutarate = 3-(4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl)-2-oxopropanoate + L-glutamate. Pyruvate or oxaloacetate can act as acceptor. Tryptophan transaminase Tryptophan aminotransferase Also acts on 5-hydroxytryptophan and, to a lesser extent, on the phenyl amino acids. Pyridoxal-phosphate L-tryptophan + 2-oxoglutarate = (indol-3-yl)pyruvate + L-glutamate. Tryptophan--phenylpyruvate aminotransferase Tryptophan--phenylpyruvate transaminase L-tryptophan + phenylpyruvate = (indol-3-yl)pyruvate + L-phenylalanine. Valine, leucine and isoleucine can replace tryptophan as amino donor. Diamine aminotransferase Diamine transaminase An alpha,omega-diamine + 2-oxoglutarate = an omega-aminoaldehyde + L-glutamate. Cysteine transaminase Cysteine aminotransferase Pyridoxal-phosphate L-cysteine + 2-oxoglutarate = mercaptopyruvate + L-glutamate. Pyridoxamine--pyruvate aminotransferase Pyridoxamine-pyruvic transaminase Pyridoxamine--pyruvate transaminase Pyridoxal-phosphate Pyridoxamine + pyruvate = pyridoxal + L-alanine. Pyridoxamine--oxaloacetate transaminase Pyridoxamine--oxaloacetate aminotransferase Pyridoxamine + oxaloacetate = pyridoxal + L-aspartate. Valine--3-methyl-2-oxovalerate aminotransferase Valine--isoleucine transaminase Valine--3-methyl-2-oxovalerate transaminase Valine--isoleucine aminotransferase http://purl.uniprot.org/mim/277100 L-valine + (S)-3-methyl-2-oxopentanoate = 3-methyl-2-oxobutanoate + L-isoleucine. dTDP-4-amino-4,6-dideoxy-D-glucose aminotransferase dTDP-4-amino-4,6-dideoxy-D-glucose transaminase Thymidine diphospho-4-keto-6-deoxy-D-glucose-glutamic transaminase TDP-4-keto-6-deoxy-D-glucose transaminase Thymidine diphospho-4-keto-6-deoxy-D-glucose transaminase Pyridoxal-phosphate dTDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate = dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate. UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase UDP-4-amino-2-acetamido-2,4,6-trideoxyglucose aminotransferase UDP-4-amino-2-acetamido-2,4,6-trideoxyglucose transaminase Pyridoxal-phosphate UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose + 2-oxoglutarate = UDP-2-acetamido-4-dehydro-2,6-dideoxyglucose + L-glutamate. Glycine--oxaloacetate aminotransferase Glycine--oxaloacetate transaminase Glycine + oxaloacetate = glyoxylate + L-aspartate. Pyridoxal-phosphate Lysine epsilon-aminotransferase L-lysine 6-transaminase L-lysine transaminase L-lysine aminotransferase The product (allysine) is converted into the intramolecularly dehydrated form, 1-piperideine 6-carboxylate. L-lysine + 2-oxoglutarate = 2-aminoadipate 6-semialdehyde + L-glutamate. Pyridoxal-phosphate (2-aminoethyl)phosphonic acid aminotransferase (2-aminoethyl)phosphonate transaminase 2-aminoethylphosphonate--pyruvate transaminase 2-aminoethylphosphonate--pyruvate aminotransferase (2-aminoethyl)phosphonate--pyruvate aminotransferase 2-aminoethylphosphonate aminotransferase 2-aminoethylarsonate can replace 2-aminoethylphosphonate as a substrate. (2-aminoethyl)phosphonate + pyruvate = 2-phosphonoacetaldehyde + L-alanine. Pyridoxal-phosphate Histidine aminotransferase Histidine transaminase L-histidine + 2-oxoglutarate = imidazol-5-yl-pyruvate + L-glutamate. 2-aminoadipate aminotransferase 2-aminoadipate transaminase L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate. Pyridoxal-phosphate Glycine transaminase Glycine aminotransferase Glycine + 2-oxoglutarate = glyoxylate + L-glutamate. Pyridoxal-phosphate Beta-aminoisobutyrate-pyruvate aminotransferase D-3-aminoisobutyrate--pyruvate transaminase D-3-aminoisobutyrate-pyruvate aminotransferase D-AIBAT D-3-aminoisobutyrate-pyruvate transaminase Beta-aminoisobutyrate--pyruvate transaminase (R)-3-amino-2-methylpropionate--pyruvate transaminase Beta-aminoisobutyrate--pyruvate aminotransferase (R)-3-amino-2-methylpropionate--pyruvate aminotransferase (R)-3-amino-2-methylpropionate transaminase D-beta-aminoisobutyrate:pyruvate aminotransferase (R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + L-alanine. The two enantiomers of the 2-methyl-3-oxopropanoate formed by the enzyme interconvert by enolization, so that this enzyme, together with EC 2.6.1.22, provide a route for interconversion of the enantiomers of 3-amino-2-methylpropanoate. http://purl.uniprot.org/mim/210100 D-methionine--pyruvate aminotransferase D-methionine--pyruvate transaminase D-methionine aminotransferase Oxaloacetate can replace pyruvate. D-methionine + pyruvate = 4-methylthio-2-oxobutanoate + L-alanine. Transaminase B Branched-chain amino acid aminotransferase Branched-chain-amino-acid transaminase L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. Also acts on L-isoleucine and L-valine. Pyridoxal-phosphate Different from EC 2.6.1.66. Aminolevulinate transaminase Aminolevulinate aminotransferase 5-aminolevulinate + pyruvate = 4,5-dioxopentanoate + L-alanine. Pyridoxal-phosphate AGT Alanine--glyoxylate aminotransferase Alanine--glyoxylate transaminase Pyridoxal-phosphate With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. L-alanine + glyoxylate = pyruvate + glycine. A second component also catalyzes the reaction of EC 2.6.1.51. http://purl.uniprot.org/mim/259900 Serine--glyoxylate aminotransferase SGAT Serine--glyoxylate transaminase Pyridoxal-phosphate L-serine + glyoxylate = 3-hydroxypyruvate + glycine. Diaminobutyrate--pyruvate transaminase Diaminobutyrate--pyruvate aminotransferase L-diaminobutyric acid transaminase L-2,4-diaminobutanoate + pyruvate = L-aspartate 4-semialdehyde + L-alanine. Pyridoxal-phosphate Alanine--oxomalonate transaminase L-alanine-ketomalonate transaminase Alanine--oxomalonate aminotransferase L-alanine + oxomalonate = pyruvate + aminomalonate. Pyridoxal-phosphate Delta-aminovalerate aminotransferase 5-aminovalerate transaminase 5-aminovalerate aminotransferase Delta-aminovalerate transaminase Pyridoxal-phosphate 5-aminopentanoate + 2-oxoglutarate = 5-oxopentanoate + L-glutamate. DOPA aminotransferase Dihydroxyphenylalanine transaminase Dihydroxyphenylalanine aminotransferase 3,4-dihydroxy-L-phenylalanine + 2-oxoglutarate = 3,4-dihydroxyphenylpyruvate + L-glutamate. Pyridoxal-phosphate Tyrosine aminotransferase TyrAT Tyrosine transaminase http://purl.uniprot.org/mim/276600 Pyridoxal-phosphate The enzyme can also catalyze the final step in the methionine-salvage pathway of Klebsiella pneumoniae. L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate. The three isoenzymic forms are interconverted by EC 3.4.22.32 and EC 3.4.22.33. L-phenylalanine can act instead of L-tyrosine. The mitochondrial enzyme may be identical with EC 2.6.1.1. Glutamine--scyllo-inosose transaminase Glutamine--scyllo-inosose aminotransferase Glutamine--scyllo-inositol transaminase L-glutamine + 2,4,6/3,5-pentahydroxycyclohexanone = 2-oxoglutaramate + 1-amino-1-deoxy-scyllo-inositol. Pyridoxal-phosphate Serine--pyruvate transaminase Serine--pyruvate aminotransferase L-serine + pyruvate = 3-hydroxypyruvate + L-alanine. Pyridoxal-phosphate The liver enzyme may be identical with EC 2.6.1.44. 3-phosphoserine aminotransferase Phosphohydroxypyruvic--glutamic transaminase Hydroxypyruvic phosphate--glutamic transaminase Phosphoserine aminotransferase PSAT 3PHP transaminase L-phosphoserine aminotransferase Phosphoserine transaminase Phosphohydroxypyruvate transaminase Non-phosphorylated forms of serine and threonine are not substrates. (2) 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. Also catalyzes the third step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate in E.coli (using reaction 2 above). Pyridoxal phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis. Pyridoxal-phosphate Catalyzes the second step in the phosphorylated pathway of serine biosynthesis in Escherichia coli. In E.coli, pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72, EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). (1) O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. Pyridoxamine-phosphate aminotransferase Pyridoxamine-phosphate transaminase Pyridoxamine 5'-phosphate + 2-oxoglutarate = pyridoxal 5'-phosphate + D-glutamate. Also acts, more slowly, on pyridoxamine. Taurine transaminase Taurine aminotransferase Taurine--2-oxoglutarate transaminase Taurine--glutamate transaminase Taurine--alpha-ketoglutarate aminotransferase Also acts on D,L-3-amino-isobutanoate, beta-alanine and 3-aminopropanesulfonate. Pyridoxal-phosphate Involved in the microbial utilization of beta-alanine. Taurine + 2-oxoglutarate = sulfoacetaldehyde + L-glutamate. 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol transaminase 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol aminotransferase L-glutamate and L-glutamine can also act as amino donors. 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol + pyruvate = 1D-1-guanidino-1-deoxy-3-dehydro-scyllo-inositol + L-alanine. Aromatic-amino-acid transaminase Oxaloacetate can act as acceptor. Pyridoxal-phosphate Controlled proteolysis converts the enzyme to EC 2.6.1.1. An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate. L-methionine can also act as donor, more slowly. Phenylalanine(histidine) aminotransferase Phenylalanine(histidine) transaminase L-histidine and L-tyrosine can act instead of L-phenylalanine; in the reverse reaction, L-methionine, L-serine and L-glutamine can replace L-alanine. L-phenylalanine + pyruvate = phenylpyruvate + L-alanine. dTDP-4-amino-4,6-dideoxygalactose aminotransferase dTDP-4-amino-4,6-dideoxygalactose transaminase Pyridoxal-phosphate dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutarate = dTDP-4-dehydro-6-deoxy-D-galactose + L-glutamate. Leucine transaminase Leucine aminotransferase Pyridoxal-phosphate L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. Aromatic-amino-acid--glyoxylate transaminase Aromatic-amino-acid--glyoxylate aminotransferase Glyoxylate, pyruvate and hydroxypyruvate can act as amino acceptors. An aromatic amino acid + glyoxylate = an aromatic oxo acid + glycine. Phenylalanine, kynurenine, tyrosine and histidine can act as amino donors. 7,8-diamino-pelargonic acid aminotransferase Adenosylmethionine--8-amino-7-oxononanoate aminotransferase DAPA aminotransferase 7,8-diaminononanoate aminotransferase Adenosylmethionine--8-amino-7-oxononanoate transaminase Pyridoxal-phosphate S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate. S-adenosylhomocysteine can also act as donor. Kynurenine--glyoxylate aminotransferase Kynurenine--glyoxylate transaminase L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine. Acts, more slowly, on L-phenylalanine, L-histidine and L-tyrosine. Glutamine--phenylpyruvate aminotransferase Glutamine--phenylpyruvate transaminase Glutamine transaminase K Pyridoxal-phosphate Has little activity on pyruvate and glyoxylate (cf. EC 2.6.1.15). L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine. L-methionine, L-histidine and L-tyrosine can act as donors. N(6)-acetyl-beta-lysine transaminase N(6)-acetyl-beta-lysine aminotransferase Pyridoxal-phosphate 6-acetamido-3-aminohexanoate + 2-oxoglutarate = 6-acetamido-3-oxohexanoate + L-glutamate. Alanine--valine transaminase Transaminase C Valine--pyruvate transaminase Valine--pyruvate aminotransferase L-valine + pyruvate = 3-methyl-2-oxobutanoate + L-alanine. Pyridoxal-phosphate Different from EC 2.6.1.42. Norleucine transaminase 2-aminohexanoate transaminase Norleucine aminotransferase 2-aminohexanoate aminotransferase Pyridoxal-phosphate L-2-aminohexanoate + 2-oxoglutarate = 2-oxohexanoate + L-glutamate. Also acts on L-leucine and, more slowly, on L-isoleucine, L-2-aminopentanoate and L-aspartate. Ornithine(lysine) aminotransferase Ornithine(lysine) transaminase The enzyme from Trichomonas vaginalis also acts on L-lysine, producing 2,3,4,5-tetrahydropyridine-2-carboxylate. L-ornithine + 2-oxoglutarate = 3,4-dihydro-2H-pyrrole-2-carboxylate + L-glutamate + H(2)O. Kynurenine--oxoglutarate transaminase Kynurenine aminotransferase Kynurenine--oxoglutarate aminotransferase The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction. Also acts on 3-hydroxykynurenine. Pyridoxal-phosphate L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. Aspartate--phenylpyruvate transaminase Aspartate--phenylpyruvate aminotransferase L-aspartate + phenylpyruvate = oxaloacetate + L-phenylalanine. The enzyme from Pseudomonas putida also acts on 4-hydroxyphenylpyruvate and, more slowly, on L-glutamate and L-histidine. Lysine--pyruvate 6-transaminase Lysine--pyruvate 6-aminotransferase L-lysine + pyruvate = L-2-aminoadipate 6-semialdehyde + L-alanine. D-4-hydroxyphenylglycine aminotransferase D-hydroxyphenylglycine aminotransferase D-4-hydroxyphenylglycine transaminase D-4-hydroxyphenylglycine + 2-oxoglutarate = 4-hydroxyphenylglyoxylate + L-glutamate. Pyridoxal-phosphate MGAT Methionine--glyoxylate transaminase L-glutamate can also act as donor. L-methionine + glyoxylate = 4-methylthio-2-oxobutanoate + glycine. Cephalosporin C aminotransferase Cephalosporin-C transaminase A number of D-amino acids, including D-alanine, D-aspartate and D-methionine can also act as amino-group donors. (7R)-7-(5-carboxy-5-oxopentanoyl)aminocephalosporinate + D-glutamate = cephalosporin C + 2-oxoglutarate. Although this enzyme acts on several free D-amino acids, it differs from EC 2.6.1.21 in that it can use cephalosporin C as an amino donor. Cysteine-conjugate transaminase A number of cysteine conjugates can also act. S-(4-bromophenyl)-L-cysteine + 2-oxoglutarate = S-(4-bromophenyl)-mercaptopyruvate + L-glutamate. Diaminobutyrate--2-oxoglutarate transaminase Diaminobutyrate transaminase Diaminibutyric acid aminotransferase DABA aminotransferase DAB aminotransferase 2,4-diaminobutyrate 4-aminotransferase Diaminobutyrate--2-oxoglutarate aminotransferase Differs from EC 2.6.1.46, which has pyruvate as the amino-group acceptor. L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartate 4-semialdehyde + L-glutamate. Potassium Pyridoxal-phosphate This is the first enzyme in the ectoine biosynthesis pathway, the other enzymes involved being EC 2.3.1.178 and EC 4.2.1.108. Taurine--pyruvate aminotransferase The enzyme from Bilophila wadsworthia is reversible, and catalyzes the first step of anaerobic taurine degradation. Pyridoxal-phosphate Taurine + pyruvate = L-alanine + 2-sulfoacetaldehyde. Hypotaurine (i.e. 2-aminoethanesulfinate) and beta-alanine are also significant donors of an amino group. Unlike, EC 2.6.1.55, 2-oxoglutarate is not an acceptor of amino groups. L-aspartate:prephenate aminotransferase Aspartate--prephenate aminotransferase PAT Prephenate transaminase Prephenate aspartate aminotransferase L-arogenate + oxaloacetate = prephenate + L-aspartate. Pyridoxal-phosphate Glutamate can also act as the amino donor, but more slowly (cf. EC 2.6.1.79). Glutamate--prephenate aminotransferase Prephenate transaminase PAT L-glutamate:prephenate aminotransferase Aspartate can also act as the amino donor, but more slowly (cf. EC 2.6.1.78). L-arogenate + 2-oxoglutarate = prephenate + L-glutamate. The enzyme from higher plants shows a marked preference for prephenate as substrate compared to pyruvate, phenylpyruvate or 4-hydroxyphenylpyruvate. Pyridoxal-phosphate 2,5-diaminovalerate aminotransferase 2,5-diaminovalerate transaminase Diamino-acid aminotransferase 2,5-diaminopentanoate + 2-oxoglutarate = 5-amino-2-oxopentanoate + L-glutamate. 2,5-diaminoglutarate can act instead of diaminopentanoate. Pyridoxal-phosphate NAAT-I NAAT Nicotianamine transaminase NAAT-III Nicotianamine aminotransferase NAAT-II Both compounds chelate Fe(2+) and Fe(3+); these chelators, called mugineic acid family phytosiderophores, are taken up by the grass, which is thereby supplied with iron. They secrete both the nicotianamine and the transaminated product into the soil around them. This enzyme is produced by grasses. Pyridoxal-phosphate Nicotianamine + 2-oxoglutarate = 3''-deamino-3''-oxonicotianamine + L-glutamate. Succinylornithine transaminase N(2)-succinylornithine 5-aminotransferase Succinylornithine aminotransferase SOAT This is the third enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine. Pyridoxal-phosphate The five enzymes involved in this pathway are EC 2.3.1.109, EC 3.5.3.23, EC 2.6.1.81, EC 1.2.1.71 and EC 3.5.1.96. In Pseudomonas aeruginosa, the arginine-inducible succinylornithine transaminase, EC 2.6.1.11 and EC 2.6.1.13 activities are catalyzed by the same enzyme, but this is not the case in all species. N(2)-succinyl-L-ornithine + 2-oxoglutarate = N-succinyl-L-glutamate 5-semialdehyde + L-glutamate. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. Also acts on N(2)-acetyl-L-ornithine and L-ornithine, but more slowly. Putrescine aminotransferase Putrescine transaminase Putrescine-alpha-ketoglutarate transaminase PAT Cadaverine and spermidine can also act as substrates. The enzymatic part of the reaction produces 4-aminobutanal that spontaneously cyclizes to form 1-pyrroline, which is a substrate for EC 1.2.1.19. Forms part of the arginine catabolism pathway. Pyridoxal-phosphate Putrescine + 2-oxoglutarate = L-glutamate + 1-pyrroline + H(2)O. LL-diaminopimelate transaminase LL-DAP aminotransferase LL-DAP-AT LL-diaminopimelate aminotransferase 2-oxoglutarate cannot be replaced by oxaloacetate or pyruvate. This is one of the final steps in the lysine biosynthesis pathway of plants (ranging from mosses to flowering plants). Meso-diaminoheptanedioate, an isomer of LL-2,6-diaminoheptanedioate, and the structurally related compounds lysine and ornithine are not substrates. Pyridoxal-phosphate It is not yet known if the substrate of the biosynthetic reaction is the cyclic or acyclic form of tetrahydropyridine-2,6-dicarboxylate. LL-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H(2)O. In vivo, the reaction occurs in the opposite direction to that shown above. Arginine:pyruvate transaminase Arginine--pyruvate transaminase Pyridoxal-phosphate L-arginine + pyruvate = 5-guanidino-2-oxopentanoate + L-alanine. This pathway is only used when the major route of arginine catabolism, i.e. the arginine succinyltransferase pathway, is blocked. This is the first catalytic enzyme of the arginine transaminase pathway for L-arginine utilization in Pseudomonas aeruginosa. While L-arginine is the best substrate, the enzyme exhibits broad substrate specificity, with L-lysine, L-methionine, L-leucine, ornithine and L-glutamine also able to act as substrates, but more slowly. Pyruvate cannot be replaced by 2-oxoglutarate as amino-group acceptor. Histidinol-phosphate aminotransferase Imidazolylacetolphosphate aminotransferase Histidinol-phosphate transaminase Imidazole acetol-phosphate transaminase L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. Pyridoxal-phosphate Oximinotransferases Oximase Transoximinase Pyruvate-acetone oximinotransferase Oximinotransferase Acetaldehyde can act instead of acetone; D-glucose oxime can act instead of pyruvate oxime. Pyruvate oxime + acetone = pyruvate + acetone oxime. Transferring other nitrogenous groups dATP(dGTP)--DNA purinetransferase (1) dATP + depurinated DNA = deoxyribose triphosphate + DNA. dATP reacts at sites of the double-stranded depurinated DNA that lack adenine, and dGTP at sites that lack guanine. (2) dGTP + depurinated DNA = deoxyribose triphosphate + DNA. The purine residue is transferred on to the apurinic site forming a normal glycosylic bond. Pyridoxine 5-phosphate phospho lyase PNP synthase Pyridoxine 5'-phosphate synthase 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = pyridoxine 5'-phosphate + phosphate + 2 H(2)O. In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72, EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5. 1-deoxy-D-xylulose cannot replace 1-deoxy-D-xylulose 5-phosphate as a substrate. Transferring phosphorous-containing groups Phosphotransferases with an alcohol group as acceptor Hexokinase type II Hexokinase type IV (glucokinase) Hexokinase Hexokinase type III Hexokinase type I ATP + D-hexose = ADP + D-hexose 6-phosphate. D-glucose, D-mannose, D-fructose, sorbitol and D-glucosamine can act as acceptors. ITP and dATP can act as donors. http://purl.uniprot.org/mim/235700 Glucose-phosphate kinase Phosphoglucokinase ATP + alpha-D-glucose 1-phosphate = ADP + alpha-D-glucose 1,6-bisphosphate. Methylthioribose kinase 5-methylthioribose kinase MTR kinase S-methyl-5-thioribose kinase Also acts, more slowly, on CTP. ATP + S-methyl-5-thio-D-ribose = ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate. Tagatose kinase D-tagatose 6-phosphate kinase ATP + D-tagatose = ADP + D-tagatose 6-phosphate. Hamamelose kinase Also acts, more slowly, on D-hamamelitol. ATP + D-hamamelose = ADP + D-hamamelose 2'-phosphate. Capreomycin phosphotransferase Viomycin phosphotransferase Viomycin kinase A serine residue in the peptide antibiotics acts as phosphate-acceptor. ATP + viomycin = ADP + O-phosphoviomycin. Also acts on capreomycins. 6-phosphofructo-2-kinase Phosphofructokinase 2 The enzyme copurifies with EC 3.1.3.46. ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate. Not identical with EC 2.7.1.11. Glucose 1,6-diphosphate synthase Glucose-1,6-bisphosphate synthetase Glucose-1,6-bisphosphate synthase 3-phospho-D-glyceroyl phosphate + alpha-D-glucose 1-phosphate = 3-phospho-D-glycerate + alpha-D-glucose 1,6-bisphosphate. Alpha-D-glucose 6-phosphate can act as acceptor, forming alpha-D-glucose 1,6-bisphosphate. Diacylglycerol kinase Diglyceride kinase DGK ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate. Dolichol kinase CTP + dolichol = CDP + dolichyl phosphate. Phosphofructokinase I Phosphohexokinase 6-phosphofructokinase http://purl.uniprot.org/mim/232800 ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. Not identical with EC 2.7.1.105. D-tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. UTP, CTP and ITP can act as donors. Deoxyguanosine kinase ATP + deoxyguanosine = ADP + dGMP. Deoxyinosine can also act as acceptor. AMP--thymidine kinase Adenylate-nucleoside phosphotransferase AMP + thymidine = adenosine + thymidine 5'-phosphate. The deoxypyrimidine kinase complex induced by Herpes simplex virus catalyzes this reaction as well as those of EC 2.7.1.21, EC 2.7.1.128, and EC 2.7.4.9. ADP--thymidine kinase ADP + thymidine = AMP + thymidine 5'-phosphate. The deoxypyrimidine kinase complex induced by Herpes simplex virus catalyzes this reaction as well as those of EC 2.7.1.21, EC 2.7.1.114 and EC 2.7.4.9. Hygromycin B phosphotransferase APH(7'') Hygromycin-B kinase ATP + hygromycin B = ADP + 7''-O-phosphohygromycin. Phosphorylates the antibiotics hygromycin B, 1-N-hygromycin B and destomycin, but not hygromycin B(2), at the 7''-hydroxy group in the destomic acid ring. Gluconokinase Gluconate kinase ATP + D-gluconate = ADP + 6-phospho-D-gluconate. Phosphoenolpyruvate--glycerone phosphotransferase Phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate. Xylitol kinase Xylitol phosphotransferase ATP + xylitol = ADP + xylitol 5-phosphate. Inositol 1,4,5-trisphosphate 3-kinase Ins(1,4,5)P(3) 3-kinase 1D-myo-inositol-trisphosphate 3-kinase IP3K Inositol-trisphosphate 3-kinase IP3 3-kinase Calcium ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate. Ketogluconokinase Dehydrogluconokinase ATP + 2-dehydro-D-gluconate = ADP + 6-phospho-2-dehydro-D-gluconate. Tetraacyldisaccharide 4'-kinase Lipid-A 4'-kinase ATP + (2-N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl phosphate) = ADP + (2-N,3-O-bis(3-hydroxytetradecanoyl)-4-O-phosphono-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl phosphate). Involved with EC 2.3.1.129 and 2.4.1.182 in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Escherichia coli. Inositol-trisphosphate 5-kinase Inositol-tetrakisphosphate 1-kinase 1D-myo-inositol-tetrakisphosphate 1-kinase Inositol-trisphosphate 6-kinase 1D-myo-inositol-trisphosphate 5-kinase 1D-myo-inositol-trisphosphate 6-kinase This enzyme also phosphorylates Ins(1,3,4)P(3) on O-5 and O-6. ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate. The phosphotransfer from ATP to either inositol 1,3,4-trisphosphate or inositol 3,4,5,6-tetrakisphosphate appears to be freely reversible to the extent that the enzyme can act like an inositol polyphosphate phosphatase in the presence of ADP. It can also catalyze an isomerization between Ins(1,3,4,5)P(4) and Ins(1,3,4,6)P(4) in the presence of ADP. Macrolide 2'-kinase Erythromycin, spiramycin and some other macrolide antibiotics can also act as acceptors. ATP + oleandomycin = ADP + oleandomycin 2'-O-phosphate. Type III phosphoinositide 3-kinase 1-phosphatidylinositol 3-kinase PI3-kinase Type I phosphatidylinositol kinase Phosphatidylinositol 3-kinase PtdIns-3-kinase ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate. Ceramide kinase Acylsphingosine kinase ATP + ceramide = ADP + ceramide 1-phosphate. Heptulokinase Sedoheptulokinase ATP + sedoheptulose = ADP + sedoheptulose 7-phosphate. Inositol-tetrakisphosphate 5-kinase 1D-myo-inositol-tetrakisphosphate 5-kinase ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate. Glycerol-3-phosphate--glucose phosphotransferase sn-glycerol 3-phosphate + D-glucose = glycerol + D-glucose 6-phosphate. Involved in the anaerobic metabolism of sugars in the bloodstream of trypanosomes. Diphosphate-purine nucleoside kinase Pyrophosphate-purine nucleoside kinase Pyrophosphate-dependent nucleoside kinase Diphosphate-dependent nucleoside kinase Diphosphate + a purine nucleoside = phosphate + a purine mononucleotide. The enzyme from the Acholeplasma class of Mollicutes catalyzes the conversion of adenosine, guanosine and inosine to AMP, GMP and IMP. ATP cannot substitute for diphosphate as a substrate. Phosphotagatokinase Tagatose-6-phosphate kinase ATP + D-tagatose 6-phosphate = ADP + D-tagatose 1,6-bisphosphate. Deoxynucleoside kinase Ms-dNK Multisubstrate deoxyribonucleoside kinase Multifunctional deoxynucleoside kinase Multispecific deoxynucleoside kinase ATP + 2'-deoxynucleoside = ADP + 2'-deoxynucleoside 5'-phosphate. The enzyme from embryonic cells of Drosophila melanogaster differs from other deoxynucleoside kinases (EC 2.7.1.76 and EC 2.7.1.113) in its broad specificity for all four common deoxynucleosides. ADP-specific phosphofructokinase ADP-6-phosphofructokinase ADP-Pfk ADP-dependent phosphofructokinase Magnesium or cobalt ADP + D-fructose 6-phosphate = AMP + D-fructose 1,6-bisphosphate. ADP can be replaced by GDP, ATP and GTP, to a limited extent. ADP-specific glucokinase ADP-dependent glucokinase The enzyme from Pyrococcus furiosus is highly specific for D-glucose; there is some activity with 2-deoxy-D-glucose, but no activity with D-fructose, D-mannose or D-galactose as the substrate. No activity is detected when ADP is replaced by ATP, GDP, phosphoenolpyruvate, diphosphate or polyphosphate. Magnesium ADP + D-glucose = AMP + D-glucose 6-phosphate. CMK CDP-ME kinase 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. Magnesium or manganese 1-phosphatidylinositol-5-phosphate 4-kinase Type II PIP kinase ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate. Ribokinase 2-deoxy-D-ribose can also act as acceptor. ATP + D-ribose = ADP + D-ribose 5-phosphate. Type III PIP kinase 1-phosphatidylinositol-3-phosphate 5-kinase Phosphatidylinositol 3-phosphate 5-kinase ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate. AtIpk2-beta Inositol-polyphosphate multikinase IpK2 AtIpk2-alpha Inositol polyphosphate 6-/3-/5-kinase IP3/IP4 6-/3-kinase IP3/IP4 dual-specificity 6-/3-kinase (2) ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate. (1) ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate. This enzyme also phosphorylates Ins(1,4,5)P(3) to Ins(1,3,4,5)P(4), Ins(1,3,4,5)P(4) to Ins(1,3,4,5,6)P(5), and Ins(1,3,4,5,6)P(4) to Ins(PP)P(4), isomer unknown. The enzyme from the plant Arabidopsis thaliana can also phosphorylate Ins(1,3,4,6)P(4) and Ins(1,2,3,4,6)P(5) at the D-5-position to produce 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate (InsP(6)), respectively. Yeast produce InsP(6) from Ins(1,4,5)P(3) by the actions of this enzyme and EC 2.7.1.158. Type I phosphoinositide 3-kinase Phosphatidylinositol-4,5-bisphosphate 3-kinase ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate. This enzyme also catalyzes the phosphorylation of PtdIns4P to PtdIns(3,4)P(2), and of PtdIns to PtdIns3P. Type II phosphoinositide 3-kinase Phosphoinositide 3-kinase C2-domain-containing phosphoinositide 3-kinase Phosphatidylinositol-4-phosphate 3-kinase This enzyme also phosphorylates PtdIns to PtdIns3P. ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate. Diphosphoinositol-pentakisphosphate kinase ATP + 5-diphospho-1D-myo-inositol pentakisphosphate = ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate (isomeric configuration unknown). AdoCbi kinase/AdoCbi-phosphate guanylyltransferase Adenosylcobinamide kinase Adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase However, both activities are not required at all times. CobU is a bifunctional enzyme that has both kinase (EC 2.7.1.156) and guanylyltransferase (EC 2.7.7.62) activities. The kinase activity has been proposed to function only when S.typhimurium is assimilating cobinamide whereas the guanylyltransferase activity is required for both assimilation of exogenous cobinamide and for de novo synthesis of adenosylcobalamin. ATP or GTP + adenosylcobinamide = adenosylcobinamide phosphate + ADP or GDP. In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC 2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73) and CobS (EC 2.7.8.26) catalyze reactions in the nucleotide loop assembly pathway, which convert adenosylcobinamide (AdoCbi) into adenosylcobalamin (AdoCbl). The final step in adenosylcobalamin biosynthesis is the condensation of AdoCbi-GDP with alpha-ribazole, which is catalyzed by CobS (EC 2.7.8.26), to yield adenosylcobalamin. The second branch of the nucleotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by CobU. CobT and CobC are involved in 5,6-dimethylbenzimidazole activation whereby 5,6-dimethylbenzimidazole is converted to its riboside, alpha-ribazole. GalNAc kinase GK2 GALK2 N-acetylgalactosamine (GalNAc)-1-phosphate kinase N-acetylgalactosamine kinase The enzyme is highly specific for GalNAc as substrate, but has slight activity with D-galactose. ATP + N-acetyl-D-galactosamine = ADP + N-acetyl-alpha-D-galactosamine 1-phosphate. Magnesium Inositol-pentakisphosphate 2-kinase Inositol polyphosphate kinase Inositol 1,3,4,5,6-pentakisphosphate 2-kinase Ins(1,3,4,5,6)P(5) 2-kinase IP5 2-kinase ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol hexakisphosphate. Inositol hexakisphosphate (phytate) accumulates in storage protein bodies during seed development and, when hydrolyzed, releases stored nutrients to the developing seedling before the plant is capable of absorbing nutrients from its envirionment. The enzyme can also use Ins(1,4,5,6)P(4) and Ins(1,4,5)P(3) as substrate. Inositol trisphosphate 5/6-kinase IP56K Inositol-1,3,4-trisphosphate 5/6-kinase Ins(1,3,4)P(3) 5/6-kinase (1) ATP + 1D-myo-inositol 1,3,4-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate. Yeast do not have this enzyme, so produce InsP(6) from Ins(1,4,5)P(3) by the actions of EC 2.7.1.151 and EC 2.7.1.158. InsP(6) is involved in many cellular processes, including mRNA export from the nucleus. (2) ATP + 1D-myo-inositol 1,3,4-trisphosphate = ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate. In humans, this enzyme, along with EC 2.7.1.127, EC 2.7.1.140 and EC 2.7.1.158 is involved in the production of inositol hexakisphosphate (InsP(6)). L-ribulokinase Ribulokinase Ribitol and L-arabinitol can also act as acceptors. ATP + L(or D)-ribulose = ADP + L(or D)-ribulose 5-phosphate. 2'-phosphotransferase Tpt1p Yeast 2'-phosphotransferase Catalyzes the final step of tRNA splicing in the yeast Saccharomyces cerevisiae. Oligonucleotides with only a terminal 5'-or 3'-phosphate are not substrates. In the second step, dephosphorylated (mature) tRNA is formed along with ADP ribose 1'',2''-cyclic phosphate. 2'-phospho-[ligated tRNA] + NAD(+) = mature tRNA + ADP ribose 1'',2''-phosphate + nicotinamide + H(2)O. The reaction takes place in two steps: in the first step, the 2'-phosphate on the RNA substrate is ADP-ribosylated, causing the relase of nicotinamide and the formation of the reaction intermediate, ADP-ribosylated tRNA. Highly specific for oligonucleotide substrates bearing an internal 2'-phosphate. Xylulose kinase Xylulokinase ATP + D-xylulose = ADP + D-xylulose 5-phosphate. Phosphoribokinase ATP + D-ribose 5-phosphate = ADP + D-ribose 1,5-bisphosphate. Phosphopentokinase Phosphoribulokinase ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate. Glucose kinase Glucokinase A group of enzymes found in invertebrates and microorganisms highly specific for glucose. ATP + D-glucose = ADP + D-glucose 6-phosphate. http://purl.uniprot.org/mim/125851 http://purl.uniprot.org/mim/602485 Adenosine kinase 2-aminoadenosine can also act as acceptor. ATP + adenosine = ADP + AMP. Thymidine kinase dGTP can also act as donor. http://purl.uniprot.org/mim/609560 The deoxypyrimidine kinase complex induced by Herpes simplex virus catalyzes this reaction as well as those of EC 2.7.1.114, EC 2.7.1.118, and EC 2.7.4.9. Deoxyuridine can also act as acceptor. ATP + thymidine = ADP + thymidine 5'-phosphate. Ribosylnicotinamide kinase ATP + N-ribosylnicotinamide = ADP + nicotinamide ribonucleotide. DPN kinase NAD(+) kinase ATP + NAD(+) = ADP + NADP(+). Dephosphocoenzyme A kinase Dephospho-CoA kinase ATP + dephospho-CoA = ADP + CoA. Adenosine 5'-phosphosulfate kinase Adenylylsulfate kinase Adenylyl-sulfate kinase APS kinase http://purl.uniprot.org/mim/603005 ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate. The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP. This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25. Flavokinase Riboflavin kinase ATP + riboflavin = ADP + FMN. Erythritol kinase ATP + erythritol = ADP + D-erythritol 4-phosphate. Triokinase Triose kinase ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate. Glycerone kinase Dihydroxyacetone kinase ATP + glycerone = ADP + glycerone phosphate. Hepatic fructokinase Ketohexokinase ATP + D-fructose = ADP + D-fructose 1-phosphate. http://purl.uniprot.org/mim/229800 D-sorbose, D-agatose and 5-dehydro-D-fructose also act as acceptors. Glycerokinase ATP:glycerol 3-phosphotransferase Glycerol kinase UTP (and, in the case of the Saccharomyces cerevisiae enzyme, ITP and GTP) can act as donors. http://purl.uniprot.org/mim/307030 ATP + glycerol = ADP + sn-glycerol 3-phosphate. Glycerone and L-glyceraldehyde can act as acceptors. Glycerate kinase ATP + (R)-glycerate = ADP + 3-phospho-(R)-glycerate. Choline kinase ATP + choline = ADP + O-phosphocholine. Ethanolamine and its methyl and ethyl derivatives can also act as acceptors. ATP:pantothenate 4'-phosphotransferase D-pantothenate kinase Pantothenic acid kinase Pantothenate kinase (phosphorylating) Pantothenate kinase ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate. http://purl.uniprot.org/mim/234200 http://purl.uniprot.org/mim/607236 Pantetheine kinase ATP + pantetheine = ADP + pantetheine 4'-phosphate. Vitamin B(6) kinase Pyridoxine kinase Pyridoxamine kinase Vitamin B6 kinase Pyridoxal kinase ATP + pyridoxal = ADP + pyridoxal 5'-phosphate. Pyridoxine, pyridoxamine and various derivatives can also act as acceptors. Mevalonate kinase CTP, GTP and UTP can also act as donors. http://purl.uniprot.org/mim/260920 http://purl.uniprot.org/mim/610377 ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate. Homoserine kinase ATP + L-homoserine = ADP + O-phospho-L-homoserine. D-fructokinase Fructokinase ATP + D-fructose = ADP + D-fructose 6-phosphate. Phosphoenolpyruvate kinase Phosphoenol transphosphorylase Pyruvate kinase http://purl.uniprot.org/mim/266200 ATP + pyruvate = ADP + phosphoenolpyruvate. UTP, GTP, CTP, ITP and dATP can also act as donors. http://purl.uniprot.org/mim/102900 Also phosphorylates hydroxylamine and fluoride in the presence of CO(2). Glucose-1-phosphate phosphodismutase 2 D-glucose 1-phosphate = D-glucose + D-glucose 1,6-bisphosphate. Riboflavin phosphotransferase Alpha-D-glucose 1-phosphate + riboflavin = D-glucose + FMN. Glucuronokinase ATP + D-glucuronate = ADP + 1-phospho-alpha-D-glucuronate. Galacturonokinase ATP + D-galacturonate = ADP + 1-phospho-alpha-D-galacturonate. 3-deoxy-2-oxo-D-gluconate kinase KDG kinase 2-dehydro-3-deoxygluconokinase 2-keto-3-deoxygluconokinase ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate. L-arabinokinase ATP + L-arabinose = ADP + beta-L-arabinose 1-phosphate. D-ribulokinase ATP + D-ribulose = ADP + D-ribulose 5-phosphate. Uridine monophosphokinase Uridine kinase GTP and ITP can act as donors. ATP + uridine = ADP + UMP. Cytidine can act as acceptor. http://purl.uniprot.org/mim/191710 Hydroxymethylpyrimidine kinase ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine. CTP, UTP and GTP can act as donors. Rhamnulokinase ATP + L-rhamnulose = ADP + L-rhamnulose 1-phosphate. Hydroxyethylthiazole kinase ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. L-fuculokinase ATP + L-fuculose = ADP + L-fuculose 1-phosphate. Fucokinase (phosphorylating) L-fucose kinase L-fucokinase Fucose kinase ATP:6-deoxy-L-galactose 1-phosphotransferase Fucokinase ATP + L-fucose = ADP + beta-L-fucose 1-phosphate. Forms part of a salvage pathway for reutilization of L-fucose. Divalent cation Can also phosphorylate D-arabinose, but more slowly. L-xylulose kinase L-xylulokinase ATP + L-xylulose = ADP + L-xylulose 5-phosphate. D-arabinokinase ATP + D-arabinose = ADP + D-arabinose 5-phosphate. Allose kinase Allokinase ATP + D-allose = ADP + D-allose 6-phosphate. 1-phosphofructokinase Fructose 1-phosphate kinase ITP, GTP or UTP can replace ATP. ATP + D-fructose 1-phosphate = ADP + D-fructose 1,6-bisphosphate. 2-keto-3-deoxy-galactonokinase 2-oxo-3-deoxygalactonate kinase 2-dehydro-3-deoxygalactonokinase ATP + 2-dehydro-3-deoxy-D-galactonate = ADP + 2-dehydro-3-deoxy-D-galactonate 6-phosphate. GlcNAc kinase N-acetylglucosamine kinase ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate. The bacterial enzyme also acts on D-glucose. Galactokinase D-galactosamine can also act as acceptor. ATP + D-galactose = ADP + alpha-D-galactose 1-phosphate. http://purl.uniprot.org/mim/230200 N-acylmannosamine kinase Acts on the acetyl and glycolyl derivatives. http://purl.uniprot.org/mim/605820 ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate. http://purl.uniprot.org/mim/600737 Acyl-phosphate--hexose phosphotransferase Acyl phosphate + D-hexose = an acid + D-hexose phosphate. Phosphorylates D-glucose and D-mannose on O-6, and D-fructose on O-1 or O-6. Phosphoramidate--hexose phosphotransferase Phosphoramidate + hexose = NH(3) + alpha-D-hexose 1-phosphate. May be identical with EC 3.1.3.9. Polyphosphate glucokinase Polyphosphate--glucose phosphotransferase Also acts on glucosamine. (Phosphate)(n) + D-glucose = (phosphate)(n-1) + D-glucose 6-phosphate. Requires a neutral salt, e.g. KCl, for maximum activity. Inositol 1-kinase Myoinositol kinase Inositol 3-kinase Myo-inositol 1-kinase ATP + myo-inositol = ADP + 1D-myo-inositol 3-phosphate. Scyllo-inosamine 4-kinase Also acts on streptamine, 2-deoxystreptamine and 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol. ATP + 1-amino-1-deoxy-scyllo-inositol = ADP + 1-amino-1-deoxy-scyllo-inositol 4-phosphate. Undecaprenol kinase Isoprenoid-alcohol kinase ATP + undecaprenol = ADP + undecaprenyl phosphate. PI kinase Phosphatidylinositol kinase PI4K-alpha Phosphatidylinositol 4-kinase Phosphatidylinositol kinase (phosphorylating) Type II phosphatidylinositol kinase PI4-kinase PtdIns-4-kinase 1-phosphatidylinositol 4-kinase ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate. PIP kinase Type I PIP kinase PtdIns(4)P-5-kinase Phosphatidylinositol 4-phosphate kinase Phosphatidylinositol-4-phosphate 5-kinase Diphosphoinositide kinase 1-phosphatidylinositol-4-phosphate 5-kinase http://purl.uniprot.org/mim/121850 The last of these reactions occurs in vivo and is physiologically relevant. ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate. This enzyme can also phosphorylate PtdIns3P in the 4-position, and PtdIns, PtdIns3P and PtdIns(3,4)P(2) in the 5-position in vitro, but to a lesser extent. PTS permease PEP--sugar phosphotransferase enzyme II Protein-N(pi)-phosphohistidine--sugar phosphotransferase Enzyme II of the phosphotransferase system Aldohexoses and their glycosides and alditols are phosphorylated on O-6; fructose and sorbose on O-1. Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate. The protein is phosphorylated in a reaction catalyzed by EC 2.7.3.9 and this acts as the phosphate donor for the above reaction. The enzyme translocates the sugar it phosphorylates into bacteria. Comprises a group of related enzymes. The protein substrate is a phosphocarrier protein of low molecular mass (9.5 kDa). Glycerone and disaccharides are also substrates. Mannokinase ATP + D-mannose = ADP + D-mannose 6-phosphate. Shikimate kinase ATP + shikimate = ADP + shikimate 3-phosphate. Streptomycin 6-phosphotransferase APH(6) Streptidine kinase Streptomycin 6-kinase Dihydrostreptomycin, streptidine and 2-deoxystreptidine can act as acceptors. dATP can replace ATP. ATP + streptomycin = ADP + streptomycin 6-phosphate. Inosine kinase Inosine-guanosine kinase ATP + inosine = ADP + IMP. Deoxycytidine kinase NTP + deoxycytidine = NDP + dCMP. Cytosine arabinoside can act as acceptor; all natural nucleoside triphosphates (except dCTP) can act as donors. Deoxyadenosine kinase Deoxyguanosine can also act as acceptor. Possibly identical with EC 2.7.1.74. ATP + deoxyadenosine = ADP + dAMP. Nucleoside phosphotransferase A nucleotide + a 2'-deoxynucleoside = a nucleoside + a 2'-deoxynucleoside 5'-phosphate. Nucleosides as well as 2'-deoxynucleosides can act as acceptors. Phenyl phosphate and nucleoside 3'-phosphates can act as donors, although not so well as nucleoside 5'-phosphates. Polynucleotide 5'-hydroxy-kinase ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA. Also acts on 5'-dephospho-RNA 3'-mononucleotides. Diphosphate--glycerol phosphotransferase Pyrophosphate--glycerol phosphotransferase Diphosphate + glycerol = phosphate + glycerol 1-phosphate. May be identical with EC 3.1.3.9. Glucosamine kinase ATP + D-glucosamine = ADP + D-glucosamine phosphate. Diphosphate--serine phosphotransferase Pyrophosphate--serine phosphotransferase Diphosphate + L-serine = phosphate + O-phospho-L-serine. Hydroxylysine kinase GTP + 5-hydroxy-L-lysine = GDP + 5-phosphonooxy-L-lysine. Both the natural 5-hydroxy-L-lysine and its 5-epimer act as acceptors. Ethanolamine kinase http://purl.uniprot.org/mim/227150 ATP + ethanolamine = ADP + O-phosphoethanolamine. Pseudouridine kinase ATP + pseudouridine = ADP + pseudouridine 5'-phosphate. Alkylglycerone kinase ATP + O-alkylglycerone = ADP + O-alkylglycerone phosphate. Beta-glucoside kinase GTP, CTP, ITP and UTP can also act as donors. Phosphorylates a number of beta-D-glucosides. ATP + cellobiose = ADP + 6-phospho-beta-D-glucosyl-(1,4)-D-glucose. NADH kinase ATP + NADH = ADP + NADPH. Specific for NADH. CTP, ITP, UTP and GTP can also act as phosphate donors (in decreasing order of activity). Activated by acetate. Streptomycin 3''-kinase Streptomycin 3''-phosphotransferase Also phosphorylates dihydrostreptomycin, 3'-deoxydihydrostreptomycin and their 6-phosphates. ATP + streptomycin = ADP + streptomycin 3''-phosphate. Dihydrostreptomycin-6-phosphate 3'-alpha-kinase 3'-deoxydihydrostreptomycin 6-phosphate can also act as acceptor. ATP + dihydrostreptomycin 6-phosphate = ADP + dihydrostreptomycin 3'-alpha,6-bisphosphate. Thiamine kinase ATP + thiamine = ADP + thiamine phosphate. 6-phosphofructokinase (diphosphate) Diphosphate--fructose-6-phosphate 1-phosphotransferase 6-phosphofructokinase (pyrophosphate) Diphosphate-dependent 6-phosphofructose-1-kinase Pyrophosphate--fructose 6-phosphate 1-phosphotransferase Pyrophosphate-dependent 6-phosphofructose-1-kinase Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate. Dihydrosphingosine kinase Sphinganine kinase ATP + sphinganine = ADP + sphinganine 1-phosphate. 5-keto-2-deoxygluconokinase 5-dehydro-2-deoxygluconokinase ATP + 5-dehydro-2-deoxy-D-gluconate = ADP + 6-phospho-5-dehydro-2-deoxy-D-gluconate. Alkylglycerol kinase ATP + 1-O-alkyl-sn-glycerol = ADP + 1-O-alkyl-sn-glycerol 3-phosphate. Monoacylglycerol kinase Acylglycerol kinase ATP + acylglycerol = ADP + acyl-sn-glycerol 3-phosphate. Acts on both 1-and 2-acylglycerols. Aminoglycoside 3'-phosphotransferase APH(3') Neomycin-kanamycin phosphotransferase Kanamycin kinase ATP + kanamycin = ADP + kanamycin 3'-phosphate. Also acts on the antibiotics neomycin, paromomycin, neamine, paromamine, vistamycin and gentamicin A. An enzyme from Pseudomonas aeruginosa also acts on butirosin. Protein-tyrosine kinases Receptor protein-tyrosine kinase Receptor protein tyrosine kinase ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. In the human genome, 58 receptor-type protein-tyrosine kinases have been identified and these are distributed into 20 subfamilies. The receptor protein-tyrosine kinases, which can be defined as having a transmembrane domain, are a large and diverse multigene family found only in metazoans. Non-specific protein-tyrosine kinase Cytoplasmic protein tyrosine kinase Unlike EC 2.7.10.1, this protein-tyrosine kinase does not have a transmembrane domain. ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. In the human genome, 32 non-specific protein-tyrosine kinases have been identified and these can be divided into 10 families. Protein-serine/threonine kinases Serine kinase Protein-serine kinase Protein phosphokinase Protein serine kinase Serine(threonine) protein kinase Serine/threonine protein kinase Threonine-specific protein kinase Serine-specific protein kinase Protein serine-threonine kinase Serine protein kinase Non-specific serine/threonine protein kinase This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. ATP + a protein = ADP + a phosphoprotein. IKK-1 CHUK IKK-2 IKBKB I-kappa-B kinase TBK1 TANK-binding kinase 1 IKBKA IKK Inhibitor of NF-kappa-B kinase If the serine residues are replaced by threonine residues, the activity of the enzyme is decreased considerably. Phosphorylates I-kappa-B proteins at specific serine residues, which marks them for destruction via the ubiquitination pathway. Subsequent degradation of the I-kappa-B complex (IKK) activates NF-kappa-B, a translation factor that plays an important role in inflammation, immunity, cell proliferation and apoptosis. ATP + [I-kappa-B protein] = ADP + [I-kappa-B phosphoprotein]. cAMP-dependent protein kinase Protein kinase A PKA PKA C The inactive holoenzyme of cAMP-dependent protein kinase is a tetramer composed of two regulatory (R) and two catalytic (C) subunits. cAMP is required to activate this enzyme. ATP + a protein = ADP + a phosphoprotein. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP molecules and two free monomeric catalytic subunits (i.e. R(2)C(2) + 4 cAMP = R(2)(cAMP)(4) + 2 C). PKG 1-beta cGMP-dependent protein kinase I-beta Guanosine 3':5'-cyclic monophosphate-dependent protein kinase cGMP-dependent protein kinase 3':5'-cyclic GMP-dependent protein kinase PKG II PKG 1-alpha PKG Binding of cGMP causes a conformational change that is associated with activation of the kinase. ATP + a protein = ADP + a phosphoprotein. The enzyme occurs as a dimer in higher eukaryotes. The enzyme also has two allosteric cGMP-binding sites (sites A and B). cGMP is required to activate this enzyme. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyzes the phosphorylation by ATP to specific serine or threonine residues in protein substrates. Protein kinase C PKC Calcium-dependent protein kinase C Calcium-independent protein kinase C NPKC Calcium/phospholipid dependent protein kinase CPKC They can be activated by calcium but have a requirement for the second messenger diacylglycerol. A family of serine-and threonine-specific protein kinases that depend on lipids for activity. http://purl.uniprot.org/mim/605361 Members of the protein kinase C family also serve as major receptors for phorbol esters, a class of tumor promoters. ATP + a protein = ADP + a phosphoprotein. Members of this group of enzymes phosphorylate a wide variety of protein targets and are known to be involved in diverse cell-signaling pathways. Rhodopsin kinase (phosphorylating) GPCR kinase 1 Cone opsin kinase RK Rhodopsin kinase Opsin kinase G-protein-coupled receptor kinase 1 Opsin kinase (phosphorylating) http://purl.uniprot.org/mim/258100 Acts on the bleached or activated form of rhodopsin. ATP + [rhodopsin] = ADP + [rhodopsin] phosphate. Does not act on casein, histones or phosphovitin. http://purl.uniprot.org/mim/268000 Also phosphorylates the beta-adrenergic receptor, but more slowly. Inhibited by Zn(2+) and digitonin (cf. EC 2.7.11.15 and EC 2.7.11.16). Beta-adrenoceptor kinase ADRBK1 BARK1 Beta-AR kinase Beta-ARK Beta-receptor kinase Adrenergic receptor kinase Beta-adrenergic-receptor kinase Beta(2)ARK Beta-adrenergic-receptor kinase (phosphorylating) [Beta-adrenergic-receptor] kinase Beta-adrenergic receptor-specific kinase Inhibited by Zn(2+) and digitonin but is unaffected by cyclic-AMP (cf. EC 2.7.11.14 and EC 2.7.11.16). Does not act on casein or histones. Acts on the agonist-occupied form of the receptor; also phosphorylates rhodopsin, but more slowly. ATP + [beta-adrenergic receptor] = ADP + [beta-adrenergic receptor] phosphate. GPCR kinase [G-protein-coupled receptor] kinase GPCRK G protein-coupled receptor kinase (cf. EC 2.7.11.14 and EC 2.7.11.15). ATP + [G-protein-coupled receptor] = ADP + [G-protein-coupled receptor] phosphate. All members of this enzyme subfamily possess a highly conserved binding site for 1-phosphatidylinositol 4,5-bisphosphate. Ca(2+)/calmodulin-dependent protein kinase kinase CaM kinase II CaMKII CaMKI Microtubule-associated protein 2 kinase Calcium/calmodulin-dependent protein kinase CaM-regulated serine/threonine kinase Caldesmon kinase (phosphorylating) CAM PKII Calcium/calmodulin-dependent protein kinase type II Ca(2+)/calmodulin-dependent protein kinase kinase beta CaMKK-alpha CaMKK-beta Calmodulin-dependent kinase II CaMKIV Ca(2+)/calmodulin-dependent protein kinase II Ca(2+)/calmodulin-dependent microtubule-associated protein 2 kinase CaM kinase Ca(2+)/calmodulin-dependent protein kinase IV Caldesmon kinase Ca(2+)/calmodulin-dependent protein kinase 1 A wide range of proteins can act as acceptor, including vimentin, synapsin, glycogen synthase, myosin light-chains and the microtubule-associated tau protein. Calcium Not identical with EC EC 2.7.11.18 or EC 2.7.11.26. Requires calmodulin. ATP + a protein = ADP + a phosphoprotein. Myosin light-chain kinase (phosphorylating) MLCkase Myosin light chain protein kinase Myosin kinase Myosin light chain kinase [Myosin light-chain] kinase [Myosin-light-chain] kinase Myosin light-chain kinase MLCK Smooth-muscle-myosin-light-chain kinase Calcium/calmodulin-dependent myosin light chain kinase Requires calmodulin for activity. The 20 kDa light chain from smooth muscle myosin is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors, more slowly. ATP + [myosin light-chain] = ADP + [myosin light-chain] phosphate. Calcium http://purl.uniprot.org/mim/192600 Glycogen phosphorylase kinase Phosphorylase kinase Phosphorylase B kinase PHK Dephosphophosphorylase kinase Phosphorylase b kinase Phosphorylase kinase (phosphorylating) For muscle phosphorylase but not liver phosphorylase, this is accompanied by a further dimerization to form a tetrameric phosphorylase. The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b. http://purl.uniprot.org/mim/306000 http://purl.uniprot.org/mim/172471 The enzyme couples muscle contraction with energy production via glycogenolysis--glycolysis by catalyzing the Ca(2+)-dependent phosphorylation and activation of glycogen phosphorylase b. 2 ATP + phosphorylase b = 2 ADP + phosphorylase a. Calcium Requires calmodulin for activity. The gamma subunit of the tetrameric alpha-beta-gamma-delta enzyme is the catalytic subunit. PDK Pyruvate dehydrogenase kinase [Pyruvate dehydrogenase (acetyl-transferring)] kinase PDH kinase PDHK Pyruvate dehydrogenase kinase (phosphorylating) Has no activating compound but is specific for its substrate. ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate. A mitochondrial enzyme associated with the pyruvate dehydrogenase complex in mammals. Phosphorylation inactivates EC 1.2.4.1. EEF2K EF2K CaM kinase III Ca/CaM-kinase III EEF2 kinase Calmodulin-dependent protein kinase III [Elongation factor 2] kinase ATP + [elongation factor 2] = ADP + [elongation factor 2] phosphate. Calcium Elongation factor 2 is phosphorylated in several cell types in response to various growth factors, hormones and other stimuli that raise intracellular Ca(2+). Can also be phosphorylated by the catalytic subunit of EC 2.7.11.11. Requires calmodulin for activity. Polo-like kinase Polo serine-threonine kinase Polo kinase PLK The enzyme associates with the spindle pole during mitosis and is thought to play an important role in the dynamic function of the mitotic spindle during chromosome segregation. ATP + a protein = ADP + a phosphoprotein. The human form of the enzyme, Plk1, does not phosphorylate histone H1, enolase and phosvitin but it can phosphorylate myelin basic protein and microtubule-associated protein MAP-2, although to a lesser extent than casein. Cdc2 kinase Cyclin-dependent kinase Cdk-activating kinase Cdk-activating protein kinase Activation of cyclin-dependent kinases requires association of the enzyme with a regulatory subunit referred to as a cyclin. ATP + a protein = ADP + a phosphoprotein. http://purl.uniprot.org/mim/312750 It is the sequential activation and inactivation of cyclin-dependent kinases, through the periodic synthesis and destruction of cyclins, that provides the primary means of cell-cycle regulation. http://purl.uniprot.org/mim/308350 CTD kinase [RNA-polymerase]-subunit kinase ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate. Does not phosphorylate casein, phosvitin or histone. Appears to be distinct from other protein phosphokinases. Brings about multiple phosphorylation of the unique C-terminal repeat domain of the largest subunit of eukaryotic EC 2.7.7.6. Mitogen-activated protein kinase ERK Microtubule-associated protein kinase MBP kinase II Microtubule-associated protein 2 kinase MBP kinase I Extracellular signal-regulated kinase JNK C-Jun N-terminal kinase Myelin basic protein kinase MAPK SAPK MAP kinase Stress-activated protein kinase Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline. Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2 is necessary for enzyme activation. Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. ATP + a protein = ADP + a phosphoprotein. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumor necrosis factor (TNF) family and envirionmental stresses such as osmotic shock, ionizing radiation and ischemeic injury. A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY). MAP3K MEK kinase MEKK MLTK MLK-like mitogen-activated protein triple kinase MAP kinase kinase kinase MAPKKK Mitogen-activated protein kinase kinase kinase This enzyme phosphorylates and activates its downstream protein kinase, EC 2.7.12.2, but requires MAPKKKK for activation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumor necrosis factor (TNF) family and envirionmental stresses such as osmotic shock, ionizing radiation and ischemeic injury. While c-Raf and c-Mos activate the classical MAPK/ERK pathway, MEKK1 and MEKK2 preferentially activate the c-Jun N-terminal protein kinase(JNK)/stress-activated protein kinase (SAPK) pathway. Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Some members of this family can be activated by p21-activated kinases (PAK/STE20) or Ras. ATP + a protein = ADP + a phosphoprotein. GSK Protein tau kinase TTK [Tau-protein] kinase Glycogen synthase kinase-3-beta Tau-tubulin kinase [Tau protein] kinase TPK Tau kinase ATP + [tau protein] = ADP + [tau protein] phosphate. Involved in the formation of paired helical filaments, which are the main fibrous component of all fibrillary lesions in brain and are associated with Alzheimer's disease. Activated by tubulin. [Acetyl-CoA carboxylase] kinase Acetyl-CoA carboxylase bound kinase Acetyl-coenzyme A carboxylase kinase AMPK I-peptide kinase Acetyl-CoA carboxylase kinase Acetyl-CoA carboxylase kinase (AMP-activated) Acetyl-CoA carboxylase kinase (cAMP-independent) Acetyl coenzyme A carboxylase kinase (phosphorylating) ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate. More active toward the dimeric form of acetyl-CoA carboxylase than the polymeric form. Phosphorylates and inactivates EC 6.4.1.2, which can be dephosphorylated and reactivated by EC 3.1.3.17. Phosphorylates serine residues. Tropomyosin kinase (phosphorylating) Tropomyosin kinase Phosphorylates casein equally well, and histone and phosvitin to a lesser extent. ATP + [tropomyosin] = ADP + [tropomyosin] phosphate. Low-density-lipoprotein kinase [Low-density-lipoprotein-receptor] kinase Low-density-lipoprotein receptor kinase (phosphorylating) LDL receptor kinase Low-density lipoprotein receptor kinase ATP + [low-density-lipoprotein receptor] = ADP + [low-density-lipoprotein receptor] phosphate. Casein can also act as a substrate but with lower affinity. Phosphorylates the last serine residue (Ser-833) in the cytoplasmic domain of the low-density lipoprotein receptor. GTP can act instead of ATP. Reductase kinase Dephospho-[reductase kinase] kinase Reductase kinase kinase AMP-activated protein kinase kinase Hydroxymethylglutaryl coenzyme A reductase kinase kinase AMP-activated kinase ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase] = ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]. Activated by AMP and is specific for its substrate. Phosphorylates and activates EC 2.7.11.31 which has been inactivated by EC 3.1.3.16. Activin receptor kinase Receptor type I serine/threonine protein kinase Receptor protein serine/threonine kinase Receptor serine/threonine protein kinase TGF-beta kinase Receptor type II serine/threonine protein kinase ATP + [receptor-protein] = ADP + [receptor-protein] phosphate. Signaling occurs by the binding of ligand to the type II receptor, which is the constitutively active kinase. The transforming growth factor beta (TGF-beta) family of cytokines regulates cell proliferation, differentiation, recognition and death. Bound TGF-beta is then recognized by receptor I, which is phosphorylated and can propagate the signal to downstream substrates. Reductase kinase [Hydroxymethylglutaryl-CoA reductase (NADPH(2))] kinase Hydroxymethylglutaryl-CoA reductase kinase [Hydroxymethylglutaryl-CoA reductase (NADPH)] kinase Hydroxymethylglutaryl coenzyme A reductase kinase (phosphorylating) AMPK HMG-CoA reductase kinase AMP-activated protein kinase 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase 3-hydroxy-3-methylglutaryl-CoA reductase kinase Beta-hydroxy-beta-methylglutaryl-CoA reductase kinase Hydroxymethylglutaryl coenzyme A reductase kinase Can also phosphorylate EC 6.4.1.2 and EC 3.1.1.79. EC 1.1.1.34 is inactivated by the phosphorylation of the enzyme protein. Activated by AMP. GTP can act instead of ATP. Thr-172 within the catalytic subunit (alpha-subunit) is the major site phosphorylated by the AMP-activated protein kinase kinase. Histones can also act as acceptors. ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate. Branched-chain 2-oxo acid dehydrogenase kinase [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase Branched-chain keto acid dehydrogenase kinase BCK BCKD kinase Branched-chain oxo acid dehydrogenase kinase (phosphorylating) Branched-chain alpha-ketoacid dehydrogenase kinase BCODH kinase ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] = ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate. Has no activating compound but is specific for its substrate. A mitochondrial enzyme associated with the branched-chain 2-oxoacid dehydrogenase complex. Phosphorylation inactivates EC 1.2.4.4. IDH kinase/phosphatase Isocitrate dehydrogenase kinase IDH-K/P Isocitrate dehydrogenase kinase (phosphorylating) IDH kinase ICDH kinase/phosphatase Isocitrate dehydrogenase kinase/phosphatase [Isocitrate dehydrogenase (NADP(+))] kinase IDHK/P Has no activating compound but is specific for its substrate. Phosphorylates and inactivates EC 1.1.1.42. ATP + [isocitrate dehydrogenase (NADP(+))] = ADP + [isocitrate dehydrogenase (NADP(+))] phosphate. [Tyrosine 3-monooxygenase] kinase Pheochromocytoma tyrosine hydroxylase-associated kinase Tyrosine 3-monooxygenase kinase (phosphorylating) Activates EC 1.14.16.2 by phosphorylation. ATP + [tyrosine-3-monooxygenase] = ADP + [tyrosine-3-monooxygenase] phosphate. Has no activating compound but is specific for its substrate, with which it copurifies. Magnesium Calmodulin-dependent myosin heavy chain kinase [Myosin heavy-chain] kinase Myosin II heavy-chain kinase Myosin I heavy-chain kinase MHCK Myosin heavy chain kinase A MIHC kinase Myosin heavy-chain kinase Myosin heavy chain kinase ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate. The enzyme from Dictyostelium sp. (slime molds) brings about phosphorylation of the heavy chains of Dictyostelium myosin, inhibiting the actin-activated ATPase activity of the myosin. One threonine residue in each heavy chain acts as acceptor. While the enzyme from some species is activated by actin, in other cases Ca(2+)/calmodulin are required for activity. Fas-activated serine/threonine kinase FASTK FAST Phosphorylation of TIA-1 precedes the onset of DNA fragmentation. ATP + [Fas-activated serine/threonine protein] = ADP + [Fas-activated serine/threonine phosphoprotein]. This enzyme is activated during Fas-mediated apoptosis. Following Fas ligation, the enzyme, which is constitutively phosphorylated, is dephosphorylated, and it is the dephosphorylated form that causes phosphorylation of TIA-1, a nuclear RNA-binding protein. Goodpasture antigen-binding protein kinase [Goodpasture-antigen-binding protein] kinase GPBPK GPBP kinase ATP + [Goodpasture antigen-binding protein] = ADP + [Goodpasture antigen-binding phosphoprotein]. This serine/threonine kinase specifically binds to and phosphorylates the N-terminal region of the human Goodpasture antigen, which is located on the alpha(3) chain of collagen IV and is involved in autoimmune disease. Dual-specificity kinases (those acting on Ser/Thr and Tyr residues) Dual-specificity kinase This family of enzymes can phosphorylate both Ser/Thr and Tyr residues. ATP + a protein = ADP + a phosphoprotein. Mitogen-activated protein kinase kinase MAP kinase kinase MEK MAPKK MAP2K MKK It is required for activation of EC 2.7.11.24. Phosphorylation of MEK1 by Raf involves phosphorylation of two serine residues. Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumor necrosis factor (TNF) family and envirionmental stresses such as osmotic shock, ionizing radiation and ischemeic injury. A dual-specific protein kinase and requires mitogen-activated protein kinase kinase kinase (MAPKKK) for activation. ATP + a protein = ADP + a phosphoprotein. Protein-histidine kinases Protein histidine kinase Protein-histidine pros-kinase HK2 Protein kinase (histidine) Histidine protein kinase Histidine kinase ATP + protein L-histidine = ADP + protein N(pi)-phospho-L-histidine. A number of histones can act as acceptor. Protein kinase (histidine) Protein-histidine tele-kinase Histidine kinase Histidine protein kinase Protein histidine kinase HK3 A number of histones can act as acceptor. ATP + protein L-histidine = ADP + protein N(tau)-phospho-L-histidine. Protein histidine kinase Histidine protein kinase Histidine kinase Protein kinase (histidine) Protein kinase HK1 This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros-or tele-nitrogen of histidine). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. A number of histones can act as acceptor. Phosphotransferases with a carboxyl group as acceptor AK Acetate kinase (phosphorylating) Acetic kinase Acetate kinase Acetokinase Both this enzyme and EC 2.7.2.15 play important roles in the production of propanoate. (2) ATP + propanoate = ADP + propanoyl phosphate. Magnesium Acetate can be converted into the key metabolic intermediate acetyl-CoA by coupling acetate kinase with EC 2.3.1.8. (1) ATP + acetate = ADP + acetyl phosphate. While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly. Phosphoglycerate kinase (GTP) GTP + 3-phospho-D-glycerate = GDP + 3-phospho-D-glyceroyl phosphate. Glutamate 5-kinase Gamma-glutamyl kinase The product rapidly cyclizes to 5-oxoproline and phosphate. http://purl.uniprot.org/mim/138250 ATP + L-glutamate = ADP + L-glutamate 5-phosphate. Acetate kinase (pyrophosphate) Acetate kinase (diphosphate) Diphosphate + acetate = phosphate + acetyl phosphate. Glutamate 1-kinase ATP + L-glutamate = ADP + alpha-L-glutamyl phosphate. Branched-chain-fatty-acid kinase Isobutyrate kinase 3-methylbutanoate, 2-methylbutanoate, pentanoate, butanoate, and propanoate can also act as acceptors (cf. EC 2.7.2.7). ATP + 2-methylpropanoate = ADP + 2-methylpropanoyl phosphate. Propionate kinase Propionate/acetate kinase Both propanoate and acetate can act as a substrate. Both this enzyme and EC 2.7.2.1 play important roles in the production of propanoate. (1) ATP + propanoate = ADP + propanoyl phosphate. Magnesium (2) ATP + acetate = ADP + acetyl phosphate. Involved in the anaerobic degradation of L-threonine in bacteria. Carbamate kinase ATP + NH(3) + CO(2) = ADP + carbamoyl phosphate. Phosphoglycerate kinase http://purl.uniprot.org/mim/311800 ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. Aspartokinase Aspartate kinase ATP + L-aspartate = ADP + 4-phospho-L-aspartate. The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 1.1.1.3. Formate kinase ATP + formate = ADP + formyl phosphate. Butyrate kinase The enzyme from Clostridium sp. also acts, more slowly on pentanoate and propanoate, and on some branched-chain fatty acids (cf. EC 2.7.1.14). ATP + butanoate = ADP + butanoyl phosphate. Acetylglutamate kinase ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate. Phosphotransferases with a nitrogenous group as acceptor Guanidinoacetate kinase Glycocyamine kinase ATP + guanidinoacetate = ADP + phosphoguanidinoacetate. Phosphagen phosphokinase Agmatine kinase ATP + agmatine = ADP + N(4)-phosphoagmatine. L-arginine can act as acceptor, more slowly. Creatine kinase ATP + creatine = ADP + phosphocreatine. N-ethylglycocyamine can also act as acceptor. Arginine kinase Arginine phosphokinase ATP + L-arginine = ADP + N(omega)-phospho-L-arginine. Taurocyamine kinase ATP + taurocyamine = ADP + N-phosphotaurocyamine. Lombricine kinase Also acts on methylated lombricines such as thalassemine; the specificity varies with the source species. ATP + lombricine = ADP + N-phospholombricine. Hypotaurocyamine kinase ATP + hypotaurocyamine = ADP + N(omega)-phosphohypotaurocyamine. Also acts, more slowly, on taurocyamine. Opheline kinase Has a little activity on taurocyamine, lombricine and phosphotaurocyamine. ATP + guanidinoethyl methyl phosphate = ADP + N'-phosphoguanidinoethyl methylphosphate. Ammonia kinase In the reverse direction, N-phosphoglycine and N-phosphohistidine can also act as phosphate donors, and ADP, dADP, GDP, CDP, dTDP, dCDP, IDP and UDP can act as phosphate acceptors (in decreasing order of activity). ATP + NH(3) = ADP + phosphoramide. Has a wide specificity. Phosphoenolpyruvate sugar phosphotransferase enzyme I Phosphoenolpyruvate--protein phosphatase Sugar--PEP phosphotransferase enzyme I Phosphopyruvate--protein factor phosphotransferase Phosphopyruvate--protein phosphotransferase Phosphoenolpyruvate--protein phosphotransferase Enzyme I of the phosphotransferase system Acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport. Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine. A similar reaction where the protein is the enzyme EC 2.7.9.2 is part of the mechanism of that enzyme. Phosphotransferases with a phosphate group as acceptor Polyphosphoric acid kinase Polyphosphate kinase ATP-polyphosphate phosphotransferase ATP + (phosphate)(n) = ADP + (phosphate)(n+1). Nucleoside-triphosphate--adenylate kinase Many nucleoside triphosphates can act as donors. NTP + AMP = NDP + ADP. (Deoxy)adenylate kinase ATP + dAMP = ADP + dADP. AMP can also act as acceptor. T(2)-induced deoxynucleotide kinase dTMP and dAMP can act as acceptors. dATP can act as donor. ATP + dGMP (or dTMP) = ADP + dGDP (or dTDP). (Deoxy)nucleoside-phosphate kinase ATP + deoxynucleoside phosphate = ADP + deoxynucleoside diphosphate. dATP can substitute for ATP. CMP kinase Deoxycytidine kinase Cytidine monophosphate kinase Cytidylate kinase dCMP kinase Deoxycytidylate kinase ATP + (d)CMP = ADP + (d)CDP. UMP and dCMP can also act as acceptors. Thiamine-diphosphate kinase ATP + thiamine diphosphate = ADP + thiamine triphosphate. Thiamine-phosphate kinase Thiamine-monophosphate kinase ATP + thiamine phosphate = ADP + thiamine diphosphate. 3-phosphoglyceroyl-phosphate--polyphosphate phosphotransferase 3-phospho-D-glyceroyl phosphate + (phosphate)(n) = 3-phosphoglycerate + (phosphate)(n+1). Farnesyl-diphosphate kinase ADP can also act as donor. ATP + farnesyl diphosphate = ADP + farnesyl triphosphate. 5-methyldeoxycytidine-5'-phosphate kinase The enzyme, from phage XP-12-infected Xanthomonas oryzae, converts m(5)dCMP into m(5)dCDP and then into m(5)dCTP. ATP + 5-methyldeoxycytidine 5'-phosphate = ADP + 5-methyldeoxycytidine diphosphate. Phosphomevalonate kinase ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate. Dolichyl-diphosphate--polyphosphate phosphotransferase Dolichyl diphosphate + (phosphate)(n) = dolichyl phosphate + (phosphate)(n+1). ATP:1D-myo-inositol-hexakisphosphate phosphotransferase Inositol-hexakisphosphate kinase (1) ATP + 1D-myo-inositol hexakisphosphate = ADP + 5-diphospho-1D-myo-inositol (1,2,3,4,6)pentakisphosphate. Three mammalian isoforms are known to exist. (2) ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP + diphospho-1D-myo-inositol tetrakisphosphate (isomeric configuration unknown). UMP-kinase UMP kinase Uridine monophosphate kinase UMPK Uridylate kinase Strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme EC 2.7.4.14 for the same purpose. ATP + UMP = ADP + UDP. Subject of feedback regulation, being inhibited by UTP and activated by GTP. Ribose 1,5-bisphosphokinase Ribose 1,5-bisphosphate phosphokinase This enzyme, found in NAD suppression mutants of Escherichia coli, synthesizes 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) without the participation of EC 2.7.6.1. ATP + ribose 1,5-bisphosphate = ADP + 5-phospho-alpha-D-ribose 1-diphosphate. Ribose, ribose 1-phosphate and ribose 5-phosphate are not substrates, and GTP cannot act as a phosphate donor. Myokinase Adenylokinase Adenylic kinase Adenylate kinase ATP + AMP = 2 ADP. http://purl.uniprot.org/mim/103000 Inorganic triphosphate can also act as donor. Nucleoside-phosphate kinase NMP-kinase Other nucleoside triphosphates can act instead of ATP. Many nucleotides can act as acceptors. ATP + nucleoside phosphate = ADP + nucleoside diphosphate. Nucleoside-diphosphate kinase NDK Nucleoside diphosphokinase Nucleoside 5'-diphosphate phosphotransferase Many nucleoside diphosphates can act as acceptors. Many ribo-and deoxyribonucleoside triphosphates can act as donors. ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. Phosphomethylpyrimidine kinase Hydroxymethylpyrimidine phosphokinase ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine. Guanosine monophosphate kinase Deoxyguanylate kinase GMP kinase Guanylate kinase ATP + GMP = ADP + GDP. dGMP can also act as acceptor. dATP can act as donor. Thymidylate kinase Thymidylic acid kinase dTMP kinase TMPK ATP + dTMP = ADP + dTDP. Diphosphotransferases Ribose-phosphate diphosphokinase Phosphoribosyl pyrophosphate synthetase Phosphoribosyl diphosphate synthetase Ribose-phosphate pyrophosphokinase dATP can also act as donor. ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. http://purl.uniprot.org/mim/311850 Thiamine diphosphokinase Thiamine kinase Thiamine pyrophosphokinase ATP + thiamine = AMP + thiamine diphosphate. 7,8-dihydro-6-hydroxymethylpterin diphosphokinase 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase 6-hydroxymethyl-7,8-dihydropterin diphosphokinase 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine = AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate. Nucleotide pyrophosphokinase Nucleotide diphosphokinase Acts on the 5'-mono-, di-and triphosphate derivatives of purine nucleosides. ATP + nucleoside 5'-phosphate = AMP + 5'-phosphonucleoside 3'-diphosphate. GTP pyrophosphokinase GTP diphosphokinase ppGpp synthetase I Guanosine 3',5'-polyphosphate synthase Stringent factor GDP can also act as acceptor. ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate. Nucleotidyltransferases Adenosine triphosphate-nicotinamide mononucleotide transadenylase NMN adenylyltransferase NAD(+) diphosphorylase Nicotinamide adenine dinucleotide pyrophosphorylase Nicotinamide mononucleotide adenylyltransferase Nicotinamide-nucleotide adenylyltransferase NAD(+) pyrophosphorylase NMNAT Diphosphopyridine nucleotide pyrophosphorylase ATP + nicotinamide ribonucleotide = diphosphate + NAD(+). Nicotinate nucleotide can also act as acceptor. See also EC 2.7.7.18. UTP--hexose-1-phosphate uridylyltransferase Galactose-1-phosphate uridylyltransferase Gal-1-P uridylyltransferase UTP + alpha-D-galactose 1-phosphate = diphosphate + UDP-galactose. Alpha-D-glucose 1-phosphate can also act as acceptor, more slowly. Xylose-1-phosphate uridylyltransferase UTP--xylose-1-phosphate uridylyltransferase UTP + alpha-D-xylose 1-phosphate = diphosphate + UDP-D-xylose. Uridyl transferase Uridylyl removing enzyme Hexose-1-phosphate uridylyltransferase UDP-glucose--hexose-1-phosphate uridylyltransferase Gal-1-P uridylyltransferase Galactose-1-phosphate uridylyltransferase UDP-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-galactose. http://purl.uniprot.org/mim/230400 Mannose-1-phosphate guanylyltransferase GTP-mannose-1-phosphate guanylyltransferase GDP-mannose pyrophosphorylase The bacterial enzyme can also use ITP and dGTP as donors. GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose. CTP:phosphoethanolamine cytidylyltransferase Ethanolamine-phosphate cytidylyltransferase Phosphorylethanolamine transferase CTP + ethanolamine phosphate = diphosphate + CDP-ethanolamine. CTP:phosphocholine cytidylyltransferase Phosphorylcholine transferase Choline-phosphate cytidylyltransferase CTP + choline phosphate = diphosphate + CDP-choline. Deamido-NAD(+) pyrophosphorylase Nicotinate-nucleotide adenylyltransferase Deamido-NAD(+) diphosphorylase ATP + nicotinate ribonucleotide = diphosphate + deamido-NAD(+). Poly(A) polymerase NTP polymerase Polynucleotide adenylyltransferase RNA adenylating enzyme Catalyzes template-independent extension of the 3'-end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. ATP + RNA(n) = diphosphate + RNA(n+1). See also EC 2.7.7.6. The primer, depending on the source of the enzyme, may be an RNA or DNA fragment or oligo(A) bearing a 3'-OH terminal group. Also acts slowly with CTP. FAD diphosphorylase FMN adenylyltransferase FAD pyrophosphorylase FAD synthetase Flavin adenine dinucleotide synthetase ATP + FMN = diphosphate + FAD. tRNA CCA-pyrophosphorylase tRNA CCA-diphosphorylase tRNA cytidylyltransferase May be identical with EC 2.7.7.25. CTP + tRNA(n) = diphosphate + tRNA(n+1). GDP-mannose pyrophosphorylase Mannose-1-phosphate guanylyltransferase (GDP) GDP-mannose phosphorylase GDP + alpha-D-mannose 1-phosphate = phosphate + GDP-mannose. N-acetylglucosamine-1-phosphate uridyltransferase UDP-N-acetylglucosamine pyrophosphorylase UDP-N-acetylglucosamine diphosphorylase UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-D-glucosamine. The enzyme from several bacteria has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157. dTDP-glucose diphosphorylase Glucose-1-phosphate thymidylyltransferase dTDP-glucose pyrophosphorylase dTDP-glucose synthase dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-glucose. CCA-adding enzyme tRNA CCA-pyrophosphorylase tRNA CCA-diphosphorylase tRNA-nucleotidyltransferase tRNA adenylyltransferase ATP + tRNA(n) = diphosphate + tRNA(n+1). May be identical with EC 2.7.7.21. ADP-glucose synthase ADP-glucose diphosphorylase ADP-glucose pyrophosphorylase Glucose-1-phosphate adenylyltransferase ATP + alpha-D-glucose 1-phosphate = diphosphate + ADP-glucose. Nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase Hexose nucleotidylating enzyme NDP-hexose diphosphorylase NTP:hexose-1-phosphate nucleotidyltransferase NDP-hexose pyrophosphorylase GDP hexose pyrophosphorylase Guanosine diphosphohexose pyrophosphorylase Nucleoside diphosphohexose pyrophosphorylase Hexose 1-phosphate nucleotidyltransferase Hexose-1-phosphate guanylyltransferase GTP:alpha-D-hexose-1-phosphate guanylyltransferase Nucleoside-triphosphate-aldose-1-phosphate nucleotidyltransferase In decreasing order of activity, guanosine, inosine and adenosine diphosphate hexoses are substrates in the reverse reaction, with either glucose or mannose as the sugar. Nucleoside triphosphate + alpha-D-aldose 1-phosphate = diphosphate + NDP-hexose. 3'-dephospho-CoA pyrophosphorylase Pantetheine-phosphate adenylyltransferase Dephospho-CoA diphosphorylase PPAT Dephospho-coenzyme A pyrophosphorylase Dephospho-CoA pyrophosphorylase Phosphopantetheine adenylyltransferase The enzyme from several bacteria (e.g. Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157. ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA. Fucose-1-phosphate guanylyltransferase GDP-fucose pyrophosphorylase GDP-fucose diphosphorylase GTP + beta-L-fucose 1-phosphate = diphosphate + GDP-L-fucose. Terminal transferase Terminal deoxynucleotidyltransferase DNA nucleotidylexotransferase Terminal deoxyribonucleotidyltransferase Terminal addition enzyme Cannot initiate a chain de novo. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Catalyzes template-independent extension of the 3'-end of a DNA strand by one nucleotide at a time. Nucleoside may be ribo-or deoxyribo-. dTDP-galactose pyrophosphorylase dTDP-galactose diphosphorylase Galactose-1-phosphate thymidylyltransferase dTTP + alpha-D-galactose 1-phosphate = diphosphate + dTDP-galactose. CDP-glucose diphosphorylase CDP-glucose pyrophosphorylase Glucose-1-phosphate cytidylyltransferase CTP + alpha-D-glucose 1-phosphate = diphosphate + CDP-glucose. Glucose-1-phosphate guanylyltransferase GDP-glucose pyrophosphorylase GDP-glucose diphosphorylase Also acts, more slowly, on D-mannose 1-phosphate. GTP + alpha-D-glucose 1-phosphate = diphosphate + GDP-glucose. ADP-ribose phosphorylase Ribose-5-phosphate adenylyltransferase ADP + D-ribose 5-phosphate = phosphate + ADP-ribose. Sugar-1-phosphate adenylyltransferase Aldose-1-phosphate adenylyltransferase ADP-sugar phosphorylase ADP-aldose phosphorylase ADP + alpha-D-aldose 1-phosphate = phosphate + ADP-aldose. NDP-sugar phosphorylase Aldose-1-phosphate nucleotidyltransferase NDP-aldose phosphorylase Sugar-1-phosphate nucleotidyltransferase NDP + alpha-D-aldose 1-phosphate = phosphate + NDP-aldose. The enzyme works on a variety of alpha-D-aldose 1-phosphates and beta-L-aldose 1-phosphates (which have the same anomeric configuration as the former). 3-deoxy-manno-octulosonate cytidylyltransferase CMP-2-keto-3-deoxyoctulosonic acid synthetase CMP-3-deoxy-D-manno-octulosonate pyrophosphorylase CMP-3-deoxy-D-manno-octulosonate diphosphorylase CMP-KDO synthetase CTP + 3-deoxy-D-manno-octulosonate = diphosphate + CMP-3-deoxy-D-manno-octulosonate. CDP-glycerol pyrophosphorylase Glycerol-3-phosphate cytidylyltransferase CDP-glycerol diphosphorylase CTP + sn-glycerol 3-phosphate = diphosphate + CDP-glycerol. Sulfate adenylyltransferase ATP-sulfurylase Sulfate adenylate transferase Sulfurylase This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25. The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP. http://purl.uniprot.org/mim/603005 ATP + sulfate = diphosphate + adenylyl sulfate. CDP-ribitol diphosphorylase D-ribitol-5-phosphate cytidylyltransferase CDP-ribitol pyrophosphorylase CTP + D-ribitol 5-phosphate = diphosphate + CDP-ribitol. CDP-diglyceride synthetase CDP-diglyceride diphosphorylase Phosphatidate cytidylyltransferase CDP-diglyceride pyrophosphorylase CDP-diacylglycerol synthase CTP + phosphatidate = diphosphate + CDP-diacylglycerol. Glutamate-ammonia-ligase adenylyltransferase Glutamine-synthetase adenylyltransferase [Glutamate--ammonia-ligase] adenylyltransferase ATP + [L-glutamate:ammonia ligase (ADP-forming)] = diphosphate + adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]. N-acylneuraminate cytidylyltransferase CMP-NeuNAc synthetase CMP-N-acetylneuraminic acid synthetase CMP-sialate pyrophosphorylase CMP-sialate diphosphorylase CMP-sialate synthase CMP-sialic acid synthetase Acts on N-acetyl-and N-glycolyl-derivatives. CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate. Glucuronate-1-phosphate uridylyltransferase UTP + 1-phospho-alpha-D-glucuronate = diphosphate + UDP-glucuronate. Also acts slowly with CTP. Guanosine-triphosphate guanylyltransferase 2 GTP = diphosphate + P(1),P(4)-bis(5'-guanosyl) tetraphosphate. Also acts, more slowly, on GDP to form P(1),P(3)-bis(5'-guanosyl) triphosphate. Gentamicin 2''-nucleotidyltransferase 2''-aminoglycoside nucleotidyltransferase The nucleotidyl residue is transferred to the 2-hydroxy group of the 3-amino-3-deoxy-D-glucose moiety in the antibiotic. Kanamycin, tobramycin and sisomicin can also act as acceptors. ATP, dATP, CTP, ITP and GTP can act as donors. Nucleoside triphosphate + gentamicin = diphosphate + 2''-nucleotidylgentamicin. Streptomycin 3''-adenylyltransferase ATP + streptomycin = diphosphate + 3''-adenylylstreptomycin. Also acts on spectinomycin. RNA nucleotidyltransferase (RNA-directed) RNA-directed RNA polymerase Catalyzes RNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. See also EC 2.7.7.6. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). Reverse transcriptase RNA-directed DNA polymerase DNA nucleotidyltransferase (RNA-directed) Revertase Requires a RNA or DNA primer. Cannot initiate a chain de novo. DNA can also serve as template. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). See also EC 2.7.7.7. Catalyzes RNA-template-directed extension of the 3'-end of a DNA strand by one deoxynucleotide at a time. Sulfate adenylyltransferase (ADP) ADP-sulfurylase Adenosine diphosphate sulfurylase ADP + sulfate = phosphate + adenylyl sulfate. mRNA guanylyltransferase GTP--RNA guanylyltransferase mRNA capping enzyme Can modify also synthetic poly(A) and poly(G) to form the structures m(7)G(5')pppAn and m(7)G(5')pppGn. GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA. Adenylylsulfate--ammonia adenylyltransferase Adenylyl sulfate + NH(3) = adenosine 5'-phosphoramidate + sulfate. TUT RNA uridylyltransferase Terminal uridylyltransferase Requires an oligoribonucleotide or polyribonucleotide with a free terminal 3'-OH as a primer. UTP + RNA(n) = diphosphate + RNA(n+1). Diadenosinetetraphosphate alpha-beta-phosphorylase AP-4-A phosphorylase Bis(5'-nucleosyl)-tetraphosphate phosphorylase (NDP-forming) ATP adenylyltransferase Diadenosine 5',5'''-P(1),P(4)-tetraphosphate phosphorylase ADP + ATP = phosphate + P(1),P(4)-bis(5'-adenosyl) tetraphosphate. GTP and adenosine tetraphosphate can also act as adenylyl acceptors. Phenylalanine adenylyltransferase Part of the system for biosynthesis of the alkaloid cyclopeptine in Penicillium cyclopium. ATP + L-phenylalanine = diphosphate + N-adenylyl-L-phenylalanine. Anthranilate adenylyltransferase Anthranilic acid adenylyltransferase ATP + anthranilate = diphosphate + N-adenylylanthranilate. Part of the system for biosynthesis of the alkaloid cyclopeptine in Penicillium cyclopium. tRNA nucleotidyltransferase Ribonuclease PH Phosphate-dependent exonuclease RNase PH tRNA(n+1) + phosphate = tRNA(n) + a nucleoside diphosphate. Not identical with EC 2.7.7.8. Brings about the final exonucleolytic trimming of the 3'-terminus of tRNA precursors in Escherichia coli by a phosphorolysis, producing a mature 3'-terminus in tRNA and nucleoside diphosphate. N-methylphosphoethanolamine cytidylyltransferase CTP + N-methylethanolamine phosphate = diphosphate + CDP-N-methylethanolamine. 2,3-dihydroxybenzoate-AMP ligase (2,3-dihydroxybenzoyl)adenylate synthase ATP + 2,3-dihydroxybenzoate = diphosphate + (2,3-dihydroxybenzoyl)adenylate. Uridylyl removing enzyme [Protein-PII] uridylyltransferase PII uridylyl-transferase UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. The enzyme uridylylates and de-uridylylates the small trimeric protein PII. RNA polymerase I RNA polymerase III DNA-dependent RNA polymerase DNA-directed RNA polymerase RNA nucleotidyltransferase (DNA-directed) RNA polymerase II See also EC 2.7.7.19 and EC 2.7.7.48. In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). Can initiate a chain de novo. Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. MEP cytidylyltransferase 4-diphosphocytidyl-2-C-methyl-D-erythritol synthase 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase MCT ATP or UTP can replace CTP, but both are less effective. Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. GTP and TTP are not substrates. CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. Magnesium or manganese Holo-ACP synthase Holo-citrate lyase synthase 2'-(5''-phosphoribosyl)-3'-dephospho-CoA transferase 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase Magnesium 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA + apo-citrate lyase = holo-citrate lyase + diphosphate. The corresponding mononucleotides are transferred to a serine of the acyl carrier protein of citrate lyase with release of diphosphate. The linkage to serine is via a phosphodiester bond. The enzyme from Escherichia coli can also use ATP, CTP, GTP and UTP as a substrate in vitro. Adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase Adenosylcobinamide-phosphate guanylyltransferase GTP:adenosylcobinamide-phosphate guanylyltransferase AdoCbi kinase/AdoCbi-phosphate guanylyltransferase GTP + adenosylcobinamide phosphate = diphosphate + adenosylcobinamide-GDP. The final step in adenosylcobalamin biosynthesis is the condensation of AdoCbi-GDP with alpha-ribazole, which is catalyzed by CobS (EC 2.7.8.26), to yield adenosylcobalamin. The guanylyltransferase reaction is a two-stage reaction with formation of a CobU-GMP intermediate. CobU is a bifunctional enzyme that has both kinase (EC 2.7.1.156) and guanylyltransferase (EC 2.7.7.62) activities. The kinase activity has been proposed to function only when S.typhimurium is assimilating cobinamide whereas the guanylyltransferase activity is required for both assimilation of exogenous cobinamide and for de novo synthesis of adenosylcobalamin. In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC 2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73) and CobS (EC 2.7.8.26) catalyze reactions in the nucleotide loop assembly pathway, which convert adenosylcobinamide (AdoCbi) into adenosylcobalamin (AdoCbl). The second branch of the nuclotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by the bifunctional enzyme CobU. However, both activities are not required at all times. CobT and CobC are involved in 5,6-dimethylbenzimidazole activation whereby 5,6-dimethylbenzimidazole is converted to its riboside, alpha-ribazole. Lipoate protein ligase LPL Lipoate-protein ligase A Lipoate--protein ligase (2) Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP. Selenolipoate, i.e. 5-(1,2-diselenolan-3-yl)pentanoic acid, and 6-sulfanyloctanoate can also act as substrates, but more slowly. Attaches lipoic acid to the lipoyl domains of these proteins. (1) ATP + lipoate = diphosphate + lipoyl-AMP. Magnesium Responsible for lipoylation in the presence of exogenous lipoic acid. It is likely that an alternative pathway, involving EC 2.3.1.181 and EC 2.8.1.8 is the normal route for lipoylation. Both 6S-and 6R-lipoates can act as substrates but there is a preference for the naturally occurring R-form. Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein). USP UDP-sugar pyrophosphorylase UTP-monosaccharide-1-phosphate uridylyltransferase The reaction can occur in either direction and it has been postulated that MgUTP and Mg-diphosphate are the actual substrates. Catalyzes the formation of UDP-Glc, UDP-Gal, UDP-GlcA, UDP-L-Ara and UDP-Xyl, showing broad substrate specificity toward monosaccharide 1-phosphates. Mannose 1-phosphate, L-fucose 1-phosphate and glucose 6-phosphate are not substrates and UTP cannot be replaced by other nucleotide triphosphates. Magnesium or manganese UTP + a monosaccharide 1-phosphate = diphosphate + UDP-monosaccharide. DNA-dependent DNA polymerase DNA-directed DNA polymerase DNA nucleotidyltransferase (DNA-directed) Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). http://purl.uniprot.org/mim/603041 Cannot initiate a chain de novo. http://purl.uniprot.org/mim/607459 http://purl.uniprot.org/mim/203700 http://purl.uniprot.org/mim/157640 http://purl.uniprot.org/mim/278750 See also EC 2.7.7.49. Requires a primer which may be DNA or RNA. http://purl.uniprot.org/mim/610131 http://purl.uniprot.org/mim/258450 Polyribonucleotide nucleotidyltransferase Polynucleotide phosphorylase ADP, IDP, GDP, UDP and CDP can act as donors. RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate. Glucose-1-phosphate uridylyltransferase UDP-glucose diphosphorylase UDP-glucose pyrophosphorylase UTP--glucose-1-phosphate uridylyltransferase UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose. Transferases for other substituted phosphate groups Ethanolaminephosphotransferase CDP-ethanolamine + 1,2-diacylglycerol = CMP + a phosphatidylethanolamine. Sphingosine cholinephosphotransferase CDP-choline + sphingosine = CMP + sphingosyl-phosphocholine. Phosphatidylinositol synthase CDP-diacylglycerol--inositol 3-phosphatidyltransferase CDP-diacylglycerol--inositol phosphatidyltransferase CDP-diacylglycerol + myo-inositol = CMP + phosphatidyl-1D-myo-inositol. CDP-glycerol glycerophosphotransferase Teichoic-acid synthase CDP-glycerol + (glycerophosphate)(n) = CMP + (glycerophosphate)(n+1). Phospho-MurNAc-pentapeptide transferase Phosphoacetylmuramoylpentapeptide translocase UDP-MurNAc-Ala-gamma-DGlu-Lys-DAla-DAla:undecaprenylphosphate transferase UDP-MurNAc-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala:C(55)-isoprenoid alcohol transferase MraY transferase Phospho-N-acetylmuramoyl pentapeptide translocase Phospho-N-acetylmuramoyl-pentapeptide-transferase UDP-MurNAc-pentapeptide phosphotransferase Phospho-NAc-muramoyl-pentapeptide translocase (UMP) Phosphoacetylmuramoylpentapeptidetransferase In Gram-negative and some Gram-positive organisms the L-lysine is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm), which is combined with adjacent residues through its L-center. The undecaprenol involved is ditrans,octacis-undecaprenol. UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. CDP-ribitol ribitolphosphotransferase Teichoic-acid synthase CDP-ribitol + (ribitol phosphate)(n) = CMP + (ribitol phosphate)(n+1). N-acetylglucosamine-1-phosphate transferase GlcNAc-1-P transferase UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase http://purl.uniprot.org/mim/608093 UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-D-glucosaminyl-diphosphodolichol. N-acetylglucosaminylphosphotransferase UDP-N-acetylglucosamine--lysosomal-enzyme N-acetylglucosaminephosphotransferase Some other glycoproteins with high-mannose can act as acceptors, but much more slowly than lysosomal enzymes. UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose = UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose. http://purl.uniprot.org/mim/252600 http://purl.uniprot.org/mim/252500 UDP-galactose--UDP-N-acetylglucosamine galactose phosphotransferase UDP-galactose + UDP-N-acetyl-D-glucosamine = UMP + UDP-N-acetyl-6-(D-galactose-1-phospho)-D-glucosamine. N-acetylglucosamine end-groups in glycoproteins can also act as acceptors. UDP-glucose--glycoprotein glucose phosphotransferase GlcPTase Penultimate mannose residues on oligomannose type glycoproteins can act as acceptors. UDP-glucose + glycoprotein D-mannose = UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose. Alkylacylglycerol cholinephosphotransferase Cholinephosphotransferase Diacylglycerol cholinephosphotransferase Phosphorylcholine--glyceride transferase 1-alkyl-2-acetylglycerol cholinephosphotransferase CDP-choline + 1,2-diacylglycerol = CMP + a phosphatidylcholine. 1-alkyl-2-acylglycerol can act as acceptor. Phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase Phosphoglycerol transferase Phosphatidylglycerol + membrane-derived-oligosaccharide D-glucose = 1,2-diacyl-sn-glycerol + membrane-derived-oligosaccharide 6-(glycerophospho)-D-glucose. 1,2-beta-and 1,6-beta-linked glucose residues in membrane polysaccharides and in synthetic glucosides can act as acceptors. Periplasmic phosphoglycerotransferase Membrane-oligosaccharide glycerophosphotransferase Phosphoglycerol cyclase Transfer of a glycerophospho group from one membrane-derived oligosaccharide to another. In the presence of low concentrations of acceptor, free cyclic 1,2-phosphoglycerol is formed. Beta-linked glucose residues in simple glucosides, such as gentiobiose, can act as acceptors. 1-alkenyl-2-acylglycerol choline phosphotransferase CDP-choline + 1-alkenyl-2-acylglycerol = CMP + plasmenylcholine. Carboxyvinyl-carboxyphosphonate phosphorylmutase Carboxyphosphonoenolpyruvate phosphonomutase CPEP phosphonomutase Catalyzes the transfer and decarboxylation of the carboxy(hydroxy)phosphoryl group, HOOC-P(O)(OH)-(phosphoryl being a 3-valent group), in the formation of an unusual C-P bond that is involved in the biosynthesis of the antibiotic bialaphos. 1-carboxyvinyl carboxyphosphonate = 3-(hydrohydroxyphosphoryl)pyruvate + CO(2). CDP-diglyceride-choline O-phosphatidyltransferase PC synthase Phosphatidylcholine synthase Manganese or magnesium CDP-diacylglycerol + choline = CMP + phosphatidylcholine. ATP:dephospho-CoA 5-triphosphoribosyl transferase Triphosphoribosyl-dephospho-CoA synthase 2'-(5''-triphosphoribosyl)-3-dephospho-CoA synthase CitG ATP + 3-dephospho-CoA = 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA + adenine. ATP cannot be replaced by GTP, CTP, UTP, ADP or AMP. 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA is the precursor of the phosphoribosyl-3-dephospho-CoA prosthetic group of the acyl carrier protein subunit of EC 4.1.3.6. Cobalamin-5'-phosphate synthase Cobalamin (5'-phosphate) synthase Cobalamin synthase Adenosylcobinamide-GDP ribazoletransferase In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC 2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73) and CobS (EC 2.7.8.26) catalyze reactions in the nucleotide loop assembly pathway, which convert adenosylcobinamide (AdoCbi) into adenosylcobalamin (AdoCbl). CobS catalyzes the final step in adenosylcobalamin biosynthesis, which is the condensation of AdoCbi-GDP with alpha-ribazole to yield adenosylcobalamin. CobT and CobC are involved in 5,6-dimethylbenzimidazole activation whereby 5,6-dimethylbenzimidazole is converted to its riboside, alpha-ribazole. (1) Adenosylcobinamide-GDP + alpha-ribazole = GMP + adenosylcobalamin. The second branch of the nucleotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by the bifunctional enzyme CobU. (2) Adenosylcobinamide-GDP + alpha-ribazole 5'-phosphate = GMP + adenosylcobalamin 5'-phosphate. SM synthase Sphingomyelin synthase Phosphatidylcholine:ceramide cholinephosphotransferase The reaction can occur in both directions. Occupies a central position in sphingolipid and glycerophospholipid metabolism. Unlike EC 2.7.8.3 CDP-choline cannot replace phosphatidylcholine as the donor of the phosphocholine moiety of sphingomyelin. A ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol. Up-and down-regulation of its activity has been linked to mitogenic and pro-apoptotic signaling in a variety of mammalian cell types. Ceramide cholinephosphotransferase CDP-choline + N-acylsphingosine = CMP + sphingomyelin. Serine-phosphoethanolamine synthase CDP-ethanolamine + L-serine = CMP + L-serine-phosphoethanolamine. CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 3-phosphatidyl-1'-glycerol-3'-phosphate synthase Glycerophosphate phosphatidyltransferase Phosphatidylglycerophosphate synthase PGP synthase CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate. Undecaprenyl-phosphate galactose phosphotransferase Poly(isoprenol)-phosphate galactosephosphotransferase UDP-galactose + undecaprenyl phosphate = UMP + alpha-D-galactosyl-diphosphoundecaprenol. Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase Holosynthase PPTase 4'-phosphopantetheinyl transferase Acyl carrier protein synthase Holo-ACP synthetase Holo-[acyl-carrier-protein] synthase ACPS Holo-ACP synthase Acyl carrier protein holoprotein (holo-ACP) synthetase L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase Acyl carrier protein synthetase P-pant transferase The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain. CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein]. The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes. Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14. All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. Magnesium CDP-diglycerine-serine O-phosphatidyltransferase Phosphatidylserine synthase CDP-diacylglycerol--serine O-phosphatidyltransferase CDP-diacylglycerol + L-serine = CMP + (3-sn-phosphatidyl)-L-serine. Phosphomannan mannosephosphotransferase GDP-mannose + (phosphomannan)(n) = GMP + (phosphomannan)(n+1). Phosphotransferases with paired acceptors Pyruvate, phosphate dikinase Pyruvate,orthophosphate dikinase Pyruvate,phosphate dikinase ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate. Pyruvate, water dikinase Pyruvate,water dikinase Phosphoenolpyruvate synthase ATP + pyruvate + H(2)O = AMP + phosphoenolpyruvate + phosphate. Manganese Selenophosphate synthase Selenide,water dikinase Selenide, water dikinase Selenium donor protein Selenophosphate synthetase Magnesium ATP + selenide + H(2)O = AMP + selenophosphate + phosphate. Alpha-glucan, water dikinase Alpha-glucan,water dikinase Starch-related R1 protein The protein phosphorylates itself with the beta-phosphate of ATP, which is then transferred to the glucan. ATP + alpha-glucan + H(2)O = AMP + phospho-alpha-glucan + phosphate. ATP appears to be the only phosphate donor. No activity could be detected using GTP, UTP, phosphoenolpyruvate or diphosphate. Magnesium The protein phosphorylates glucans exclusively at O-6 of glucosyl residues. Phosphoglucan, water dikinase ATP + (phospho-alpha-glucan) + H(2)O = AMP + O-phospho-(phospho-alpha-glucan) + phosphate. The protein phosphorylates itself with the beta-phosphate of ATP, which is then transferred to the glucan. In contrast to EC 2.7.9.4, which phosphorylates the glucose groups in glucans predominantly on O-6, this enzyme phosphorylates glucose groups in phosphorylated starch predominantly on O-3. The enzyme phosphorylates granular starch that has previously been phosphorylated by EC 2.7.9.4; there is no activity with unphosphorylated glucans. It transfers the beta-phosphate of ATP to the phosphoglucan, whereas the gamma-phosphate is transferred to water. Other protein kinases Pyrophosphate-protein phosphotransferase Diphosphate--protein phosphotransferase Triphosphate--protein phosphotransferase DiPPT Triphosphate + [microsomal-membrane protein] = diphosphate + [microsomal-membrane protein] phosphate. This enzyme was originally thought to use diphosphate as substrate but this has since been disproved. Tripolyphosphate is a contaminant of (gamma-(32)P)ATP. The activity is observed as the second part of a biphasic reaction after depletion of ATP. Transferring sulfur-containing groups Sulfurtransferases Thiosulfate sulfurtransferase Rhodanese Thiosulfate cyanide transsulfurase Thiosulfate thiotransferase A few other sulfur compounds can act as donors. Thiosulfate + cyanide = sulfite + thiocyanate. 3-mercaptopyruvate sulfurtransferase 3-mercaptopyruvate + cyanide = pyruvate + thiocyanate. Sulfite, sulfinates, mercaptoethanol and mercaptopyruvate can also act as acceptors. Zinc Glutathione-dependent thiosulfate reductase Thiosulfate--thiol sulfurtransferase Sulfane reductase L-cysteine can also act as acceptor. Thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide. The primary product is glutathione hydrodisulfide, which reacts with glutathione to give glutathione disulfide and sulfide. tRNA sulfurtransferase L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide. A group of enzymes transferring sulfur to various nucleotides in a tRNA chain, producing residues such as 4-thiouridylate. With some enzymes mercaptopyruvate can act as sulfur donor. Thiosulfate--dithiol sulfurtransferase Thiosulfate reductase The enzyme probably transfers the sulfur atom onto one thiol group to form -S-S(-), and sulfide is spontaneously expelled from this by reaction with the other thiol group. Thiosulfate + dithioerythritol = sulfite + 4,5-cis-dihydroxy-1,2-dithiacyclohexane + sulfide. May be identical with EC 2.8.1.1. The enzyme from Chlorella shows very little activity toward monothiols such as glutathione and cysteine (cf. EC 2.8.1.3). Biotin synthetase Biotin synthase Sulfur insertion into dethiobiotin takes place with retention of configuration. The enzyme has both a [2Fe-2S] and a [4Fe-4S] center, and the latter is believed to donate the electron. This single-turnover enzyme is a member of the 'AdoMet radical' (radical SAM) family, all members of which produce the 5'-deoxyadenosin-5'-yl radical and methionine from AdoMet (i.e. S-adenosylmethionine, or S-5'-(deoxyadenosin-5'-yl)methionine), by the addition of an electron from an iron-sulfur center. Two molecules of AdoMet are converted into radicals; these activate positions 6 and 9 of dethiobiotin by abstracting a hydrogen atom from each, and thereby forming 5'-deoxyadenosine. Dethiobiotin + sulfur + 2 S-adenosyl-L-methionine = biotin + 2 L-methionine + 2 5'-deoxyadenosine. Iron-sulfur The sulfur donor has not been identified to date -it is neither elemental sulfur nor from SAM, but it has been postulated that it may be from the [2Fe-2S] center. Cysteine desulfurase Cysteine desulfurylase The reaction shown is the first part of a catalytic reaction, which is completed by passing on its extra sulfur to other acceptors. L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine. Pyridoxal-phosphate The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) and functions by mobilizing sulfur. In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation. Lipoyl synthase Lipoate synthase Protein N(6)-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosyl. Member of the 'AdoMet radical' (radical SAM) family, all members of which produce the 5'-deoxyadenosin-5'-yl radical and methionine from AdoMet (i.e. S-adenosylmethionine, or S-(5'-deoxyadenosin-5'-yl)methionine), by the addition of an electron from an iron-sulfur center. An alternative lipoylation pathway involves EC 2.7.7.63, which can lipoylate apoproteins using exogenous lipoic acid (or its analogs). Examples of such lipoylated proteins include pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system. Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. Catalyzes the final step in the de-novo biosynthesis of the lipoyl cofactor, with the other enzyme involved being EC 2.3.1.181. The radical is converted into 5'-deoxyadenosine when it abstracts a hydrogen atom from C-6 and C-8, leaving reactive radicals at these positions so that they can add sulfur, with inversion of configuration. Sulfotransferases Aryl sulfotransferase Sulfokinase Phenol sulfotransferase 3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate. Organic hydroxylamines are not substrates (cf. EC 2.8.2.9). A number of aromatic compounds can act as acceptors. Luciferin sulfotransferase Renilla-luciferin sulfotransferase The product may be identical with Watasenia luciferin. 3'-phosphoadenylyl sulfate + Renilla luciferin = adenosine 3',5'-bisphosphate + luciferyl sulfate. Galactosylceramide sulfotransferase Also acts on lactosylceramide and monogalactosylalkylacylglycerol. 3'-phosphoadenylyl sulfate + a galactosylceramide = adenosine 3',5'-bisphosphate + a galactosylceramidesulfate. Psychosine sulfotransferase 3'-phosphoadenylyl sulfate + galactosylsphingosine = adenosine 3',5'-bisphosphate + psychosine sulfate. Glycolithocholate sulfotransferase Bile salt:3'phosphoadenosine-5'-phosphosulfate:sulfotransferase Bile-salt sulfotransferase Bile acid:3'-phosphoadenosine-5'-phosphosulfate sulfotransferase BAST I Bile acid sulfotransferase I This enzyme is both a bile salt and a 3-hydroxysteroid sulfotransferase. May be identical to EC 2.8.2.2. (2) 3'-phosphoadenylyl sulfate + taurolithocholate = adenosine 3',5'-bisphosphate + taurolithocholate sulfate. In addition to the 5-beta-bile acid glycolithocholate, deoxycholate, 3-beta-hydroxy-5-cholenoate and dehydroepiandrosterone (3-beta-hydroxyandrost-5-en-17-one) also act as substrates (see also EC 2.8.2.2 and EC 2.8.2.34). (1) 3'-phosphoadenylyl sulfate + glycolithocholate = adenosine 3',5'-bisphosphate + glycolithocholate 3-sulfate. The formation of sulfate esters of bile acids is an essential step in the prevention of toxicity by monohydroxy bile acids in many species. Steroid sulfotransferase 3'-phosphoadenylyl sulfate + a phenolic steroid = adenosine 3',5'-bisphosphate + steroid O-sulfate. Broad specificity resembling EC 2.8.2.2, but also acts on estrone. Thiol sulfotransferase 3'-phosphoadenylyl sulfate + a thiol = adenosine 3',5'-bisphosphate + an S-alkyl thiosulfate. Also acts on dithiols; substrates include glutathione, dithioerythritol and 2,3-mercaptopropanol. Chondroitin 6-sulfotransferase Not identical with EC 2.8.2.5. http://purl.uniprot.org/mim/608637 The sulfation is at the 6-position of N-acetylgalactosamine residues of chondroitin. 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate. Cortisol sulfotransferase Glucocorticosteroid sulfotransferase 3'-phosphoadenylyl sulfate + cortisol = adenosine 3',5'-bisphosphate + cortisol 21-sulfate. Triglucosylalkylacylglycerol sulfotransferase 3'-phosphoadenylyl sulfate + alpha-D-glucosyl-1,6-alpha-D-glucosyl-1,6-alpha-D-glucosyl-1,3-1-O-alkyl-2-O-acylglycerol = adenosine 3',5'-bisphosphate + 6-sulfo-alpha-D-glucosyl-1,6-alpha-D-glucosyl-1,6-alpha-D-glucosyl-1,3-1-O-alkyl-2-O-acylglycerol. Hydroxysteroid sulfotransferase Alcohol sulfotransferase 3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate. Primary and secondary alcohols, including aliphatic alcohols, ascorbate, chloramphenicol, ephedrine and hydroxysteroids, but not phenolic steroids, can act as acceptors (cf. EC 2.8.2.15). Protein-tyrosine sulfotransferase Tyrosylprotein sulfotransferase 3'-phosphoadenylyl sulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate. The tyrosine residues of some specific proteins of rat pheochromocytoma cells act as acceptors. Keratan sulfotransferase Not identical with EC 2.8.2.5, EC 2.8.2.6 or EC 2.8.2.17. Sulfation takes place at the 6-position of galactosyl and N-acetylglucosaminyl residues in keratan, a proteoglycan. 3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'-bisphosphate + keratan 6'-sulfate. Arylsulfate sulfotransferase Hydroxy groups of tyrosine residues in peptides such as angiotensin can act as acceptors. An aryl sulfate + a phenol = a phenol + an aryl sulfate. Does not act on 3'-phosphoadenylyl sulfate or adenosine 3',5'-bisphosphate. Heparan sulfate D-glucosaminyl 3-O-sulfotransferase [Heparan sulfate]-glucosamine 3-sulfotransferase 1 Glucosaminyl 3-O-sulfotransferase 3-OST-1 Heparin-glucosamine 3-O-sulfotransferase 3'-phosphoadenylyl-sulfate:heparin-glucosamine 3-O-sulfotransferase If the heparan sulfate substrate lacks 2-O-sulfation of GlcA residues, then enzyme specificity is expanded to modify selected glucosamine residues preceded by IdoA as well as GlcA. These precursors are variants of the consensus sequence: -> Glc(N2S>NAc)+-6S->GlcA->GlcN2S*+-6S->GlcA>IdoA+-2S-> Glc(N2S/NAc)+-6S->. This enzyme differs from EC 2.8.2.29 and EC 2.8.2.30 by being the most selective for a precursor of the antithrombin-binding site. 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate. It has a minimal acceptor sequence of: -> GlcNAc6S->GlcA-> GlcN2S*+-6S->IdoA2S->GlcN2S->. It can also modify other precursor sequences within heparan sulfate but this action does not create functional antithrombin-binding sites. Desulfoglucosinolate sulfotransferase 3'-phosphoadenylyl sulfate + desulfoglucotropeolin = adenosine 3',5'-bisphosphate + glucotropeolin. Involved with EC 2.4.1.195 in the biosynthesis of thioglycosides in cruciferous plants. Flavonol 3-sulfotransferase Also acts on some other flavonol aglycones. 3'-phosphoadenylyl sulfate + quercetin = adenosine 3',5'-bisphosphate + quercetin 3-sulfate. Quercetin-3-sulfate 3'-sulfotransferase 3'-phosphoadenylyl sulfate + quercetin 3-sulfate = adenosine 3',5'-bisphosphate + quercetin 3,3'-bissulfate. Quercetin-3-sulfate 4'-sulfotransferase 3'-phosphoadenylyl sulfate + quercetin 3-sulfate = adenosine 3',5'-bisphosphate + quercetin 3,4'-bissulfate. Quercetin-3,3'-bissulfate 7-sulfotransferase Quercetin 3,4'-bissulfate can also act as acceptor. 3'-phosphoadenylyl sulfate + quercetin 3,3'-bissulfate = adenosine 3',5'-bisphosphate + quercetin 3,3',7-trissulfate. [Heparan sulfate]-glucosamine 3-sulfotransferase 2 Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 2 3-OST-2 Glucosaminyl 3-O-sulfotransferase 2 Preference for GlcN2S versus unmodified GlcN has not yet been established. Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant. 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate. This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamine residues preceded by GlcA2S; EC 2.8.2.23 prefers GlcA or IdoA, whereas EC 2.8.2.30 prefers IdoA2S. This enzyme sulfates the residues marked with an asterisk in sequences containing at least ->IdoA2S->GlcN*-> or ->GlcA2S->GlcN*->. Amine sulfotransferase Arylamine sulfotransferase Amine N-sulfotransferase 3'-phosphoadenylyl sulfate + an amine = adenosine 3',5'-bisphosphate + a sulfamate. A large number of primary and secondary amines can act as acceptors, including aniline, 2-naphthylamine, cyclohexylamine and octylamine. [Heparan sulfate]-glucosamine 3-sulfotransferase 3 3-OST-3 Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3 Glucosaminyl 3-O-sulfotransferase 3 Modification of selected sequences containing N-sulfo-glucosamine residues cannot yet be excluded. Two major substrates contain the tetrasaccharides: -> undetermined 2-sulfo-uronic acid->GlcN2S->IdoA2S->GlcN*-> and -> undetermined 2-sulfo-uronic acid->GlcN2S->IdoA2S->GlcN6S*-> with modification of the N-unsubstituted glucosamine residue (shown with an asterisk). 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate. It is inefficient at modifying precursors of the antithrombin binding site (in contrast to EC 2.8.2.23) and it does not modify glucosamine preceded by GlcA2S (unlike EC 2.8.2.29). The 3-O-sulfated heparan sulfate can be utilized by Herpes simplex virus type 1 as an entry receptor to infect the target cells. There are two isozymes, known as 3-OST-3(A) and 3-OST-3(B), which have identical catalytic domains but are encoded by different mammalian genes. The specificity of this enzyme differs from that of the other [heparan sulfate]-glucosamine 3-sulfotransferases. PZ-SULT Petromyzonol sulfotransferase The enzyme from the lamprey Petromyzon marinus can also use the corresponding 3-ketone as a substrate. 3'-phosphoadenylyl sulfate + 5-alpha-cholan-3-alpha,7-alpha,12-alpha,24-tetrol = adenosine 3',5'-bisphosphate + 5-alpha-cholan-3-alpha,7-alpha,12-alpha-triol 24-sulfate. It is stereoselective (5-alpha-cholane) and regioselective, exhibiting a preference for an hydroxy group at C-24. The enzyme is inactive when allocholic acid, which has a carboxy group at C-24, is used as a substrate. Scymnol sulfotransferase 3'-phosphoadenosine 5'-phosphosulfate + 5-beta-scymnol = adenosine 3',5'-bisphosphate + 5-beta-scymnol sulfate. Enzyme activity is activated by Mg(2+) but inhibited by the product 5-beta-scymnol sulfate. The enzyme from the shark Heterodontus portusjacksoni is able to sulfate the C(27) bile salts 5-beta-scymnol (the natural bile salt) and 5-alpha-cyprinol (the carp bile salt). N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase GalNAc4S-6ST Oligosaccharides derived from chondroitin sulfate also serve as acceptors but chondroitin sulfate E, keratan sulfate and heparan sulfate do not. (1) 3'-phosphoadenylyl sulfate + dermatan = adenosine 3',5'-bisphosphate + dermatan 6'-sulfate. Divalent cation Differs from EC 2.8.2.17 in being able to use both chondroitin and dermatan as effective substrates. Glutathione (2) 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate. The enzyme from human transfers sulfate to position 6 of both internal residues and nonreducing terminal GalNAc 4-sulfate residues of chondroitin sulfate. Glycochenodeoxycholate sulfotransferase Bile acid:PAPS:sulfotransferase BAST Bile acid:3'-phosphoadenosine-5'-phosphosulfate sulfotransferase 3'-phosphoadenylyl sulfate + glycochenodeoxycholate = adenosine 3',5'-bisphosphate + glycochenodeoxycholate 7-sulfate. Specifically sulfates glycochenodeoxycholate at the 7-alpha-position (see also EC 2.8.2.14). The monohydroxy bile acids glycolithocholate, chenodeoxycholate and ursodeoxycholate act as inhibitors. Estrone sulfotransferase 3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate. Chondroitin 4-sulfotransferase The sulfation is at the 4-position of N-acetylgalactosamine residues of chondroitin. Not identical with EC 2.8.2.17. 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate. Choline sulfotransferase 3'-phosphoadenylyl sulfate + choline = adenosine 3',5'-bisphosphate + choline sulfate. UDP-N-acetylgalactosamine-4-sulfate sulfotransferase 3'-phosphoadenylyl sulfate + UDP-N-acetyl-D-galactosamine 4-sulfate = adenosine 3',5'-bisphosphate + UDP-N-acetyl-D-galactosamine 4,6-bissulfate. Heparan sulfate sulfotransferase 3'-phosphoadenylyl-sulfate:N-desulfoheparin N-sulfotransferase Heparin N-sulfotransferase Heparan sulfate N-deacetylase/N-sulfotransferase N-heparan sulfate sulfotransferase N-HSST N-desulfoheparin sulfotransferase PAPS:DSH sulfotransferase 3'-phosphoadenylylsulfate:N-desulfoheparin sulfotransferase Heparitin sulfotransferase Heparan sulfate N-sulfotransferase Desulfoheparin sulfotransferase [Heparan sulfate]-glucosamine N-sulfotransferase PAPS:N-desulfoheparin sulfotransferase Heparan sulfate 2-N-sulfotransferase 3'-phosphoadenylyl-sulfate:heparitin N-sulfotransferase Glucosaminyl N-deacetylase/N-sulfotransferase The enzyme also catalyzes the sulfation of chondroitin 4-sulfate and dermatan sulfate, but to a much more limited extent. 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine. Tyrosine-ester sulfotransferase 3'-phosphoadenylyl sulfate + L-tyrosine methyl ester = adenosine 3',5'-bisphosphate + L-tyrosine methyl ester 4-sulfate. Phenols and organic hydroxylamines can act as acceptors (cf. EC 2.8.2.1). CoA-transferases Propionate CoA-transferase Acetyl-CoA + propanoate = acetate + propanoyl-CoA. Butanoate and lactate can also act as acceptors. Citrate CoA-transferase Acetyl-CoA + citrate = acetate + (3S)-citryl-CoA. Also catalyzes the transfer of thioacyl carrier protein from its acetyl thioester to citrate. Component of EC 4.1.3.6. Citramalate CoA-transferase Also catalyzes the transfer of thioacyl carrier protein from its acetyl thioester to citramalate. Component of EC 4.1.3.22. Acetyl-CoA + citramalate = acetate + (3S)-citramalyl-CoA. Glutaconate CoA-transferase Acetyl-CoA + (E)-glutaconate = acetate + glutaconyl-1-CoA. Glutarate, (R)-2-hydroxyglutarate, propenoate and propanoate, but not (Z)-glutaconate, can also act as acceptors. Succinate--hydroxymethylglutarate CoA-transferase Succinyl-CoA + (S)-3-hydroxy-3-methylglutarate = succinate + 3-hydroxy-3-methylglutaryl-CoA. Malonyl-CoA can also act as donor, more slowly. 5-hydroxyvalerate CoA-transferase 5-hydroxypentanoate CoA-transferase Propanoyl-CoA, acetyl-CoA, butanoyl-CoA and some other acyl-CoAs can act as substrates, more slowly than 5-hydroxypentanoyl-CoA. Acetyl-CoA + 5-hydroxypentanoate = acetate + 5-hydroxypentanoyl-CoA. Succinyl-CoA:(R)-benzylsuccinate CoA-transferase Benzylsuccinate CoA-transferase Involved in anaerobic catabolism of toluene and is a strictly toluene-induced enzyme that catalyzes the reversible regio-and enantio-selective synthesis of (R)-2-benzylsuccinyl-CoA. Succinyl-CoA + (R)-2-benzylsuccinate = succinate + (R)-2-benzylsuccinyl-CoA. The enzyme from Thauera aromatica is inactive when (R)-benzylsuccinate is replaced by (S)-benzylsuccinate. Formyl-CoA oxalate CoA-transferase Formyl-CoA transferase Formyl-coenzyme A transferase Formyl-CoA + oxalate = formate + oxalyl-CoA. The enzyme from Oxalobacter formigenes can also catalyze the transfer of CoA from formyl-CoA to succinate. FldA Cinnamoyl-CoA:phenyllactate CoA-transferase The enzyme from Clostridium sporogenes is specific for derivatives of 3-phenylpropionate and 4-phenylbutyrate. 3-phenylproprionate is a better CoA acceptor than (R)-phenyllactate in vitro. (E)-cinnamoyl-CoA + (R)-phenyllactate = (E)-cinnamate + (R)-phenyllactyl-CoA. Succinyl--beta-ketoacyl-CoA transferase Oxalate CoA-transferase Succinyl-CoA + oxalate = succinate + oxalyl-CoA. Malonate CoA-transferase The enzyme from Pseudomonas ovalis also catalyzes the reaction of EC 4.1.1.9. Acetyl-CoA + malonate = acetate + malonyl-CoA. 3-oxoacid CoA-transferase Succinyl-CoA:3-ketoacid-CoA transferase Succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA. Malonyl-CoA can act instead of succinyl-CoA. Acetoacetate or, more slowly, 3-oxopropanoate, 3-oxopentanoate, 3-oxo-4-methylpentanoate or 3-oxohexanoate can act as acceptor. http://purl.uniprot.org/mim/245050 Beta-ketoadipate:succinyl-CoA transferase 3-oxoadipate CoA-transferase Succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA. Succinate--citramalate CoA-transferase Itaconate CoA-transferase Citramalate CoA-transferase Succinyl-CoA + citramalate = succinate + citramalyl-CoA. Itaconate can also act as acceptor. Acetate CoA-transferase Acetyl-CoA:acetoacetate CoA transferase Acyl-CoA + acetate = a fatty acid anion + acetyl-CoA. Acts on butanoyl-CoA and pentanoyl-CoA. Butyrate--acetoacetate CoA-transferase Butanoate, acetoacetate and their CoA thioesters are the preferred substrates, but the enzyme also acts, more slowly, on the derivatives of a number of C(2) to C(6) monocarboxylic acids. Butanoyl-CoA + acetoacetate = butanoate + acetoacetyl-CoA. Transferring alkylthio groups Methyl-CoM reductase Methyl coenzyme M reductase Coenzyme-B sulfoethylthiotransferase 2-(methylthio)ethanesulfonate (methyl-CoM) + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) = CoM-S-S-CoB + methane. Highly specific for coenzyme B with a heptanoyl chain; ethyl CoM and difluoromethyl CoM are poor substrates. Coenzyme F430 The sulfide sulfur can be replaced by selenium but not by oxygen. Transferring selenium-containing groups Selenotransferases L-seryl-tRNA(Sec) selenium transferase Selenocysteine synthase Cysteinyl-tRNA(Sel)-selenium transferase Cysteinyl-tRNA(Sec)-selenium transferase L-selenocysteinyl-tRNA(Sec) synthase L-selenocysteinyl-tRNA(Sel) synthase Recognizes specifically tRNA(Sec)-species. Binding of tRNA(Sec) also occurs in the absence of the seryl group. L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate. 2-aminoacryloyl-tRNA, bound to the enzyme as an imine with the pyridoxal phosphate, is an intermediate in the reaction. Since the selenium atom replaces oxygen in serine, the product may also be referred to as L-selenoseryl-tRNA(Sel). The abbreviation Sel has also been used for selenocysteine but Sec is preferred. Pyridoxal-phosphate Hydrolases Acting on ester bonds Carboxylic ester hydrolases Methylbutyrase Carboxylesterase Ali-esterase B-esterase Cocaine esterase Monobutyrase Procaine esterase The enzymes from microsomes also catalyze the reactions of EC 3.1.1.2, EC 3.1.1.5, EC 3.1.1.6, EC 3.1.1.23, EC 3.1.1.28, EC 3.1.2.2, EC 3.5.1.4, and EC 3.5.1.13. http://purl.uniprot.org/mim/114835 Wide specificity; also hydrolyzes vitamin A esters. A carboxylic ester + H(2)O = an alcohol + a carboxylate. Atropine acylhydrolase Atropinesterase Tropinesterase Also acts on cocaine and other tropine esters. Atropine + H(2)O = tropine + tropate. Pectin methylesterase Pectinesterase Pectin methoxylase Pectin demethoxylase Pectin + n H(2)O = n methanol + pectate. Triterpenol esterase Cholesterol esterase Sterol esterase Cholesterol ester synthase A steryl ester + H(2)O = a sterol + a fatty acid. A group of enzymes of broad specificity, acting on esters of sterols and long-chain fatty acids, that may also bring about the esterification of sterols. Activated by bile salts. http://purl.uniprot.org/mim/278000 Chlorophyllase Also catalyzes chlorophyllide transfer, e.g. converts chlorophyll to methylchlorophyllide. Chlorophyll + H(2)O = phytol + chlorophyllide. L-arabinonolactonase L-arabinono-1,4-lactone + H(2)O = L-arabinonate. Aldonolactonase Gluconolactonase Lactonase Acts on a wide range of hexono-1,5-lactones. D-glucono-1,5-lactone + H(2)O = D-gluconate. Uronolactonase D-glucurono-6,2-lactone + H(2)O = D-glucuronate. A-esterase Arylesterase Paraoxonase Acts on many phenolic esters. The natural substrates of the paraoxonases are lactones, with (+-)-5-hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being the best substrate. A phenyl acetate + H(2)O = a phenol + acetate. It is likely that the three forms of human paraoxonase are lactonases rather than aromatic esterases. Tannase Also hydrolyzes ester links in other tannins. Digallate + H(2)O = 2 gallate. Retinyl-palmitate esterase Retinyl palmitate + H(2)O = retinol + palmitate. Hydroxybutyrate-dimer hydrolase (R)-3-((R)-3-hydroxybutanoyloxy)butanoate + H(2)O = 2 (R)-3-hydroxybutanoate. Monoacylglycerol lipase Acylglycerol lipase Hydrolyzes glycerol monoesters of long-chain fatty acids. 3-oxoadipate enol-lactonase Beta-ketoadipate enol-lactone hydrolase Beta-ketoadipic enol-lactone hydrolase 3-oxoadipic enol-lactone hydrolase 3-ketoadipate enol-lactonase Carboxymethylbutenolide lactonase 3-oxoadipate enol-lactone + H(2)O = 3-oxoadipate. Acts on the product of EC 4.1.1.44. Gamma-lactonase 1,4-lactonase Does not hydrolyze simple aliphatic esters, acetylcholine, sugar lactones or substituted aliphatic lactones, e.g. 3-hydroxy-4-butyrolactone. A 1,4-lactone + H(2)O = a 4-hydroxyacid. Calcium Specific for 1,4-lactones with 4-8 carbon atoms. Galactolipase Also acts on 2,3-di-O-acyl-1-O-(6-O-alpha-D-galactosyl-beta-D-galactosyl)-D-glycerol, and phosphatidylcholine and other phospholipids. 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + 2 H(2)O = 3-beta-D-galactosyl-sn-glycerol + 2 carboxylates. 4-pyridoxolactonase 4-pyridoxolactone + H(2)O = 4-pyridoxate. Acylcarnitine hydrolase Highest activity is with O-decanoyl-L-carnitine. Acts on higher fatty acid (C(6) to C(18)) esters of L-carnitine. O-acylcarnitine + H(2)O = a fatty acid + L-carnitine. Peptidyl-tRNA hydrolase Aminoacyl-tRNA hydrolase N-substituted aminoacyl-tRNA + H(2)O = N-substituted amino acid + tRNA. Lipase Triacylglycerol lipase Triglyceride lipase Tributyrase Triacylglycerol + H(2)O = diacylglycerol + a carboxylate. http://purl.uniprot.org/mim/246600 The pancreatic enzyme acts only on an ester-water interface; the outer ester links are preferentially hydrolyzed. http://purl.uniprot.org/mim/609812 http://purl.uniprot.org/mim/151670 D-arabinonolactonase D-arabinono-1,4-lactone + H(2)O = D-arabinonate. 6-phosphogluconolactonase 6-phospho-D-glucono-1,5-lactone + H(2)O = 6-phospho-D-gluconate. Phospholipase A(1) Phospholipase A1 Has a much broader specificity than EC 3.1.1.4. Calcium Phosphatidylcholine + H(2)O = 2-acylglycerophosphocholine + a carboxylate. 6-acetylglucose deacetylase 6-acetyl-D-glucose + H(2)O = D-glucose + acetate. Diglyceride lipase Lipoprotein lipase Diacylglycerol lipase Clearing factor lipase Hydrolyzes triacylglycerols in chylomicrons and very low-density lipoproteins (VLDL). http://purl.uniprot.org/mim/238600 Triacylglycerol + H(2)O = diacylglycerol + a carboxylate. Also hydrolyzes diacylglycerol. Dihydrocoumarin hydrolase Dihydrocoumarin + H(2)O = melilotate. Also hydrolyzes some other benzenoid 1,4-lactones. Limonin-D-ring-lactonase Limonoate D-ring-lactone + H(2)O = limonoate. Limonoate is a triterpenoid. Steroid-lactonase Testololactone + H(2)O = testolate. Triacetate-lactonase Triacetate lactone + H(2)O = triacetate. Actinomycin lactonase Actinomycin + H(2)O = actinomycinic monolactone. Phospholipase A(2) Phosphatidase Phosphatidolipase Phosphatidylcholine 2-acylhydrolase Phospholipase A2 Lecithinase A Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position. Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate. Calcium Orsellinate-depside hydrolase Lecanorate hydrolase Orsellinate depside + H(2)O = 2 orsellinate. Will only hydrolyze those substrates based on the 2,4-dihydroxy-6-methylbenzoate structure that also have a free hydroxyl ortho to the depside linkage. Cephalosporin-C deacetylase Hydrolyzes the acetyl ester bond on the 10-position of the antibiotic cephalosporin C. Cephalosporin C + H(2)O = deacetylcephalosporin C + acetate. Chlorogenate hydrolase Chlorogenase No other substrates are known. Chlorogenate + H(2)O = caffeate + quinate. Also acts, more slowly, on isochlorogenate. Alpha-amino-acid ester hydrolase Alpha-amino-acid esterase Also catalyzes alpha-aminoacyl transfer to a number of amine nucleophiles. An alpha-amino acid ester + H(2)O = an alpha-amino acid + an alcohol. 4-methyloxaloacetate esterase Oxaloacetate 4-methyl ester + H(2)O = oxaloacetate + methanol. Dienelactone hydrolase Carboxymethylenebutenolidase Maleylacetate enol-lactonase 4-carboxymethylenebut-2-en-4-olide + H(2)O = 4-oxohex-2-enedioate. Deoxylimonate A-ring-lactonase Opens the A-ring-lactone of the triterpenoid deoxylimonic acid, leaving the D-ring-lactone intact. Deoxylimonate + H(2)O = deoxylimononic acid D-ring-lactone. Platelet-activating factor acetylhydrolase PAF 2-acylhydrolase PAF acetylhydrolase LDL-PLA(2) LDL-associated phospholipase A(2) 2-acetyl-1-alkylglycerophosphocholine esterase 1-alkyl-2-acetylglycerophosphocholine esterase 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H(2)O = 1-alkyl-sn-glycero-3-phosphocholine + acetate. http://purl.uniprot.org/mim/601690 Ornithine esterase Fusarinine-C ornithinesterase N(5)-acyl-L-ornithine ester + H(2)O = N(5)-acyl-L-ornithine + an alcohol. Hydrolyzes the three ornithine ester bonds in fusarinine C. Also acts on N(5)-dinitrophenyl-L-ornithine methyl ester. Sinapine esterase Sinapoylcholine + H(2)O = sinapate + choline. Lecithinase B Phospholipase B Lysolecithinase Lysophospholipase 2-lysophosphatidylcholine + H(2)O = glycerophosphocholine + a carboxylate. Wax-ester hydrolase A wax ester + H(2)O = a long-chain alcohol + a long-chain carboxylate. Also acts on long-chain acylglycerol, but not diacyl-or triacylglycerols. Phorbol-diester hydrolase Diacylphorbate 12-hydrolase Phorbol 12,13-dibutanoate + H(2)O = phorbol 13-butanoate + butanoate. Hydrolyzes the 12-ester bond in a variety of 12,13-diacylphorbols (phorbol is a diterpenoid). This reaction inactivates tumor promoter 12-O-tetradecanoylphorbol-13-acetate from croton oil. Phosphatidylinositol deacylase Phosphatidylinositol phospholipase A2 1-phosphatidyl-D-myo-inositol + H(2)O = 1-acylglycerophosphoinositol + a carboxylate. Sialate O-acetylesterase N-acetyl-O-acetylneuraminate + H(2)O = N-acetylneuraminate + acetate. Acts mainly on 4-O-and 9-O-acetyl groups. Acts on free and glycosidically-bound N-acetyl-or N-glycoloylneuraminic acid. Also acts on some other O-acetyl esters, both cyclic and acyclic compounds, which are not sialic acids. Acetoxybutynylbithiophene deacetylase 5-(4-acetoxybut-1-ynyl)-2,2'-bithiophene + H(2)O = 5-(4-hydroxybut-1-ynyl)-2,2'-bithiophene + acetate. Highly specific. Aspirin esterase Acetylsalicylate deacetylase The activity of the liver cytosol enzyme is highest with acetyl esters of aryl alcohols, and thioesters are also hydrolyzed. The microsomal enzyme also hydrolyzes some other negatively charged esters. Not identical with EC 3.1.1.1, EC 3.1.1.2, EC 3.1.1.7 or EC 3.1.1.8. Acetylsalicylate + H(2)O = salicylate + acetate. Best substrates were esters of salicylate with long-chain alcohols. Methylumbelliferyl-acetate deacetylase Esterase D Acts on short-chain acyl esters of 4-methylumbelliferone, but not on naphthyl, indoxyl or thiocholine esters. 4-methylumbelliferyl acetate + H(2)O = 4-methylumbelliferone + acetate. 2-pyrone-4,6-dicarboxylate lactonase 2-pyrone-4,6-dicarboxylate + H(2)O = 4-carboxy-2-hydroxyhexa-2,4-dienedioate. The product isomerizes to 4-oxalmesaconate. N-acetylgalactosaminoglycan deacetylase N-acetyl-D-galactosaminoglycan + H(2)O = D-galactosaminoglycan + acetate. JH esterase Juvenile-hormone esterase Demethylates the insect juvenile hormones, JH(1) and JH(3), but does not hydrolyze the analogous ethyl or isopropyl esters. Methyl (2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate + H(2)O = (2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate + methanol. Acetylesterase C-esterase (in animal tissues) An acetic ester + H(2)O = an alcohol + acetate. Bis(2-ethylhexyl)phthalate esterase Bis(2-ethylhexyl)phthalate + H(2)O = 2-ethylhexyl phthalate + 2-ethylhexan-1-ol. Also acts on 4-nitrophenyl esters, with optimum acyl chain length C(6) to C(8). Protein methylesterase CheB methylesterase Protein methyl-esterase Protein-glutamate methylesterase Protein carboxyl methylesterase Methylesterase CheB PME Chemotaxis-specific methylesterase Methyl-accepting chemotaxis protein methyl-esterase Protein L-glutamate O(5)-methyl ester + H(2)O = protein L-glutamate + methanol. Hydrolyzes the products of EC 2.1.1.77, EC 2.1.1.78, EC 2.1.1.80 and EC 2.1.1.100. 11-cis-retinyl-palmitate hydrolase 11-cis-retinyl palmitate + H(2)O = 11-cis-retinol + palmitate. Activated by bile salts. All-trans-retinyl-palmitate hydrolase All-trans-retinyl palmitate + H(2)O = all-trans-retinol + palmitate. Requires detergents for activity. L-rhamnono-1,4-lactonase L-rhamnono-1,4-lactone + H(2)O = L-rhamnonate. 5-(3,4-diacetoxybut-1-ynyl)-2,2'-bithiophene deacetylase 5-(3,4-diacetoxybut-1-ynyl)-2,2'-bithiophene + H(2)O = 5-(3-hydroxy-4-acetoxybut-1-ynyl)-2,2'-bithiophene + acetate. A highly specific enzyme from Tagetes patula. FAEE synthase Fatty-acyl-ethyl-ester synthase FAEES A long-chain-fatty-acyl ethyl ester + H(2)O = a long-chain-fatty acid + ethanol. In the reverse reaction, forms ethyl esters from fatty acids and ethanol in the absence of coenzyme A or ATP. Best substrates are unsaturated octadecanoic acids; palmitate, stearate and arachidonate also act, more slowly. Xylono-1,4-lactonase D-xylono-1,4-lactone + H(2)O = D-xylonate. Acetylcholinesterase Choline esterase I Cholinesterase True cholinesterase Also catalyzes transacetylations. Acts on a variety of acetic esters. http://purl.uniprot.org/mim/112100 Acetylcholine + H(2)O = choline + acetate. Cetraxate benzylesterase Cetraxate benzyl ester + H(2)O = cetraxate + benzyl alcohol. Acts on a number of benzyl esters of substituted phenyl propanoates, and on the benzyl esters of phenylalanine and tyrosine. Alkylacetylglycerol acetylhydrolase Acetylalkylglycerol acetylhydrolase Hydrolysis of the acetyl group from the 1-alkyl-2-acetyl and 1-alkyl-3-acetyl substrates occurs at apparently identical rates. Differs from EC 3.1.1.34 since 1,2-diacetyl-sn-glycerols are not substrates. It also differs from EC 3.1.1.47. 2-acetyl-1-alkyl-sn-glycerol + H(2)O = 1-alkyl-sn-glycerol + acetate. Acetylxylan esterase Deacetylation of xylans and xylo-oligosaccharides. Does not act on acetylated mannan or pectin. Catalyzes the hydrolysis of acetyl groups from polymeric xylan, acetylated xylose, acetylated glucose, alpha-napthyl acetate, p-nitrophenyl acetate but not from triacetylglycerol. Ferulic acid esterase Hydroxycinnamoyl esterase Cinnamoyl ester hydrolase Feruloyl esterase They are sometimes called hemicellulase accessory enzymes, since they help xylanases and pectinases to break down plant cell wall hemicellulose. Feruloyl-polysaccharide + H(2)O = ferulate + polysaccharide. p-nitrophenol acetate and methyl ferulate are poorer substrates. Catalyzes the hydrolysis of the 4-hydroxy-3-methoxycinnamoyl (feruloyl) group from an esterified sugar, which is usually arabinose in 'natural' substrates. All microbial ferulate esterases are secreted into the culture medium. Cutinase Cutin hydrolase It is however inactive toward several esters that are substrates for non-specific esterases. Cutin, a polymeric structural component of plant cuticles, is an hydroxy fatty acid polymer, usually C(16) or C(18) and that contains one to three hydroxyl groups. The enzyme from several fungal sources also hydrolyzes the p-nitrophenyl esters of hexadecanoic acid. Cutin + H(2)O = cutin monomers. Poly(3HB) depolymerase Poly(3-hydroxybutyrate) depolymerase Poly(HA) depolymerase Poly(HA(SCL)) depolymerase Poly((R)-hydroxyalkanoic acid) depolymerase PHB depolymerase Reaction also occurs with esters of other short-chain-length (C(1)-C(5)) hydroxyalkanoic acids (HA). There are two types of polymers: native (intracellular) granules are amorphous and have an intact surface layer; denatured (extracellular) granules either have no surface layer or a damaged surface layer and are partially crystalline. Poly((R)-3-hydroxybutanoate)(n) + H(2)O = poly((R)-3-hydroxybutanoate)(n-1 to 5) + poly((R)-3-hydroxybutanoate)(1-5). PHA depolymerase Poly(3-hydroxyoctanoate) depolymerase Poly((R)-3-hydroxyoctanoate) hydrolase PHO depolymerase Poly(3HO) depolymerase Poly(HA) depolymerase Poly(HA(MCL)) depolymerase Poly((R)-hydroxyalkanoic acid) depolymerase It also hydrolyzes p-nitrophenyl esters of fatty acids. Hydrolyzes the polyester poly(oxycarbonyl((R)-2-pentylethylene)) to oligomers. Polymers of short-chain-length hydroxyalkanoic acids such as poly((R)-3-hydroxybutanoic acid) and poly((R)-3-hydroxypentanoic acid) are not hydrolyzed. The main product after prolonged incubation is the dimer. Besides hydrolyzing polymers of 3-hydroxyoctanoic acid, the enzyme also hydrolyzes other polymers derived from medium-chain-length (C(6)-C(12)) hydroxyalkanoic acids and copolymers of mixtures of these. Acyloxyacyl hydrolase It also possesses a wide range of phospholipase and acyltransferase activities (e.g. EC 3.1.1.4, EC 3.1.1.5, EC 3.1.1.32 and EC 3.1.1.52), hydrolyzing diacylglycerol and phosphatidyl compounds, but not triacylglycerols. Both residues carry 3-(acyloxy)acyl groups on N-2 and O-3. The substrate is lipid A on the reducing end of the toxic lipopolysaccharide (LPS) of Salmonella typhimurium and related organisms. It consists of diglucosamine, beta-D-GlcN-(1->6)-D-GlcN, attached by glycosylation on O-6 of its non-reducing residue, phosphorylated on O-4 of this residue and on O-1 of its potentially reducing residue. It has a preference for saturated C(12)-C(16) acyl groups. The enzyme from human leukocytes detoxifies the lipid by hydrolyzing the secondary acyl groups from O-3 of the 3-hydroxyacyl groups on the disaccharide (LPS). 3-(acyloxy)acyl group of bacterial toxin = 3-hydroxyacyl group of bacterial toxin + a fatty acid. PNAE Polyneuridine aldehyde esterase Polyneuridine-aldehyde esterase Also acts on akuammidine aldehyde (the 16-epimer of polyneuridine aldehyde). Following hydrolysis of this indole alkaloid ester, the carboxylic acid decarboxylates spontaneously giving the sarpagan skeleton. Polyneuridine aldehyde + H(2)O = 16-epivellosimine + CO(2) + methanol. Hormone-sensitive lipase HSL The enzyme shows little preference for the fatty acids in the triacylglycerol, although there is some increase in activity with decreasing chain length. This enzyme is a serine hydrolase. (3) Monoacylglycerol + H(2)O = glycerol + a carboxylate. The enzyme activity is increased in response to hormones that elevate intracellular levels of cAMP. Compared with other lipases, hormone-sensitive lipase has a uniquely broad substrate specificity. It hydrolyzes all acylglycerols (triacylglycerol, diacylglycerol and monoacylglycerol) as well as cholesteryl esters, steroid fatty acid esters, retinyl esters and p-nitrophenyl esters. (1) Diacylglycerol + H(2)O = monoacylglycerol + a carboxylate. It exhibits a preference for the 1-or 3-ester bond of its acylglycerol substrate compared with the 2-ester bond. (2) Triacylglycerol + H(2)O = diacylglycerol + a carboxylate. Cholinesterase Benzoylcholinesterase Butyrylcholine esterase Choline esterase II (unspecific) Acylcholine acylhydrolase Pseudocholinesterase Non-specific cholinesterase http://purl.uniprot.org/mim/177400 An acylcholine + H(2)O = choline + a carboxylate. Acts on a variety of choline esters and a few other compounds. Acetylajmalan esterase Acetylajmaline esterase 2-beta-(R)-17-O-acetylajmalan:acetylesterase AAE (2) 17-O-acetylnorajmaline + H(2)O = norajmaline + acetate. Highly specific for the substrates 17-O-acetylajmaline and 17-O-acetylnorajmaline as the structurally related acetylated alkaloids vinorine, vomilenine, 1,2-dihydrovomilenine and 1,2-dihydroraucaffricine cannot act as substrates. (1) 17-O-acetylajmaline + H(2)O = ajmaline + acetate. Responsible for the last stages in the biosynthesis of the indole alkaloid ajmaline. Exodeoxyribonucleases producing 5'-phosphomonoesters E.coli exonuclease I Exonuclease I Exodeoxyribonuclease I Similar enzymes; mammalian DNase III, exonuclease IV, T2-and T4-induced exodeoxyribonucleases. The Escherichia coli enzyme hydrolyzes glucosylated DNA. Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. Preference for single-stranded DNA. Exonuclease III E.coli exonuclease III Exodeoxyribonuclease III Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. http://purl.uniprot.org/mim/225750 Similar enzyme: Haemophilus influenzae exonuclease. Has endonucleolytic activity near apurinic sites on DNA. Preference for double-stranded DNA. Lambda exonuclease Exodeoxyribonuclease (lambda-induced) Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates. Does not attack single-strand breaks. Similar enzymes: T4, T5 and T7 exonucleases, mammalian DNase IV. Preference for double-stranded DNA. Exodeoxyribonuclease (phage SP3-induced) Phage SP3 DNase DNA 5'-dinucleotidohydrolase Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates. Preference for single-stranded DNA. Exonuclease V Exodeoxyribonuclease V E.coli exonuclease V Preference for double-stranded DNA. Possesses DNA-dependent ATPase activity. Acts endonucleolytically on single-stranded circular DNA. Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides. Similar enzyme: Haemophilus influenzae ATP-dependent DNase. E.coli exonuclease VII Exodeoxyribonuclease VII Exonuclease VII Preference for single-stranded DNA. Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates. Similar enzyme: Micrococcus luteus exonuclease. Exoribonucleases producing 5'-phosphomonoesters Ribonuclease II Exoribonuclease II Preference for single-stranded RNA. The enzyme processes 3'-terminal extra-nucleotides of monomeric tRNA precursors, following the action of EC 3.1.26.5. Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. Similar enzymes: RNase Q, RNase BN, RNase PIII, RNase Y. Exoribonuclease H Found in certain oncorna viruses and animal cells. Exonucleolytic cleavage to 5'-phosphomonoester oligonucleotides in both 5'- to 3'- and 3'- to 5'- directions. Attacks RNA in duplex with DNA strand. Oligonucleotidase Exonucleolytic cleavage of oligonucleotides to yield nucleoside 5'-phosphates. Also hydrolyzes NAD(+) to NMN and AMP. Poly(A)-specific ribonuclease Cleaves poly(A) in either the single-or double-stranded form. Exonucleolytic cleavage of poly(A) to 5'-AMP. RNase D Ribonuclease D Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides. Alteration of the 3'-terminal base has no effect on the rate of hydrolysis whereas modification of the 3'-terminal sugar has a major effect. tRNA terminating with a 3'-phosphate is completely inactive. This enzyme can convert a tRNA precursor into a mature tRNA. Magnesium or cobalt or manganese Exoribonucleases producing 3'-phosphomonoesters Yeast ribonuclease Exonucleolytic cleavage to nucleoside 3'-phosphates. Similar enzyme: RNase U4. Exonucleases active with either ribo- or deoxyribonucleic acid and producing 5'-phosphomonoesters Venom phosphodiesterase Venom exonuclease Preference for single-stranded substrate. Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. Similar enzymes: hog kidney phosphodiesterase, Lactobacillus exonuclease. Exonucleases active with either ribo- or deoxyribonucleic acid and producing 3'-phosphomonoesters Spleen exonuclease 3'-exonuclease Spleen phosphodiesterase Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates. Preference for single-stranded substrate. Similar enzymes: Lactobacillus acidophilus nuclease, Bacillus subtilis nuclease, salmon testis nuclease. Thiolester hydrolases Acetyl-CoA deacylase Acetyl-CoA acylase Acetyl-CoA hydrolase Acetyl-CoA + H(2)O = CoA + acetate. Formyl-CoA hydrolase Formyl-CoA + H(2)O = CoA + formate. Acetoacetyl-CoA hydrolase Acetoacetyl-CoA + H(2)O = CoA + acetoacetate. S-formylglutathione hydrolase Also hydrolyzes S-acetylglutathione, more slowly. S-formylglutathione + H(2)O = glutathione + formate. S-succinylglutathione hydrolase S-succinylglutathione + H(2)O = glutathione + succinate. Acyl-[acyl-carrier-protein] hydrolase S-acyl fatty acid synthase thioesterase Oleoyl-[acyl-carrier-protein] hydrolase Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-carrier-protein] + oleate. Acts on [acyl-carrier-protein] thioesters of fatty acids from C(12) to C(18), but the derivative of oleic acid is hydrolyzed much more rapidly than any other compound tested. Ubiquitin carboxy-terminal esterase Ubiquitin thioesterase Ubiquitin thiolesterase Ubiquitin carboxy-terminal hydrolase http://purl.uniprot.org/mim/400042 Ubiquitin C-terminal thioester + H(2)O = ubiquitin + a thiol. http://purl.uniprot.org/mim/132700 Also acts on AMP-ubiquitin. Acts on esters formed between thiols such as dithiothreitol or glutathione and the C-terminal glycine residue of the polypeptide ubiquitin. http://purl.uniprot.org/mim/415000 [Citrate-(pro-3S)-lyase] thioesterase [Citrate-(pro-3S)-lyase] thiolesterase Citrate lyase deacetylase [Citrate (pro-3S)-lyase](acetyl form) + H(2)O = [citrate (pro-3S)-lyase](thiol form) + acetate. Hydrolysis by this enzyme inactivates EC 4.1.3.6. (S)-methylmalonyl-CoA hydrolase (S)-methylmalonyl-CoA + H(2)O = methylmalonate + CoA. ADP-dependent short-chain-acyl-CoA hydrolase Acyl-CoA + H(2)O = CoA + a carboxylate. Requires ADP; inhibited by NADH. Maximum activity is shown with propanoyl-CoA. ADP-dependent medium-chain-acyl-CoA hydrolase Acyl-CoA + H(2)O = CoA + a carboxylate. Maximum activity is shown with nonanoyl-CoA. Requires ADP; inhibited by NADH. Palmitoyl-CoA hydrolase Long-chain fatty-acyl-CoA hydrolase Also hydrolyzes CoA thioesters of other long-chain fatty acids. Palmitoyl-CoA + H(2)O = CoA + palmitate. http://purl.uniprot.org/mim/607748 Acyl-CoA hydrolase Broad specificity for medium-to long-chain acyl-CoA. Acyl-CoA + H(2)O = CoA + a carboxylate. Insensitive to NAD(+) (cf. EC 3.1.2.19). Dodecanoyl-acyl-carrier-protein hydrolase Dodecyl-[acyl-carrier protein] hydrolase Lauryl-[acyl-carrier protein] hydrolase Dodecanoyl-[acyl-carrier-protein] hydrolase Acts on the acyl-carrier protein thioester of C(12) and, with a much lower activity, C(14) fatty acids. The derivative of oleic acid is hydrolyzed very slowly. Dodecanoyl-[acyl-carrier-protein] + H(2)O = [acyl-carrier-protein] + dodecanoate. Palmitoyl-protein thioesterase Palmitoyl-protein hydrolase Hydrolyzes fatty acids from S-acylated cysteine residues in proteins, palmitoyl cysteine and palmitoyl-CoA. http://purl.uniprot.org/mim/204300 Specific for long-chain thioesters of fatty acids. http://purl.uniprot.org/mim/256730 Palmitoyl-protein + H(2)O = palmitate + protein. 4-hydroxybenzoyl-CoA thioesterase This enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway. 4-hydroxybenzoyl-CoA + H(2)O = 4-hydroxybenzoate + CoA. Phenylacetyl-CoA hydrolase Phenylglyoxylyl-CoA + H(2)O = phenylglyoxylate + CoA. This is the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1. Bile acid-coenzyme A hydrolase Bile-acid-CoA hydrolase Deoxycholoyl-CoA + H(2)O = CoA + deoxycholate. Choloyl-CoA, 3-dehydrocholoyl-CoA and chenodeoxycholoyl-CoA can also act as substrates, but acetyl-CoA, isovaleryl-CoA, palmitoyl-CoA and phenylacetyl-CoA cannot. Choloyl-coenzyme A thioesterase Peroxisomal acyl-CoA thioesterase 2 Choloyl-CoA hydrolase PTE-2 Chenodeoxycholoyl-coenzyme A thioesterase Also acts on chenodeoxycholoyl-CoA and to a lesser extent on short-and medium-to long-chain acyl-CoA's, and other substrates, including trihydroxycoprostanoyl-CoA, hydroxymethylglutaryl-CoA and branched chain acyl-CoA's, all of which are present in peroxisomes. Choloyl-CoA + H(2)O = cholate + CoA. The enzyme is strongly inhibited by CoA and may be involved in controlling CoA levels in the peroxisome. Succinyl-CoA hydrolase Succinyl-CoA acylase Succinyl-CoA + H(2)O = CoA + succinate. 3-hydroxyisobutyryl-CoA hydrolase 3-hydroxy-2-methylpropanoyl-CoA + H(2)O = CoA + 3-hydroxy-2-methylpropanoate. Also hydrolyzes 3-hydroxypropanoyl-CoA. http://purl.uniprot.org/mim/250620 Hydroxymethylglutaryl-CoA hydrolase (S)-3-hydroxy-3-methylglutaryl-CoA + H(2)O = CoA + 3-hydroxy-3-methylglutarate. Glyoxalase II Hydroxyacylglutathione hydrolase Also hydrolyzes S-acetoacetylglutathione, more slowly. S-(2-hydroxyacyl)glutathione + H(2)O = glutathione + a 2-hydroxy carboxylate. http://purl.uniprot.org/mim/138760 Glutathione thioesterase Glutathione thiolesterase S-acylglutathione + H(2)O = glutathione + a carboxylate. Endodeoxyribonucleases producing 5'-phosphomonoesters Pancreatic DNase Thymonuclease Deoxyribonuclease I DNase Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products. Preference for double-stranded DNA. Similar enzymes: streptococcal DNase (streptodornase), T4 endonuclease II, T7 endonuclease II, Escherichia coli endonuclease I, 'nicking' nuclease of calf thymus, colicin E2 and E3. Deoxyribonuclease IV (phage-T(4)-induced) Endonuclease IV Deoxyribonuclease IV (phage T4-induced) Endodeoxyribonuclease IV (phage T4-induced) Endodeoxyribonuclease IV (phage T(4)-induced) Similar enzymes: DNase V (mammalian), Aspergillus sojae DNase, Bacillus subtilis endonuclease, T4 endonuclease III, T7 endonuclease I, Aspergillus DNase K2, vaccinia virus DNase VI, Saccharomyces cerevisiae DNase, Chlorella DNase. Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products. Preference for single-stranded DNA. Type I site-specific deoxyribonuclease Type I restriction enzyme Large group of enzymes that have an absolute requirement for ATP (or dATP) and S-adenosyl-L-methionine. Multifunctional proteins which also catalyze the reactions of EC 2.1.1.72 and EC 2.1.1.73, with similar site specificity. Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates; ATP is simultaneously hydrolyzed. See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/ They recognize specific short DNA sequences and cleave at sites remote from the recognition sequence. Type II restriction enzyme Type II site-specific deoxyribonuclease Magnesium Large group of enzymes which recognize specific short DNA sequences and cleave either within, or at a short specific distance from, the recognition site. Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/ Type III site-specific deoxyribonuclease Type III restriction enzyme See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/ Exist as complexes with enzymes of similar specificity listed under EC 2.1.1.72 or EC 2.1.1.73. Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. Recognize specific short DNA sequences and cleave a short distance away from the recognition sequence. Has an absolute requirement for ATP, but does not hydrolyze it; S-adenosyl-L-methionine stimulates the reaction, but is not absolutely required. Streptomyces glaucescens exocytoplasmic endodeoxyribonuclease 5'-CC-3'-preferring endodeoxyribonuclease CC-preferring endodeoxyribonuclease Streptomyces glaucescens exocytoplasmic endonuclease Endonucleolytic cleavage to give 5'-phosphooligonucleotide end-products, with a preference for cleavage within the sequence CC. Produces nicks, generating double-stranded fragments with 5'-and/or 3'-protruding single-stranded tails. Prefers CC sites in double-stranded circular and linear DNA. Greater affinity for double-stranded than single-stranded DNA. Magnesium Endonuclease V Deoxyribonuclease V Escherichia coli endodeoxyribonuclease V DNase V Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-phosphate. Previously classified erroneously as EC 3.1.22.3. Endodeoxyribonucleases producing other than 5'-phosphomonoesters Deoxyribonuclease II DNase II Lysosomal DNase II Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products. Preference for double-stranded DNA. Similar enzymes: crab testis DNase, snail DNase, salmon testis DNase, liver acid DNase, human acid DNases of gastric mucosa and cervix. Aspergillus DNase K1 Aspergillus deoxyribonuclease K(1) Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products. Preference for single-stranded DNA. SpCCe1 Holliday junction resolvase Holliday junction resolvase Endonuclease RuvC Holliday junction endonuclease CCE1 Crossover junction endoribonuclease RuvC endonuclease Resolving enzyme CCE1 RusA endonuclease Endo X3 Cruciform-cutting endonuclease Holliday junction-cleaving endonuclease Endonuclease VII Crossover junction endodeoxyribonuclease Holliday junction nuclease Hje endonuclease RusA Holliday junction resolvase Holliday junction-resolving endoribonuclease Endonuclease X3 The enzyme from Saccharomyces cerevisiae has no endonuclease or exonuclease activity on single-stranded or double-stranded DNA molecules that do not contain Holliday junctions. Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction). Deoxyribonuclease X Inhibited by single-stranded DNA, ATP and AMP. Preference for supercoiled DNA; little activity on linear double-stranded DNA. Endonucleolytic cleavage of supercoiled plasma DNA to linear DNA duplexes. Site-specific endodeoxyribonucleases specific for altered bases Endodeoxyribonuclease (pyrimidine dimer) Deoxyribonuclease (pyrimidine dimer) Endonucleolytic cleavage near pyrimidine dimers to products with 5'-phosphate. Acts on a damaged strand, 5' from the damaged site. Similar enzymes: T4 endonuclease V, Escherichia coli endonuclease III and V, correndonuclease II. Endoribonucleases producing 5'-phosphomonoesters Physarum polycephalum ribonuclease Endonucleolytic cleavage to 5'-phosphomonoester. Ribonuclease IX Endonucleolytic cleavage of poly(U) or poly(C) to fragments terminated by 3'-hydroxy and 5'-phosphate groups. Acts on poly(U) and poly(C), with a higher affinity for poly(C), but does not act on poly(A) or poly(G). Ribonuclease Z tRNA 3 endonuclease tRNase Z RNase Z 3 tRNase No cofactor requirements. Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule. Ribonuclease alpha Specific for O-methylated RNA. Endonucleolytic cleavage to 5'-phosphomonoester. Ribonuclease 3 RNase III Ribonuclease III An endoribonuclease that cleaves double-stranded RNA molecules. RNase III is involved in both rRNA processing and mRNA processing and decay. Specificity is conferred by negative determinants, i.e., the presence of certain Watson-Crick base-pairs at specific positions that strongly inhibit cleavage. Endonucleolytic cleavage to 5'-phosphomonoester. The cleavage can be either a single-stranded nick or double-stranded break in the RNA, depending in part upon the degree of base-pairing in the region of the cleavage site. RNase H Ribonuclease H Endoribonuclease H Acts on RNA-DNA hybrids. Endonucleolytic cleavage to 5'-phosphomonoester. http://purl.uniprot.org/mim/610333 Ribonuclease P Similar enzyme: RNase P3. Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. Essential for tRNA processing; generates 5'-termini of mature tRNA molecules. Poly(A)-specific ribonuclease Ribonuclease IV Endoribonuclease IV Forms oligonucleotides with an average chain length of 10. Endonucleolytic cleavage of poly(A) to fragments terminated by 3'-hydroxy and 5'-phosphate groups. Ribonuclease P4 Endonucleolytic cleavage of RNA, removing 3'-extranucleotides from tRNA precursor. RNase M5 Ribonuclease M5 5S ribosomal maturation nuclease Converts the 5S-rRNA precursor from Bacillus subtilis into 5S-rRNA, with 5'-phosphate and 3'-hydroxy groups. Endonucleolytic cleavage of RNA, removing 21 and 42 nucleotides, respectively, from the 5'- and 3'-termini of a 5S-rRNA precursor. Ribonuclease (poly-(U)-specific) Endonucleolytic cleavage of poly(U) to fragments terminated by 3'-hydroxy and 5'-phosphate groups. Forms oligonucleotides with chain length 6-12. Endoribonucleases producing other than 5'-phosphomonoesters Ribonuclease II Ribonuclease T(2) Ribonuclease T2 Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates. Similar enzymes: plant RNase, Escherichia coli RNase I, RNase N2, microbial RNase II. rRNA endonuclease Alpha-sarcin Also acts on bacterial rRNA. Hydrolysis of the phosphodiester linkage between guanosine and adenosine residues at one specific position in 28S rRNA from rat ribosomes. Bacillus subtilis ribonuclease Similar enzymes: Azotobacter agilis RNase, Proteus mirabilis RNase. Endonucleolytic cleavage to 2',3'-cyclic nucleotides. Ribonuclease T(1) Aspergillus oryzae ribonuclease Guanyloribonuclease Ribonuclease T1 RNase N1 RNase N2 Similar enzymes: Neurospora crassa RNase N1 and N2, Ustilago sphaerogena RNase, Chalaropsis RNase, Bacillus subtilis RNase, microbial RNase I. Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in G-P with 2',3'-cyclic phosphate intermediates. Ribonuclease U2 Ribonuclease U(2) Similar enzymes: RNase U3, Pleospora RNase, Trichoderma koningi RNase III. Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in A-P or G-P with 2',3'-cyclic phosphate intermediates. Ribonuclease I Pancreatic RNase Pancreatic ribonuclease RNase A RNase RNase I Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates. Similar enzymes: venom RNase, Thiobacillus thioparus RNase, Xenopus laevis RNase, Rhizopus oligosporus RNase, ribonuclease M. Enterobacter ribonuclease Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates. Preference for cleavage at CpA. Homopolymers of A, U or G are not hydrolyzed. RNase F Ribonuclease F Cleavage takes place between a cytosine and an adenine. Endonucleolytic cleavage of RNA precursor into two, leaving 5'-hydroxy and 3'-phosphate groups. Endoribonuclease V Ribonuclease V Also hydrolyzes poly(U). Hydrolysis of poly(A), forming oligoribonucleotides and ultimately 3'-AMP. tRNA-intron endonuclease tRNA-splicing endonuclease Endonucleolytic cleavage of pre-tRNA, producing 5'-hydroxy and 2',3'-cyclic phosphate termini, and specifically removing the intron. The enzyme catalyzes the final stage in the maturation of tRNA molecules. Phosphoric monoester hydrolases Alkaline phosphomonoesterase Glycerophosphatase Alkaline phosphatase Phosphomonoesterase http://purl.uniprot.org/mim/146300 Active at a high pH optimum. Zinc Magnesium Also catalyzes transphosphorylations. http://purl.uniprot.org/mim/241510 A phosphate monoester + H(2)O = an alcohol + phosphate. http://purl.uniprot.org/mim/241500 Wide specificity. Some enzymes hydrolase diphosphate (cf. EC 3.6.1.1). Glucose-1-phosphatase Also acts, more slowly, on alpha-D-galactose 1-phosphate. Alpha-D-glucose 1-phosphate + H(2)O = D-glucose + phosphate. Hexose diphosphatase Fructose-bisphosphatase Fructose 1,6-bisphosphatase The animal enzyme also acts on sedoheptulose 1,7-bisphosphate. http://purl.uniprot.org/mim/229700 D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate. Trehalose-phosphatase Trehalose 6-phosphate phosphatase Trehalose 6-phosphate + H(2)O = trehalose + phosphate. Bisphosphoglycerate phosphatase http://purl.uniprot.org/mim/222800 http://purl.uniprot.org/mim/261670 2,3-bisphospho-D-glycerate + H(2)O = 3-phospho-D-glycerate + phosphate. Methylphosphothioglycerate phosphatase S-methyl-3-phospho-1-thio-D-glycerate + H(2)O = S-methyl-1-thio-D-glycerate + phosphate. Histidinol-phosphatase L-histidinol phosphate + H(2)O = L-histidinol + phosphate. Protein phosphatase-2A Protein phosphatase-2C Protein phosphatase-2B Serine/threonine specific protein phosphatase Phosphoprotein phosphatase Protein phosphatase-1 A phosphoprotein + H(2)O = a protein + phosphate. The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1). A group of enzymes removing the serine-or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48). [Phosphorylase] phosphatase [Phosphorylase a] + 4 H(2)O = 2 [phosphorylase b] + 4 phosphate. Phosphoglycolate phosphatase 2-phosphoglycolate + H(2)O = glycolate + phosphate. Glycerol-2-phosphatase Glycerol 2-phosphate + H(2)O = glycerol + phosphate. Acid phosphatase Glycerophosphatase Acid phosphomonoesterase Phosphomonoesterase Wide specificity. Also catalyzes transphosphorylations. A phosphate monoester + H(2)O = an alcohol + phosphate. http://purl.uniprot.org/mim/200950 Phosphoglycerate phosphatase D-glycerate 2-phosphate + H(2)O = D-glycerate + phosphate. Glycerol-1-phosphatase The enzyme from Saccharomyces cerevisiae also acts on propane-1,2-diol 1-phosphate, but not on a variety of other phosphate esters. Glycerol 1-phosphate + H(2)O = glycerol + phosphate. The Dunaliella enzyme acts more rapidly on sn-glycerol 1-phosphate than on the 3-phosphate. Mannitol-1-phosphatase D-mannitol 1-phosphate + H(2)O = D-mannitol + phosphate. Sugar-phosphatase Sugar phosphate + H(2)O = sugar + phosphate. Has a wide specificity, acting on aldohexose 1-phosphates, ketohexose 1-phosphates, aldohexose 6-phosphates, ketohexose 6-phosphates, both phosphate ester bonds of fructose 1,6-bisphosphate, phosphoric esters of disaccharides, and on pentose and triose phosphates, but at a slower rate. Sucrose-phosphatase Sucrose 6(F)-phosphate + H(2)O = sucrose + phosphate. Inositol-1(or 4)-monophosphatase Myo-inositol monophosphatase Inositol 1-phosphatase Inositol-phosphate phosphatase Myo-inositol-1(or 4)-phosphate phosphohydrolase Myo-inositol-1(or 4)-monophosphatase Myo-inositol 1-phosphatase Myo-inositol-1-phosphatase L-myo-inositol-1-phosphate phosphatase Inositol monophosphate phosphatase Inositol phosphatase Myo-inositol phosphate + H(2)O = myo-inositol + phosphate. It also acts on adenosine 2'-phosphate (but not the 3'-or 5'-phosphates), sn-glycerol 3-phosphate and glycerol 2-phosphate, but does not act on inositol bisphosphates or more phosphorylated inositols. Acts on five of the six isomers of myo-inositol phosphate, all except myo-inositol 2-phosphate, but does not act on myo-inositol bearing more than one phosphate group. 4-phytase 6-phytase (rdfs:label based on 1L-numbering system and not 1D-numbering) Phytate 6-phosphatase Phytase Myo-inositol hexakisphosphate + H(2)O = 1D-myo-inositol 1,2,3,4,5-pentakisphosphate + phosphate. Phosphatidylglycerophosphatase Phosphatidylglycerophosphate + H(2)O = phosphatidylglycerol + phosphate. ADP-phosphoglycerate phosphatase Also acts on 2,3-diphosphoglycerate. 3-(ADP)-2-phosphoglycerate + H(2)O = 3-(ADP)-glycerate + phosphate. N-acylneuraminate-9-phosphatase N-acylneuraminate 9-phosphate + H(2)O = N-acylneuraminate + phosphate. Phosphoserine phosphatase http://purl.uniprot.org/mim/172480 O-phospho-L(or D)-serine + H(2)O = L(or D)-serine + phosphate. Nucleotidase A wide specificity for 2', 3'-and 5'-nucleotides; also hydrolyzes glycerol phosphate and 4-nitrophenyl phosphate. A nucleotide + H(2)O = a nucleoside + phosphate. 2'(3')-polynucleotidase Polynucleotide 3'-phosphatase A 3'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate. Also hydrolyzes nucleoside 2'-, 3'-and 5'-monophosphates, but only 2'-and 3'-phosphopolynucleotides. Polynucleotide 5'-phosphatase 5'-polynucleotidase Polynucleotide 5'-triphosphatase Does not act on nucleoside monophosphates. A 5'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate. Induced in Escherichia coli by T-even phages. 3'-deoxynucleotidase Deoxynucleotide 3'-phosphatase Also catalyzes the selective removal of 3'-phosphate groups from DNA and oligodeoxynucleotides. Induced in Escherichia coli by T-even phages. A deoxynucleoside 3'-phosphate + H(2)O = a deoxynucleoside + phosphate. Thymidylate 5'-nucleotidase Thymidylate 5'-phosphatase Acts on 5-methyl-dCMP and on TMP, but more slowly than on dTMP. Thymidylate + H(2)O = thymidine + phosphate. Phosphatidylinositol 4,5-bisphosphate phosphatase Phosphatidylinositol-bisphosphatase Type II inositol-1,4,5-trisphosphate 5-phosphatase Phosphoinositide 5-phosphatase Inositol 1,4,5-triphosphate 5-phosphomonoesterase IP(3) phosphatase Inositol triphosphate 5-phosphomonoesterase Polyphosphoinositol lipid 5-phosphatase Triphosphoinositide phosphomonoesterase Type II inositol polyphosphate 5-phosphatase Phosphatidyl-inositol-bisphosphate phosphatase PtdIns(4,5)P(2) phosphatase Diphosphoinositide phosphatase Phosphatidyl-myo-inositol-4,5-bisphosphate phosphatase Triphosphoinositide phosphatase These enzymes can also remove the 5-phosphate from Ins(1,4,5)P(3) and/or Ins(1,3,4,5)P(4). http://purl.uniprot.org/mim/300555 http://purl.uniprot.org/mim/309000 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate. All of them can use either or both of PtdIns(4,5)P(2) and PtdIns(3,4,5)P(3) as substrates; this is the main property that distinguishes them from EC 3.1.3.56. They are thought to use inositol lipids rather than inositol phosphates as substrates in vivo. They are a diverse family of enzymes, with differing abilities to catalyze two or more of the four reactions listed. Sedoheptulose-bisphosphatase Sedoheptulose-1,7-bisphosphatase Sedoheptulose 1,7-bisphosphate + H(2)O = sedoheptulose 7-phosphate + phosphate. 3-phosphoglycerate phosphatase Wide specificity, but 3-phosphoglycerate is the best substrate. D-glycerate 3-phosphate + H(2)O = D-glycerate + phosphate. Streptomycin-6-phosphatase Also acts on dihydrostreptomycin 3'-alpha,6-bisphosphate and streptidine 6-phosphate. Streptomycin 6-phosphate + H(2)O = streptomycin + phosphate. Phosphatidic acid phosphatase Phosphatidate phosphatase A 3-sn-phosphatidate + H(2)O = a 1,2-diacyl-sn-glycerol + phosphate. Guanidinodeoxy-scyllo-inositol-4-phosphatase 1-guanidino-1-deoxy-scyllo-inositol 4-phosphate + H(2)O = 1-guanidino-1-deoxy-scyllo-inositol + phosphate. 4-nitrophenylphosphatase A number of other substances, including phenyl phosphate, 4-nitrophenyl sulfate, acetyl phosphate and glycerol phosphate, are not substrates. 4-nitrophenyl phosphate + H(2)O = 4-nitrophenol + phosphate. [Glycogen-synthase-D] phosphatase [Glycogen-synthase D] + H(2)O = [glycogen-synthase I] + phosphate. The product is EC 2.4.1.11. [Pyruvate dehydrogenase (lipoamide)]-phosphatase [Pyruvate dehydrogenase (lipoamide)] phosphate + H(2)O = [pyruvate dehydrogenase (lipoamide)] + phosphate. A mitochondrial enzyme associated with EC 1.2.4.1 in the pyruvate dehydrogenase complex. http://purl.uniprot.org/mim/608782 [Acetyl-CoA carboxylase]-phosphatase Simultaneously dephosphorylates and activates EC 6.4.1.2. [Acetyl-CoA carboxylase] phosphate + H(2)O = [acetyl-CoA carboxylase] + phosphate. Not identical with EC 3.1.3.17 or EC 3.1.3.43. Acts similarly on EC 1.1.1.88, EC 2.4.1.1 and EC 2.4.1.11, and dephosphorylates phosphoprotamine and 4-nitrophenyl phosphate. 3-deoxy-manno-octulosonate-8-phosphatase 3-deoxy-D-manno-octulosonate 8-phosphate + H(2)O = 3-deoxy-D-manno-octulosonate + phosphate. Fructose-2,6-bisphosphate 2-phosphatase Fructose-2,6-bisphosphatase The enzyme copurifies with EC 2.7.1.105 (cf. EC 3.1.3.54). Beta-D-fructose 2,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate. Reductase phosphatase [Hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase [Hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + H(2)O = [hydroxymethylglutaryl-CoA reductase (NADPH)] + phosphate. Acts on the product of the reaction catalyzed by EC 2.7.11.31, simultaneously dephosphorylating and activating EC 1.1.1.34. Phosphotyrosine phosphatase Protein-tyrosine-phosphatase PTPase Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2. Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. [Pyruvate kinase]-phosphatase [Pyruvate kinase] phosphate + H(2)O = [pyruvate kinase] + phosphate. Simultaneously dephosphorylates and activates EC 2.7.1.40 which has been inactivated by protein kinase. 5'-nucleotidase A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate. Wide specificity for 5'-nucleotides. http://purl.uniprot.org/mim/266120 Sorbitol-6-phosphatase Acts, very slowly, on hexose 6-phosphates. Sorbitol 6-phosphate + H(2)O = sorbitol + phosphate. Dolichyl-phosphatase Dolichol phosphate phosphatase Dolichyl phosphate + H(2)O = dolichol + phosphate. Branched-chain oxo-acid dehydrogenase phosphatase [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphatase A mitochondrial enzyme associated with the 3-methyl-2-oxobutanoate dehydrogenase complex. Simultaneously dephosphorylates and activates EC 1.2.4.4 which has been inactivated by phosphorylation. [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate + H(2)O = [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] + phosphate. [Myosin-light-chain] phosphatase Myosin light-chain kinase phosphatase Myosin phosphatase The holoenzyme dephosphorylates myosin light chains and EC 2.7.11.31, but not myosin; the catalytic subunit acts on all three substrates. Composed of three subunits. [Myosin light-chain] phosphate + H(2)O = [myosin light-chain] + phosphate. Fructose-2,6-bisphosphate 6-phosphatase Cf. EC 3.1.3.46. Beta-D-fructose 2,6-bisphosphate + H(2)O = beta-D-fructofuranose 2-phosphate + phosphate. Caldesmon-phosphatase Dephosphorylation activates the calmodulin-and actin-binding ability of caldesmon. [Caldesmon] phosphate + H(2)O = [caldesmon] + phosphate. Inositol-polyphosphate 5-phosphatase Inosine triphosphatase D-myo-inositol(1,4,5)/(1,3,4,5)-polyphosphate 5-phosphatase L-myo-inositol 1,4,5-trisphosphate-monoesterase InsP(3)/Ins(1,3,4,5)P(4) 5-phosphatase D-myo-inositol 1,4,5-triphosphate 5-phosphatase Inositol phosphate 5-phosphomonoesterase 5PTase D-myo-inositol 1,4,5-trisphosphate 5-phosphatase Inositol 1,4,5-trisphosphate phosphatase Inositol-1,4,5-trisphosphate/1,3,4,5-tetrakisphosphate 5-phosphatase Ins(1,4,5)P(3) 5-phosphatase Inositol-1,4,5-trisphosphate 5-phosphatase Myo-inositol-1,4,5-trisphosphate 5-phosphatase Type I inositol-polyphosphate phosphatase Inositol polyphosphate-5-phosphatase Inositol trisphosphate phosphomonoesterase This enzyme is distinguished from the family of enzymes classified under EC 3.1.3.36 by its inability to dephosphorylate inositol lipids. (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H(2)O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate. (1) D-myo-inositol 1,4,5-trisphosphate + H(2)O = myo-inositol 1,4-bisphosphate + phosphate. Inositol polyphosphate 1-phosphatase Inositol-1,4-bisphosphate 1-phosphatase Does not act on inositol 1-phosphate, inositol 1,4,5-trisphosphate or inositol 1,3,4,5-tetrakisphosphate. 1D-myo-inositol 1,4-bisphosphate + H(2)O = 1D-myo-inositol 4-phosphate + phosphate. Acts on inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate (forming inositol 3,4-bisphosphate) with similar V(max) for both substrates, but with a 5 times higher affinity for the bisphosphate. Xylitol-5-phosphatase Sugar-terminal-phosphatase Acts on sugars and polyols phosphorylated on the terminal carbon, with a preference for sugars with a D-erythro-configuration, e.g. good substrates are glucose 6-phosphate, mannose 6-phosphate, 6-phosphogluconate, erythrose 4-phosphate and xylitol 5-phosphate. D-glucose 6-phosphate + H(2)O = D-glucose + phosphate. Alkylacetylglycerophosphatase Involved in the biosynthesis of thrombocyte activating factor in animal tissues. 1-alkyl-2-acetyl-sn-glycero-3-phosphate + H(2)O = 1-alkyl-2-acetyl-sn-glycerol + phosphate. 3'-nucleotidase Wide specificity for 3'-nucleotides. A 3'-ribonucleotide + H(2)O = a ribonucleoside + phosphate. Phosphoenolpyruvate phosphatase Phosphoenolpyruvate + H(2)O = pyruvate + phosphate. Also acts, more slowly, on a wide range of other monophosphates. Multiple inositol-polyphosphate phosphatase Inositol-1,3,4,5-tetrakisphosphate 3-phosphatase Inositol 1,3,4,5-tetrakisphosphate 3-phosphomonoesterase Inositol 1,3,4,5-tetrakisphosphate-5-phosphomonoesterase Inositol tetrakisphosphate phosphomonoesterase Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase MIPP Also acts on Ins(1,3,4,5)P(4) to yield Ins(1,4,5)P(3). Myo-inositol hexakisphosphate + H(2)O = myo-inositol pentakisphosphate (mixed isomers) + phosphate. 2-carboxy-D-arabinitol-1-phosphatase 2-carboxy-D-arabinitol 1-phosphate + H(2)O = 2-carboxy-D-arabinitol + phosphate. D-myo-inositol-1,3-bisphosphate 3-phosphohydrolase Phosphatidylinositol-3-phosphatase Inositol 1,3-bisphosphate phosphatase Phosphatidyl-3-phosphate 3-phosphohydrolase Inositol-1,3-bisphosphate 3-phosphatase Inositol-polyphosphate 3-phosphatase This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyzes Ins(1,3)P(2) to Ins-1-P. 1-phosphatidyl-1D-myo-inositol 3-phosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol + phosphate. Inositol polyphosphate 4-phosphatase Inositol-3,4-bisphosphate 4-phosphatase Phosphoinositide 4-phosphatase Phosphatidylinositol-3,4-bisphosphate 4-phosphatase D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase Inositol polyphosphate 4-phosphatase type II Magnesium-independent. This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyzes Ins(1,3,4)P(3) to Ins(1,3)P(2). 1-phosphatidyl-myo-inositol 3,4-bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate. It also converts Ins(3,4)P(2) into Ins-3-P. Phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase Phosphatidylinositol 3,4,5-trisphosphate + H(2)O = phosphatidylinositol 4,5-bisphosphate + phosphate. http://purl.uniprot.org/mim/176920 http://purl.uniprot.org/mim/158350 http://purl.uniprot.org/mim/137800 http://purl.uniprot.org/mim/153480 This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyzes Ins(1,3,4,5)P(4) to Ins(1,4,5)P(3). http://purl.uniprot.org/mim/605309 Magnesium Does not dephosphorylate inositol 4,5-bisphosphate. http://purl.uniprot.org/mim/276950 2-deoxyglucose-6-phosphate phosphatase 2-deoxyglucose-6-phosphatase Also active toward fructose 1-phosphate. 2-deoxy-D-glucose 6-phosphate + H(2)O = 2-deoxy-D-glucose + phosphate. Glucosylglycerol 3-phosphatase 2-(beta-D-glucosyl)-sn-glycerol-3-phosphate + H(2)O = 2-(beta-D-glucosyl)-sn-glycerol + phosphate. Acts with EC 2.4.1.213 to form glucosylglycerol, an osmolyte that endows cyanobacteria with resistance to salt. 3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase Phosphoadenylate 3'-nucleotidase 3'(2'),5'-bisphosphate nucleotidase DPNPase 3'-phosphoadenylylsulfate 3'-phosphatase Also acts on 3'-phosphoadenylylsulfate, and on the corresponding 2'-phosphates. Adenosine 3',5'-bisphosphate + H(2)O = adenosine 5'-phosphate + phosphate. Mannosyl-3-phosphoglycerate phosphatase 2(alpha-D-mannosyl)-3-phosphoglycerate + H(2)O = 2(alpha-D-mannosyl)-D-glycerate + phosphate. Magnesium The enzyme from Pyrococcus horikoshii is specific for alpha-D-mannosyl-3-phosphoglycerate and forms part of the pathway for the synthesis of mannosylglycerate. 2-phosphosulfolactate phosphatase ComB phosphatase (2R)-phosphosulfolactate phosphohydrolase (2R)-2-phospho-3-sulfolactate + H(2)O = (2R)-3-sulfolactate + phosphate. This enzyme can also hydrolyze phosphate monoesters of (R)-2-hydroxycarboxylic acids such as (S)-2-phospho-3-sulfolactate and (R)-2-phosphomalate, which, presumably, bind to the enzyme in opposite orientations. The enzyme from Methanococcus jannaschii acts on both stereoisoimers of the substrate and also hydrolyzes a number of phosphate monoesters of (S)-2-hydroxycarboxylic acids, including 2-phosphomalate, 2-phospholactate and 2-phosphoglycolate. Magnesium 5-phytase Myo-inositol hexakisphosphate + H(2)O = 1L-myo-inositol 1,2,3,4,6-pentakisphosphate + phosphate. The enzyme attacks the product of the above reaction more slowly to yield Ins(1,2,3)P(3). Alpha-ribazole phosphatase In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC 2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73) and CobS (EC 2.7.8.26) catalyze reactions in the nucleotide loop assembly pathway, which convert adenosylcobinamide (AdoCbi) into adenosylcobalamin (AdoCbl). Alpha-ribazole 5'-phosphate + H(2)O = alpha-ribazole + phosphate. The second branch of the nuclotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by the bifunctional enzyme CobU. CobS catalyzes the final step in adenosylcobalamin biosynthesis, which is the condensation of AdoCbi-GDP with alpha-ribazole to yield adenosylcobalamin. CobT and CobC are involved in 5,6-dimethylbenzimidazole activation whereby 5,6-dimethylbenzimidazole is converted to its riboside, alpha-ribazole. PNP phosphatase Vitamin B6 (pyridoxine) phosphatase Pyridoxal phosphatase Vitamin B6-phosphate phosphatase PLP phosphatase Vitamin B(6) (pyridoxine) phosphatase Vitamin B(6)-phosphate phosphatase Pyridoxal 5'-phosphate + H(2)O = pyridoxal + phosphate. This reaction can also be carried out by EC 3.1.3.1 and EC 3.1.3.2, but these enzymes have very broad substrate specificities. Magnesium This enzyme is specific for phosphorylated vitamin B6 compounds: it acts not only on pyridoxal phosphate (PLP), but also on pyridoxine phosphate (PNP), pyridoxamine phosphate (PMP), 4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate. PHOSPHO1 3X11A Phosphoethanolamine/phosphocholine phosphatase (2) Phosphocholine + H(2)O = choline + phosphate. The enzyme is highly specific for phosphoethanolamine and phosphocholine. Magnesium or cobalt or manganese (1) O-phosphoethanolamine + H(2)O = ethanolamine + phosphate. Lipid-phosphate phosphatase Hydroxy fatty acid phosphatase Dihydroxy fatty acid phosphatase Hydroxy lipid phosphatase Soluble epoxide hydrolase The best substrates for this enzyme are 10-hydroxy-9-(phosphonooxy)octadecanoates, with the threo-form being a better substrate than the erythro-form. The phosphatase activity is not found in plant EC 3.3.2.10 or in mammalian EC 3.3.2.9. The enzyme from mammals is a bifunctional enzyme: the N-terminal domain exhibits lipid-phosphate-phosphatase activity and the C-terminal domain has the activity of EC 3.3.2.10. Magnesium (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H(2)O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate. E-1 enolase-phosphatase Acireductone synthase The acireductone represents a branch point in the methione salvage pathway as it is used in the formation of formate, CO and 3-(methylthio)propanoate by EC 1.13.11.53 and of formate and 4-methylthio-2-oxobutanoate either by a spontaneous reaction under aerobic conditions or by EC 1.13.11.54. This bifunctional enzyme first enolizes the substrate to form the intermediate 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate, which is then dephosphorylated to form the acireductone 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one. 5-(methylthio)-2,3-dioxopentyl phosphate + H(2)O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate. Phytase Myo-inositol-hexaphosphate 3-phosphohydrolase Phytate 6-phosphatase 3-phytase Phytate 3-phosphatase Phytate 1-phosphatase 1-phytase Myo-inositol hexakisphosphate + H(2)O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate. Glucose-6-phosphatase Wide distribution in animal tissues. Also catalyzes potent transphosphorylations from carbamoyl phosphate, hexose phosphates, diphosphate, phosphoenolpyruvate and nucleoside di-and triphosphates, to D-glucose, D-mannose, 3-methyl-D-glucose, or 2-deoxy-D-glucose (cf. EC 2.7.1.62, EC 2.7.1.79, and EC 3.9.1.1). D-glucose 6-phosphate + H(2)O = D-glucose + phosphate. http://purl.uniprot.org/mim/232200 Endoribonucleases active with either ribo- or deoxyribonucleic acid and producing 5'-phosphomonoesters Single-stranded-nucleate endonuclease Aspergillus nuclease S(1) Endonuclease S1 Aspergillus nuclease S1 Deoxyribonuclease S1 Zinc Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products. Similar enzymes: Neurospora crassa nuclease, mung bean nuclease, Penicillium citrinum nuclease P1. Preference for single-stranded substrate. Serratia marcescens nuclease Endonuclease (Serratia marcescens) Hydrolyzes double-or single-stranded substrate. Similar enzymes: silkworm nuclease, potato nuclease, Azotobacter nuclease. Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products. Endoribonucleases active with either ribo- or deoxyribonucleic acid and producing 3'-phosphomonoesters Micrococcal endonuclease Micrococcal nuclease Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products. Similar enzymes: Chlamydomonas nuclease, spleen phosphodiesterase, spleen endonuclease. Hydrolyzes double-or single-stranded substrate. Phosphoric diester hydrolases PDE I 5'-nucleotide phosphodiesterase Nucleotide pyrophosphatase/phosphodiesterase I 5'-PDase Oligonucleate 5'-nucleotidohydrolase Exonuclease I Phosphodiesterase 5'-phosphodiesterase Orthophosphoric diester phosphohydrolase 5' nucleotide phosphodiesterase/alkaline phosphodiesterase I 5'-NPDase Phosphodiesterase I 5'NPDE Alkaline phosphodiesterase 5'-PDE 5'-exonuclease http://purl.uniprot.org/mim/208000 http://purl.uniprot.org/mim/602475 Hydrolyzes both ribonucleotides and deoxyribonucleotides. Has low activity toward polynucleotides. A 3'-phosphate terminus on the substrate inhibits hydrolysis. Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides. Phosphatidylinositol phospholipase C 1-phosphatidyl-D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase Phosphoinositidase C PI-PLC 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase Phosphoinositide phospholipase C Triphosphoinositide phosphodiesterase Monophosphatidylinositol phosphodiesterase They show activity toward phosphatidylinositol, i.e., the activity of EC 4.6.1.13 in vitro at high calcium concentration. 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. These enzymes form some of the cyclic phosphate Ins(cyclic 1,2)P(4,5)P(2) as well as Ins(1,4,5)P(3). http://purl.uniprot.org/mim/610725 Sphingomyelin phosphodiesterase Acid sphingomyelinase Neutral sphingomyelinase http://purl.uniprot.org/mim/257200 Has very little activity on phosphatidylcholine. http://purl.uniprot.org/mim/607616 Sphingomyelin + H(2)O = N-acylsphingosine + choline phosphate. Serine-ethanolaminephosphate phosphodiesterase Serine phosphoethanolamine + H(2)O = serine + ethanolamine phosphate. Acts only on those phosphodiesters that have ethanolamine as a component part of the molecule. ACP phosphodiesterase [Acyl-carrier-protein] phosphodiesterase [Acyl-carrier-protein] 4'-pantetheine-phosphohydrolase ACP hydrolyase The enzyme cleaves acyl-[acyl-carrier-protein] species with acyl chains of 6-16 carbon atoms although it appears to demonstrate a preference for the unacylated acyl-carrier-protein (ACP) and short-chain ACPs over the medium-and long-chain species. Activation of apo-ACP to form the holoenzyme is carried out by EC 2.7.8.7. Holo-[acyl-carrier-protein] + H(2)O = 4'-phosphopantetheine + apo-[acyl-carrier-protein]. Deletion of the gene encoding this enzyme abolishes ACP prosthetic-group turnover in vivo. Adenylyl-[glutamate--ammonia ligase] hydrolase Adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H(2)O = adenylate + [L-glutamate:ammonia ligase (ADP-forming)]. 2',3'-cyclic-nucleotide 2'-phosphodiesterase Nucleoside 2',3'-cyclic phosphate + H(2)O = nucleoside 3'-phosphate. Similar reactions are carried out by EC 3.1.27.3 and EC 3.1.27.5. Also hydrolyzes 3'-nucleoside monophosphates and bis-4-nitrophenyl phosphate, but not 3'-deoxynucleotides. Cyclic AMP phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase Acts on 3',5'-cyclic AMP, 3',5'-cyclic dAMP, 3',5'-cyclic IMP, 3',5'-cyclic GMP and 3',5'-cyclic CMP. http://purl.uniprot.org/mim/610475 http://purl.uniprot.org/mim/610024 Nucleoside 3',5'-cyclic phosphate + H(2)O = nucleoside 5'-phosphate. Glycerophosphocholine phosphodiesterase sn-glycero-3-phosphocholine + H(2)O = choline + sn-glycerol 3-phosphate. Also acts on sn-glycero-3-phosphoethanolamine. Lipophosphodiesterase I Lecithinase C Clostridium oedematiens beta- and gamma-toxins Phospholipase C Clostridium welchii alpha-toxin The bacterial enzyme also acts on sphingomyelin and phosphatidylinositol. Zinc The enzyme from seminal plasma does not act on phosphatidylinositol. A phosphatidylcholine + H(2)O = 1,2-diacylglycerol + choline phosphate. 3',5'-cyclic-GMP phosphodiesterase http://purl.uniprot.org/mim/268000 http://purl.uniprot.org/mim/610475 Guanosine 3',5'-cyclic phosphate + H(2)O = guanosine 5'-phosphate. http://purl.uniprot.org/mim/163500 2',3'-cyclic-nucleotide 3'-phosphodiesterase Cyclic-CMP phosphodiesterase An enzyme from liver acts on 2',3'-cyclic CMP more rapidly than on the purine derivatives; it also hydrolyzes the corresponding 3',5'-cyclic phosphates, more slowly. Nucleoside 2',3'-cyclic phosphate + H(2)O = nucleoside 2'-phosphate. The brain enzyme acts on 2',3'-cyclic AMP more rapidly than on the UMP or CMP derivatives. This latter enzyme has been called cyclic-CMP phosphodiesterase. Glycerophosphocholine cholinephosphodiesterase No activity on sn-3-glycerophosphoethanolamine. sn-glycero-3-phosphocholine + H(2)O = glycerol + choline phosphate. Lysophospholipase D Alkylglycerophosphoethanolamine phosphodiesterase 1-alkyl-sn-glycero-3-phosphoethanolamine + H(2)O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine. Also acts on acyl and choline analogs. Choline phosphatase Lecithinase D Lipophosphodiesterase II Phospholipase D A phosphatidylcholine + H(2)O = choline + a phosphatidate. Also acts on other phosphatidyl esters. CMP-sialate hydrolase CMP-N-acylneuraminate phosphodiesterase CMP-N-acylneuraminate + H(2)O = CMP + N-acylneuraminate. Sphingomyelin phosphodiesterase D Sphingomyelin + H(2)O = ceramide phosphate + choline. Does not act on phosphatidylcholine, but hydrolyzes 2-lysophosphatidylcholine to choline and 2-lysophosphatidate. Glycerol-1,2-cyclic-phosphate 2-phosphodiesterase Glycerol 1,2-cyclic phosphate + H(2)O = glycerol 1-phosphate. Acts on both stereoisomers of the substrate and also, more slowly, on 3',5'-cyclic AMP and on 2',3'-cyclic AMP. D-myo-inositol 1:2-cyclic phosphate 2-phosphohydrolase Inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase 1,2-cyclic-inositol-phosphate phosphodiesterase Glycerophosphoinositol inositolphosphodiesterase D-inositol 1,2-cyclic phosphate 2-phosphohydrolase D-myo-inositol 1,2-cyclic phosphate 2-phosphohydrolase 1-(sn-glycero-3-phospho)-1D-myo-inositol + H(2)O = glycerol + 1D-myo-inositol 1-phosphate. This enzyme also hydrolyzes Ins(cyclic 1,2)P to Ins-1-P. sn-glycero(3)phosphoinositol glycerophosphohydrolase sn-glycero-3-phospho-1-inositol glycerophosphohydrolase Glycerophosphoinositol glycerophosphodiesterase 1-(sn-glycero-3-phospho)-1D-myo-inositol + H(2)O = myo-inositol + sn-glycerol 3-phosphate. N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase Alpha-N-acetylglucosaminyl phosphodiesterase Lysosomal alpha-N-acetylglucosaminidase Glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H(2)O = N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose. Acts on a variety of compounds in which N-acetyl-D-glucosamine is alpha-linked to a phosphate group, including the biosynthetic in intermediates of the high mannose oligosaccharide components of some lysosomal enzymes and the product of EC 2.7.8.17. Glycerophosphoryl diester phosphodiesterase Glycerophosphodiester phosphodiesterase Broad specificity for glycerophosphodiesters; glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol and bis(glycerophospho)-glycerol are hydrolyzed. A glycerophosphodiester + H(2)O = an alcohol + sn-glycerol 3-phosphate. Dolichylphosphate-glucose phosphodiesterase Dolichyl beta-D-glucosyl phosphate + H(2)O = dolichyl phosphate + D-glucose. Mannosylphosphodolichol phosphodiesterase Dolichylphosphate-mannose phosphodiesterase Dolichyl beta-D-mannosyl phosphate + H(2)O = dolichyl phosphate + D-mannose. Glycosylphosphatidylinositol phospholipase D Phosphatidylinositol phospholipase D GPI-PLD Phosphatidylinositol-specific phospholipase D Glycoprotein phospholipase D Phosphatidylinositol-glycan-specific phospholipase D It therefore cleaves proteins from the lipid part of the glycosylphosphatidylinositol (GPI) anchors, but does so by hydrolysis, whereas EC 4.6.1.14 does so by elimination. This enzyme is also active when O-4 of the glucosamine is substituted by carrying the oligosaccharide that can link a protein to the structure. It acts on plasma membranes only after solubilization of the substrate with detergents or solvents, but it may act on intracellular membranes. 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H(2)O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + phosphatidate. Glucose-1-phospho-D-mannosylglycoprotein phosphodiesterase Alpha-glucose-1-phosphate phosphodiesterase 6-(D-glucose-1-phospho)-D-mannosylglycoprotein + H(2)O = alpha-D-glucose 1-phosphate + D-mannosylglycoprotein. This enzyme is specific for the product of EC 2.7.8.19. Triphosphoric monoester hydrolases dGTPase Deoxyguanosinetriphosphate triphosphohydrolase Deoxy-GTPase dGTP + H(2)O = deoxyguanosine + triphosphate. Also acts on GTP. Sulfuric ester hydrolases Aryl-sulfate sulphohydrolase Arylsulfatase Sulfatase A phenol sulfate + H(2)O = a phenol + sulfate. A group of enzymes with rather similar specificities. Chondro-6-sulfatase Also acts on the saturated analog and N-acetyl-D-galactosamine 4,6-disulfate, but not higher oligosaccharides, nor any 4-sulfate. 4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine 6-sulfate + H(2)O = 4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine + sulfate. N-sulfoglucosamine-6-sulfatase Disulfoglucosamine-6-sulfatase May be identical with EC 3.1.6.14. N,6-O-disulfo-D-glucosamine + H(2)O = N-sulfo-D-glucosamine + sulfate. Arylsulfatase B Chondroitinase Chondroitinsulfatase N-acetylgalactosamine-4-sulfatase http://purl.uniprot.org/mim/272200 Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate. Also acts on N-acetylglucosamine 4-sulfate. http://purl.uniprot.org/mim/253200 Iduronate-2-sulfatase Chondroitinsulfatase Hydrolysis of the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate and heparin. http://purl.uniprot.org/mim/309900 Glucosamine-6-sulfatase Chondroitinsulfatase N-acetylglucosamine-6-sulfatase http://purl.uniprot.org/mim/252940 May be identical with EC 3.1.6.11. Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. N-sulfoglucosamine-3-sulfatase Chondroitinsulfatase Hydrolysis of the 3-sulfate groups of the N-sulfo-D-glucosamine 3-O-sulfate units of heparin. The enzyme from Flavobacterium heparinum also hydrolyzes N-acetyl-D-glucosamine 3-O-sulfate; the mammalian enzyme acts only on the disulfated residue. Monomethyl-sulfatase Monomethyl sulfate + H(2)O = methanol + sulfate. Highly specific; does not act on monoethyl sulfate, monoisopropyl sulfate or monododecyl sulfate. D-lactate-2-sulfatase Highly specific. (S)-2-O-sulfolactate + H(2)O = (S)-lactate + sulfate. Glucuronate-2-sulfatase Chondro-2-sulfatase Hydrolysis of the 2-sulfate groups of the 2-O-sulfo-D-glucuronate residues of chondroitin sulfate, heparin and heparitin sulfate. Does not act on iduronate 2-sulfate residues (cf. EC 3.1.6.13). Arylsulfatase C Steryl-sulfate sulfohydrolase Steroid sulfatase Steryl-sulfatase Also acts on some related steryl sulfates. 3-beta-hydroxyandrost-5-en-17-one 3-sulfate + H(2)O = 3-beta-hydroxyandrost-5-en-17-one + sulfate. http://purl.uniprot.org/mim/308100 Glucosulfatase Glycosulfatase Also acts on other sulfates of mono-and disaccharides and on adenosine 5'-sulfate. D-glucose 6-sulfate + H(2)O = D-glucose + sulfate. Chondroitinsulfatase Chondroitinase Galactose-6-sulfate sulfatase N-acetylgalactosamine-6-sulfatase http://purl.uniprot.org/mim/253000 Hydrolysis of the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of chondroitin sulfate and of the D-galactose 6-sulfate units of keratan sulfate. Choline-sulfatase Choline sulfate + H(2)O = choline + sulfate. Cellulose-polysulfatase Hydrolysis of the 2- and 3-sulfate groups of the polysulfates of cellulose and charonin. Cerebroside-sulfatase Arylsulfatase A A cerebroside 3-sulfate + H(2)O = a cerebroside + sulfate. http://purl.uniprot.org/mim/272200 http://purl.uniprot.org/mim/250100 Also hydrolyzes ascorbate 2-sulfate and many phenol sulfates. Hydrolyzes galactose-3-sulfate residues in a number of lipids. Chondro-4-sulfatase Also acts on the saturated analog but not on higher oligosaccharides, nor any 6-sulfates. 4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine 4-sulfate + H(2)O = 4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine + sulfate. Diphosphoric monoester hydrolases Prenyl-diphosphatase Prenyl-pyrophosphatase Farnesyl diphosphate is the best substrate so far tested. Prenyl diphosphate + H(2)O = prenol + diphosphate. Guanosine-3',5'-bis(diphosphate) 3'-diphosphatase Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase (ppGpp)ase Penta-phosphate guanosine-3'-diphosphohydrolase Penta-phosphate guanosine-3'-pyrophosphohydrolase Guanosine 3',5'-bis(diphosphate) + H(2)O = guanosine 5'-diphosphate + diphosphate. Monoterpenyl-pyrophosphatase Bornyl pyrophosphate hydrolase Monoterpenyl-diphosphatase Bornyl diphosphate hydrolase One has highest activity on sterically-hindered compounds such as (+)-bornyl diphosphate; another has highest activity on the diphosphates of primary alylic alcohols such as geraniol. A group of enzymes with varying specificity for the monoterpenol moiety. Monoterpenyl diphosphate + H(2)O = monoterpenol + diphosphate. Phosphoric triester hydrolases Phosphotriesterase A-esterase Aryldialkylphosphatase Paraoxon hydrolase Paraoxonase Aryltriphosphatase Inhibited by chelating agents. Previously regarded as identical with EC 3.1.1.2. Acts on organophosphorus compounds (such as paraoxon) including esters of phosphonic and phosphinic acids. An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol. Divalent cation Organophosphorus acid anhydrolase OPAA OPA anhydrase Tabunase Somanase DFPase Diisopropyl-fluorophosphatase Related to EC 3.1.8.1. Acts on phosphorus anhydride bonds (such as phosphorus-halide and phosphorus-cyanide) in organophosphorus compounds (including nerve gases). Divalent cation Inhibited by chelating agents. Diisopropyl fluorophosphate + H(2)O = diisopropyl phosphate + fluoride. Acting on sulfur-nitrogen bonds Acting on sulfur-nitrogen bonds N-sulfoglucosamine sulfohydrolase Sulfoglucosamine sulfamidase Sulphamidase http://purl.uniprot.org/mim/252900 N-sulfo-D-glucosamine + H(2)O = D-glucosamine + sulfate. Cyclamate sulfamatase Cyclamate sulfamidase Cyclamate sulfohydrolase Also readily hydrolyzes aliphatic sulfamates with 3 to 8 carbons. Cyclohexylsulfamate + H(2)O = cyclohexylamine + sulfate. Acting on carbon-phosphorus bonds Acting on carbon-phosphorus bonds Phosphonatase Phosphonoacetylaldehyde phosphonohydrolase 2-phosphonoacetylaldehyde phosphonohydrolase Phosphonoacetaldehyde hydrolase This enzyme destabilizes the C-P bond, by forming an imine between one of its lysine residues and the carbonyl group of the substrate, thus allowing this, normally stable, bond to be broken. Phosphonoacetaldehyde + H(2)O = acetaldehyde + phosphate. The mechanism is similar to that used by EC 4.1.2.13 to break a C-C bond. Magnesium Phosphonoacetate hydrolase Phosphonoacetate + H(2)O = acetate + phosphate. Zinc Phosphonopyruvate hydrolase PPH Cobalt or Magnesium or Manganese The reaction is not inhibited by phosphate but is inhibited by the phosphonates phosphonoformic acid, hydroxymethylphosphonic acid and 3-phosphonopropanoic acid. 3-phosphonopyruvate + H(2)O = pyruvate + phosphate. Highly specific for phosphonopyruvate as substrate. Acting on sulfur-sulfur bonds Acting on sulfur-sulfur bonds Trithionate hydrolase Trithionate + H(2)O = thiosulfate + sulfate + 2 H(+). Acting on carbon-sulfur bonds Acting on carbon-sulfur bonds Sulfite:UDP-glucose sulfotransferase UDP-sulfoquinovose synthase The enzyme from Arabidopsis thaliana is specific for UDP-Glc and sulfite. NAD NAD(+) appears to oxidize the substrate to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite can add; the reaction is completed when the substrate is rehydrogenated at C-4. UDP-glucose + sulfite = UDP-6-sulfoquinovose + H(2)O. 2-(2-hydroxyphenyl)benzenesulfinate desulfinase 2'-hydroxybiphenyl-2-sulfinate desulfinase 2-(2-hydroxyphenyl) benzenesulfinate:H(2)O hydrolase 2-(2-hydroxyphenyl)benzenesulfinate hydrolase HPBS desulfinase HBPSi desulfinase 2-(2'-hydroxyphenyl)benzenesulfinate desulfinase Dibenzothiophene desulfurization enzyme B 2-(2-hydroxyphenyl) benzenesulfinate sulfohydrolase FMN The enzyme has a narrow substrate specificity with biphenyl-2-sulfinate being the only other substrate known to date. 2'-hydroxybiphenyl-2-sulfinate + H(2)O = 2-hydroxybiphenyl + sulfite. Glycosylases Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds Glycogenase 1,4-alpha-D-glucan glucanohydrolase Alpha-amylase Endohydrolysis of 1,4-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides. Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. Sucrase-isomaltase Oligosaccharide alpha-1,6-glucosidase Isomaltase Oligo-1,6-glucosidase Differs from EC 3.2.1.33 in its preference for short-chain substrates and in its not requiring the 6-glucosylated residue to be at a branch point, i.e. linked at both C-1 and C-4. http://purl.uniprot.org/mim/222900 It also hydrolyzes isomaltulose (palatinose), isomaltotriose and panose, but has no action on glycogen or phosphorylase limit dextrin. The enzyme from intestinal mucosa is a single polypeptide chain that also catalyzes the reaction of EC 3.2.1.48. This enzyme, like EC 3.2.1.33, can release an alpha-1->6-linked glucose, whereas the shortest chain that can be released by EC 3.2.1.41, EC 3.2.1.142, and EC 3.2.1.68 is maltose. Hydrolysis of 1,6-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (alpha-amylase), and in isomaltose. Exo-1,4-beta-mannobiohydrolase Mannan 1,4-beta-mannobiosidase Mannan 1,4-mannobiosidase Hydrolysis of 1,4-beta-D-mannosidic linkages in 1,4-beta-D-mannans, to remove successive mannobiose residues from the non-reducing chain ends. Endo-alpha-1->6-D-mannanase Mannan endo-1,6-alpha-mannosidase Endo-1,6-beta-mannanase 1,6-beta-D-mannan mannanohydrolase Exo-1,6-beta-mannanase Random hydrolysis of 1,6-alpha-D-mannosidic linkages in unbranched 1,6-mannans. Endo-beta-galactosidase Blood-group-substance endo-1,4-beta-galactosidase Hydrolyzes the 1,4-beta-D-galactosyl linkages adjacent to a 1,3-alpha-D-galactosyl or N-acetylgalactosaminyl residues and a 1,2-alpha-D-fucosyl residue. Endohydrolysis of 1,4-beta-D-galactosidic linkages in blood group A and B substances. Endo-beta-galactosidase Keratan-sulfate endo-1,4-beta-galactosidase Hydrolyzes the 1,4-beta-D-galactosyl linkages adjacent to 1,3-beta-D-N-acetylglucosaminyl residues. Also acts on some non-sulfated oligosaccharides, but only acts on blood group substances when the 1,2-linked fucosyl residues have been removed (cf. EC 3.2.1.102). Endohydrolysis of 1,4-beta-D-galactosidic linkages in keratan sulfate. Steryl-beta-glucosidase Acts on glucosides of cholesterol and sitosterol, but not on some related sterols such as coprostanol. Cholesteryl-beta-D-glucoside + H(2)O = D-glucose + cholesterol. Strictosidine beta-glucosidase Strictosidine + H(2)O = D-glucose + strictosidine aglycone. Strictosidine is a precursor of indole alkaloids. Does not act on a number of closely related glycosides. Processing A-glucosidase I Mannosyl-oligosaccharide glucosidase Involved in the formation of high-mannose and complex glycoproteins. Exohydrolysis of the non-reducing terminal glucose residues in the mannosyl-oligosaccharide Glc(3)Man(9)GlcNAc(2). http://purl.uniprot.org/mim/606056 Also acts, more slowly, on the corresponding glycolipids and glycopeptides. Protein-glucosylgalactosylhydroxylysine glucosidase Requires free, positively charged epsilon-amino group of hydroxylysine. Protein alpha-D-glucosyl-1,2-beta-D-galactosyl-L-hydroxylysine + H(2)O = D-glucose + protein beta-D-galactosyl-L-hydroxylysine. Lactase The enzyme from intestinal mucosa is isolated as a complex which also catalyzes the reaction of EC 3.2.1.62 (cf. EC 3.2.1.23). http://purl.uniprot.org/mim/223000 http://purl.uniprot.org/mim/223100 Lactose + H(2)O = D-galactose + D-glucose. Endogalactosaminidase Endohydrolysis of 1,4-alpha-D-galactosaminidic linkages in poly(D-galactosamine). Dextranase Alpha-1,6-glucan-6-glucanohydrolase Endohydrolysis of 1,6-alpha-D-glucosidic linkages in dextran. Mucinaminylserine mucinaminidase D-galactosyl-3-(N-acetyl-beta-D-galactosaminyl)-L-serine + H(2)O = D-galactosyl-3-N-acetyl-beta-D-galactosamine + L-serine. Almond emulsin fucosidase I 1,3-alpha-L-fucosidase Hydrolysis of 1,3-linkages between alpha-L-fucose and N-acetylglucosamine residues in glycoproteins. Not identical with EC 3.2.1.63. 2-deoxyglucosidase A 2-deoxy-alpha-D-glucoside + H(2)O = 2-deoxy-D-glucose + an alcohol. Mannosidase 1A Man9-mannosidase ManI Mannosyl-oligosaccharide 1,2-alpha-mannosidase Mannosidase 1B Involved in the synthesis of glycoproteins. Hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2). Mannosidase II ManII Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase Involved in the synthesis of glycoproteins. Hydrolysis of the terminal 1,3- and 1,6-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man(5)(GlcNAc)(3). Dextran alpha-1,2 debranching enzyme Branched-dextran exo-1,2-alpha-glucosidase Hydrolysis of 1,2-alpha-D-glucosidic linkages at the branch points of dextrans and related polysaccharides, producing free D-glucose. Does not hydrolyze disaccharides or oligosaccharides containing linear 1,2-alpha-glucosidic linkages. Glucan 1,4-alpha-maltotriohydrolase Exo-maltotriohydrolase Hydrolysis of 1,4-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotriose residues from the non-reducing chain ends. Cf. EC 3.2.1.2, EC 3.2.1.60, and EC 3.2.1.98. The products of all these enzymes have the alpha-configuration. Amygdalin beta-glucosidase Highly specific; does not act on prunasin, linamarin, gentiobiose or cellobiose (cf. EC 3.2.1.21). (R)-amygdalin + H(2)O = (R)-prunasin + D-glucose. Prunasin beta-glucosidase (R)-prunasin + H(2)O = D-glucose + mandelonitrile. Highly specific; does not act on amygdalin, linamarin or gentiobiose (cf. EC 3.2.1.21). Vicianin beta-glucosidase (R)-vicianin + H(2)O = mandelonitrile + vicianose. Also hydrolyzes, more slowly, (R)-amygdalin and (R)-prunasin, but not gentiobiose, linamarin or cellobiose. Isoprimeverose-producing oligoxyloglucan hydrolase Oligoxyloglucan beta-glycosidase Hydrolysis of 1,4-beta-D-glucosidic links in oligoxyloglucans so as to remove successive isoprimeverose (i.e. alpha-xylo-1,6-beta-D-glucosyl-) residues from the non-reducing chain ends. Polymannuronate hydrolase Endohydrolysis of the D-mannuronide linkages of polymannuronate. Does not act on alginic acid, which is a copolymer of polymannuronate. Phospho-alpha-glucosidase Maltose-6'-phosphate glucosidase Hydrolyzes a variety of 6-phospho-D-glucosides, including maltose 6-phosphate, a,a-trehalose 6-phosphate, sucrose 6-phosphate and p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate (as a chromogenic substrate). The enzyme is activated by Fe(2+), Mn(2+), Co(2+) and Ni(2+). Maltose 6'-phosphate + H(2)O = D-glucose + D-glucose 6-phosphate. It is rapidly inactivated in air. Endo-glucosylceramidase Endoglycosylceramidase Endoglycoceramidase An enzyme from Rhodococcus sp. which degrades various acidic and neutral glycosphingolipids to oligosaccharides and ceramides, by cleaving a glucosyl bond. Oligoglycosylglucosylceramide + H(2)O = ceramide + oligoglycosylglucose. Does not act on monoglycosylceramides (cf. EC 3.2.1.62). 3-deoxy-2-octulosonidase The enzyme from a bacteriophage catalyzes the depolymerization of capsular polysaccharides containing 3-deoxy-2-octulosonide in the cell wall of Escherichia coli. Endohydrolysis of the beta-ketopyranosidic linkages of 3-deoxy-D-manno-2-octulosonate in capsular polysaccharides. Raucaffricine beta-glucosidase Raucaffricine + H(2)O = D-glucose + vomilenine. Highly specific; some other ajmalan glucoside alkaloids are hydrolyzed, more slowly. Coniferin beta-glucosidase A plant cell-wall enzyme involved in the biosynthesis of lignin. Also hydrolyzes syringin, 4-cinnamyl alcohol beta-glucoside and, more slowly, some other aryl beta-glycosides. Coniferin + H(2)O = D-glucose + coniferol. 1,6-alpha-L-fucosidase The enzyme from Aspergillus niger does not act on 1,2-, 1,3-, or 1,4-L-fucosyl linkages. Hydrolysis of 1,6-linkages between alpha-L-fucose and N-acetyl-D-glucosamine in glycopeptides such as immunoglobulin G glycopeptide and fucosyl-asialo-agalacto-fetuin. Glycyrrhizinate beta-glucuronidase The enzyme from Aspergillus niger is specific for the hydrolysis of the triterpenoid glycoside glycyrrhizinate from roots of Glycyrrhiza sp. Glycyrrhizinate + H(2)O = 1,2-beta-D-glucuronosyl-D-glucuronate + glycyrrhetinate. Endo-alpha-sialidase Poly(alpha-2,8-sialosyl) endo-N-acetylneuraminidase Endo-N-acetylneuraminidase Endoneuraminidase Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids. See also 4.2.2.15. Although the rdfs:label endo-N-acetylneuraminidase has also been used for this enzyme, this is misleading since its activity is not restricted to acetyl-substituted substrates. An exo-alpha-sialidase activity is listed as EC 3.2.1.18. Glycoprotein endo-alpha-1,2-mannosidase Hydrolysis of the terminal alpha-D-glucosyl-(1,3)-D-mannosyl unit from the GlcMan(9)(GlcNAc)(2) oligosaccharide component of the glycoprotein produced in the Golgi membrane. Involved in the synthesis of glycoproteins. Xylan alpha-1,2-glucuronosidase Hydrolysis of alpha-D-1,2-(4-O-methyl)glucuronosyl links in the main chain of hardwood xylans. Chitosanase The only constant property is the endohydrolysis of GlcN-GlcN links, which is common to all known chitosanases. A whole spectrum of chitosanases are now known that can hydrolyze various types of links in chitosan. One known chitosanase is limited to this link recognition, while the majority can also recognize GlcN-GlcNAc links or GlcNAc-GlcN links but not both. Endohydrolysis of beta-1,4-linkages between D-glucosamine residues in a partly acetylated chitosan. They also do not recognize GlcNAc-GlcNAc links in partly acetylated chitosan. Maltogenic alpha-amylase Glucan 1,4-alpha-maltohydrolase The product is alpha-maltose; cf. EC 3.2.1.2. Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains. Acts on starch and related polysaccharides and oligosaccharides. Difructose-anhydride synthase Produces difructose anhydride by the reverse reaction of partial hydrolysis, forming an alpha-fructosidic linkage. Bis-D-fructose 2',1:2,1'-dianhydride + H(2)O = inulobiose. Neopullulanase Cf. EC 3.2.1.41 and EC 3.2.1.57. Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose). Feraxan endoxylanase Glucuronoarabinoxylan endo-1,4-beta-xylanase High activity toward feruloylated arabinoxylans from cereal plant cell walls. Endohydrolysis of 1,4-beta-D-xylosyl links in some glucuronoarabinoxylans. Mannan exo-1,2-1,6-alpha-mannosidase Mannose residues linked alpha-D-1,3-are also released very slowly. Hydrolysis of 1,2-alpha-D- and 1,6-alpha-D- linkages in yeast mannan, releasing D-mannose. Alpha-glucosiduronase Alpha-glucuronidase Considerable differences in the specificities of the enzymes from different fungi for alpha-D-glucosiduronates have been reported. An alpha-D-glucuronoside + H(2)O = an alcohol + D-glucuronate. 1,4-beta-poly-N-acetylglucosaminidase Chitinase Poly-beta-glucosaminidase Chitodextrinase Random hydrolysis of N-acetyl-beta-D-glucosaminide 1,4-beta-linkages in chitin and chitodextrins. Some chitinases also display the activity defined in EC 3.2.1.17. Oligosaccharide lacto-N-biosylhydrolase Lacto-N-biosidase Lacto-N-hexaose (beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) is hydrolyzed to form first lacto-N-tetraose plus lacto-N-biose, with the subsequent formation of lactose. (1) Beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + H(2)O = beta-D-Gal-(1->3)-D-GlcNAc + beta-D-Gal-(1->4)-D-Glc. (2) Lacto-N-tetraose + H(2)O = lacto-N-biose + lactose. Asialo GM1 tetraose (beta-D-Gal-(1->3)-beta-D-GalNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) is hydrolyzed very slowly, but lacto-N-neotetraose (beta-D-Gal-(1->4)-beta-D-GalNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) is not a substrate. Oligosaccharides in which the non-reducing terminal Gal or the penultimate GlcNAc are replaced by fucose or sialic acid are not substrates. The enzyme from Streptomyces specifically hydrolyzes the terminal lacto-N-biosyl residue (beta-D-Gal-(1->3)-D-GlcNAc) from the non-reducing end of oligosaccharides with the structure beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->R). Malto-oligosyltrehalose trehalohydrolase 4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase Maltooligosyl trehalose trehalohydrolase Hydrolysis of alpha-(1->4)-D-glucosidic linkage in 4-alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to yield trehalose and alpha-(1->4)-D-glucan. R-enzyme Amylopectin-1,6-glucosidase Limit dextrinase Plant enzymes with little or no action on glycogen. Maltose is the smallest sugar it can release from an alpha-(1->6)-linkage. Action on amylopectin is incomplete, but action on alpha-limit dextrins is complete. Hydrolysis of (1->6)-alpha-D-glucosidic linkages in alpha- and beta-limit dextrins of amylopectin and glycogen, and in amylopectin and pullulan. Poly(ADP-ribose) glycohydrolase Hydrolyzes poly(ADP-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-ribose. Specific to (1''-2') linkage of ribose-ribose bond of poly(ADP-ribose). Alpha-Kdo-ase 3-deoxyoctulosonase Releases Kdo (alpha-and beta-linked 3-deoxy-D-manno-octulosonic acid) from different lipopolysaccharides, including Re-LPS from Escherichia coli and Salmonella, Rd-LPS from S.minnesota, and de-O-acyl-re-LPS. 4-methylumbelliferyl-alpha-Kdo (alpha-Kdo-OMec) is also a substrate. 3-deoxyoctulosonyl-lipopolysaccharide + H(2)O = 3-deoxyoctulosonic acid + lipopolysaccharide. Galactan 1,3-beta-galactosidase This enzyme removes not only free galactose, but also 6-glycosylated residues, e.g., (1->6)-beta-D-galactobiose, and galactose bearing oligosaccharide chains on O-6. Hence, it releases branches from (arabino-galacto-(1->6))-(1->3)-beta-D-galactans. Hydrolysis of terminal, non-reducing beta-D-galactose residues in (1->3)-beta-D-galactopyranans. Exo-beta-D-galactofuranosidase Beta-D-galactofuranosidase Exo-beta-galactofuranosidase Beta-galactofuranosidase The enzyme from Helminthosporium sacchari detoxifies helminthosporoside, a bis(digalactosyl)terpene produced by this fungus, by releasing its four molecules of bound galactose. Hydrolysis of terminal non-reducing beta-D-galactofuranosides, releasing galactose. Myrosinase Thioglucosidase Sinigrinase Sinigrase Has a wide specificity for thioglycosides. A thioglucoside + H(2)O = a sugar + a thiol. Beta-primeverosidase In addition to beta-primeverosides (i.e. 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranosides), it also hydrolyzes 6-O-(beta-D-apiofuranosyl)-beta-D-glucopyranosides and, less rapidly, beta-vicianosides and 6-O-(alpha-L-arabinofuranosyl)-beta-D-glucopyranosides, but not beta-glucosides. The enzyme is responsible for the formation of the alcoholic aroma in oolong and black tea. A 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranoside + H(2)O = 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranose + an alcohol. Geranyl-, linaloyl-, benzyl-and p-nitrophenol glycosides are all hydrolyzed. Polygalacturonase Pectinase Pectin depolymerase Random hydrolysis of 1,4-alpha-D-galactosiduronic linkages in pectate and other galacturonans. Oligoxyloglucan reducing-end-specific cellobiohydrolase The substrate is a hemicellulose found in plant cell walls. Hydrolysis of cellobiose from the reducing end of xyloglucans consisting of a beta-1,4-linked glucan carrying alpha-D-xylosyl groups on O-6 of the glucose residues. To be a substrate, the first residue must be unsubstituted, the second residue may bear a xylosyl group, whether further glycosylated or not, and the third residue, which becomes the new terminus by the action of the enzyme, is preferably xylosylated, but this xylose residue must not be further substituted. The enzyme is found in the fungus Geotrichum sp. M128. Xyloglucanendohydrolase XEG Xyloglucan endo-beta-1,4-glucanase Xyloglucanase Xyloglucan-specific endo-beta-1,4-glucanase 1,4-beta-D-glucan glucanohydrolase The enzyme from Aspergillus aculeatus is specific for xyloglucan and does not hydrolyze other cell-wall components. Xyloglucan + H(2)O = xyloglucan oligosaccharides. The reaction involves endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues. Endo-beta-mannosidase Mannosylglycoprotein endo-beta-mannosidase The substrate group is a substituent on N-4 of an asparagine residue in the glycoprotein. The enzyme was obtained from the lily, Lilium longiflorum. The mannose residue at the non-reducing end of the sequence may carry further alpha-D-mannosyl groups on O-3 or O-6, but such a substituent on O-3 of the beta-D-mannosyl group prevents the action of the enzyme. Hydrolysis of the alpha-D-mannosyl-(1->6)-beta-D-mannosyl-(1->4)-beta-D-N-acetylglucosaminyl-(1->4)-beta-D-N-acetylglucosaminyl sequence of glycoprotein to alpha-D-mannosyl-(1->6)-D-mannose and beta-D-N-acetylglucosaminyl-(1->4)-beta-D-N-acetylglucosaminyl sequences. 1-FEH w1 1-FEH w2 Inulinase Fructan beta-(2,1)-fructosidase 1-fructan exohydrolase Beta-(2-1)-linkage-specific fructan-beta-fructosidase 1-FEH II Beta-(2-1)-D-fructan fructohydrolase Beta-(2-1)fructan exohydrolase Hydrolysis of terminal, non-reducing 2,1-linked beta-D-fructofuranose residues in fructans. Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases. While the best substrates are the inulin-type fructans, such as 1-kestose (beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl alpha-D-glucopyranoside) and 1,1-nystose (beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl alpha-D-glucopyranoside), some (but not all) levan-type fructans can also be hydrolyzed, but more slowly (see EC 3.2.1.154). Possesses one of the activities of EC 3.2.1.80. Levanase 6-FEH Beta-(2-6)-fructan exohydrolase Fructan beta-(2,6)-fructosidase Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases. Hydrolysis of terminal, non-reducing 2,6-linked beta-D-fructofuranose residues in fructans. While the best substrates are the levan-type fructans such as 6-kestotriose (beta-D-fructofuranosyl-(2->6)-beta-D-fructofuranosyl alpha-D-glucopyranoside) and 6,6-kestotetraose (beta-D-fructofuranosyl-(2->6)-beta-D-fructofuranosyl-(2->6)-beta-D-fructofuranosyl alpha-D-glucopyranoside), some (but not all) inulin-type fructans can also be hydrolyzed, but more slowly (cf. EC 3.2.1.153). Possesses one of the activities of EC 3.2.1.80. Xyloglucan-specific exo-beta-1,4-glucanase The enzyme from Chrysosporium lucknowense is an endoglucanase, i.e. acquires the specificity of EC 3.2.1.151, when it acts on linear substrates without bulky substituents on the polymeric backbone (e.g. carboxymethylcellulose); however, it switches to an exoglucanase mode of action when bulky side chains are present (as in the case of xyloglucan). Xyloglucan + H(2)O = xyloglucan oligosaccharides (exohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan). Can also act on barley beta-glucan, but more slowly. Oligosaccharide reducing-end xylanase Rex Reducing end xylose-releasing exo-oligoxylanase Hydrolysis of 1,4-beta-D-xylose residues from the reducing end of oligosaccharides. It also acts on longer oligosaccharides that have this structure at their reducing ends. The enzyme acts rapidly on the beta-anomer of beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose, leaving the new reducing end in the a configuration. The penultimate residue must be xylose, but replacing either of the other two residues with glucose merely slows the rate greatly. Iota-carrageenase Unlike EC 3.2.1.81 and EC 3.2.1.83, this enzyme proceeds with inversion of the anomeric configuration. The main products of hydrolysis are iota-neocarratetraose sulfate and iota-neocarrahexaose sulfate. Iota-neocarraoctaose is the shortest substrate oligomer that can be cleaved. Iota-carrageenan differs from kappa-carrageenan by possessing a sulfo group on O-2 of the 3,6-anhydro-D-galactose residues, in addition to that present in the kappa-compound on O-4 of the D-galactose residues. Endohydrolysis of 1,4-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose-2-sulfate in iota-carrageenans. Agarase A33 Alpha-agarase Endohydrolysis of 1,3-alpha-L-galactosidic linkages in agarose, yielding agarotetraose as the major product. While the enzyme can also hydrolyze the highly sulfated agarose porphyran very efficiently, it cannot hydrolyze kappa-carrageenan and iota-carrageenan. Calcium The enzyme from Thalassomonas sp. can use agarose, agarohexaose and neoagarohexaose as substrate. The products of agarohexaose hydrolysis are dimers and tetramers, with agarotetraose being the predominant product, whereas hydrolysis of neoagarohexaose gives rise to two types of trimer. Alpha-neoagarooligosaccharide hydrolase Alpha-neoagaro-oligosaccharide hydrolase Alpha-NAOS hydrolase With neoagarotetraose as substrate, the products are predominantly agarotriose and 3,6-anhydro-L-galactose. In Vibrio sp. the actions of EC 3.2.1.81 and EC 3.2.1.159 can be used to degrade agarose to 3,6-anhydro-L-galactose and D-galactose. When neoagarohexaose is used as a substrate, the oligosaccharide is cleaved at the non-reducing end to produce 3,6-anhydro-L-galactose and agaropentaose, which is further hydrolyzed to agarobiose and agarotriose. Hydrolysis of the 1,3-alpha-L-galactosidic linkages of neoagaro-oligosaccharides that are smaller than a hexamer, yielding 3,6-anhydro-L-galactose and D-galactose. Xyloglucan-specific exo-beta-1,4-glucanase The enzyme from Chrysosporium lucknowense is an endoglucanase, i.e., acquires the specificity of EC 3.2.1.151, when it acts on linear substrates without bulky substituents on the polymeric backbone (e.g. carboxymethylcellulose). However, it switches to an exoglucanase mode of action when bulky side chains are present (as in the case of xyloglucan). Xyloglucan + H(2)O = xyloglucan oligosaccharides (exohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan). Can also act on barley beta-glucan, but more slowly. Isoflavonoid 7-O-beta-apiosyl-glucoside beta-glucosidase Furcatin hydrolase Isoflavonoid-7-O-beta(D-apiosyl-(1->6)-beta-D-glucoside) disaccharidase Beta-apiosyl-beta-glucosidase Daidzin and genistin are also substrates. Removes disaccharides from the natural substrates dalpatein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside and 7-hydroxy-2',4',5',6-tetramethoxy-7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside (dalnigrein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside) although it can also remove a single glucose residue from isoflavonoid 7-O-glucosides. 7-(beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranosyloxy)isoflavonoid + H(2)O = a 7-hydroxyisoflavonoid + beta-D-apiofuranosyl-(1->6)-D-glucose. Endo-beta-1,4-carrageenose 2,6,2'-trisulfate-hydrolase Lambda-carrageenase Endohydrolysis of beta-1,4-linkages in the backbone of lambda-carrageenan, resulting in the tetrasaccharide alpha-D-Galp2,6S(2)-(1->3)-beta-D-Galp2S-(1->4)-alpha-D-Galp2,6S(2)-(1->3)-D-Galp2S. The enzyme from Pseudoalteromonas sp. is specific for lambda-carrageenan. Iota-carrageenan (see EC 3.2.1.157), kappa-carrageenan (see EC 3.2.1.83), agarose and porphyran are not substrates. 1,6-alpha-D-mannosidase Specific for (1->6)-linked mannobiose and has no activity toward any other linkages, or toward p-nitrophenyl-alpha-D-mannopyranoside or mannan from Saccharomyces cerevisiae (baker's yeast). It is strongly inhibited by Mn(2+) but does not require Ca(2+) or any other metal cofactor for activity. Hydrolysis of the 1,6-linked alpha-D-mannose residues in alpha-D-Manp-(1->6)-D-Manp. Lysozyme Muramidase Hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Cf. EC 3.2.1.14. http://purl.uniprot.org/mim/105200 N-acylneuraminate glycohydrolase Neuraminidase Sialidase Exo-alpha-sialidase Alpha-neuraminidase Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates. See also EC 4.2.2.15. The enzyme does not act on 4-O-acetylated sialic acids. http://purl.uniprot.org/mim/256550 An endo-alpha-sialidase activity is listed as EC 3.2.1.129. Glycogenase Saccharogen amylase 1,4-alpha-D-glucan maltohydrolase Beta-amylase Acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion. Hydrolysis of 1,4-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains. Acid maltase Maltase Maltase-glucoamylase Glucoinvertase Glucosidosucrase Lysosomal alpha-glucosidase Alpha-glucosidase The intestinal enzyme also hydrolyzes polysaccharides, catalyzing the reactions of EC 3.2.1.3, and, more slowly, hydrolyzes 1,6-alpha-D-glucose links. Group of enzymes whose specificity is directed mainly toward the exohydrolysis of 1,4-alpha-glucosidic linkages, and that hydrolyze oligosaccharides rapidly, relative to polysaccharides, which are hydrolyzed relatively slowly, or not at all. Hydrolysis of terminal, non-reducing 1,4-linked alpha-D-glucose residues with release of alpha-D-glucose. http://purl.uniprot.org/mim/232300 Amygdalase Gentobiase Beta-glucosidase Cellobiase Beta-D-glucoside glucohydrolase Hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose. Wide specificity for beta-D-glucosides. Some examples also hydrolyze one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides and beta-D-fucosides. Alpha-galactosidase Melibiase Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase. NAD Also hydrolyzes alpha-D-fucosides. Magnesium http://purl.uniprot.org/mim/301500 Lactase Exo-(1->4)-beta-D-galactanase Beta-galactosidase Some enzymes in this group hydrolyze alpha-L-arabinosides; some animal enzymes also hydrolyze beta-D-fucosides and beta-D-glucosides (cf. EC 3.2.1.108). http://purl.uniprot.org/mim/230600 http://purl.uniprot.org/mim/230650 http://purl.uniprot.org/mim/253010 http://purl.uniprot.org/mim/230500 Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Alpha-mannosidase Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides. http://purl.uniprot.org/mim/248500 Also hydrolyzes alpha-D-lyxosides and heptopyranosides with the same configuration at C-2, C-3 and C-4 as mannose. Mannase Beta-mannosidase Mannanase Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. http://purl.uniprot.org/mim/248510 Beta-fructosidase Invertase Saccharase Beta-fructofuranosidase Substrates include sucrose. Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides. Also catalyzes fructotransferase reactions. Trehalase Alpha,alpha-trehalase http://purl.uniprot.org/mim/253220 Alpha,alpha-trehalose + H(2)O = 2 D-glucose. Exo-1,4-alpha-glucosidase Amyloglucosidase Glucoamylase Lysosomal alpha-glucosidase Gamma-amylase 1,4-alpha-D-glucan glucohydrolase Glucan 1,4-alpha-glucosidase EC 3.2.1.20 from mammalian intestine can catalyze similar reactions. This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. Most forms of the enzyme can rapidly hydrolyze 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyze 1,6-and 1,3-alpha-D-glucosidic bonds in other polysaccharides. Hydrolysis of terminal 1,4-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. Beta-glucuronidase http://purl.uniprot.org/mim/253220 A beta-D-glucuronoside + H(2)O = D-glucuronate + an alcohol. Xylanase Endo-1,3-beta-xylanase Xylan endo-1,3-beta-xylosidase Random hydrolysis of 1,3-beta-D-glycosidic linkages in 1,3-beta-D-xylans. Dextrin 6-alpha-D-glucosidase Amylo-alpha-1,6-glucosidase Amylo-1,6-glucosidase The other activity is similar to that of EC 2.4.1.25, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can then hydrolyze. Together, these two activities constitute the glycogen debranching system. This enzyme hydrolyzes an unsubstituted (1->6)-alpha-glucose residue that forms a branch point on an alpha-(1->4)-linked glucose chain. Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin. http://purl.uniprot.org/mim/232400 The enzyme activity found in mammals and Saccharomyces cerevisiae is in a polypeptide chain containing two active centers. Chondroitinase I Hyaluronidase Hyaluronoglucosidase Hyalurononglucosaminidase Chondroitinase http://purl.uniprot.org/mim/601492 Also hydrolyzes 1,4-beta-D-glycosidic linkages between N-acetyl-galactosamine or N-acetylgalactosamine sulfate and glucuronic acid in chondroitin, chondroitin 4-and 6-sulfates, and dermatan. Random hydrolysis of 1->4-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate. Hyaluronoglucuronidase Hyaluronidase Random hydrolysis of 1,3-linkages between beta-D-glucuronate and N-acetyl-D-glucosamine residues in hyaluronate. 1,4-beta-D-xylan xylohydrolase Beta-xylosidase Xylan 1,4-beta-xylosidase Exo-1,4-beta-xylosidase Xylobiase Hydrolysis of 1,4-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini. Also hydrolyzes xylobiose. Some other exoglycosidase activities have been found associated with this enzyme in sheep liver. Beta-D-fucosidase Enzymes from some sources also hydrolyze beta-D-galactosides and/or beta-D-glucosides and/or alpha-L-arabinosides. The activity of EC 3.2.1.37 is an associated activity found in some sources (e.g. liver). Hydrolysis of terminal non-reducing beta-D-fucose residues in beta-D-fucosides. Glucan endo-1,3-beta-D-glucosidase (1->3)-beta-glucan endohydrolase Laminarinase Endo-1,3-beta-glucanase Very limited action on mixed-link (1,3-1,4-)-beta-D-glucans. Hydrolyzes laminarin, paramylon and pachyman. Hydrolysis of 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans. Different from EC 3.2.1.6. Endo-1,4-beta-glucanase Avicelase Beta-1,4-glucanase Carboxymethyl cellulase Endoglucanase Celludextrinase Cellulase Beta-1,4-endoglucan hydrolase Endo-1,4-beta-D-glucanase Endo-1,4-beta-D-glucanohydrolase Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Will also hydrolyze 1,4-linkages in beta-D-glucans also containing 1,3-linkages. Alpha-L-rhamnosidase Hydrolysis of terminal non-reducing alpha-L-rhamnose residues in alpha-L-rhamnosides. Alpha-dextrin endo-1,6-alpha-glucosidase Pullulan 6-glucanohydrolase Debranching enzyme Pullulanase Limit dextrinase Amylopectin 6-glucanohydrolase Maltose is the smallest sugar that it can release from an alpha-(1->6)-linkage. Its action on amylopectin is complete. Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan and in amylopectin and glycogen, and the alpha- and beta-limit dextrins of amylopectin and glycogen. Different from EC 3.2.1.142 in its action on glycogen, and its rate of hydrolysis of limit dextrins. GDP-glucosidase GDP-glucose + H(2)O = D-glucose + GDP. Beta-L-rhamnosidase Hydrolysis of terminal, non-reducing beta-L-rhamnose residues in beta-L-rhamnosides. Fucoidanase Endohydrolysis of 1,2-alpha-L-fucoside linkages in fucoidan without release of sulfate. Beta-glucocerebrosidase Acid beta-glucosidase D-glucosyl-N-acylsphingosine glucohydrolase Glucosylceramidase Also acts on glucosylsphingosine (cf. EC 3.2.1.62). http://purl.uniprot.org/mim/230800 http://purl.uniprot.org/mim/231000 http://purl.uniprot.org/mim/231005 http://purl.uniprot.org/mim/608013 D-glucosyl-N-acylsphingosine + H(2)O = D-glucose + N-acylsphingosine. http://purl.uniprot.org/mim/230900 Galactosylceramide beta-galactosidase Galactocerebrosidase Galactocerebroside beta-galactosidase Galactosylceramidase Galcerase D-galactosyl-N-acylsphingosine + H(2)O = D-galactose + N-acylsphingosine. Cf. EC 3.2.1.62. http://purl.uniprot.org/mim/245200 Galactosylgalactosylglucosylceramidase D-galactosyl-D-galactosyl-D-glucosyl-N-acylsphingosine + H(2)O = D-galactose + lactosyl-N-acylsphingosine. Sucrase-isomaltase Sucrose alpha-glucohydrolase Sucrose alpha-glucosidase Sucrase Isolated from intestinal mucosa as a single polypeptide chain also displaying activity toward isomaltose (EC 3.2.1.10). http://purl.uniprot.org/mim/222900 Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action. Alpha-NAGA Alpha-galactosidase B Alpha-N-acetylgalactosaminidase Splits N-acetylgalactosaminyl groups from O-3 of Ser and Thr. http://purl.uniprot.org/mim/609242 Hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides. http://purl.uniprot.org/mim/609241 Alpha-N-acetylglucosaminidase NAG N-acetyl-alpha-glucosaminidase http://purl.uniprot.org/mim/252920 Hydrolyzes UDP-N-acetylglucosamine. Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides. Alpha-L-fucosidase Alpha-L-fucoside fucohydrolase http://purl.uniprot.org/mim/230000 An alpha-L-fucoside + H(2)O = L-fucose + an alcohol. Hexosaminidase N-acetyl-beta-glucosaminidase Beta-hexosaminidase Beta-N-acetylhexosaminidase Acts on N-acetylglucosides and N-acetylgalactosides. Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. http://purl.uniprot.org/mim/268800 http://purl.uniprot.org/mim/272800 Beta-N-acetylgalactosaminidase Hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-beta-D-galactosaminides. Cyclomaltodextrinase Also hydrolyzes linear maltodextrin. Cyclomaltodextrin + H(2)O = linear maltodextrin. Alpha-N-arabinofuranosidase Alpha-L-arabinofuranosidase Arabinosidase Arabinofuranosidase Some EC 3.2.1.23 and EC 3.2.1.38 enzymes also hydrolyze alpha-L-arabinosides. Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. Acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)-and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Glucuronosyl-disulfoglucosamine glucuronidase 3-D-glucuronosyl-N(2),6-disulfo-beta-D-glucosamine + H(2)O = D-glucuronate + N(2),6-disulfo-D-glucosamine. Isopullulanase The enzyme has practically no action on starch. Panose (4-alpha-isomaltosylglucose) is hydrolyzed to isomaltose and glucose. Cf. EC 3.2.1.41 and EC 3.2.1.135. Hydrolysis of pullulan to isopanose (6-alpha-maltosylglucose). Exo-1,3-beta-glucosidase Exo-1,3-beta-glucanase Glucan 1,3-beta-glucosidase Successive hydrolysis of beta-D-glucose units from the non-reducing ends of 1,3-beta-D-glucans, releasing alpha-glucose. Acts on oligosaccharides, but very slowly on laminaribiose. Endo-1,3-alpha-glucanase Glucan endo-1,3-alpha-glucosidase Endohydrolysis of 1,3-alpha-D-glucosidic linkages in isolichenin, pseudonigeran and nigeran. Products from pseudonigeran (1,3-alpha-D-glucan) are nigerose and alpha-D-glucose. Laminarinase Endo-1,4-beta-glucanase Endo-1,3(4)-beta-glucanase Endo-1,3-beta-glucanase Different from EC 3.2.1.39 and EC 3.2.1.52. Endohydrolysis of 1,3- or 1,4-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolyzed is itself substituted at C-3. Substrates include laminarin, lichenin and cereal D-glucans. Glucan 1,4-alpha-maltotetraohydrolase Maltotetraose-forming amylase Exo-maltotetraohydrolase G4-amylase Glucan 1,4-alpha-maltotetrahydrolase Compare EC 3.2.1.2, which removes successive maltose residues, and EC 3.2.1.98 and EC 3.2.1.116. Hydrolysis of 1,4-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends. Mycodextranase Products are nigerose and 4-alpha-D-nigerosylglucose. Endohydrolysis of 1,4-alpha-D-glucosidic linkages in alpha-D-glucans containing both 1,3- and 1,4-bonds. No hydrolysis of alpha-D-glucans containing only 1,3-or 1,4-bonds. Phlorizin hydrolase Phloretin-glucosidase Glycosylceramidase The intestinal enzyme is a complex which also catalyzes the reaction of EC 3.2.1.108. Broad specificity (cf. EC 3.2.1.45 and EC 3.2.1.46). Glycosyl-N-acylsphingosine + H(2)O = N-acylsphingosine + a sugar. Also hydrolyzes phlorizin to phloretin and glucose. http://purl.uniprot.org/mim/223100 http://purl.uniprot.org/mim/223000 Almond emulsin fucosidase II 1,2-alpha-L-fucosidase Not identical with EC 3.2.1.111. Methyl-2-alpha-L-fucopyranosyl-beta-D-galactoside + H(2)O = L-fucose + methyl beta-D-galactoside. Highly specific for non-reducing terminal L-fucose residues linked to D-galactose residues by 1,2-alpha-linkage. 2,6-beta-fructan 6-levanbiohydrolase Levanbiose-producing levanase Beta-2,6-fructan-6-levanbiohydrolase 2,6-beta-D-fructan 6-levanbiohydrolase 2,6-beta-D-fructan 6-beta-D-fructofuranosylfructohydrolase Hydrolysis of 2,6-beta-D-fructofuranan, to remove successive disaccharide residues as levanbiose, i.e. 6-(beta-D-fructofuranosyl)-D-fructose, from the end of the chain. Levanase Random hydrolysis of 2,6-beta-D-fructofuranosidic linkages in 2,6-beta-D-fructans (levans) containing more than 3 fructose units. Quercitrinase Quercitrin is quercetin 3-L-rhamnoside. Quercitrin + H(2)O = L-rhamnose + quercetin. Exopolygalacturonase Poly(galacturonate) hydrolase Galacturan 1,4-alpha-galacturonidase (1,4-alpha-D-galacturonide)(n) + H(2)O = (1,4-alpha-D-galacturonide)(n-1) + D-galacturonate. Debranching enzyme Isoamylase Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins. Also readily hydrolyzes amylopectin. Maltose is the smallest sugar it can release from an alpha-(1->6)-linkage. Differs from EC 3.2.1.41 and EC 3.2.1.142 by its inability to hydrolyze pullulan, and by limited action on alpha-limit dextrins. Inulinase Inulase Endohydrolysis of 2,1-beta-D-fructosidic linkages in inulin. Glucodextranase Glucan 1,6-alpha-glucosidase Exo-1,6-alpha-glucosidase Hydrolysis of (1->6)-alpha-D-glucosidic linkages in 1->6-alpha-D-glucans and derived oligosaccharides. Dextrans and isomaltosaccharides are hydrolyzed, as is isomaltose, but very slowly. The enzyme from some sources also possesses the activity of EC 3.2.1.59. Hydrolysis is accompanied by inversion at C-1, so that new reducing ends are released in the beta-configuration. Endo-1,2-beta-glucanase Glucan endo-1,2-beta-glucosidase Random hydrolysis of 1,2-glucosidic linkages in 1,2-beta-D-glucans. Exo-1,3-beta-xylosidase Xylan 1,3-beta-xylosidase Hydrolysis of successive xylose residues from the non-reducing termini of 1,3-beta-D-xylans. Beta-glucanase Licheninase Mixed linkage beta-glucanase Endo-beta-1,3-1,4 glucanase 1,3-1,4-beta-D-glucan 4-glucanohydrolase Lichenase Hydrolysis of 1,4-beta-D-glucosidic linkages in beta-D-glucans containing 1,3- and 1,4-bonds. Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3-or 1,4-bonds. Exo-1,4-beta-D-glucosidase 1,4-beta-D-glucan glucohydrolase Exo-1,4-beta-glucanase Exo-1,4-beta-glucosidase Glucan 1,4-beta-glucosidase Cellobiose is hydrolyzed, but very slowly. Acts on 1,4-beta-D-glucans and related oligosaccharides. Hydrolysis of 1,4-linkages in 1,4-beta-D-glucans, to remove successive glucose units. Endo-1,6-beta-D-glucanase Endo-1,6-beta-glucanase Beta-1,6-glucanase Glucan endo-1,6-beta-glucosidase Random hydrolysis of 1,6-linkages in 1,6-beta-D-glucans. Acts on lutean, pustulan and 1,6-oligo-beta-D-glucosides. L-iduronidase http://purl.uniprot.org/mim/607016 Hydrolysis of unsulfated alpha-L-iduronosidic linkages in dermatan sulfate. http://purl.uniprot.org/mim/607015 http://purl.uniprot.org/mim/607014 Exo-1,2-1,3-alpha-mannosidase Mannan 1,2-(1,3)-alpha-mannosidase A 1,6-alpha-D-mannan backbone remains after action on Saccharomyces cerevisiae mannan. Hydrolysis of 1,2- and 1,3-linkages in yeast mannan, releasing mannose. This is further attacked, but slowly. Endo-1,4-mannanase Beta-mannanase Mannan endo-1,4-beta-mannosidase Random hydrolysis of 1,4-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans. Endo-1,4-beta-xylanase 1,4-beta-D-xylan xylanohydrolase Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans. Exo-beta-D-fructosidase Fructanase Fructan beta-fructosidase Hydrolyzes inulin and levan, and also sucrose. Hydrolysis of terminal, non-reducing 2,1- and 2,6-linked beta-D-fructofuranose residues in fructans. Beta-agarase Endo-beta-agarase Agarase Cleaves the beta-(1->4) linkages of agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place. The end products of hydrolysis are neoagarotetraose and neoagarohexaose in the case of AgaA from the marine bacterium Zobellia galactanivorans, and neoagarotetraose and neoagarobiose in the case of AgaB. Also acts on porphyran, but more slowly. Hydrolysis of 1,4-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product. Exopolygalacturanosidase Exo-poly-alpha-galacturonosidase Hydrolysis of pectic acid from the non-reducing end, releasing digalacturonate. Kappa-carrageenase Kappa-carrageenan 4-beta-D-glycanohydrolase Unlike EC 3.2.1.157, but similar to EC 3.2.1.81, this enzyme proceeds with retention of the anomeric configuration. The main products of hydrolysis are neocarrabiose-sulfate and neocarratetraose-sulfate. Endohydrolysis of 1,4-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans. Exo-1,3-alpha-glucanase Glucan 1,3-alpha-glucosidase Does not act on nigeran. Hydrolysis of terminal 1,3-alpha-D-glucosidic links in 1,3-alpha-D-glucans. Beta-D-phosphogalactoside galactohydrolase 6-phospho-beta-galactosidase 6-Phospho-beta-D-galactosidase A 6-phospho-beta-D-galactoside + H(2)O = 6-phospho-D-galactose + an alcohol. Phospho-beta-glucosidase 6-phospho-beta-glucosidase Phosphocellobiase 6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H(2)O = D-glucose + D-glucose 6-phosphate. Also hydrolyzes several other phospho-beta-D-glucosides, but not their non-phosphorylated forms. Capsular-polysaccharide endo-1,3-alpha-galactosidase Polysaccharide depolymerase Hydrolyzes the galactosyl-alpha-1,3-D-galactose linkages only in the complex substrate, bringing about depolymerization. Random hydrolysis of 1,3-alpha-D-galactosidic linkages in Aerobacter aerogenes capsular polysaccharide. Vicianosidase Beta-L-arabinosidase A beta-L-arabinoside + H(2)O = L-arabinose + an alcohol. Endo-1,4-beta-galactanase Arabinogalactanase Galactanase Arabinogalactan endo-1,4-beta-galactosidase Endohydrolysis of 1,4-beta-D-galactosidic linkages in arabinogalactans. 1,4-beta-cellobiohydrolase Exocellobiohydrolase Cellulose 1,4-beta-cellobiosidase Exo-1,4-beta-D-glucanase 1,4-beta-D-glucan cellobiohydrolase Exoglucanase Avicelase Hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains. Peptidoglycan beta-N-acetylmuramidase Exo-beta-N-acetylmuramidase Hydrolysis of terminal, non-reducing N-acetylmuramic residues. Alpha,alpha-phosphotrehalase Trehalose-6-phosphate hydrolase Alpha,alpha-trehalose 6-phosphate + H(2)O = D-glucose + D-glucose 6-phosphate. Glucan 1,6-alpha-isomaltosidase Exo-isomaltohydrolase Isomalto-dextranase Hydrolysis of 1,6-alpha-D-glucosidic linkages in polysaccharides, to remove successive isomaltose units from the non-reducing ends of the chains. Optimum activity is on those 1,6-alpha-D-glucans containing 6, 7 and 8 glucose units; those containing 3, 4 and 5 glucose units are hydrolyzed at slower rates. Dextran 1,6-alpha-isomaltotriosidase Exo-isomaltotriohydrolase Hydrolysis of 1,6-alpha-D-glucosidic linkages in dextrans, to remove successive isomaltotriose units from the non-reducing ends of the chains. Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase Endo-beta-N-acetylglucosaminidase Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)(2))Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Glycopeptide alpha-N-acetylgalactosaminidase The aglycone may be serine or threonine. Hydrolysis of terminal D-galactosyl-N-acetyl-alpha-D-galactosaminidic residues from a variety of glycopeptides and glycoproteins. Maltohexaose-producing amylase G6-amylase Exo-maltohexaohydrolase Glucan 1,4-alpha-maltohexaosidase The products have the alpha-configuration. Cf. EC 3.2.1.116, which removes successive maltotriose residues. Hydrolysis of 1,4-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non-reducing chain ends. Cf. EC 3.2.1.3, which removes successive glucose residues. Cf. EC 3.2.1.2, which removes successive maltose residues. Cf. EC 3.2.1.60, which removes successive maltotetraose residues. Endo-1,5-alpha-L-arabinanase Arabinan endo-1,5-alpha-L-arabinosidase Also acts on beet-arabinan, more slowly. Endohydrolysis of 1,5-alpha-arabinofuranosidic linkages in 1,5-arabinans. Hydrolyzing N-glycosyl compounds Nucleoside hydrolase Purine nucleoside hydrolase IAG-nucleoside hydrolase Inosine-adenosine-guanosine preferring nucleoside hydrolase IAG-NH N-ribosyl purine ribohydrolase Ribonucleoside hydrolase Purine beta-ribosidase Purine ribonucleosidase Purine-specific nucleoside N-ribohydrolase Nucleosidase Nucleosidase g N-D-ribosylpurine ribohydrolase Purine nucleosidase The enzyme from the bacterium Ochrobactrum anthropi specifically catalyzes the irreversible N-riboside hydrolysis of purine nucleosides. A purine nucleoside + H(2)O = D-ribose + a purine base. Pyrimidine nucleosides, purine and pyrimidine nucleotides, NAD(+), NADP(+) and nicotinaminde mononucleotide are not substrates. Pyrimidine-5'-nucleotide nucleosidase Pyr5N Also acts on dUMP, dTMP and dCMP. A pyrimidine 5'-nucleotide + H(2)O = D-ribose 5-phosphate + a pyrimidine base. Beta-aspartyl-N-acetylglucosaminidase 1-beta-aspartyl-N-acetyl-D-glucosaminylamine + H(2)O = L-asparagine + N-acetyl-D-glucosamine. Inosinate nucleosidase 5'-inosinate + H(2)O = D-ribose 5-phosphate + hypoxanthine. 1-methyladenosine nucleosidase 1-methyladenosine + H(2)O = 1-methyladenine + D-ribose. NMN nucleosidase NMNase Nicotinamide D-ribonucleotide + H(2)O = D-ribose 5-phosphate + nicotinamide. DNA-deoxyinosine glycosylase DNA-deoxyinosine glycosidase DNA(hypoxanthine) glycohydrolase Hydrolyzes DNA and polynucleotides, releasing free hypoxanthine. MeSAdo nucleosidase MTA nucleosidase Methylthioadenosine nucleosidase 5'-methylthioadenosine nucleosidase Methylthioadenosine methylthioribohydrolase Does not act on S-adenosylhomocysteine (cf. EC 3.2.2.9). S-methyl-5'-thioadenosine + H(2)O = S-methyl-5-thio-D-ribose + adenine. Deoxyribodipyrimidine endonucleosidase Pyrimidine dimer DNA-glycosylase Cleaves the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue. ADP-ribose-L-arginine cleaving enzyme [Protein ADP-ribosylarginine] hydrolase N(omega)-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase ADP-ribosylarginine hydrolase ADP-ribose-L-arginine cleavage enzyme The enzyme will remove ADP-ribose from arginine residues in ADP-ribosylated proteins. (1) Protein-N(omega)-(ADP-D-ribosyl)-L-arginine + H(2)O = ADP-ribose + protein-L-arginine. (2) N(omega)-(ADP-D-ribosyl)-L-arginine + H(2)O = ADP-ribose + L-arginine. Inosinase Inosine nucleosidase Inosine + H(2)O = D-ribose + hypoxanthine. DNA glycosidase I DNA-3-methyladenine glycosidase I DNA-3-methyladenine glycosylase I Hydrolysis of alkylated DNA, releasing 3-methyladenine. DNA glycosidase II DNA-3-methyladenine glycosylase II DNA-3-methyladenine glycosidase II Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine. rRNA N-glycosylase rRNA N-glycosidase Naked rRNA from Escherichia coli is cleaved at a corresponding position. Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA. Naked rRNA is attacked more slowly than rRNA in intact ribosomes. Ricin A-chain and related toxins show this activity. Fapy-DNA glycosylase DNA-formamidopyrimidine glycosylase Formamidopyrimidine-DNA glycosylase May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents. Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine. Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA. ADP-ribosyl glycohydrolase Dinitrogenase reductase activating glycohydrolase ADP-ribosyl-[dinitrogen reductase] hydrolase Together with EC 2.4.2.37, controls the level of activity of EC 1.18.6.1. ADP-D-ribosyl-[dinitrogen reductase] = ADP-D-ribose + [dinitrogen reductase]. 7-methylxanthosine nucleosidase N-methyl nucleoside hydrolase N-methyl nucleosidase Methylpurine nucleosidase N-meNase Hydrolysis of 7-methylxanthosine to form 7-methylxanthine is the second step in the caffeine-biosynthesis pathway. 7-methylxanthosine + H(2)O = 7-methylxanthine + D-ribose. Preferentially hydrolyzes 3-and 7-methylpurine nucleosides, such as 3-methylxanthosine, 3-methyladenosine and 7-methylguanosine. Uridine nucleosidase Uridine ribohydrolase Uridine + H(2)O = D-ribose + uracil. AMP nucleosidase AMP + H(2)O = D-ribose 5-phosphate + adenine. ADP-ribosyl cyclase DPNase NADase Diphosphopyridine nucleosidase Nicotinamide adenine dinucleotide nucleosidase NAD glycohydrolase NAD nucleosidase NAD(+) nucleosidase Nicotinamide adenine dinucleotide glycohydrolase DPN hydrolase NAD(+) + H(2)O = ADP-ribose + nicotinamide. This enzyme can also hydrolyze NADP(+) to yield phospho-ADP-ribose and nicotinamide, but more slowly. NAD(P)(+) nucleosidase Also catalyzes transfer of ADP-ribose(P) residues. NAD(P)(+) + H(2)O = ADP-ribose(P) + nicotinamide. Adenosine nucleosidase Adenosinase Also acts on adenosine N-oxide. Adenosine + H(2)O = D-ribose + adenine. Ribosylpyrimidine nucleosidase Pyrimidine nucleosidase N-ribosylpyrimidine nucleosidase N-ribosylpyrimidine ribohydrolase Nucleoside ribohydrolase A pyrimidine nucleoside + H(2)O = D-ribose + a pyrimidine base. 2'-, 3'-and 5'-deoxynucleosides are not substrates. Also hydrolyzes purine D-ribonucleosides, more slowly. S-adenosylhomocysteine hydrolase S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase 5'-methyladenosine nucleosidase AdoHcy/MTA nucleosidase S-adenosylhomocysteine nucleosidase Adenosylhomocysteine nucleosidase (1) S-adenosyl-L-homocysteine + H(2)O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine. (2) S-methyl-5'-thioadenosine + H(2)O = 5-methyl-5-thio-D-ribose + adenine. Acting on ether bonds Thioether and trialkylsulfonium hydrolases Adenosylhomocysteinase S-adenosylhomocysteine synthase SAHase S-adenosylhomocysteine hydrolase AdoHcyase Adenosylhomocysteine hydrolase S-adenosylhomocysteinase S-adenosyl-L-homocysteine + H(2)O = L-homocysteine + adenosine. http://purl.uniprot.org/mim/180960 The NAD(+) cofactor appears to bring about a transient oxidation at C-3' of the 5'-deoxyadenosine residue, thus labilizing the thioether bond cf. EC 5.5.1.4. NAD Methylmethionine-sulfonium-salt hydrolase S-adenosylmethionine cleaving enzyme S-adenosyl-L-methionine hydrolase Adenosylmethionine hydrolase S-adenosyl-L-methionine + H(2)O = L-homoserine + methylthioadenosine. Also hydrolyzes methylmethionine sulfonium salt to dimethyl sulfide and homoserine. Ether hydrolases 2,3 dihydro-2,3 dihydroxybenzoate synthase Isochorismatase Isochorismate + H(2)O = 2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate. Soluble epoxide hydrolase Cytosolic epoxide hydrolase Arene-oxide hydratase Epoxide hydratase Epoxide hydrase Trans-stilbene oxide hydrolase Aryl epoxide hydrase Catalyzes the hydrolysis of trans-substituted epoxides, such as trans-stilbene oxide, as well as various aliphatic epoxides derived from fatty-acid metabolism. An epoxide + H(2)O = a glycol. Like EC 3.3.2.9, it is probable that the reaction involves the formation of an hydroxyalkyl-enzyme intermediate. The enzyme from mammals is a bifunctional enzyme: the C-terminal domain exhibits epoxide-hydrolase activity and the N-terminal domain has the activity of EC 3.1.3.76. It is involved in the metabolism of arachidonic epoxides (epoxyeicosatrienoic acids; EETs) and linoleic acid epoxides. The enzyme can also use leukotriene A(4), the substrate of EC 3.3.2.6, but it forms 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than leukotriene B(4) as the product. Cholesterol-epoxide hydrolase Cholesterol-5,6-oxide hydrolase ChEH (1) 5,6-alpha-epoxy-5-alpha-cholestan-3-beta-ol + H(2)O = cholestane-3-beta,5-alpha,6-beta-triol. (2) 5,6-beta-epoxy-5-beta-cholestan-3-beta-ol + H(2)O = cholestane-3-beta,5-alpha,6-beta-triol. The product is a competitive inhibitor of the reaction. The enzyme appears to work equally well with both diastereoisomers of cholesterol 5,6-epoxide. Alkenylglycerophosphocholine hydrolase 1-(1-alkenyl)-sn-glycero-3-phosphocholine + H(2)O = an aldehyde + sn-glycero-3-phosphocholine. Trans-epoxysuccinate hydrolase Trans-epoxysuccinate hydratase Trans-2,3-epoxysuccinate + H(2)O = meso-tartrate. Acts on both optical isomers of the substrate. Alkenylglycerophosphoethanolamine hydrolase 1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H(2)O = an aldehyde + sn-glycero-3-phosphoethanolamine. Leukotriene-A4 hydrolase Leukotriene A(4) hydrolase Leukotriene-A(4) hydrolase LTA-4 hydrolase It also converts leukotriene A(4) into leukotriene B(4), unlike EC 3.2.2.10 which converts leukotriene A(4) into 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid. (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H(2)O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate. It preferentially cleaves tripeptides at an arginyl bond, with dipeptides and tetrapeptides being poorer substrates. Zinc A bifunctional zinc metalloprotease that displays both epoxide hydrolase and aminopeptidase activities. Hepoxilin-epoxide hydrolase Hepoxylin hydrolase Hepoxilin A(3) hydrolase Hepoxilin epoxide hydrolase Highly specific for the substrate, having only slight activity with other epoxides such as leukotriene A(4) and styrene oxide. Probably plays a modulatory role in inflammation, vascular physiology, systemic glucose metabolism and neurological function. Converts hepoxilin A(3) into trioxilin A(3). (5Z,9E,14Z)-(8-xi,11R,12S)-11,12-epoxy-8-hydroxyicosa-5,9,14-trienoate + H(2)O = (5Z,9E,14Z)-(8-xi,11-xi,12S)-8,11,12-trihydroxyicosa-5,9,14-trienoate. Limonene-1,2-epoxide hydrolase Limonene oxide hydrolase Involved in the monoterpene degradation pathway of the actinomycete Rhodococcus erythropolis. It differs from the previously described epoxide hydrolases (EC 3.3.2.4, EC 3.3.2.6, EC 3.3.2.7, EC 3.3.2.9 and EC 3.3.2.10) as it is not inhibited by 2-bromo-4'-nitroacetophenone, diethyl pyrocarbonate, 4-fluorochalcone oxide or 1,10-phenanthroline. The enzyme hydrolyzes several alicyclic and 1-methyl-substituted epoxides, such as 1-methylcyclohexene oxide, indene oxide and cyclohexene oxide. Limonene-1,2-epoxide + H(2)O = limonene-1,2-diol. MEH Arene-oxide hydratase Microsomal epoxide hydrase Microsomal epoxide hydrolase Cis-epoxide hydrolase Benzo[a]pyrene-4,5-oxide hydratase Epoxide hydrase Aryl epoxide hydrase Microsomal epoxide hydratase Epoxide hydratase The reaction involves the formation of an hydroxyalkyl-enzyme intermediate. http://purl.uniprot.org/mim/607784 Involved in the metabolism of numerous xenobiotics, such as 1,3-butadiene oxide, styrene oxide and the polycyclic aromatic hydrocarbon benzo[a]pyrene 4,5-oxide. Cis-stilbene oxide + H(2)O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol. In a series of oxiranes with a lipophilic substituent of sufficient size (styrene oxides), monosubstituted as well as 1,1-and cis-1,2-disubstituted oxiranes serve as substrates or inhibitors of the enzyme, while trans-1,2-disubstituted, tri-and tetra-substituted oxiranes are not substrates. Acting on peptide bonds (peptide hydrolases) Aminopeptidases Peptidase S Cytosol aminopeptidase Leucine aminopeptidase Leucyl aminopeptidase Belongs to peptidase family M17. Is activated by heavy metal ions. Zinc Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Bacterial leucyl aminopeptidase Aeromonas proteolytica aminopeptidase Similar aminopeptidases were isolated from Escherichia coli and Staphylococcus thermophilus. Belongs to peptidase families M17 and M28. Zinc Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Clostridial aminopeptidase Clostridium histolyticum aminopeptidase Release of any N-terminal amino acid, including proline and hydroxyproline, but no cleavage of Xaa-|-Pro. A secreted enzyme from Clostridium histolyticum. Manganese or cobalt Soluble alanyl aminopeptidase Puromycin-sensitive aminopeptidase Aminopolypeptidase Liver aminopeptidase Arylamidase Cytosol alanyl aminopeptidase Cytosol aminopeptidase III Zinc or cobalt Release of an N-terminal amino acid, preferentially alanine, from a wide range of peptides, amides and arylamides. A puromycin-sensitive, cobalt-activated zinc-sialoglycoprotein that is generally cytosolic. Multiple forms are widely distributed in mammalian tissues and body fluids. Aminopeptidase Co Aminopeptidase (cobalt-activated) Aminopeptidase Y Lysyl aminopeptidase Belongs to peptidase family M28B. Hydrolyzes L-lysyl-4-nitroanilide and, more slowly, L-arginyl-4-nitroanilide. Inhibited by Zn(2+) and Mn(2+). Cobalt Preferentially, release of N-terminal lysine. Aminopeptidase W Aminopeptidase X-Trp X-Trp aminopeptidase Xaa-Trp aminopeptidase Zinc Release of a variety of N-terminal residues (especially glutamate and leucine) from peptides, provided tryptophan (or at least phenylalanine or tyrosine) is the penultimate residue. Also acts on Glu-|-Trp, Leu-|-Trp and a number of other dipeptides. Tryptophan aminopeptidase Tryptophanyl aminopeptidase Also acts on L-tryptophanamide. From Trichosporon cutaneum. Manganese Preferential release of N-terminal tryptophan. Peptidase M Methionine aminopeptidase Methionyl aminopeptidase Membrane-bound enzyme present in both prokaryotes and eukaryotes. Cobalt Removes the amino-terminal methionine from nascent proteins. Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. Belongs to peptidase family M24A. D-stereospecific aminopeptidase Release of an N-terminal D-amino acid from a peptide, Xaa-|-Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-amino acid amides and methyl esters also are hydrolyzed, as is glycine amide. A homolog of EC 3.4.16.4. Not metal dependent; probably has serine at the active center. Belongs to peptidase family S12. A thiol-dependent peptidase known from the bacterium Ochrobactrum anthropi. Membrane aminopeptidase I Particle-bound aminopeptidase Aminopeptidase N Microsomal aminopeptidase Amino-oligopeptidase Membrane alanyl aminopeptidase Aminopeptidase M Peptidase E Membrane alanine aminopeptidase Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide. Is not activated by heavy metal ions. Belongs to peptidase family M1. Zinc Aminopeptidase Ey Zinc Belongs to peptidase family M1. From the plasma fraction of chicken egg yolk. Differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyze peptides of four or five residues that contain Pro in the P1' position. Aspartyl aminopeptidase Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate. Aminoacyl-arylamides are poor substrates. Belongs to peptidase family M18. Vacuolar aminopeptidase I Aminopeptidase yscI Aminopeptidase III Leucine aminopeptidase IV Aminopeptidase I Belongs to peptidase family M18. Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates. PepB aminopeptidase Peptidase B Aminopeptidase B Xaa is preferably Glu or Asp but may be other amino acids, including Leu, Met, His, Cys and Gln. The pH optimum is in the alkaline range and activity is stimulated by KCl. Belongs to peptidase family M17. A 270-kDa protein composed of six 46.3-kDa subunits. Release of an N-terminal amino acid, Xaa, from a peptide or arylamide. Oxytocinase Cystinyl aminopeptidase Cystine aminopeptidase Cystyl-aminopeptidase Release of an N-terminal amino acid, Cys-|-Xaa-, in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however. Zinc Belongs to peptidase family M1. Lymphopeptidase Aminotripeptidase Imidoendopeptidase Aminoexotripeptidase Tripeptidase Tripeptide aminopeptidase Peptidase B Widely distributed in mammalian tissues. Release of the N-terminal residue from a tripeptide. Zinc Belongs to peptidase family M9. Proline iminopeptidase Pro-X aminopeptidase Proline aminopeptidase Prolyl aminopeptidase Cytosol aminopeptidase V Present in the cytosol of mammalian and microbial cells. The mammalian enzyme, which is not specific for prolyl bonds, is possibly identical with EC 3.4.11.1. Release of N-terminal proline from a peptide. Manganese In contrast to the mammalian form, the bacterial form of the enzyme hydrolyzes both polyproline and prolyl-2-naphthylamide. Belongs to peptidase family S33. Aminopeptidase B Arylamidase II Arginyl aminopeptidase Arginine aminopeptidase Cytosol aminopeptidase IV Belongs to peptidase family M1. Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys. Cytosolic or membrane-associated enzyme from mammalian tissues, activated by chloride ions and low concentrations of thiol compounds. Zinc One of the activities of the bifunctional enzyme EC 3.3.2.6. Glutamyl peptidase Angiotensinase A Aminopeptidase A Glutamyl aminopeptidase Aspartate aminopeptidase Membrane aminopeptidase II Zinc Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide. Belongs to peptidase family M1. Calcium-activated and generally membrane-bound. Also acts on L-alpha-glutamyl-peptides. Xaa-Pro aminopeptidase Aminopeptidase P X-Pro aminopeptidase Aminoacylproline aminopeptidase Proline aminopeptidase Generally membrane bound enzyme present in both mammalian and bacterial cells. Belongs to peptidase family M24B. Manganese or cobalt Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Dipeptidases Methionyl dipeptidase Met-Xaa dipeptidase Dipeptidase M Met-X dipeptidase Escherichia coli enzyme with thiol dependence. Manganese Hydrolysis of Met-|-Xaa dipeptides. D-(or L-)aminoacyl-dipeptidase Peptidyl-D-amino acid hydrolase Non-stereospecific dipeptidase Hydrolysis of dipeptides containing either D- or L-amino acids or both. A digestive enzyme of cephalopods. Cytosol non-specific dipeptidase N(2)-beta-alanylarginine dipeptidase Prolinase Cytosol nonspecific dipeptidase Glycyl-glycine dipeptidase Glycyl-leucine dipeptidase Peptidase A Pro-X dipeptidase Prolylglycine dipeptidase Prolyl dipeptidase Belongs to peptidase family M20. Activated and stabilized by dithiothreitol and manganese. Broad specificity, varying somewhat with source species. Inhibited by bestatin and leucine. Zinc Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids. Dehydropeptidase I DPH I Renal dipeptidase Microsomal dipeptidase Membrane dipeptidase Inhibited by bestatin and cilastatin. Hydrolysis of dipeptides. Zinc Abundant in the kidney cortex. Belongs to peptidase family M19. Membrane bound, with broad specificity. Beta-Ala-His dipeptidase Serum carnosinase Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine. Present in the serum of humans and higher primates, but not in the serum of other mammals. Activated by Cd(2+) and citrate. Belongs to peptidase family M20. PepE gene product (Salmonella typhimurium) Dipeptidase E Aspartyl dipeptidase Peptidase E The enzyme is most active near pH 7.0, and is not inhibited by di-isopropylfluorophosphate or phenylmethanesulfonyl fluoride. Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides. Belongs to peptidase family S51. Asp-NH-Np is hydrolyzed and is a convenient substrate for routine assay. A free carboxy group is not absolutely required in the substrate since Asp-Phe-NH(2) and Asp-Phe-OMe are hydrolyzed somewhat more slowly than dipeptides with free C-termini. No peptide larger than a C-blocked dipeptide is known to be a substrate. D-alanyl-D-alanine dipeptidase D-Ala-D-Ala dipeptidase The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. Reduces the availability of the free dipeptide D-Ala-D-Ala, which is the precursor for this pentapeptide sequence, allowing D-Ala-(R)-lactate (for which vancomycin has much less affinity) to be added to the cell wall instead. Zinc Protects Enterococcus faecium from the antibiotic vancomycin, which can bind to the -D-Ala-D-Ala sequence at the C-terminus of the peptidoglycan pentapeptide. D-Ala-D-Ala + H(2)O = 2 D-Ala. Belongs to peptidase family M15. Homocarnosinase X-His dipeptidase Aminoacyl-histidine dipeptidase Carnosinase Xaa-His dipeptidase http://purl.uniprot.org/mim/212200 A mammalian cytosolic enzyme. http://purl.uniprot.org/mim/236130 This enzyme may be identical with EC 3.4.13.18. Hydrolysis of Xaa-|-His dipeptides. Also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Belongs to peptidase family M25. Zinc Activated by thiols; inhibited by metal-chelating agents. Aminoacyl-lysine dipeptidase N(2)-(4-amino-butyryl)-L-lysine hydrolase X-Arg dipeptidase Xaa-Arg dipeptidase Preferential hydrolysis of Xaa-|-Arg, Xaa-|-Lys or Xaa-|-ornithine dipeptides. Widely distributed in mammals. X-methyl-His dipeptidase Xaa-methyl-His dipeptidase Aminoacyl-methylhistidine dipeptidase Anserinase Identical with acetylhistidine deacetylase. Hydrolysis of anserine (beta-alanyl-|-N(pi)-methyl-L-histidine), carnosine, homocarnosine, glycyl-|-leucine and other dipeptides with broad specificity. Alpha-glutamyl-glutamate dipeptidase Glu-Glu dipeptidase Hydrolysis of the Glu-|-Glu dipeptide. It is unclear whether the specificity of this enzyme extends to other alpha-glutamyl dipeptides. Prolidase Xaa-Pro dipeptidase Imidodipeptidase Peptidase D Proline dipeptidase X-Pro dipeptidase Gamma-peptidase Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro. Possibly thiol dependent. Manganese http://purl.uniprot.org/mim/170100 Belongs to peptidase family M24A. Cytosolic from most animal tissues. Dipeptidyl-peptidases and tripeptidyl-peptidases Cathepsin C Dipeptidyl-peptidase I Dipeptidyl transferase Dipeptidyl aminopeptidase I Cathepsin J http://purl.uniprot.org/mim/245010 Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro. Also polymerizes dipeptide amides, arylamides and esters at neutral pH. http://purl.uniprot.org/mim/170650 Belongs to peptidase family C1. Cl(-)-dependent lysosomal cysteine-type peptidase. http://purl.uniprot.org/mim/245000 Tripeptidyl-peptidase II Tripeptidyl peptidase Tripeptidyl aminopeptidase Belongs to peptidase family S8. A cytosolic enzyme active at neutral pH. Inhibited by diisopropyl fluorophosphate. Release of an N-terminal tripeptide from a polypeptide. X-Pro dipeptidyl-peptidase X-prolyl dipeptidyl aminopeptidase Xaa-Pro dipeptidyl-peptidase EC 3.4.14.5 catalyzes a similar reaction. Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile. Belongs to peptidase family S15. Prolyltripeptidyl amino peptidase Xaa-Xaa-Pro tripeptidyl-peptidase Prolyltripeptidyl aminopeptidase PTP-A TPP Prolyl tripeptidyl peptidase The enzyme possesses an absolute requirement for a proline residue at the P1 position but is completely inactivated by a proline residue at the P1' position. This cell-surface-associated serine exopeptidase is found in the Gram-negative, anaerobic bacterium Porphyromonas gingivalis, which has been implicated in adult periodontal disease. Hydrolysis of Xaa-Xaa-Pro-|-Yaa- releasing the N-terminal tripeptide of a peptide with Pro as the third residue (position P1) and where Yaa is not proline. The size of the peptide does not affect the rate of reaction. The enzyme releases tripeptides from the free amino terminus of peptides and small proteins, such as interleukin-6. Dipeptidyl arylamidase II Carboxytripeptidase Dipeptidyl-peptidase II DPP II Quiescent cell proline dipeptidase Dipeptidyl aminopeptidase II Cleaves Lys-Ala-naphthylamide. A lysosomal serine-type peptidase maximally active at acidic pH. Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides. Belongs to peptidase family S28. DPP III Dipeptidyl arylamidase III Red cell angiotensinase Enkephalinase B Dipeptidyl aminopeptidase III Dipeptidyl-peptidase III A cytosolic peptidase that is active at neutral pH. Active in the hydrolysis of enkephalins. Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides. It has broad activity on peptides, although it is highly selective for Arg-Arg-2-naphthylamide, at pH 9.2. Belongs to peptidase family M49. Gly-Pro naphthylamidase Dipeptidyl aminopeptidase IV Xaa-Pro-dipeptidylaminopeptidase DPP IV Post-proline dipeptidyl aminopeptidase IV Dipeptidyl-peptidase IV EC 3.4.14.11 catalyzes a similar reaction. Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to peptidase family S9B. A membrane-bound serine-type peptidase in mammals. Dipeptidyl ligase Dipeptidyl-dipeptidase Tetrapeptide dipeptidase Dipeptidyl tetrapeptide hydrolase Tetrapeptides are formed from Ala-Ala, Gly-Gly, Ala-Gly and Gly-Ala without prior activation of the carboxy group. From cabbage (Brassica oleracea). Preferential release of dipeptides from a tetrapeptide, e.g. Ala-Gly-|-Ala-Gly. Acts more slowly on Ala-Ala-|-Ala-Ala and Gly-Gly-|-Gly-Gly. Activated by thiols. Tripeptidyl aminopeptidase Tripeptidyl peptidase Tripeptidyl-peptidase I Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity. http://purl.uniprot.org/mim/204500 Belongs to peptidase family S53. A lysosomal enzyme that is active at acidic pH. Peptidyl-dipeptidases Peptidase P Dipeptidyl carboxypeptidase I Angiotensin I-converting enzyme Kininase II ACE Peptidyl-dipeptidase A Carboxycathepsin Peptidyl dipeptidase I Belongs to peptidase family M2. Zinc A glycoprotein that is generally membrane-bound. Only single dipeptides are released from angiotensin I and bradykinin because of the lack of activity on bonds involving proline. Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II. Active at neutral pH. Cl(-)-dependent. Atrial di-(tri-)peptidyl carboxylase Peptidyl-dipeptidase B Atriopeptin convertase Dipeptidyl carboxyhydrolase Although it is capable of converting the 126-residue atriopeptin III directly to atriopeptin I by releasing a C-terminal tripeptide Phe-Arg-Tyr, it is generally restricted to the release of dipeptides. In contrast to EC 3.4.15.1 it displays no chlorine dependence and shows no action on angiotensin I. Release of a C-terminal dipeptide or exceptionally a tripeptide. Conversely, peptidyl-dipeptidase a is unable to release Phe-Arg from the C-terminus of atriopeptin II. A membrane-bound, zinc metallopeptidase located in mammalian atrial, but not ventricular, myocytes. Zinc Dipeptidyl carboxypeptidase Peptidyl-dipeptidase Dcp Belongs to peptidase family M3. Hydrolysis of unblocked, C-terminal dipeptides from oligopeptides, with broad specificity. Does not hydrolyze bonds in which P1' is Pro, or both P1 and P1' are Gly. Inhibited by captopril, as is peptidyl-dipeptidase A. Zinc Serine-type carboxypeptidases Angiotensinase C Lysosomal carboxypeptidase C Prolyl carboxypeptidase Lysosomal Pro-X carboxypeptidase Lysosomal Pro-Xaa carboxypeptidase Proline carboxypeptidase Cleavage of a -Pro-|-Xaa bond to release a C-terminal amino acid. A lysosomal peptidase active at acidic pH that inactivates angiotensin II. Inhibited by diisopropyl fluorophosphate. Belongs to peptidase family S28. DD-transpeptidase DD-peptidase D-alanyl-D-alanine carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase Distinct from EC 3.4.17.14. Inhibited by beta-lactam antibiotics, which acylate the active site serine in the enzyme. Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine. A group of bacterial enzymes, membrane-bound. Belongs to peptidase families S11, S12 and S13. Serine-type carboxypeptidase I Carboxypeptidase C Lysosomal protective protein Cathepsin A Carboxypeptidase Y Release of a C-terminal amino acid with broad specificity. Belongs to peptidase family S10. This enzyme is probably also identical to lysosomal tyrosine carboxypeptidase. Carboxypeptidases of broad specificity with optimum pH 4.5-6.0, inhibited by the action of diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents. http://purl.uniprot.org/mim/256540 Carboxypeptidase KEX1 Carboxypeptidase D Carboxypeptidase S1 Belongs to peptidase family S10. Preferential release of a C-terminal arginine or lysine residue. Carboxypeptidases of broad specificity with optimum pH 4.5-6.0, inhibited by the action of diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents. Metallocarboxypeptidases Carboxypolypeptidase Carboxypeptidase A Zinc Belongs to peptidase family M14. Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro. Isolated from cattle, pig and dogfish pancreas, and other sources including mast cells and skeletal muscle. http://purl.uniprot.org/mim/126800 Enkephalin convertase Carboxypeptidase E Carboxypeptidase H Belongs to peptidase family M14. pH optimum 5.6. Zinc Release of C-terminal arginine or lysine residues from polypeptides. Inhibited by 1,10-phenanthroline and other chelating agents. Activated by Co(2+). Distinct from EC 3.4.17.2 and EC 3.4.17.3. Located in storage granules of secretory cells, and active in processing of protein hormones and bioactive peptides. Carboxypeptidase G2 Carboxypeptidase G1 Glutamate carboxypeptidase Carboxypeptidase G Belongs to peptidase family M20A. Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl and pteroyl groups. Its ability to hydrolyze pteroyl-L-glutamate (folic acid) has led to its use as a folate-depleting, antitumor agent. Produced by pseudomonads, Flavobacterium sp. and Acinetobacter sp. Zinc Carboxypeptidase M Cleavage of C-terminal arginine or lysine residues from polypeptides. Distinct from EC 3.4.17.3 and EC 3.4.17.10. A membrane-bound enzyme optimally active at neutral pH. Zinc Belongs to peptidase family M14. Carboxypeptidase IIW Muramoyltetrapeptide carboxypeptidase Cleavage of the bond: N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-lysyl-|-D-alanine. Stimulated by divalent cations such as magnesium and calcium, but not zinc. Variants are known from various microorganisms. Inhibited by thiol-blocking reagents, but unaffected by penicillin. Involved in peptidoglycan synthesis, catalyzing both decarboxylation and transpeptidation. D-alanyl-D-alanine hydrolase Zinc D-Ala-D-Ala carboxypeptidase Zn(2+) G peptidase Zinc Cleavage of the bond: (Ac)(2)-L-lysyl-D-alanyl-|-D-alanine. Catalyzes carboxypeptidation but not transpeptidation reactions involved in bacterial cell wall metabolism. Distinct from EC 3.4.16.4. Weakly inhibited by beta-lactams. Carboxypeptidase A2 Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues. Zinc Belongs to peptidase family M14. Isolated from rat pancreas but not present in cattle pancreas. Microsomal carboxypeptidase Membrane Pro-Xaa carboxypeptidase Carboxypeptidase P Membrane Pro-X carboxypeptidase One of the renal brush border exopeptidases. Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond. Tubulinyl-Tyr carboxypeptidase Soluble carboxypeptidase Carboxypeptidase-tubulin Active at neutral pH, from brain. Cleavage of the -Glu-|-Tyr bond to release the C-terminal tyrosine residue from the native tyrosinated tubulin. Inactive on Z-Glu-Tyr. Carboxypeptidase T Belongs to peptidase family M14. Zinc Releases a C-terminal residue, which may be hydrophobic or positively charged. Thermostable carboxypeptidase 1 Carboxypeptidase Taq Belongs to peptidase family M32. Zinc Most active at 80 degrees Celsius. Release of a C-terminal amino acid with broad specificity, except for -Pro. Carboxypeptidase B Protaminase Preferential release of a C-terminal lysine or arginine amino acid. Isolated from cattle, pig and dogfish pancreas, and other sources, including skin fibroblasts and adrenal medulla. Belongs to peptidase family M14. Zinc Thrombin-activatable fibrinolysis inhibitor TAFI Carboxypeptidase B2 Carboxypeptidase U Carboxypeptidase R Plasma carboxypeptidase B Arginine carboxypeptidase Zinc Pro-carboxypeptidase U in plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U. Release of C-terminal Arg and Lys from a polypeptide. Activity similar to that of the more stable lysine carboxypeptidase, except no preference is shown for Lys over Arg. Belongs to peptidase family M14. NAALADase Pteroylpoly-gamma-glutamate carboxypeptidase N-acetylated-gamma-linked-acidic dipeptidase Glutamate carboxypeptidase II Folate hydrolase Belongs to peptidase family M28. The release of C-terminal glutamate from folylpoly-gamma-glutamates is also catalyzed by EC 3.4.17.11 and EC 3.4.19.9. Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates. With folylpoly-gamma-glutamates, shows processive carboxypeptidase activity to produce pteroylmonoglutamate. Hydrolyzes alpha-peptide bonds in Ac-Asp-Glu, Asp-Glu, and Glu-Glu, but also gamma-glutamyl bonds in gamma-Glu-Glu and folylpoly-gamma-glutamates. Does not hydrolyze Ac-beta-Asp-Glu. Zinc Inhibited by quisqualic acid, Ac-beta-Asp-Glu, and 2-phosphonomethyl-pentanedioate. Metallocarboxypeptidase D Carboxypeptidase D Releases C-terminal Arg and Lys from polypeptides. Zinc Activated by cobalt. Belongs to peptidase family M14. Inhibited by guanidinoethylmercaptosuccinic acid. Carboxypeptidase N Lysine carboxypeptidase Arginine carboxypeptidase Lysine(arginine) carboxypeptidase Kininase I Anaphylatoxin inactivator Release of a C-terminal basic amino acid, preferentially lysine. Belongs to peptidase family M14. Inactivates bradykinin and anaphylatoxins in blood plasma. http://purl.uniprot.org/mim/212070 Zinc Carboxypeptidase A Glycine carboxypeptidase Gly-Xaa carboxypeptidase Carboxypeptidase S Gly-X carboxypeptidase Belongs to peptidase family M20A. Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly-|-Leu. Alanine carboxypeptidase The enzyme from Corynebacterium equi also hydrolyzes N-benzoylglycine and N-benzoyl-L-aminobutyric acid. Peptide can be replaced by a pteroyl group or variety of acyl groups. Release of a C-terminal alanine from a peptide or a variety of pteroyl or acyl groups. D-alanyl-D-alanine carboxypeptidase D-alanine-D-alanine-carboxypeptidase PBP5 Penicillin binding protein 5 D-alanine carboxypeptidase Carboxypeptidase D-alanyl-D-alanine UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase Muramoylpentapeptide carboxypeptidase D-alanyl-D-alanine peptidase DD-peptidase DD-carboxypeptidase Cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-|-D-alanine. Does not cleave the C-terminal D-alanine from the product of the above reaction, UDP-N-acetyl-muramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanine. Belongs to peptidase family M15. Zinc Competitively inhibited by penicillins and cephalosporins. Cysteine-type carboxypeptidases Cathepsin Z Cysteine-type carboxypeptidase Cathepsin X Acid carboxypeptidase Cathepsin IV Lysosomal carboxypeptidase B Cathepsin B(2) The pH optimum is dependent on the substrate and is 5.0 for the carboxypeptidase activity. Compound E-64, leupeptin and antipain are inhibitors, but not cystatin C. Deamidates Z-Arg-NH(2), but shows no action on the arylamide derivatives. Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity. Belongs to peptidase family C1. The propeptide is extremely short (38 amino acid residues) and the proenzyme is catalytically active. Cathepsin X is a lysosomal cysteine peptidase of family C1 (papain family). Human gene locus: 20q13. Inhibited by thiol-blocking reagents. Cathepsin X is ubiquitously distributed in mammalian tissues. Unstable above pH 7.0. Omega peptidases Acylaminoacyl-peptidase Acylamino-acid-releasing enzyme N-acylpeptide hydrolase Group of similar enzymes liberating N-acetyl or N-formyl amino acid from proteins and peptides. Belongs to peptidase family S9C. Display dipeptidyl-peptidase activity on glycyl-peptides, perhaps as a result of misrecognition of the glycyl residue as an uncharged N-acyl group. Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide. Best if P1 = Ser, Ala, Met; poor if P1 = Gly, Tyr, Asp, Asn or Pro. Inhibited by diisopropyl fluorophosphate. Several variants of this enzyme exist; the human erythrocyte enzyme is relatively specific for removal of N-acetylalanine from peptides. Active at neutral pH. Endopeptidase I Gamma-D-glutamyl-meso-diaminopimelate peptidase Gamma-D-glutamyl-L-diamino acid endopeptidase I Gamma-D-glutamyl-meso-diaminopimelate peptidase I Metallopeptidase from Bacillus sphaericus, the substrates being components of the bacterial spore wall. Belongs to peptidase family M14. Hydrolysis of gamma-D-glutamyl bonds to the L-terminus (position 7) of meso-diaminopimelic acid (meso-A(2)pm) in 7-(L-Ala-gamma-D-Glu)-meso-A(2)pm and 7-(L-Ala-gamma-D-Glu)-7-(D-Ala)-meso-A(2)pm. It is required that the D-terminal amino and carboxy groups of meso-A(2)pm are unsubstituted. Ubiquitin carboxyl-terminal hydrolase Ubiquitin C-terminal hydrolase Ubiquitinyl hydrolase 1 Ubiquitin thiolesterase Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals. Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Belongs to peptidase family C12. Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides. Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde). Peptidyl carboxyamidase Peptidyl-glycinamidase Carboxyamidase The toad skin enzyme is inhibited by diisopropyl fluorophosphate. Inactivates vasopressin and oxytocin by splitting off glycinamide. Although glycinamide is by far the preferred leaving group, other aminoacylamides may also be released, e.g. phenylalaninamide. Cleavage of C-terminal glycinamide from polypeptides. Also cleaves ester substrates of trypsin and chymotrypsin. Pyroglutamyl aminopeptidase Pyrrolidone-carboxylate peptidase Pyroglutamyl-peptidase I 5-oxoprolyl-peptidase Pyrrolidone carboxyl peptidase PYRase Inhibited by thiol-blocking reagents. Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro. Belongs to peptidase family C15. Removes 5-oxoproline from various penultimate amino acid residues except L-proline. Beta-aspartyl-peptidase Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide. Other isopeptide bonds, e.g. gamma-glutamyl and beta-alanyl, are not hydrolyzed. Thyrotropin-releasing hormone degrading ectoenzyme PAP-II TRH-DE TRH-specific aminopeptidase TRH-degrading ectoenzyme Pyroglutamyl-peptidase II Thyroliberinase Pyroglutamyl aminopeptidase II Highly specific for thyrotropin releasing hormone (pyroglutamyl-histidyl-prolylamide). Inhibited by metal chelators. Will not cleave the pyroglutamyl-histidyl bond of luteinizing hormone releasing hormone. Belongs to peptidase family M1. Zinc Found in serum and brain. Release of the N-terminal pyroglutamyl group from pGlu-|-His-Xaa tripeptides and pGlu-|-His-Xaa-Gly tetrapeptides. (fMet)-releasing enzyme N-formylmethionyl-peptidase Will not cleave methionyl peptides or N-formyl derivatives of amino acids other than methionine. Highly specific for N-formylmethionyl-peptides. Inhibited by heavy metals and activated by chloride. Isolated from liver. Release of an N-terminal, formyl-methionyl residue from a polypeptide. Gamma-Glu-X carboxypeptidase Carboxypeptidase G Folate conjugase Lysosomal gamma-glutamyl carboxypeptidase Conjugase Gamma-glutamyl hydrolase Pteroyl-poly-alpha-glutamate hydrolase A lysosomal or secreted, thiol-dependent peptidase, most active at acidic pH. Final products are pteroyl-alpha-glutamate (folic acid) and free glutamate. Action on gamma-glutamyl bonds is independent of an N-terminal pteroyl moiety, but it is not known whether an N-terminal gamma-Glu residue can be hydrolyzed. Highly specific for the gamma-glutamyl bond, but not for the C-terminal amino acid (leaving group). Hydrolysis of a gamma-glutamyl bond. Commonly studied with folylpoly-gamma-glutamate as substrate, with which the initial cleavage may release glutamate or poly-gamma-glutamate of two or more residues, according to the species of origin of the enzyme. Belongs to peptidase family C26. Serine endopeptidases Alpha-chymotrypsin Chymotrypsin Chymotrypsin B Chymotrypsin A Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa. Belongs to peptidase family S1. Acrosin Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa. Occurs in spermatozoa. Belongs to peptidase family S1. Inhibited by naturally occurring trypsin inhibitors. Pseudomonapepsin Pseudomonalisin pepstatin-insensitive carboxyl proteinase Pseudomonas sp Hydrolysis of the B chain of insulin at 13-Glu-|-Ala-14, 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 and angiotensin I at 4-Tyr-|-Ile-5. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-|-Phe(NO(2))-Arg-Leu. Inhibited by tyrostatin, a peptide aldehyde. Optimum pH 4. Belongs to peptidase family S53. It is distinguished from EC 3.4.21.101 by its insensitivity to EPNP and from EC 3.4.23.31 by this property and by its unrelated amino-acid sequence. An enzyme secreted by Pseudomonas sp. No. 101. Xanthomonalisin Xanthomonapepsin Xanthomonas aspartic proteinase Sedolisin-B Cleavage of casein. Belongs to peptidase family S53. Secreted by the bacterium Xanthomonas sp. Protease Re C-terminal processing peptidase Photosystem II D1 protein processing peptidase Tsp protease Tail-specific protease Belongs to peptidase family S41. The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II; this proteolytic processing is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation. Dictyostelium discoideum aspartic proteinase E Physarolisin Physarum flavicomum aspartic proteinase Physaropepsin Physarum polycephalum acid proteinase Physarum aspartic proteinase Dictyostelium discoideum aspartic proteinase Is not inhibited by pepstatin, but is blocked by methyl 2-diazoacetamidohexanoate. Closely similar enzymes are found in Dictyostelium discoideum and P.flavicomum. Milk clotting activity. Preferential cleavage of 8-Gly-|-Ser-9 in B chain of insulin most rapidly, followed by 11-Leu-|-Val-12, 19-Cys(SO(3)H)-|-Gly and 24-Phe-|-Phe-25. No action on Ac-Phe-Tyr(I)(2). Belongs to peptidase family S53. From the slime mold Physarum polycephalum. Mannose-binding lectin-associated serine protease-2 MASP2 Mannan-binding lectin-associated serine peptidase 2 Mannan-binding lectin-associated serine protease-2 MBP-associated serine protease-2 MASP-2 It also cleaves C4 and C2 with efficiencies that are relatively higher than those of EC 3.4.21.42. http://purl.uniprot.org/mim/605102 Selective cleavage after Arg-223 in complement component C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile). Mannan-binding lectin (MBL) recognizes patterns of neutral carbohydrates, such as mannose and N-acetylglucosamine, on a wide range of microbial surfaces and is able to initiate activation of the lectin pathway of complement. Displays C1s-like esterolytic activity (cf. EC 3.4.21.42). Belongs to peptidase family S1A. Rhomboid protease Belongs to peptidase family S54. Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite. Cleaves type-1 transmembrane domains using a catalytic triad composed of serine, histidine and asparagine contributed by different transmembrane domains. Important for embryo development in Drosophila melanogaster. These endopeptidases are multi-spanning membrane proteins. Their catalytic site is embedded within the membrane and they cleave type-1 transmembrane domains. Rhomboid is a key regulator of EGF receptor signaling and is responsible for cleaving Spitz, the main ligand of the Drosophila EGF receptor pathway. Hepsin The enzyme has been shown to activate blood coagulation factor VII by cleavage of the 152-Arg-|-Ile-153 peptide bound in BHK cells, thus indicating a possible role in the initiation of blood coagulation. There is no cleavage after aromatic or aliphatic residues. The nature of the residue at S3 also affects hydrolysis, with Gln being much more favorable than Ala. Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys. Belongs to peptidase family S1A. The occupancy of the S2 site is an absolute requirement for catalysis and a basic residue at that site is preferred to an aliphatic residue. This type-II membrane-associated serine peptidase has been implicated in cell growth and development. Protease Do Peptidase Do HrtA heat shock protein High temperature requirement protease A The peptidase acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val. The enzyme has weak peptidase activity with casein and other non-native substrates. Natural substrates of the enzyme include colicin A lysis protein, pilin subunits and MalS from E.coli. This serine endopeptidase is essential for the clearance of denatured or aggregated proteins from the inner-membrane and periplasmic space in Escherichia coli. If attempts at refolding fail, then irreversibly damaged proteins are degraded by peptidases such as this enzyme. Molecular chaperones and peptidases control the folded state of proteins by recognizing hydrophobic stretches of polypeptide that become exposed by misfolding or unfolding. They then bind these hydrophobic substrates to prevent aggregation or assist in protein refolding. Belongs to peptidase family S1B. HtrA2 peptidase HtrA2 protease High temperature requirement protein A2 Serine proteinase OMI Omi stress-regulated endoprotease Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues. Can induce apoptosis in a caspase-independent manner through its peptidase activity and in a caspase-dependent manner by disrupting the interaction between caspase and the inhibitor of apoptosis (IAP). Up-regulated in mammalian cells in response to stress induced by both heat shock and tunicamycin treatment. Belongs to peptidase family S1B. Membrane-type serine protease 1 Epithin MT-SP1 Serine protease 14 Serine protease TADG-15 Serine endopeptidase SNC19 Tumor-associated differentially-expressed gene 15 protein Prostamin Matriptase Cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position. This trypsin-like integral-membrane serine peptidase has been implicated in breast cancer invasion and metastasis. Belongs to peptidase family S1A. Can also activate urokinase plasminogen activator (uPA), which initiates the matrix-degrading peptidase cascade. Can activate hepatocyte growth factor/scattering factor (HGF/SF) by cleavage of the two-chain form at an Arg residue to give active alpha-and beta-HGF, but it does not activate plasminogen, which shares high homology with HGF. C5a peptidase SCP Streptococcal C5a peptidase Surface-associated subtilisin-like serine peptidase with very specific substrate specificity. The primary cleavage site is at 67-His-|-Lys-68 in human C5a with a minor secondary cleavage site at 58-Ala-|-Ser-59. Belongs to peptidase family S8A. Virulent strains of streptococci, including Streptococcus pyogenes, can evade human detection and phagocytosis by destroying the complement chemotaxin C5a. Cleavage of human C5a by this enzyme reduces the ability of C5a to bind receptors on the surface of polymorphonuclear neutrophil leukocytes (PMNLs) and thereby abolishes its chemotactic properties. Aqualysin 1 Caldolysin It has three subsites, S1, S2, and S3, in the substrate binding site. These specificities are similar to those of EC 3.4.21.62 and EC 3.4.21.64. This enzyme from the extreme thermophile, Thermus aquaticus, is an alkaline serine peptidase. Exhibits low specificity toward esters of amino acids with small hydrophobic or aromatic residues at the P1 position. Belongs to peptidase family S8A. The enzyme displays broad specificity for cleavage of insulin B-chain and hydrolyzes elastin substrates such as succinyl-(Ala)(n)-p-nitroanilide (n = 1,2,3) and some peptide esters. The preferred amino acids at the S1 site are Ala and Phe, at the S2 site are Ala and norleucine and at the S3 site are Phe and Ile. S1P protease Sterol regulatory element-binding protein proteinase Site-1 peptidase SKI-1 Subtilase SKI-1/S1P Sterol regulatory element-binding protein site 1 protease Mammalian subtilisin/kexin isozyme 1 SREBP-1 proteinase Sterol-regulated luminal protease Subtilase SKI-1 Proprotein convertase SKI-1 Subtilisin/kexin isozyme 1 Proprotein convertase SKI-1/S1PPS1 Site-1 protease SREBP S1 protease Membrane-bound transcription factor site-1 protease SREBP-2 proteinase S1P endopeptidase SREBP proteinase The enzyme also processes pro-brain-derived neurotrophic factor and undergoes autocatalytic activation in the endoplasmic reticulum through sequential cleavages. Cleaves sterol regulatory element-binding proteins (SREBPs) and thereby initiates a process by which the active fragments of the SREBPs translocate to the nucleus and activate genes controlling the synthesis and uptake of cholesterol and unsaturated fatty acids into the bloodstream. Belongs to peptidase family S8A. Processes precursors containing basic and hydrophobic/aliphatic residues at P4 and P2, respectively, with a relatively relaxed acceptance of amino acids at P1 and P3. The enzyme can also process the unfolded protein response stress factor ATF6 at an Arg-His-Lys-Lys-|-site, and the envelope glycoprotein of the highly infectious Lassa virus and Crimean Congo hemorrhagic fever virus at Arg-Arg-Lys-Lys-|-. BDV NS3 endopeptidase Border disease virus NS3 endopeptidase Bovine viral diarrhea virus NS3 endopeptidase CSFV NS3 endopeptidase Classical swine fever virus NS3 endopeptidase Pestivirus NS3 polyprotein peptidase BVDV NS3 endopeptidase The polyprotein of noncytopathogenic pestiviruses is cleaved co-and post-translationally into at least 11 proteins (N(pro), C, E(rns), E1, E2, p7, NS2-3, NS4A, NS4B, NS5A, and NS5B). Leu is conserved at position P1 for all four cleavage sites. Alanine is found at position P1' of the NS4A-NS4B cleavage site, whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A and NS5A-NS5B cleavage sites. Belongs to peptidase family S31. The genomes of cytopathogenic pestivirus strains express at least one additional protein, called NS3 (p80). This enzyme, which resides in the N-terminal region of NS3 (nonstructural protein 3), is essential for generation of its own C-terminus and for processing of the downstream cleavage sites, leading to the release of the pestivirus nonstructural proteins NS4A, NS4B, NS5A and NS5B. Equine arterivirus serine peptidase 3C-like serine protease Nonstructural protein 4 serine protease 3CLSP 3C-like Ser protease Chymotrypsin-like serine proteinase nsp4 Arterivirus NSP4 Equine arteritis virus serine peptidase Cleavage of (Glu/Gln)-|-(Gly/Ser/Ala) in arterivirus replicase translation products ORF1a and ORF1ab. In the equine arterivirus (EAV), the replicase gene is translated into open reading frame 1a (ORF1a) and ORF1ab polyproteins. Belongs to peptidase family S32. Cleavage of ORF1ab by this enzyme is essential for viral replication. It combines the catalytic system of a chymotrypsin-like serine peptidase (His-Asp-Ser catalytic triad) with the substrate specificity of a 3C-like serine peptidase (Glu or Gln) at the P1 position and a small amino-acid residue (Gly, Ser or Ala) at the P1' position. This enzyme is the main viral proteinase and processes five cleavage sites in the ORF1a protein and three in the ORF1b-encoded part of the ORF1ab protein to yield nonstructural proteins (nsp5-nsp12). NS protease Vp4 protease IPNV Vp4 protease IPNV Vp4 peptidase NS-associated protease Infectious pancreatic necrosis virus protease Infectious pancreatic necrosis birnavirus Vp4 peptidase pVP2 is converted into VP2 by cleavage near the carboxy end of pVP2; this cleavage is most likely due to host-cell proteases rather than VP4. Infectious pancreatic necrosis virus (IPNV) is a birnavirus that causes an acute, contagious disease in young salmonid fish. Cleaves the (Ser/Thr)-Xaa-Ala-|-(Ser/Ala)-Gly motif in the polyprotein NH(2)-pVP2-VP4-VP3-COOH of infectious pancreatic necrosis virus at the pVP2-VP4 and VP4-VP3 junctions. Belongs to peptidase family S50. Differs from most serine peptidases in not having the catalytic triad Ser-His-Asp. As with most viruses that infect eukaryotic cells, the proteolytic processing of viral precursor proteins is a crucial step in the life cycle of this virus. Sporulation factor IV B protease Stage IV sporulation protein B SpoIVB peptidase Belongs to peptidase family S55. This enzyme plays a central role in a regulatory checkpoint (the sigma(K) checkpoint), which coordinates gene expression during the later stages of spore formation in Bacillus subtilis. The enzyme is also essential for the formation of heat-resistant spores. The enzyme is also subject to secondary proteolysis, which presumably inactivates SpoIVB. Self-cleaves 52-Val-|-Asn-53, 62-Ala-|-Phe-63 and 74-Val-|-Thr-75 at the N-terminus of SpoIVB. The enzyme activates proteolytic processing of a sporulation-specific sigma factor, pro-sigma(K), to its mature and active form, sigma(K), by self-cleavage. Kallikrein 7 Stratum corneum chymotryptic enzyme Serine protease 6 SCCE It cleaves the B chain of bovine insulin at 6-Leu-|-Cya-7 (cysteic acid), 16-Tyr-|-Leu-17, 25-Phe-|-Tyr-26 and 26-Tyr-|-Thr-27. Belongs to peptidase family S1A. Cleavage of proteins with aromatic side chains in the P1 position. It is thought to play a role in the desquamation (skin-shedding) of the outer layer of skin, the stratum corneum, by degrading intercellular cohesive structures. This enzyme has wide substrate specificity, being able to degrade heat-denatured bovine casein and the alpha-chain of native human fibrinogen. Ovasin Kallikrein 8 Neuropsin TADG-14 Serine protease 19 Tumor-associated differentially expressed gene 14 Activated by removal of an N-terminal prepropeptide. The highest amidolytic activity is observed using Boc-Val-Pro-Arg-|-7-amido-4-methylcoumarin, which is a substrate of alpha-thrombin. Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys. Belongs to peptidase family S1A. Degrades casein, fibronectin, gelatin, collagen type IV, fibrinogen, and high-molecular-mass kininogen and is associated with diseases such as ovarian cancer and Alzheimer's disease. Substrates lacking basic amino acids in the P1 position are not cleaved. Prorenin converting enzyme 1 PRECE-1 PRECE Kallikrein 13 Prorenin-converting enzyme Epidermal growth factor-binding protein type B MGK-13 Proteinase P Also able to process pro-interleukin-1-beta (pro-IL-1-beta) in mouse submandibular gland to form IL-1-beta. Specific for prorenin from the mouse submandibular gland, as prorenin from the mouse kidney (Ren1) and human prorenin are not substrates. Hydrolyzes mouse Ren2 protein (a species of prorenin present in the submandibular gland) on the carboxy side of the arginine residue at the Lys-Arg-|- pair in the N-terminus, to yield mature renin. Site-directed mutagenesis studies have shown that the enzyme will also cleave prorenin when Lys-Arg is replaced by Arg-Arg or Gln-Arg but the rate of reaction is much slower when Lys-Lys is used. Belongs to peptidase family S1A. Alpha-lytic protease Alpha-lytic endopeptidase Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell walls, elastin and other proteins. Belongs to peptidase family S1E. Ovochymase-2 Oviductal protease Oviductin The egg envelope of the South African clawed frog (Xenopus laevis) is modified during transit of the egg through the pars rectus oviduct, changing the egg envelope from an unfertilizable form to a fertilizable form. It is thought that the enzymatically active protease molecule comprises the N-terminal protease domain coupled to two C-terminal CUB domains, which are related to the mammalian spermadhesin molecules implicated in mediating sperm-envelope interactions. Belongs to peptidase family S1. Preferential cleavage at 371-Gly-Ser-Arg-|-Trp-374 of glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41. Also found in the Japanese toad (Bufo japonicus). This process involves the conversion of glycoprotein gp43 to gp41 (ZPC) by the pars recta protease oviductin. Protease V8 Staphylococcal serine proteinase V8 proteinase Endoproteinase Glu-C Glutamyl endopeptidase Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa. Bonds involving bulky side-chains of hydrophobic amino acids are cleaved at a lower rate. Belongs to peptidase family S1B. In appropriate buffer the specificity is restricted to Glu-|-Xaa. Caldecrin Chymotrypsin C Reacts more readily with Tos-Leu-CH(2)Cl than Tos-Phe-CH(2)Cl, in contrast to chymotrypsin. Preferential cleavage: Leu-|-Xaa, Tyr-|-Xaa, Phe-|-Xaa, Met-|-Xaa, Trp-|-Xaa, Gln-|-Xaa, Asn-|-Xaa. Belongs to peptidase family S1. Cathepsin G From azurophil granules of polymorphonuclear leukocytes. Specificity similar to chymotrypsin C. Belongs to peptidase family S1. Coagulation factor VIIa Formed from the precursor factor VII. http://purl.uniprot.org/mim/227500 Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa. http://purl.uniprot.org/mim/134430 Belongs to peptidase family S1. The cattle enzyme is more readily inhibited by diisopropyl fluorophosphate than the human. Christmas factor Coagulation factor IXa The proenzyme factor IX is activated by EC 3.4.21.27. Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa. http://purl.uniprot.org/mim/306900 Belongs to peptidase family S1. Cucumisin Belongs to peptidase family S8. From the sarcocarp of the musk melon (Cucumis melo). Other endopeptidases from plants, which are less well characterized but presumably of serine-type, include euphorbain from Euphorbia cerifera, solanain from horse-nettle Solanum elaeagnifolium, hurain from Hura crepitans and tabernamontanain from Tabernamontana grandiflora. Hydrolysis of proteins with broad specificity. Prolyl oligopeptidase Prolyl endopeptidase Post-proline cleaving enzyme Post-proline endopeptidase Found in vertebrates, plants and Flavobacterium. Generally cytosolic, commonly activated by thiol compounds. Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides. Belongs to peptidase family S9A. Plasma thromboplastin antecedent Coagulation factor XIa Belongs to peptidase family S1. http://purl.uniprot.org/mim/264900 Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa. The proenzyme XI is activated by EC 3.4.21.38. Sea anemone protease A Metridin Metridium proteinase A Preferential cleavage: Tyr-|-Xaa, Phe-|-Xaa, Leu-|-Xaa; little action on Trp-|-Xaa. Digestive enzyme from the sea anemone Metridium senile. Brachyurin Collagenolytic protease Belongs to peptidase family S1. From hepatopancreas of the fiddler crab (Uca pugilator). Hydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus. Low activity on small molecule substrates of both trypsin and chymotrypsin. Other serine endopeptidases that degrade collagen, but are not listed separately here, include a second endopeptidase from U.pugilator, digestive enzymes from other decapod crustacea, and an enzyme from the fungus Entomophthora coronata. Serum kallikrein Plasma kallikrein Kininogenin Selective for Arg > Lys in P1, in small molecule substrates. Formed from plasma prokallikrein (Fletcher factor) by factor XIIa. Belongs to peptidase family S1. http://purl.uniprot.org/mim/229000 Cleaves selectively Arg-|-Xaa and Lys-|-Xaa bonds, including Lys-|-Arg and Arg-|-Ser bonds in (human) kininogen to release bradykinin. Activates coagulation factors XII, VII and plasminogen. Glandular kallikrein Kininogenin Tissue kallikrein A large number of tissue kallikrein-related sequences have been reported for rats and mice, though fewer seem to exist in other mammals. The few that have been isolated and tested on substrates include mouse EC 3.4.21.54, submandibular proteinase a, epidermal growth-factor-binding protein, nerve growth factor gamma-subunit, rat tonin, submaxillary proteinases A and B, T-kininogenase, kallikreins K7 and K8. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa. Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Belongs to peptidase family S1. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-|-Xaa bonds. Formed from tissue prokallikrein by activation with trypsin. Pancreatic elastase I Pancreatic elastase Pancreatopeptidase E Belongs to peptidase family S1. Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa. Formed by activation of proelastase from mammalian pancreas by trypsin. Bone marrow serine protease Medullasin Neutrophil elastase Leukocyte elastase Lysosomal elastase Belongs to peptidase family S1. Hydrolysis of proteins, including elastin. Preferential cleavage: Val-|-Xaa > Ala-|-Xaa. Differs from pancreatic elastase in specificity on synthetic substrates and in inhibitor sensitivity. http://purl.uniprot.org/mim/162800 Hageman factor Coagulation factor XIIa http://purl.uniprot.org/mim/610618 http://purl.uniprot.org/mim/234000 Formed from the proenzyme, factor XII, by plasma kallikrein or factor XIIa. Selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa. Belongs to peptidase family S1. Also activates plasma prekallikrein and plasminogen. Mast cell protease I Skeletal muscle (SK) protease Chymase Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa > Leu-|-Xaa. In mast cell granules. Belongs to peptidase family S1. Trypsin Alpha-trypsin Beta-trypsin http://purl.uniprot.org/mim/167800 Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa. Belongs to peptidase family S1. Complement subcomponent C1r Activates C1s by proteolytic cleavage so that it can, in turn, activate C2 and C4. Activated from proenzyme C1r in plasma by autocatalytic mechanism during activation of the complement system by the 'classical' route. Selective cleavage of Lys(or Arg)-|-Ile bond in complement subcomponent C1s to form the active form of C1s (EC 3.4.21.42). Belongs to peptidase family S1. http://purl.uniprot.org/mim/216950 C1s esterase Complement subcomponent C1s Cleavage of Arg-|-Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)-|-Lys bond in complement component C2 to form C2a and C2b: the 'classical' pathway C3 convertase. Belongs to peptidase family S1. http://purl.uniprot.org/mim/120580 Activated from proenzyme C1s in plasma by the activated complement subcomponent C1r. Complement C2 C5 convertase Classical-complement-pathway C3/C5 convertase C3 convertase http://purl.uniprot.org/mim/217000 A complex of complement fragments C4b, C2a and C2b. Belongs to peptidase family S1. Selective cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to form C5a and C5b. C3b/C4b inactivator Complement component C3b inactivator Complement factor I C3b inactivator Belongs to peptidase family S1. http://purl.uniprot.org/mim/217030 Inactivates complement subcomponents C3b, iC3b and C4b by proteolytic cleavage. http://purl.uniprot.org/mim/235400 Cleavage of complement subcomponent C3b requires its binding to cofactor H or complement receptor CR1; cleavage of iC3b requires complement receptor CR1; cleavage of C4b requires C4b-binding protein. Complement factor D C3 proactivator convertase C3 convertase activator This reaction is analogous to the activation of complement component C2 by activated complement subcomponent C1s. Belongs to peptidase family S1. Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor. A component of the alternative pathway of complement activation. C5 convertase Properdin factor B C3 convertase Complement factor B C3 proactivator Alternative-complement-pathway C3/C5 convertase Complement component C3/C5 convertase (alternative) Cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to yield C5a and C5b. Cleavage of complement component C5 requires additional C3b which binds C5 and renders it susceptible to cleavage by C3b,Bb complex. Belongs to peptidase family S1. C3b,Bb is stabilized in plasma by factor P. Bb is formed by cleavage of proenzyme factor B by factor D. A bimolecular complex of complement fragment Bb with either C3b or cobra venom factor; Bb contains the active site. Cerevisin Yeast proteinase B Proteinase yscB Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides. Belongs to peptidase family S8. Contains a Cys residue near the active site His, and is inhibited by mercurials. Proteinase ycaB is a similar enzyme from the yeast Candida albicans. Hypodermin C Hypoderma collagenase Belongs to peptidase family S1. Hydrolysis of proteins including native collagen at Xaa-|-Ala bond leaving an N-terminal (75%) and a C-terminal (25%) fragment. Little action on small molecule substrates of trypsin, chymotrypsin, elastase or microbial collagenases. Thrombin Fibrinogenase Belongs to peptidase family S1. Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B. More selective than trypsin and plasmin. http://purl.uniprot.org/mim/176930 Lysyl bond specific proteinase Lysyl endopeptidase Achromobacter proteinase I Enzymes with similar specificity are produced by Lysobacter enzymogenes (endoproteinase Lys-C) and Pseudomonas aeruginosa (Ps-1). Isolated from Achromobacter lyticus. Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro. Belongs to peptidase family S1. ATP-dependent serine proteinase Endopeptidase La ATP-dependent protease La ATP hydrolysis is linked with peptide bond hydrolysis. Hydrolysis of proteins in presence of ATP. Belongs to peptidase family S16. Vanadate inhibits both reactions. A similar enzyme occurs in animal mitochondria. Gamma-renin Cleavage of the Leu-|-Leu bond in synthetic tetradecapeptide renin substrate, to produce angiotensin I, but not active on natural angiotensinogen. Also hydrolyzes Bz-Arg-p-nitroanilide. Belongs to peptidase family S1. Unlike EC 3.4.23.15, does not act on natural angiotensinogen. A member of the tissue kallikrein family, from submandibular glands of male mice. Bitis gabonica serine proteinase Gabonase Venombin AB From the venom of the Gaboon viper Bitis gabonica. Activates factor XIII. Preferential cleavage: Arg-|-Xaa bonds in fibrinogen to form fibrin and release fibrinopeptides A and B. Not inhibited by antithrombin III/heparin or hirudin, unlike EC 3.4.21.5. Plant Leu-proteinase Leucine-specific serine proteinase Leucyl endopeptidase Hydrolysis of proteins. Preferential cleavage: Leu-|-Xaa in small molecule substrates. The enzyme from spinach leaves shows high specificity for leucine in peptides and 4-nitroanilides. Pituitary tryptase Lung tryptase Mast cell tryptase Tryptase Skin tryptase Mast cell protease II Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin. Not inhibited by alpha-1-proteinase inhibitor of alpha-2-macroglobulin. Occurs as a tetrameric molecule with high affinity for heparin, in mast cell granules. Belongs to peptidase family S1. Prothrombase Prothrombinase Coagulation factor Xa Stuart factor Thrombokinase Scutelarin (cf. EC 3.4.21.60) has similar specificity. Formed from the proenzyme factor X by limited proteolysis. Belongs to peptidase family S1. http://purl.uniprot.org/mim/227600 Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin. Scutelarin Taipan activator Similar enzymes are known from the venom of other Australian elapid snakes Pseudonaja textilis, Oxyuranus microlepidotus and Demansia nuchalis affinis. Converts prothrombin to thrombin in the absence of coagulation factor Va, and is potentiated by phospholipid and calcium. From the venom of Taipan snake (Oxyuranus scutellatus). Specificity is similar to that of factor Xa. Selective cleavage of Arg-|-Thr and Arg-|-Ile in prothrombin to form thrombin and two inactive fragments. Binds calcium via gamma-carboxyglutamic acid residues. Kexin Yeast KEX2 protease Proteinase yscF Prohormone-processing endoprotease Paired-basic endopeptidase Inhibited by p-mercuribenzoate. Calcium activated. Belongs to peptidase family S8. Cleavage of -Lys-Arg-|-Xaa- and -Arg-Arg-|-Xaa- bonds to process yeast alpha-factor pheromone and killer toxin precursors. Subtilisin Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides. Subtilisin is a serine endopeptidase that evolved independently of chymotrypsin. It contains no cysteine residues (although these are found in homologous enzymes). Belongs to peptidase family S8. Species variants include subtilisin BPN' (also subtilisin B, subtilopeptidase C, nagarse, nagarse proteinase, subtilisin Novo, bacterial proteinase Novo) and subtilisin Carlsberg (subtilisin A, subtilopeptidase A, alcalase Novo). Similar enzymes are produced by various Bacillus subtilis strains and other Bacillus species. Aspergillopeptidase B Oryzin Aspergillus alkaline proteinase Predominant extracellular alkaline endopeptidase of the mold Aspergillus oryzae. Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides. Belongs to peptidase family S8. Identical or closely related enzymes are produced by A.flavus and A.sojae. Tritirachium alkaline proteinase Proteinase K Endopeptidase K Peptidase K Tritirachium album proteinase K Belongs to peptidase family S8. From the mold Tritirachium album Limber. Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyzes peptide amides. Contains two disulfide bridges and one free Cys near the active site His. Thermomycolase Thermomycolin Belongs to peptidase family S8. Very thermostable. From the thermophilic fungus Malbranchea pulchella var. sulfurea. Rather non-specific hydrolysis of proteins. Preferential cleavage: -Ala-|-Xaa-, -Tyr-|-Xaa-, -Phe-|-Xaa- in small molecular substrates. Contains Cys, but not inhibited by p-mercuribenzoate. Thermitase Thermophilic Streptomyces serine protease The amino acid composition and properties of the thermostable enzyme from Streptomyces rectus var. proteolyticus are closely similar. The N-terminal extension of the polypeptide chain relative to subtilisin contributes to calcium-binding and the high thermostability. Hydrolysis of proteins, including collagen. From Thermoactinomyces vulgaris containing a single Cys, near the active site His, and inhibited by p-mercuribenzoate. Belongs to peptidase family S8. Endopeptidase So E.coli cytoplasmic proteinase Cytoplasmic peptidase. Hydrolysis of proteins, but not Bz-Tyr-OEt, Ac-Phe-beta-naphthylester, or Bz-Arg-OEt. Inhibited by Tos-Phe-CH(2)Cl, but not by Tos-Lys-CH(2)Cl. T-plasminogen activator tPA Tissue plasminogen activator Tissue-type plasminogen activator Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin. Activity is considerably enhanced by fibrin. Belongs to peptidase family S1. http://purl.uniprot.org/mim/173370 Secreted as a single chain precursor which is cleaved to a two-chain form by plasmin. From a wide variety of mammalian tissues, especially endothelial cells. Autoprothrombin IIA Activated blood coagulation factor XIV Protein C (activated) Belongs to peptidase family S1. http://purl.uniprot.org/mim/188050 Formed from protein C, the proenzyme that circulates in plasma, by the action of a complex of thrombin with thrombomodulin, or by serine endopeptidases present in several snake venoms. One of the gamma-carboxyglutamic acid-containing coagulation factors. http://purl.uniprot.org/mim/176860 Degradation of blood coagulation factors Va and VIIIa. Fibrinase Plasmin Fibrinolysin Formed from plasminogen by proteolysis which results in multiple forms of the active plasmin. http://purl.uniprot.org/mim/217090 Converts fibrin into soluble products. Belongs to peptidase family S1. Preferential cleavage: Lys-|- > Arg-|-; higher selectivity than trypsin. http://purl.uniprot.org/mim/188050 Cholesterol-binding proteinase Pancreatic endopeptidase E Elastase III Belongs to peptidase family S1. Preferential cleavage: Ala-|-Xaa. Does not hydrolyze elastin. Binds cholesterol. Unlike elastases, has an acidic pI. From pancreatic juice. Pancreatic elastase II Usually, only one of the pancreatic elastases (see also EC 3.4.21.36) is expressed in a given species; human pancreatic elastase is of type II. Belongs to peptidase family S1. Formed by activation of proelastase II from mammalian pancreas by trypsin. Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin. IgA-specific serine endopeptidase Immunoglobulin A1 protease IgA protease Some other bacterial endopeptidases with similar specificity are of metallotype (see EC 3.4.24.13). Species variants differing slightly in specificity are secreted by Gram-negative bacteria Neisseria gonorrhoeae and Haemophilus influenzae. Belongs to peptidase family S6. Cleavage of immunoglobulin A molecules at certain Pro-|-Xaa bonds in the hinge region. No small molecule substrates are known. Cellular plasminogen activator U-plasminogen activator Urinary plasminogen activator Urokinase Formed from the inactive precursor by action of plasmin or plasma kallikrein. Differs in structure from EC 3.4.21.68, and does not bind to fibrin. Belongs to peptidase family S1. Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin. Venombin A Does not require activation by calcium. Species variants of the enzyme include ancrod from Agkistrodon rhodostoma (Malayan pit viper), batroxobin from Bothrops atrox (South American pit viper) and crotalase from Crotalus adamanteus (Eastern diamondback rattlesnake). A somewhat thrombin-like enzyme from venoms of snakes of the viper/rattlesnake group. Belongs to peptidase family S1. Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme. Furin Paired basic amino acid residue cleaving enzyme Dibasic processing enzyme Prohormone convertase Activated by calcium. Belongs to peptidase family S8. Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors. Myeloblastin Proteinase 3 Wegener's autoantigen Leukocyte proteinase 3 Belongs to peptidase family S1. Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-|-Xaa- > -Val-|-Xaa-. Not inhibited by secretory leukocyte proteinase inhibitor. Semenogelase Prostate-specific antigen Gamma-seminoprotein P-30 antigen Seminin Slowly inhibited by alpha-1-antichymotrypsin. Preferential cleavage: -Tyr-|-Xaa-. Belongs to peptidase family S1. Granzyme A Cytotoxic T-lymphocyte proteinase 1 From cytotoxic T lymphocyte granules. The human enzyme does not cleave Phe-|-Xaa. Belongs to peptidase family S1. Hydrolysis of proteins, including fibronectin, type IV collagen and nucleolin. Preferential cleavage: -Arg-|-Xaa-, -Lys-|-Xaa- >> -Phe-|-Xaa-in small molecule substrates. Cytotoxic t-lymphocyte proteinase 2 Granzyme B Belongs to peptidase family S1. Preferential cleavage: -Asp-|-Xaa- >> -Asn-|-Xaa- > -Met-|-Xaa-, -Ser-|-Xaa-. From cytotoxic T lymphocyte granules. Streptomyces protease A SGPA Streptogrisin A Pronase enzyme A Not inhibited by Tos-Phe-CH(2)Cl or ovomucoid. Hydrolysis of proteins with specificity similar to chymotrypsin. Belongs to peptidase family S1E. SGPB Streptomyces protease B Pronase enzyme B Streptogrisin B Hydrolysis of proteins with trypsin-like specificity. Belongs to peptidase family S1E. Glutamyl endopeptidase II Glutamic acid-specific protease GluSGP Belongs to peptidase family S1E. Preferential cleavage: -Glu-|-Xaa- >> -Asp-|-Xaa-. Preference for Pro or Leu at P2 and Phe at P3. Cleavage of -Glu-|-Asp- and -Glu-|-Pro- bonds is slow. Inhibited by (18-Leu->Glu) modified turkey ovomucoid third domain. Protease II Oligopeptidase B Inhibited by Tos-Lys-CH(2)Cl. Hydrolysis of -Arg-|-Xaa- and -Lys-|-Xaa- bonds in oligopeptides, even when P1' residue is proline. Belongs to peptidase family S9A. Limulus clotting factor C Factor C is activated by Gram-negative bacterial lipopolysaccharides and chymotrypsin. Belongs to peptidase family S1. Inhibited by antithrombin III. Selective cleavage of 103-Arg-|-Ser-104 and 124-Ile-|-Ile-125 bonds in Limulus clotting factor B to form activated factor B. Cleavage of -Pro-Arg-|-Xaa- bonds in synthetic substrates. From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus. Limulus clotting factor B Selective cleavage of 98-Arg-|-Ile-99 bond in Limulus proclotting enzyme to form active clotting enzyme. Factor B is activated by factor C. From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus. Limulus clotting enzyme Selective cleavage of 18-Arg-|- and 47-Arg-|- bonds in coagulogen to form coagulin and fragments. From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus. Limulus clotting enzyme is activated by factor B. Belongs to peptidase family S1. Repressor lexA Belongs to peptidase family S24. In the presence of single-stranded DNA, the recA protein interacts with lexA causing an autocatalytic cleavage which disrupts the DNA-binding part of lexA, leading to derepression of the SOS regulon and eventually DNA repair. Hydrolysis of Ala-|-Gly bond in repressor lexA. The activity was previously attributed to the recA protein (formerly EC 3.4.99.37). SPase I Phage-procoat-leader peptidase Signal peptidase I Bacterial leader peptidase I Unaffected by inhibitors of most serine peptidases, but site-directed mutagenesis implicates a Ser/Lys catalytic dyad in activity. Cleaves a single bond -Ala-|-Ala-in M13 phage procoat protein, producing free signal peptide and coat protein. Eukaryote signal peptidases that may have somewhat different specificity are known from the endoplasmic reticulum membrane and mitochondrial inner membrane. Belongs to peptidase family S26. Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins. Enteropeptidase Enterokinase Not inhibited by protein inhibitors of trypsin. Activates trypsinogen. Belongs to peptidase family S1. Activation of trypsinogen by selective cleavage of 6-Lys-|-Ile-7 bond. http://purl.uniprot.org/mim/226200 Sindbis virus protease NsP2 proteinase Togavirin Once released, the core protein does not retain catalytic activity. Belongs to peptidase family S3. Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond. Yellow fever virus protease NS2B-3 proteinase Flavivirin Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala. Endopeptidase Ti Protease Ti Caseinolytic protease Endopeptidase Clp Belongs to peptidase family S14. Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). Prohormone convertase I Proprotein convertase 1 Neuroendocrine convertase 1 PC1 NEC 1 Usually processing of prodynorphin occurs at a bond in which P2 is Thr. Release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds. http://purl.uniprot.org/mim/600955 Present in the regulated secretory pathway of neuroendocrine cells, commonly actin co-operatively with prohormone convertase 2. Belongs to peptidase family S8. Unlike prohormone convertase 2, does not cleave proluteinizing-hormone-releasing hormone. A calcium dependent enzyme, maximally active at about pH 5.5. Substrates include pro-opiomelanocortin, prorenin, proenkephalin, prodynorphin, prosomatostatin and proinsulin. NEC 2 Neuroendocrine convertase 2 Proprotein convertase 2 Prohormone convertase II PC2 Usually processing of prodynorphin occurs at a bond in which P2 is Thr. A calcium dependent enzyme, maximally active at about pH 5.5. Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds. Unlike prohormone convertase 1, does not cleave prorenin or prosomatostatin. Specificity is broader than that of prohormone convertase 1. Belongs to peptidase family S8. Substrates include pro-opiomelanocortin, proenkephalin, prodynorphin, proinsulin and proluteinizing-hormone-releasing hormone. Present in the regulated secretory pathway of neuroendocrine cells, commonly actin co-operatively with prohormone convertase 1. Factor V-activating proteinase Snake venom factor V activator RVV-V component Belongs to peptidase family S1. Fully activates human clotting factor V by a single cleavage at the 1545-Trp-Tyr-Leu-Arg-|-Ser-Asn-Asn-Gly-1552 bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO(2). Inhibited by diisopropyl fluorophosphate. Extracellular lactococcal proteinase Lactococcal cell envelope-associated proteinase Lactocepin Wall-associated serine proteinase Endopeptidase activity with very broad specificity, although some subsite preference have been noted, e.g. large hydrophobic residues in the P1 and P4 positions, and Pro in the P2 position. Best known for its action on caseins, although it has been shown to hydrolyze hemoglobin and oxidized insulin B-chain. Specificity differences between lactocepins from different starter strains may be partly responsible for imparating different flavor qualities to cheese. Responsible for the hydrolysis of casein in milk and the provision of peptides essential for cell growth. Belongs to peptidase family S8. Assemblin Involved in the breakdown of the scaffold protein during the late stages of assembly of the herpes-virus virion. Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein. Belongs to peptidase family S21. Inhibited by diisopropyl fluorophosphate. Cpro-2 Hepatitis C virus NS3 serine proteinase Hepacivirin The enzyme is greatly activated by binding of the 54-residue NS4A 'cofactor' protein also derived from the viral polyprotein. Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'. Belongs to peptidase family S29. Encoded by the genome of the viruses of the hepatitis C group, and contributes to the maturation of the precursor polyproteins. Spermosin Belongs to peptidase family S1. Hydrolyzes arginyl bonds, preferably with Pro in the P2 position. The enzyme from the ascidian (Prochordate) Halocynthia roretzi is localized in the sperm head, and released during sperm activation. A proline-rich region is involved in binding to the vitelline coat of the egg. Cysteine endopeptidases Cathepsin B1 Cathepsin B An intracellular (lysosomal) enzyme. Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides. Belongs to peptidase family C1. Streptococcus peptidase A Streptopain Streptococcal proteinase Streptococcal cysteine proteinase Belongs to peptidase family C10. From the bacterium, group A Streptococcus. Formed from the proenzyme by limited proteolysis. Preferential cleavage with hydrophobic residues at P2, P1 and P1'. Actinidia anionic protease Actinidain Actinidin Specificity close to that of papain. From the kiwi fruit or Chinese gooseberry (Actinidia chinensis). Belongs to peptidase family C1. Cathepsin L Belongs to peptidase family C1. Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity. A lysosomal enzyme that is readily inhibited by the diazomethane inhibitor Z-Phe-Phe-CHN(2) or the epoxide inhibitor E-64. Cathepsin H Cathepsin B3 N-benzoylarginine-beta-naphthylamide hydrolase Aleurain Cathepsin BA Because of the combination of endopeptidase and aminopeptidase activity it can be considered as 'endoaminopeptidase'. Present in lysosomes of mammalian cells. Belongs to peptidase family C1. Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase. Papain Papaya peptidase I Inhibited by compound E-64 and proteins of the cystatin family. Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'. From latex of the papaya (Carica papaya). Belongs to peptidase family C1. Cathepsin T Interconversion of the three forms of EC 2.6.1.5. Degrades azocasein and denatured hemoglobin; the only native protein on which it has been shown to act is EC 2.6.1.5. Papaya proteinase IV Papaya peptidase B Glycyl endopeptidase Belongs to peptidase family C1. Preferential cleavage: Gly-|-Xaa, in proteins and in small molecule substrates. Not inhibited by chicken cystatin, unlike most other homologs of papain. From the papaya plant, Carica papaya. Cancer procoagulant Apparently produced only by malignant and fetal cells. Specific cleavage of Arg-|-Ile bond in Factor X to form Factor Xa. Cathepsin S Belongs to peptidase family C1. A lysosomal cysteine endopeptidase that is unusual among such enzymes for its stability to neutral pH. Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|-Xaa compound. Foot-and-mouth protease 3C Picornain 3C Rhinovirus protease 3C Poliovirus protease 3C Picornavirus endopeptidase 3C Larger than the homologous virus picornain 2A. Belongs to peptidase family C3. Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly. From entero-, rhino-, aphto-and cardioviruses. Picornavirus endopeptidase 2A Picornain 2A Poliovirus protease 2A Rhinovirus protease 2A Belongs to peptidase family C3. Smaller than the homologous virus picornain 3C. From entero-, rhino-, aphto-and cardioviruses. Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. Ficin Ficain Belongs to peptidase family C1. Cysteine endopeptidases with similar properties are present in other members of the large genus Ficus. The major proteolytic component of the latex of fig, Ficus glabrata. Specificity similar to that of papain. Caricain Papaya peptidase II Papaya proteinase Q Papaya proteinase III Papaya proteinase Omega Papaya peptidase A Belongs to peptidase family C1. From the papaya plant, Carica papaya. Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain. Ananain From stem of pineapple plant, Ananas comosus. Differs from stem and fruit bromelains in being inhibited by chicken cystatin. Belongs to peptidase family C1. Hydrolysis of proteins with broad specificity for peptide bonds. Best reported small molecule substrate Bz-Phe-Val-Arg-|-NHMec, but broader specificity than fruit bromelain. Stem bromelain Bromelain The most abundant of cysteine endopeptidases of the stem of the pineapple plant, Ananas comosus. Scarcely inhibited by chicken cystatin and also very slowly inactivated by E-64. Belongs to peptidase family C1. Distinct from the bromelain found in the pineapple fruit (EC 3.4.22.33). Broad specificity for cleavage of proteins, but strong preference for Z-Arg-Arg-|-NHMec among small molecule substrates. Fruit bromelain Belongs to peptidase family C1. Another cysteine endopeptidase, with similar action on small molecule substrates, pinguinain (formerly EC 3.4.99.18), is obtained from the related plant, Bromelia pinguin, but pinguinain differs from fruit bromelain in being inhibited by chicken cystatin. Scarcely inhibited by chicken cystatin. From the pineapple plant, Ananas comosus. Hydrolysis of proteins with broad specificity for peptide bonds. Bz-Phe-Val-Arg-|-NHMec is a good synthetic substrate, but there is no action on Z-Arg-Arg-|-NHMec (c.f. stem bromelain). Legumain Bean endopeptidase Hemoglobinase Phaseolin Vicilin peptidohydrolase Asparaginyl endopeptidase Belongs to peptidase family C13. Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa-bonds. Not inhibited by compound E-64. Best known from legume seeds, the trematode Schistosoma mansoni and mammalian lysosomes. Histolysin Histolysain Belongs to peptidase family C1. Hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg-|-Xaa in small molecule substrates including Z-Arg-Arg-|-NHMec. From the protozoan, Entamoeba histolytica. Interleukin-1-beta convertase Caspase-1 Interleukin 1-beta converting enzyme Interleukin-1 beta convertase precursor Interleukin 1-beta-converting endopeptidase Prointerleukin 1-beta protease Pro-interleukin 1-beta proteinase Caspase-11 plays a critical role in the activation of caspase-1 in mice whereas caspase-4 enhances its activation in humans. Cleaves pro-interleukin-1-beta (pro-IL-1-beta) to form mature IL-1-beta, a potent mediator of inflammation. Belongs to peptidase family C14. Part of the family of inflammatory-caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-gamma-inducing factor. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-. Inhibited by Ac-Tyr-Val-Ala-Asp-CHO. Argingipain Arg-gingipain Gingipain-1 Gingipain R Hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1. Strongly activated by glycine and stabilized by calcium. Belongs to peptidase family C25. Cathepsin O Cathepsin X Cathepsin O2 Cathepsin K Broad proteolytic activity. With small-molecule substrates and inhibitors, the major determinant of specificity is P2, which is preferably Leu, Met > Phe, and not Arg. Prominently expressed in mammalian osteoclasts, and believed to play a role in bone resorption. Belongs to peptidase family C1. http://purl.uniprot.org/mim/265800 Adenain Belongs to peptidase family C5. A cysteine endopeptidase from adenoviruses. Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly-Xaa-|-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid). Activity is greatly stimulated by the binding to the enzyme of an 11-residue peptide from the adenovirus capsid protein pre-VI at a site separate from the active site. Bleomycin hydrolase Aminopeptidase C (Lactococcus lactis) Hydrolase H from chicken muscle has many similarities to bleomycin hydrolase, but hydrolyzes Ph-CO-Arg-2-naphthylamine as well as aminopeptidase substrates. Known from bacteria as well as eukaryotic organisms. Bleomycin can scarcely be the natural substrate, and there are reports of limited endopeptidase activity. Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred. Belongs to peptidase family C1. The active sites are on the walls of a central channel through the molecule, and access of substrate molecules to them is obstructed by this and by the C-terminus of each polypeptide chain. Cathepsin F The recombinant enzyme cleaves synthetic substrates with Phe and Leu (better than Val) in P2, with high specificity constant (k(cat)/K(m)) comparable to that of cathepsin L. The enzyme is unstable at neutral pH values and is inhibited by compound E-64. Belongs to peptidase family C1. Cathepsin O The recombinant human enzyme hydrolyzes synthetic endopeptidase substrates including Z-Phe-Arg-NHMec and Z-Arg-Arg-NHMec. Belongs to peptidase family C1. The recombinant human enzyme is catalytically active at pH 6.0 and is inhibited by compound E-64. Cathepsin U Cathepsin L2 Cathepsin V Compound E-64, leupeptin and chicken cystatin are inhibitors. Belongs to peptidase family C1. The recombinant enzyme hydrolyzes proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec). Maximally active at pH 5.7 and unstable at neutral pH. Nuclear-inclusion-a endopeptidase Potyvirus NIa protease Belongs to peptidase family C4. Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved. The potyviruses cause diseases in plants, and inclusion bodies appear in the host cell nuclei, protein a of these being the endopeptidase. It is also reported that transgenic plants expressing the enzyme are resistant to viral infection. The enzyme finds practical use when encoded in vectors for the artificial expression of recombinant fusion proteins, since it can confer on them the capacity for autolytic cleavage. HC-Pro Helper-component proteinase Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein. Known from many potyviruses. Belongs to peptidase family C6. The N-terminal region is required for aphid transmission and efficient genome amplification, the central region is required for long-distance movement in plants, and the C-terminal domain has cysteine endopeptidase activity. The helper component-proteinase of the tobacco etch virus is a multifunctional protein with several known activities. L-peptidase Belongs to peptidase family C28. Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-. The tertiary structure reveals a distant relationship to papain and, consistent with this, compound E-64 is inhibitory. Destruction of initiation factor eIF-4G has the effect of shutting off host-cell protein synthesis while allowing synthesis of viral proteins to continue. Best known from foot-and-mouth disease virus, but occurs in other aphthoviruses and cardioviruses. Lys-gingipain Gingipain K PrtP proteinase Known from the bacterium Porphyromonas gingivalis and contributes to the pathogenicity of the organism. Belongs to peptidase family C25. Endopeptidase with strict specificity for lysyl bonds. Activity is stimulated by glycine. Staphopain Staphylopain Broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates. Assays are conveniently made with hemoglobin, casein or Z-Phe-Arg-NHMec as substrate. Known from species of Staphylococcus. Belongs to peptidase family C47. Separase Separin All bonds known to be hydrolyzed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by an hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage. S.cerevisiae separase is also known to cleave the Rec8 subunit of a meiotic cohesin complex and the kinetochore protein Slk19. Belongs to peptidase family C50. In both Saccharomyces cerevisiae and human cells, cleavage of the cohesin subunit Scc1 by separase is required for sister chromatid separation in mitosis. V-cath endopeptidase Viral cathepsin Baculovirus cathepsin Contributes to the liquefaction of the tissues of the insect host in the late stages of infection by the baculovirus. Belongs to peptidase family C1. Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B. Evansain Cruzipain Congopain Trypanopain Cruzain Is located in the digestive vacuoles of the parasitic trypanosome and contributes to the nutrition of the organism by digestion of host proteins. Broad endopeptidase specificity similar to that of cathepsin L. Belongs to peptidase family C1. Calcium-activated neutral protease I Calpain-1 Mu-calpain Broad endopeptidase specificity. Calcium The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC 3.4.22.53. Belongs to peptidase family C2. Cytosolic in animal cells. Milli-calpain Calcium-activated neutral protease II M-calpain Calpain-2 The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC 3.4.22.52. Calcium Cytosolic in animal cells. Broad endopeptidase specificity. Belongs to peptidase family C2. Calpain-3 Calpain p94 CANP 3 CAPN3 Calpain L3 Muscle-specific calcium-activated neutral protease 3 Calcium-activated neutral proteinase 3 Broad endopeptidase activity. Found in skeletal muscle. Substrates include the protein itself and connectin/titin. Calcium Activated by autoproteolytic cleavage of insertion sequence 1 (IS1), which allows substrates and inhibitors gain access to the active site. Belongs to peptidase family C2. http://purl.uniprot.org/mim/253600 NEDD-2 ICH-1 Neural precursor cell expressed developmentally down-regulated protein 2 Caspase-2 CASP-2 NEDD2 protein Two forms of caspase-2 exist that have antagonistic effects: caspase-2L induces programd cell death and caspase-2S suppresses cell death. Belongs to peptidase family C14. Caspase-2 is activated by caspase-3 (EC 3.4.22.56), or by a caspase-3-like protease. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Activation involves cleavage of the N-terminal prodomain, followed by self-proteolysis between the large and small subunits of pro-caspase-2 and further proteolysis into smaller fragments. Alpha-II-spectrin, a component of the membrane cytoskeleton, is a substrate of the large isoform of pro-caspase-2 (caspase-2L) but not of the short isoform (caspase-2S). Apart from itself, the enzyme can cleave golgin-16, which is present in the Golgi complex and has a cleavage site that is unique for caspase-2. Strict requirement for an Asp residue at P1, with 316-asp being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-. Caspase-2 is an initiator caspase, as are caspases-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.64). Proteolysis occurs at Asp residues and the preferred substrate for this enzyme is a pentapeptide rather than a tetrapeptide. Yama protein CASP-3 Apopain CPP32 Caspase-3 Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position. These caspases are responsible for the proteolysis of the majority of cellular polypeptides, (e.g. poly(ADP-ribose) polymerase (PARP)), which leads to the apoptotic phenotype. Activation occurs by inter-domain cleavage followed by removal of the N-terminal prodomain. Caspase-3 is an effector/executioner caspase, as are caspase-6 (EC 3.4.22.59) and caspase-7 (EC 3.4.22.60). While Asp-Glu-(Val/Ile)-Asp is thought to be the preferred cleavage sequence, the enzyme can accommodate different residues at P2 and P3 of the substrate. Belongs to peptidase family C14. Caspase-3 can activate procaspase-2 (EC 3.4.22.55). Like caspase-2, a hydrophobic residue at P5 of caspase-3 leads to more efficient hydrolysis, e.g. (Val/Leu)-Asp-Val-Ala-Asp-|-is a better substrate than Asp-Val-Ala-Asp-|-. This is not the case for caspase-7. Procaspase-3 can be activated by caspase-1 (EC 3.4.22.36), caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63) as well as by the serine protease granzyme B. CASP-4 ICE(rel)II ICErel-II Caspase-4 Ich-2 Belongs to peptidase family C14. Able to cleave itself and the p30 caspase-1 precursor, but, unlike caspase-1, it is very inefficient at generating mature interleukin-1-beta (IL-1-beta) from pro-IL-1-beta. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. The caspase-1 inhibitor Ac-Tyr-Val-Ala-Asp-CHO can also inhibit this enzyme, but more slowly. Both this enzyme and caspase-5 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17). Strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but also cleaves at Asp-Glu-Val-Asp-|-. Part of the family of inflammatory-caspases, which also includes caspase-1 (EC 3.4.22.36) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Ich-3 CASP-5 Caspase-5 ICH-3 protease ICErel-III Strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but also cleaves at Asp-Glu-Val-Asp-|-. The enzyme is able to cleave itself and the p30 caspase-1 precursor, but is very inefficient at generating mature interleukin-1-beta (IL-1-beta) from pro-IL-1-beta. Both this enzyme and caspase-4 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17). This enzyme is part of the family of inflammatory-caspases, which also includes caspase-1 (EC 3.4.22.36) and caspase-4 (EC 3.4.22.57) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Unlike caspase-4, this enzyme can be induced by lipopolysaccharide. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Belongs to peptidase family C14. Caspase-6 Mch2 Apoptotic protease Mch-2 CASP-6 Caspase-6 can cleave its prodomain to produce mature caspase-6, which directly activates caspase-8 (EC 3.4.22.61) and leads to cytochrome c release from the mitochondria; the release of cytochrome c, which is an essential component of the intrinsic apoptosis pathway. Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-. Caspase-6 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-7 (EC 3.4.22.60). Can also cleave and inactivate lamins, the intermediate filament scaffold proteins of the nuclear envelope, leading to nuclear fragementation in the final phases of apoptosis. These caspases are responsible for the proteolysis of the majority of cellular polypeptides, (e.g. poly(ADP-ribose) polymerase (PARP)), which lead to the apoptotic phenotype. Belongs to peptidase family C14. Chymopapain Papaya proteinase II Specificity similar to that of papain. It has multiple chromatographic forms. Belongs to peptidase family C1. The major endopeptidase of papaya (Carica papaya) latex. Mch3 ICE-like apoptotic protease 3 CASP-7 ICE-LAP3 CMH-1 Apoptotic protease Mch-3 Caspase-7 Although a hydrophobic residue at P5 of caspase-2 (EC 3.4.22.55) and caspase-3 leads to more efficient hydrolysis, the amino-acid residue at this location in caspase-7 has no effect. Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-. Caspase-7 is activated by the initiator caspases (caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63)). These caspases are responsible for the proteolysis of the majority of cellular polypeptides, (e.g. poly(ADP-ribose) polymerase (PARP)), which lead to the apoptotic phenotype. Removal of the N-terminal prodomain occurs before cleavage in the linker region between the large and small subunits. Belongs to peptidase family C14. Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59). Apoptotic cysteine protease Apoptotic protease Mch-5 Mch5 FLICE Mammalian Ced-3 homolog 5 CASP-8 FADD-homologous ICE/CED-3-like protease CAP4 FADD-like ICE MACH Caspase-8 ICE-like apoptotic protease 5 MORT1-associated CED-3 homolog Strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala). Linked to cell surface death receptors such as Fas. http://purl.uniprot.org/mim/607271 Has very broad P4 specificity, tolerating substrates with Asp, Val or Leu in this position. Has a preference for Glu at P3 and prefers small residues, such as Gly, Ser and Ala at the P1' position. Endogenous substrates for caspase-8 include procaspase-3, the pro-apoptotic Bcl-2 family member Bid, RIP, PAK2 and the caspase-8 activity modulator FLIP(L). When Fas is aggregated by the Fas ligand, procaspase-8 is recruited to the death receptor where it is activated. Caspase-8 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63). Belongs to peptidase family C14. Apical activator of the extrinsic (death receptor) apoptosis pathway, triggered by death receptor ligation. Contains two tandem death effector domains (DEDs) in its N-terminal prodomain, which play a role in procaspase activation. Caspase-9 Apoptotic protease-activating factor 3 CASP-9 Apoptotic protease Mch-6 APAF-3 ICE-like apoptotic protease 6 ICE-LAP6 Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Phosphorylation of caspase-9 from some species by Akt, a serine-threonine protein kinase, inhibits caspase activity in vitro and caspase activation in vivo. Belongs in peptidase family C14. An alternatively spliced version of caspase-9 also exists, caspase-9S, that inhibits apoptosis, similar to the situation found with caspase-2. Procaspase-3 is the enzyme's physiological substrate. The activity of caspase-9 is increased dramatically upon association with the apoptosome but the enzyme can be activated without proteolytic cleavage. Caspase-9 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) and caspase-10 (EC 3.4.22.63). Mch4 CASP-10 Caspase-10 FLICE2 ICE-like apoptotic protease 4 FAS-associated death domain protein interleukin-1-beta-converting enzyme 2 Apoptotic protease Mch-4 Belongs to peptidase family C14. The p15 fragment is N-myristoylated and enhances cytochrome c release from mitochondria (which initiatiates the intrinsic apoptosis pathway). http://purl.uniprot.org/mim/603909 Bid can be further cleaved by caspase-10 and granzyme B but not by caspase-3 and caspase-8 at Ile-Glu-Thr-Asp-|-to yield a p13 fragment that is not N-myristoylated. Caspase-10 is an initiator caspase, as are caspase-2 (EC 3.4.22.44), caspase-8 (EC 3.4.22.61) and caspase-9 (EC 3.4.22.62). Has many overlapping substrates in common with caspase-8, such as RIP (the cleavage of which impairs NF-kappa-B survival signaling and starts the cell-death process) and PAK2 (associated with some of the morphological features of apoptosis, such as cell rounding and apoptotic body formation). Bid, a Bcl2 protein, can be cleaved by caspase-3 (EC 3.4.22.56), caspase-8 and caspase-10 at Lys-Gln-Thr-Asp-|-to yield the pro-apoptotic p15 fragment. Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Leu-Gln-Thr-Asp-|-Gly. Like caspase-8, it contains two tandem death effector domains (DEDs) in its N-terminal prodomain, which play a role in procaspase activation. CASP-11 Caspase-11 Belongs to peptidase family C14. Part of the family of inflammatory-caspases, which also includes caspase-1 (EC 3.4.22.36), caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Not only activates caspase-1, which is required for the maturation of proinflammatory cytokines such as interleukin-1-beta (IL-1-beta) and IL-18, but it also activates caspase-3 (EC 3.4.22.56), which leads to cellular apoptosis under pathological conditions. Strict requirement for Asp at the P1 position and has a preferred cleavage sequence of (Ile/Leu/Val/Phe)-Gly-His-Asp-|-. Like caspase-5, but unlike caspase-4, this enzyme can be induced by lipopolysaccharide. Endopeptidase 1 (mite) Peptidase 1 (mite) Allergen Der p 1 Major mite fecal allergen Der p 1 The enzyme shows only a slight preference for basic amino acids in the P1 and P3 positions and a preference for aliphatic amino acids such as Ile, Pro, Val, Leu and norleucine in the P4 position. Broad endopeptidase specificity. This enzyme, derived from the house dust mite, is a major component of the allergic immune response. Belongs to peptidase family C1A. The substrate specificity of this enzyme is not altogether clear; it cleaves the low-affinity IgE receptor CD23 at 298-Glu-|-Ser-299 and 155-Ser-|-Ser-156. Using a positional scanning combinatorial library, it was found that the major substrate-specificity determinant is for Ala in the P2 position. It also cleaves the pulmonary structural proteins occludin and claudin at Leu-|-Leu, Asp-|-Leu and at Gly-|-Thr bonds, and it can also cleave the alpha subunit of the interleukin-2 (IL-2) receptor (CD25). Asclepain It has multiple forms. Specificity similar to that of papain. From the latex of milkweed, Asclepias syriaca. Belongs to peptidase family C1. Clostripain Clostridiopeptidase B Belongs to peptidase family C11. From the bacterium Clostridium histolyticum. Preferential cleavage: Arg-|-Xaa, including Arg-|-Pro bond, but not Lys-|-Xaa. Activated by calcium; inhibited by EDTA. Aspartic endopeptidases Pepsin A Pepsin The predominant endopeptidase in the gastric juice of vertebrates, formed from pepsinogen A by limited proteolysis. Belongs to peptidase family A1. Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin. Nepenthes aspartic proteinase Nepenthesin Aspartic endopeptidases are probably present in many other plants, including lotus and sorghum. Similar to pepsin, but also cleaves on either side of Asp and at Lys-|-Arg. From the insectivorous plants Nepenthes sp. (secretions) and Drosera peltata (ground-up leaves). Angiotensin-forming enzyme Renin Angiotensinogenase Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I. Belongs to peptidase family A1. Human immunodeficiency virus type 1 protease HIV-1 retropepsin Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro. Present in human immunodeficiency virus type 1. Contributes to the maturation of the viral particle, and is a target of antiviral drugs. Similar enzymes occur in other retroviruses. Active enzyme is a dimer of identical 11-kDa subunits. Belongs to peptidase family A2. Prohormone converting enzyme Pro-opiomelanocortin converting enzyme A 70 kDa membrane-bound enzyme isolated from cattle pituitary secretory vesicle. Cleavage at paired basic residues in certain prohormones, either between them, or on the carboxyl side. Aspergillopepsin F Aspergillopeptidase A Aspergillopepsin A Trypsinogen kinase Awamorin Proteinase B Proctase B Aspergillopepsin I Found in a variety of Aspergillus species (imperfect fungi): A.awamori, A.foetidus, A.fumigatus, A.kawachii, A.niger, A.oryzae, A.saitoi, and A.sojae. Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk. Belongs to peptidase family A1. Aspergillus niger var macrosporus aspartic proteinase Proteinase A Aspergillopepsin II Proctase A Belongs to peptidase family A4. Isolated from Aspergillus niger var. macrosporus, distinct from aspergillopepsin I in specificity and insensitivity to pepstatin. Preferential cleavage in B chain of insulin: 3-Asn-|-Gln-4, 13-Gly-|-Ala-14, and 26-Tyr-|-Thr-27. Parapepsin I Pepsin B Degradation of gelatin; little activity on hemoglobin. Specificity on B chain of insulin more restricted than that of pepsin A; does not cleave 1-Phe-|-Val-2, 4-Gln-|-His-5 or 23-Gly-|-Phe-24. Belongs to peptidase family A1. Peptidase A Penicillopepsin Penicillium janthinellum aspartic protease Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen. Belongs to peptidase family A1. Closely related enzymes have been isolated from P.roqueforti and P.duponti. From the imperfect fungus Penicillium janthinellum. Rhizopus aspartic proteinase Rhizopuspepsin Belongs to peptidase family A1. From the zygomycete fungi Rhizopus chinensis and R.niveus. Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of insulin. Endothia aspartic proteinase Endothiapepsin Hydrolysis of proteins with specificity similar to that of pepsin A, prefers hydrophobic residues at P1 and P1', but does not cleave 14-Ala-|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk. Belongs to peptidase family A1. From the ascomycete Endothia parasitica. Mucor rennin Mucorpepsin Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen. Belongs to peptidase family A1. Hydrolysis of proteins, favoring hydrophobic residues at P1 and P1'. Isolated from the zygomycete fungi Mucor pusillus and M.miehei. Candidapepsin Candida albicans aspartic proteinase Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin. Belongs to peptidase family A1. This endopeptidase from the imperfect yeast Candida albicans is inhibited by pepstatin, but not by methyl 2-diazoacetamido-hexanoate or 1,2-epoxy-3-(p-nitrophenoxy)propane. Saccharopepsin Yeast endopeptidase A Saccharomyces aspartic proteinase Belongs to peptidase family A1. Located in the vacuole. Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg. Rhodotorula aspartic proteinase Rhodotorulapepsin Somewhat similar enzymes have been isolated from the imperfect yeast-like organism Cladosporium sp. and the imperfect fungus Paecilomyces varioti. From the imperfect yeast Rhodotorula glutinis. Specificity similar to that of pepsin A. Cleaves Z-Lys-|-Ala-Ala-Ala and activates trypsinogen. Acrocylindrium proteinase Acrocylindropepsin Has a very low pH optimum on casein of 2.0. Preference for hydrophobic residue at P1 and P1'. Action on the B chain of insulin is generally similar to that of pepsin A, but it also cleaves 6-Leu-|-Cys(SO(3)H)-7, 21-Glu-|-Arg-22 and 3-Asn-|-Gln-4, although not 4-Gln-|-His-5. From the imperfect fungus Acrocylindrium sp. Polyporus aspartic proteinase Polyporopepsin Belongs to peptidase family A1. Milk clotting activity, broad specificity, but fails to cleave 15-Leu-|-Tyr-16 or 16-Tyr-|-Leu-17 of insulin B chain. From the basidiomycete Irpex lacteus (also known as Polyporus tulipiferae). Gastricsin Pepsin C Seminal plasma contains a zymogen that is immunologically identical with progastricsin. Formed from progastricsin, apparently in the gastric juice of most vertebrates. Belongs to peptidase family A1. More restricted specificity than pepsin A, but shows preferential cleavage at Tyr-|-Xaa bonds. High activity on hemoglobin. In addition to the fundus, progastricsin is also secreted in antrum and proximal duodenum. Proteinase Ia Pycnoporopepsin Specificity similar to pepsin A, but narrower, cleaving only three bonds in the B chain of insulin: 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17, and 24-Phe-|-Phe-25. From the basidiomycete Pycnoporus sanguineus, formerly known as P.coccineus and Trametes sanguinea. Scytalidium aspartic proteinase A Scytalidopepsin A A related enzyme from the same organism, proteinase C, is also insensitive to these inhibitors and has molecular weight 406 kDa. Isolated from the imperfect fungus Scytalidium lignicolum. Hydrolysis of proteins with specificity similar to that of pepsin A, but also cleaves 7-Cys(SO(3)H)-|-Gly-8 and 17-Leu-|-Val-18 in the B chain of insulin. Not inhibited by pepstatin-Ac, methyl 2-diazoacetamidohexanoate or 1,2-epoxy-3-(p-nitrophenyl)propane. Scytalidium aspartic proteinase B Scytalidopepsin B 1,2-epoxy-3-(p-nitrophenoxy)propane reacts with Glu-53, which replaces one of the aspartic residues at the active center. One of the smallest aspartic endopeptidases active as the monomer, with molecular weight 22 kDa. Belongs to peptidase family G1. Similarly inhibitor-resistant endopeptidases are found in the basidiomycetes Lentinus edodes and Ganoderma lucidum, and in Polyporus tulipiferae (a second endopeptidase distinct from polyporopepsin), but these are of typical aspartic endopeptidase size. A second endopeptidase from S.lignicolum (see scytalidopepsin A) that is insensitive to pepstatin and methyl 2-diazoacetamidohexanoate. Isolated from the imperfect fungus Scytalidium lignicolum. Hydrolysis of proteins with broad specificity, cleaving 24-Phe-|-Phe-25, but not 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 in the B chain of insulin. Slow-moving proteinase Cathepsin E Erythrocyte membrane aspartic proteinase Found in stomach, spleen, erythrocyte membrane; not lysosomal. Pro-cathepsin E is an 86 kDa disulfide-linked dimer; activation or reduction produces monomers. Belongs to peptidase family A1. Similar to cathepsin D, but slightly broader specificity. Extracellular 'barrier' protein Bar proteinase Barrierpepsin Selective cleavage of 6-Leu-|-Lys-7 bond in the pheromone alpha-mating factor. Belongs to peptidase family A1. SPase II Signal peptidase II Lipoprotein signal peptidase Prolipoprotein-signal peptidase Premurein-leader peptidase Bacterial leader peptidase I Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains. Belongs to peptidase family A8. Release of signal peptides from bacterial membrane prolipoproteins. Inhibited by pepstatin and the antibiotic globomycin. PfAPG Plasmepsin I Aspartic hemoglobinase I Belongs to peptidase family A1. Inhibited by pepstatin. Hydrolysis of the 33-Phe-|-Leu-34 bond in the alpha-chain of hemoglobin, leading to denaturation of molecule. Aspartic hemoglobinase II PfAPD Plasmepsin II Belongs to peptidase family A1. Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves small molecules substrates such as Ala-Leu-Glu-Arg-Thr-Phe-|-Phe(NO(2))-Ser-Phe-Pro-Thr. Inhibited by pepstatin. Chymosin Rennin Belongs to peptidase family A1. Broad specificity similar to that of pepsin A. Clots milk by cleavage of a single 105-Ser-Phe-|-Met-Ala-108 bond in kappa-chain of casein. Found among mammals with postnatal uptake of immunoglobins. Neonatal gastric enzyme with high milk clotting and weak general proteolytic activity, formed from prochymosin. Phytepsin Belongs to peptidase family A1. Known particularly fron barley grain, but present in other plants also. Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S albumin from plant seeds. Yapsin 1 Yeast aspartic protease 3 Aspartic proteinase 3 The homologous product of the MKC7 gene (S.cerevisiae) has similar catalytic activity and has been termed yapsin 2. Can partially substitute for kexin in a deficient strain of Saccharomyces cerevisiae. Belongs to peptidase family A1. Weakly inhibited by pepstatin. Hydrolyzes various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favorable in both non-prime and prime positions. Thermopsin Belongs to peptidase family A5. Specificity similar to pepsin A, prefers bulky hydrophobic side-chains on either side of the scissible bond. Isolated from cells and culture medium of the thermophilic archae Sulfolobus acidocaldarius, optimum digestion at pH 2 and 90 degrees Celsius, inhibited by pepstatin. Another thermostable bacterial endopeptidase has been isolated from Bacillus sp., but this is not inhibited by pepstatin. Prepilin peptidase Although both peptide-bond hydrolysis and N-methylation are catalyzed by the same molecule, the methylation can be inhibited without affecting peptidase activity, and it is believed that the enzyme has two separate catalytic sites. Before assembly, the prepilin molecules require proteolytic processing, which is done by the prepilin peptidase. Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine. Many species of bacteria carry pili on their cell surfaces. Belongs to peptidase family A24. Prepilin peptidase and its homologs play a central role not only in type IV pilus biogenesis but also in transport of macromolecules across cell membranes. These are virulence determinants in pathogenic strains, and are assembled biosynthetically from type IV prepilin subunits. Nodavirus endopeptidase Flock House virus endopeptidase Black Beetle virus endopeptidase Belongs to peptidase family A6. The enzyme is known from several nodaviruses that are pathogens of insects. Hydrolysis of an asparaginyl bond involved in the maturation of the structural protein of the virus, typically -Asn-|-Ala- or -Asn-|-Phe-. A single aspartic residue is critical for activity, and inhibition by EDTA indicates that a metal ion is also important. BACE2 Down region aspartic protease ASP1 Beta-secretase Memapsin 1 Membrane-associated aspartic protease 1 Beta-site APP-cleaving enzyme 2 Beta-site Alzheimer's amyloid precursor protein cleaving enzyme 2 Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein. Can cleave beta-amyloid precursor protein to form the amyloidogenic beta-peptide that is implicated in the pathology of Alzheimer's disease, but is not significantly expressed in human brain. Belongs to peptidase family A1. BACE1 Memapsin 2 Beta-secretase Beta-site APP-cleaving enzyme 1 Beta-site Alzheimer's amyloid precursor protein cleaving enzyme 1 Membrane-associated aspartic protease 2 Suggested to be the major 'beta-secretase' responsible for the cleavage of the beta-amyloid precursor protein to form the amyloidogenic beta-peptide that is implicated in the pathology of Alzheimer's disease. Belongs to peptidase family A1. Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein. HIV-2 retropepsin Belongs to peptidase family A2. Responsible for the post-translational processing of the human immunodeficiency virus polyprotein. Endopeptidase for which the P1 residue is preferably hydrophobic. Coagulase/fibrinolysin Plasminogen activator Pla From the bacterium Yersinia pestis that causes plague. Converts human Glu-plasminogen to plasmin by cleaving the 560-Arg-|-Val-561 peptide bond that is also hydrolyzed by the mammalian u-plasminogen activator and t-plasminogen activator. Also cleaves arginyl bonds in other proteins. Belongs to peptidase family A26. Outer membrane protein 3B Omptin Protease A Protease VII Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. Belongs to peptidase family A26. Shows a preference for cleavage between consecutive basic amino acids, but is capable of cleavage when P1' is a non-basic residue. Cathepsin D http://purl.uniprot.org/mim/610127 Belongs to peptidase family A1. Occurs intracellularly, in lysosomes. Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin. Metalloendopeptidases Crotalus atrox alpha-proteinase Crotalus atrox metalloproteinase Hemorrhagic toxin a Atrolysin A The 60 kDa hemorrhagic toxin 1 of Crotalus ruber ruber shows identical specificity. A hemorrhagic endopeptidase of 68 kDa, one of six hemorrhagic toxins in the venom of the western diamondback rattlesnake. Cleavage of 3-Asn-|-Gln-4, 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in insulin B chain; removes C-terminal Leu from small peptides. Belongs to peptidase family M12B. Zinc Neutral endopeptidase Kidney-brush-border neutral proteinase Enkephalinase Endopeptidase-2 Neprilysin Membrane metalloendopeptidase Belongs to peptidase family M13. Zinc Inhibited by phosphoramidon and thiorphan. Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'. A membrane-bound glycoprotein widely distributed in animal tissues. Hatching enzyme Envelysin Sea-urchin-hatching proteinase Hydrolysis of proteins of the fertilization envelope and dimethylcasein. Zinc Calcium Belongs to peptidase family M10B. Dissolves fertilization envelope in embryos of sea urchin. IgA protease Immunoglobulin A1 proteinase IgA-specific metalloendopeptidase Zinc Found in several pathogenic species of Streptococcus such as S.sanguis and S.pneumoniae. Cleavage of Pro-|-Thr bond in the hinge region of the heavy chain of human IgA. There is also an IgA-specific prolyl endopeptidase of serine-type (see EC 3.4.21.72). Belongs to peptidase family M26. Procollagen N-proteinase Procollagen N-endopeptidase Belongs to peptidase family M12. Cleaves the N-propeptide of collagen chain alpha-1(I) at Pro-|-Gln and of alpha-1(II) and alpha-2(I) at Ala-|-Gln. Does not cleave type III procollagen. Zinc Removes N-terminal propeptides of type I and II collagens prior to fibril assembly. http://purl.uniprot.org/mim/225410 Thimet oligopeptidase Soluble metalloendopeptidase Endopeptidase 24.15 Pz-peptidase Endo-oligopeptidase A Zinc Thiol compounds activate at low concentrations. Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues. Belongs to peptidase family M3. Neurotensin endopeptidase Neurolysin No absolute requirement for a prolyl bond; the enzyme acts on some peptides, such as dynorphin 1-8, that do not contain proline, and does not act on some others that do. Belongs to peptidase family M3. Preferential cleavage in neurotensin: 10-Pro-|-Tyr-11. Zinc Matrix metalloproteinase 3 Proteoglycanase Transin Stromelysin 1 Extracellular endopeptidase of vertebrate tissues. Belongs to peptidase family M10B. Preferential cleavage where P1', P2' and P3' are hydrophobic residues. Degradation of proteoglycans, fibronectin, collagen type III, IV, V and IX and activates procollagenase. Calcium Zinc Endopeptidase-2 Meprin A A membrane-bound metalloendopeptidase of rat and mouse kidney and intestinal brush borders, and salivary ducts. Differences from EC 3.4.24.11 include insensitivity to phosphoramidon and thiorphan. Zinc Belongs to peptidase family M12A. PABA-peptide hydrolase is a very similar enzyme found in human intestinal microvilli. Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues. Procollagen C-endopeptidase Zinc Cleavage of the C-terminal propeptide at Ala-|-Asp in type I and II procollagens and at Arg-|-Asp in type III. The activity is increased by calcium and by an enhancer glycoprotein. Armillaria mellea neutral proteinase Peptidyl-Lys metalloendopeptidase A similar specificity is shown by Myxobacter sp. AL-1 proteinase II (endoproteinase Lys-C). From the honey fungus Armillaria mellea. Preferential cleavage in proteins: -Xaa-|-Lys- (in which Xaa may be Pro). Crayfish small-molecule proteinase Astacin Astacus proteinase Zinc A digestive endopeptidase from the cardia of the crayfish Astacus fluviatilis. Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'. Belongs to peptidase family M12A. Transin 2 Stromelysin 2 Matrix metalloproteinase 10 Digests gelatin types I, III, IV, V, fibronectin and proteoglycan. Zinc Similar to stromelysin 1, but action on collagen types III, IV and V is weak. Belongs to peptidase family M10B. Calcium Matrilysin Matrin Matrix metalloproteinase 7 Uterine metalloendopeptidase Putative (or punctuated) metalloproteinase-1 PUMP-1 Zinc Calcium Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha-2(I) > alpha-1(I). Belongs to peptidase family M10B. Similar in specificity to stromelysin, but more active on azocoll. 72-kDa gelatinase Matrix metalloproteinase 2 Gelatinase A Type IV collagenase Zinc Belongs to peptidase family M10B. Calcium Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln. Aeromonas proteolytica neutral proteinase Aeromonolysin Vibriolysin Thermostable enzyme from Vibrio proteolyticus (formerly Aeromonas proteolytica). Specificity related to, but distinct from, those of the thermolysin and Bacillus subtilis endopeptidase. Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favored residue, which distinguished this enzyme from thermolysin. Zinc Belongs to peptidase family M4. Pseudolysin Pseudomonas aeruginosa neutral metalloproteinase Pseudomonas elastase Calcium Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects. Belongs to peptidase family M4. Causes tissue damage. Zinc Thermolysin Bacillus thermoproteolyticus neutral proteinase A thermostable extracellular metalloendopeptidase containing four calcium ions. Zinc Calcium Enzymes that may be species variants of thermolysin are reported from Micrococcus caseolyticus and Aspergillus oryzae. Belongs to peptidase family M4. Closely related but distinct enzymes are aeromonolysin, pseudolysin, bacillolysin, aureolysin and mycolysin. Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe. Megateriopeptidase Bacillus metalloendopeptidase Bacillus subtilis neutral proteinase Bacillolysin Calcium Zinc Belongs to peptidase family M4. Similar, but not identical, to that of thermolysin. Variants of this enzyme have been found in species of Bacillus including B.subtilis, B.amyloliquefaciens, B.megaterium, B.mesentericus, B.cereus and B.stearothermophilus. Aureolysin Staphylococcus aureus neutral proteinase Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1' residues. Activates the glutamyl endopeptidase (EC 3.4.21.19) of Staphylococcus aureus. Belongs to peptidase family M4. Zinc Calcium Earlier confused with staphylokinase. Clostridium histolyticum collagenase Clostridiopeptidase A Collagenase A Collagenase I Microbial collagenase Class I has forms alpha (68 kDa), beta (115 kDa) and gamma (79 kDa); class II has delta (100 kDa), epsilon (110 kDa) and zeta (125 kDa). The enzymes also act as peptidyl-tripeptidases. Variants of the enzyme have been purified from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio, Vibrio B-30 (ATCC 21250) and V.alginolyticus (previously Achromobacter iophagus). Zinc Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1'; Pro and Ala at P2 and P2'; and hydroxyproline, Ala or Arg at P3'. Belongs to peptidase family M9. Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum. Also known from Streptomyces sp. The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary. Coccolysin Streptococcus thermophilus intracellular proteinase Zinc Belongs to peptidase family M4. A 30 kDa endopeptidase found intracellularly in Streptococcus thermophilus and S.diacetilactis and in the medium of Enterococcus faecalis. Preferential cleavage: Xaa-|-Leu, Xaa-|-Phe, Xaa-|-Tyr, Xaa-|-Ala. Streptomyces griseus neutral proteinase Pronase component Mycolysin From Streptomyces griseus, S.naraensis, and S.cacaoi. Belongs to peptidase family M5. Zinc Preferential cleavage of bonds with hydrophobic residues in P1'. Specificity similar to that of thermolysin, but much more sensitive to inhibition by mercaptoacetyl-Phe-Leu. Beta-lytic metalloendopeptidase Myxobacter beta-lytic proteinase Achromopeptidase component Cleavage of N-acetylmuramoyl-|-Ala, and of the insulin B chain at 23-Gly-|-Phe-24 > 18-Val-|-Cys(SO(3)H). Digests bacterial cell walls. Myxobacter sp. AL-1 proteinase I also has characteristics of this enzyme. Zinc From Achromobacter lyticus and Lysobacter enzymogenes. Belongs to peptidase family M23. Endoproteinase Asp-N Peptidyl-Asp metalloendopeptidase A metalloenzyme isolated from Pseudomonas fragi. Cleavage of Xaa-|-Asp, Xaa-|-Glu and Xaa-|-cysteic acid bonds. Belongs to peptidase family M72. Useful in protein sequencing applications because of its limited specificity. Neutrophil collagenase Matrix metalloproteinase 8 Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I. Zinc Similar to interstitial collagenase in specificity. Belongs to peptidase family M10B. Calcium Stored in the specific granules of neutrophil leukocytes. 92-kDa gelatinase Type V collagenase 92-kDa type IV collagenase Macrophage gelatinase Matrix metalloproteinase 9 Gelatinase B Calcium Cleavage of gelatin types I and V and collagen types IV and V. Zinc Belongs to peptidase family M10B. Promastigote surface endopeptidase Leishmanolysin Glycoprotein gp63 The enzyme can activate its proenzyme by cleavage of the 100-Val-|-Val-101 bond. Contains consensus sequence for a zinc binding site; Z-Tyr-Leu-NHOH is a strong inhibitor. Belongs to peptidase family M8. Calcium Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-. Zinc A membrane-bound glycoprotein found on the promastigote of various species of Leishmania protozoans. An acidic pH optimum is found with certain protein substrates. Proteinase yscD Oligopeptidase yscD Saccharolysin Yeast cysteine proteinase D Belongs to peptidase family M3. Cleavage of Pro-|-Phe and Ala-|-Ala bonds. Zinc Chlamydomonas cell wall degrading protease Gametolysin Lysin Autolysin Gamete lytic enzyme Belongs to peptidase family M11. Zinc Inhibited by phosphoramidon, but also thiol-dependent. Cleavage of the proline- and hydroxyproline-rich proteins of the Chlamydomonas cell wall; also cleaves azocasein, gelatin and Leu-Trp-Met-|-Arg-Phe-Ala. Acid metalloproteinase Microbial neutral proteinase II Deuterolysin Penicillium roqueforti protease II Proteolytic activity found in Penicillium roqueforti, P.caseicolum, Aspergillus sojae and A.oryzae. Optimum pH of 5 for digesting various proteins. Belongs to peptidase family M35. A distinct A.sojae endopeptidase is larger and has neutral pH optimum. Insensitive to phosphoramidon. Preferential cleavage of bonds with hydrophobic residues in P1'; also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain. Strong action on protamine and histones. Zinc Serralysin Pseudomonas aeruginosa alkaline protease Serratia marcescens extracellular proteinase Escherichia freundii proteinase There is broad specificity in cleavage of the insulin B chain, with some species variations. An extracellular endopeptidase from Pseudomonas aeruginosa, Escherichia freundii, Serratia marcescens and Erwinia chrysanthemi. The pH optimum for digesting various proteins is about 9-10. Preferential cleavage of bonds with hydrophobic residues in P1'. Zinc Belongs to peptidase family M10A. Ht-b Crotalus atrox metalloendopeptidase b Hemorrhagic toxin b Atrolysin B Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 23-Gly-|-Phe-24 of insulin B chain; identical to the cleavage of insulin B chain by atrolysin C. Also cleaves Xaa-|-Ser bonds in glucagon. Zinc From the venom of the western diamondback rattlesnake (Crotalus atrox). Belongs to peptidase family M12B. Atrolysin C Crotalus atrox metalloendopeptidase c Hemorrhagic toxin c Ht-c Hemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox). Belongs to peptidase family M12B. Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 23-Gly-|-Phe-24 of insulin B chain. With small molecule substrates prefers hydrophobic residue at P2' and small residue such as Ala, Gly at P1. Digests type IV collagen. Phosphoramidon inhibits in the 0.1 mM range. Exist as two forms, c and d. Zinc Hemorrhagic toxin-2 of C.ruber ruber has the same molecular weight and specificity. Atroxase Belongs to peptidase family M12B. Cleaves fibrinogen. A nonhemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox). Cleavage of 5-His-|-Leu-6, 9-Ser-|-His-10, 10-His-|-Leu-11, 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in insulin B chain. Zinc Atrolysin E Crotalus atrox metalloendopeptidase e Hemorrhagic toxin e Such action is believed to contribute to the hemorrhagic property by weakening capillary walls. Digests basement membrane components, including the triple helix of type IV collagen. Hemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox). Cleavage of 3-Asn-|-Gln-4, 9-Ser-|-His-10 and 14-Ala-|-Leu-15 bonds in insulin B chain and 14-Tyr-|-Gln-15 and 8-Thr-|-Ser-9 in A chain. Cleaves type IV collagen at 73-Ala-|-Gln-74 in alpha-1-(IV) and at 7-Gly-|-Leu-8 in alpha-2-(IV). Zinc Belongs to peptidase family M12B. Atrolysin F Hemorrhagic toxin f Crotalus atrox metalloendopeptidase f Hemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox). Digests the gamma chain of fibrinogen. Belongs to peptidase family M12B. Zinc Cleavage of 2-Val-|-Asn-3, 4-Gln-|-His-5, 6-Leu-|-Cys-7, 10-His-|-Leu-11, 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 bonds in insulin B chain. Proteinase I and II Crotalus adamanteus metalloendopeptidase Adamalysin Two isoenzymes of approximately 24 kDa that inactivate alpha-1-proteinase inhibitor by a single cleavage. From the venom of the eastern diamondback rattlesnake (Crotalus adamanteus). Cleavage of 1-Phe-|-Val-2, 5-His-|-Leu-6, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, and 16-Tyr-|-Leu-17 of insulin B chain. Zinc Belongs to peptidase family M12B. Hemorrhagic proteinase IV Crotalus horridus metalloendopeptidase Horrilysin Zinc Cleaves basement membrane, hide powder and fibrinogen. Cleavage of only the single bond 14-Ala-|-Leu-15 in the insulin B chain, 12-Ser-|-Leu-13 in the A chain, and Ile-|-Gly, Pro-|-Ala, and Ser-|-Trp in mellitin. Hemorrhagic endopeptidase from the venom of the timber rattlesnake (Crotalus horridus horridus). Belongs to peptidase family M12B. Hemorrhagic metalloproteinase HT-2 Ruberlysin Hemorrhagic toxin II Crotalus ruber metalloendopeptidase II Belongs to peptidase family M12B. Cleavage of 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 23-Gly-|-Phe-24 bonds of the B chain of insulin; His-|-Pro, Pro-|-Phe, and Trp-|-Ser of angiotensin I; and Gly-|-Phe of Met enkephalin. Cleaves fibrinogen. Hemorrhagic endopeptidase from the venom of the red rattlesnake (Crotalus ruber ruber). Zinc Bothropasin Zinc Caseinolytic endopeptidase of jararaca snake (Bothrops jararaca) venom. Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 in insulin B chain. Belongs to peptidase family M12B. J protease Bothrops metalloendopeptidase J Bothrolysin Endopeptidase from the venom of the jararaca snake (Bothrops jararaca). Zinc Belongs to peptidase family M12B. Insensitive to phosphoramidon at 0.5 mM. Cleavage of 4-Gln-|-His-5, 9-Ser-|-His-10 and 14-Ala-|-Leu-15 of insulin B chain and Pro-|-Phe of angiotensin I. Ophiolysin Ophiophagus metalloendopeptidase Belongs to peptidase family M12B. Endopeptidase from the venom of the king cobra (Ophiophagus hannah). Zinc Cleavage of 3-Asn-|-Gln-4, 4-Gln-|-His-5, 10-His-|-Leu-11, 14-Ala-|-Leu-15, and 16-Tyr-|-Leu-17 in insulin B chain. Hemorrhagic proteinase HR1a Trimeresurus metalloendopeptidase I Trimerelysin I Cleavage of only two bonds: 10-His-|-Leu-11 and 14-Ala-|-Leu-15, in the insulin B chain. Belongs to peptidase family M12B. Zinc Hemorrhagic endopeptidase of pI 4.4 from the venom of the habu snake (Trimeresurus flavoviridis). Trimeresurus metalloendopeptidase II Proteinase H(2) Trimerelysin II Nonhemorrhagic endopeptidase from the venom of the habu snake (Trimeresurus flavoviridis). Zinc Belongs to peptidase family M12B. Cleavage of 3-Asn-|-Gln-4, 10-His-|-Leu-11 and 14-Ala-|-Leu-15 in the insulin B chain, and the bond Z-Gly-Pro-|-Leu-Gly-Pro in a small molecule substrate of microbial collagenase. Mucrolysin Mucrotoxin A Trimeresurus metalloendopeptidase A Cleavage of 9-Ser-|-His-10, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16 and 16-Tyr-|-Leu-17 bonds in the insulin B chain. Belongs to peptidase family M12B. Hemorrhagic and fibrinogenolytic endopeptidase from the Chinese habu snake (Trimeresurus mucrosquamatus) venom. Zinc Protease Pi Pitrilysin Protease III Zinc Belongs to peptidase family M16. Inhibited by EDTA and 1,10-phenanthroline; not thiol dependent. From the periplasmic space of Escherichia coli. Preferential cleavage of 16-Tyr-|-Leu-17 and 25-Phe-|-Tyr-26 bonds of oxidized insulin B chain. Also acts on other substrates of Mw less than 7 kDa such as insulin and glucagon. Insulin protease Insulin-degrading enzyme Insulysin Insulinase Zinc Inhibited by bacitracin, chelating agents EDTA and 1,10-phenanthroline, and by thiol-blocking reagents such as N-ethylmaleimide, but not by phosphoramidon. Belongs to peptidase family M16. Cytosolic enzyme, known from mammals and Drosophila melanogaster. Degradation of insulin, glucagon and other polypeptides. No action on proteins. Glycoprotease O-sialoglycoprotein endopeptidase Inhibited by EDTA (100 mM) and 1,10-phenanthroline. Belongs to peptidase family M22. Hydrolysis of O-sialoglycoproteins; cleaves 31-Arg-|-Asp-32 bond in glycophorin A. Does not cleave unglycosylated proteins, desialylated glycoproteins or glycoproteins that are only N-glycosylated. Russell's viper venom factor X activator Blood-coagulation factor X-activating enzyme Russellysin RVV-X Calcium Zinc Belongs to peptidase family M12B. Specifically activates several components of the blood clotting system, including coagulation factor X, coagulation factor IX and protein C by cleavage of Arg-|-Xaa bonds. Has no action on insulin B chain. Mitochondrial intermediate peptidase Zinc Belongs to peptidase family M3. Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion. Natural substrates are precursor proteins that have already been processed by mitochondrial processing peptidase. Leucolysin Leucostoma neutral proteinase From the venom of the western cottonmouth moccasin snake (Agkistrodon piscivorus leucostoma). Zinc Calcium Cleavage of 1-Phe-|-Val-2, 5-His-|-Leu-6, 14-Ala-|-Leu-15, 20-Gly-|-Glu-21, 23-Gly-|-Phe-24 and 24-Phe-|-Phe-25 bonds in insulin B chain as well as N-blocked dipeptides. Dactylysin Peptide hormone inactivating endopeptidase Hydrolysis of peptides of at least six residues, with bulky hydrophobic residues in the P1' position. Shows a preference for hydrophobic doublets such as -Phe-|-Phe- and -Phe-|-Leu- in somatostatin-(1-14)-peptide and dynorphin A-(1-6)-peptide, respectively. Resembles neprilysin in insensitivity to 1 uM captopril, but differs in being insensitive to thiorphan and unable to digest (5-Met)-enkephalin, (5-Leu)-enkephalin, oxytocin and substance P-(7-11)-peptide. An endopeptidase of 100 kDa secreted from the skin of Xenopus laevis. Nardilysin NRD convertase N-arginine dibasic convertase Unusually for a metallopeptidase, inhibited by bestatin, amastin and ethylmaleimide. Zinc Hydrolysis of polypeptides, preferably at -Xaa-|-Arg-Lys-, and less commonly at -Arg-|-Arg-Xaa-, in which Xaa is not Arg or Lys. Belongs to peptidase family M16. Neurosecretory granule protease cleaving pro-ocytocin/neurophysin Magnolysin Inhibited by EDTA. Hydrolysis of polypeptides with Arg or Lys in P1 and P2, e.g. to hydrolyze pro-oxytocin at -Lys-Arg-|-Ala-Val-. The specificity further depends on the organization of a beta-turn-alpha-helix of nine or more residues containing the paired basic amino acids near the center. Meprin B Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of 5-His-|-Leu-6, 6-Leu-|-Cys-7, 14-Ala-|-Leu-15 and 19-Cys-|-Gly-20 bonds in insulin B chain. Inhibited by EDTA and 1,10-phenanthroline, but not by phosphoramidon, captopril or thiorphan. Belongs to peptidase family M12A. Zinc Mitochondrial processing peptidase Processing enhancing peptidase Zinc Known from the mitochondrial matrix of fungi and mammals. Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2. Belongs to peptidase family M16. Metalloelastase Macrophage elastase Matrix metalloproteinase 12 Calcium Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin. Belongs to peptidase family M10B. Zinc Teleost hatching enzyme Choriolysin L Low choriolytic enzyme Zinc Belongs to peptidase family M12A. Hydrolysis of the inner layer of fish egg envelope. Also hydrolysis of casein and small molecule substrates such as succinyl-Leu-Leu-Val-Tyr-|-7-(4-methyl)coumarylamide. Teleost hatching enzyme High choriolytic enzyme Choriolysin H Zinc Hydrolysis of the inner layer of fish egg envelope. Also hydrolysis of casein and small molecule substrates such as succinyl-Leu-Leu-Val-Tyr-|-7-(4-methyl)coumarylamide. Belongs to peptidase family M12A. Tentoxilysin Tetanus neurotoxin Belongs to peptidase family M27. Hydrolysis of 76-Gln-|-Phe-77 bond in synaptobrevin 2. Zinc Bontoxilysin Botulinum neurotoxin Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates. Belongs to peptidase family M27. Zinc Vertebrate collagenase Interstitial collagenase Matrix metalloproteinase 1 Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue. Zinc Belongs to peptidase family M10B. Alpha-macroglobulins are cleaved much more rapidly. The enzyme takes its rdfs:label from substrates of the interstitial collagen group -types I, II and III, all of which are cleaved in the helical domain. The enzyme is widely distributed in vertebrate animals. Oligopeptidase A Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)(5). Zinc Differs from thimet oligopeptidase in lack of thiol activation. Belongs to peptidase family M3. Endothelin-converting enzyme 1 ECE-1 Zinc http://purl.uniprot.org/mim/142623 Phosphoramidon-sensitive. Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1. Belongs to peptidase family M13. Fibrinolytic proteinase Fibrolase Belongs to peptidase family M12. Hydrolysis of 14-Ala-|-Leu-15 in insulin B chain and 413-Lys-|-Leu-414 in alpha-chain of fibrinogen. Zinc HF2-proteinase Jararhagin Belongs to peptidase family M12. Cleavage of 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 bonds in insulin B chain. Zinc Hemorrhagic endopeptidase from the venom of the jararaca snake. Bacteroides fragilis enterotoxin Fragilysin Also degrades intracellular, cytoskeletal proteins actin, myosin and others. Thought to be a cause of diarrhea. Belongs to peptidase family M10. Zinc Hydrolyzes extracellular matrix proteins, and disrupts tight junctions of intstinal cells. Broad proteolytic specificity, bonds hydrolyzed includes -Gly-|-Leu-, -Met-|-Leu-, -Phe-|-Leu-, -Cys-|-Leu-, -Leu-|-Gly-. Lysostaphin Glycyl-glycine endopeptidase Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans. Zinc Belongs to peptidase family M23. Lyses cells of Staphylococcus aureus in particular, by its action on the cross-bridge of the cell wall. Flavastacin Belongs to peptidase family M12. The specificity is similar to that of EC 3.4.24.33, but the two are reported to be structurally dissimilar. Zinc Hydrolyzes polypeptides on the amino-side of Asp in -Xaa-|-Asp-. Acts very slowly on -Xaa-|-Glu. Snapalysin Small neutral protease Zinc Belongs to peptidase family M7. Has no action on amino-acid p-nitroanilides. Hydrolyzes proteins with a preference for Tyr or Phe in the P1' position. Germination proteinase GPR endopeptidase Germination protease Spore protease Belongs to peptidase family M63. Initiates the degradation of small, acid-soluble proteins during spore germination in Bacillus megaterium. Endopeptidase action with P4 Glu or Asp, P1 preferably Glu > Asp, P1' hydrophobic and P2' Ala. Pappalysin-1 Insulin-like growth factor binding protein-4 protease Pregnancy-associated plasma protein-A The rate of hydrolysis of IGFBP-4 is increased about 20-fold by the presence of insulin-like growth factor (IGF), whereas that of IGFBP-5 is decreased about two-fold. Zinc Cleavage of the 135-Met-|-Lys-136 bond in insulin-like growth factor binding protein (IGFBP)-4, and the 143-Ser-|-Lys-144 bond in IGFBP-5. Circulates in human pregnancy mainly as a complex with the proform of eosinophil major basic protein, which acts as an inhibitor of the peptidase. Belongs to peptidase family M43. Matrix metalloproteinase 14 Membrane-type matrix metalloproteinase-1 Believed to play an important role in the activation of progelatinase A at cell surfaces. Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain. Belongs to peptidase family M10. Zinc Myelin-associated disintegrin metalloproteinase ADAM10 endopeptidase Kuzbanian protein Zinc Endopeptidase of broad specificity. Belongs to peptidase family M12. Work with ADAM10-deficient mice supports a role in Notch signaling. Partially responsible for the 'alpha-secretase' activity in brain that degrades the potentially harmful beta-amyloid peptide. ADAMTS-4 endopeptidase Aggrecanase-1 Thought to be biologically significant for the degradation of the aggrecan component of cartilage matrix. Zinc Glutamyl endopeptidase; bonds cleaved include 370-Thr-Glu-Gly-Glu-|-Ala-Arg-Gly-Ser-377 in the interglobular domain of mammalian aggrecan. Belongs to peptidase family M12. Anthrax lethal factor endopeptidase Lethal toxin Cleaves several MAP kinase kinases near their N-termini, preventing them from phosphorylating the downstream mitogen-activated protein kinases. Preferred amino acids around the cleavage site can be denoted BBBBxHx-|-H, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. The only known protein substrates are mitogen-activated protein (MAP) kinase kinases. Zinc Belongs to peptidase family M34. One of three proteins that are collectively termed anthrax toxin. From the bacterium Bacilus anthracis that causes anthrax. CAAX prenyl protease 1 Ste24 endopeptidase Prenyl protein-specific endoprotease 1 http://purl.uniprot.org/mim/608612 Subsequently, the S-isoprenylated cysteine residue that forms the new C-terminus is methyl-esterified and forms a hydrophobic membrane-anchor. Zinc The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids. One of two enzymes that can catalyze this processing step for mating a-factor in Saccharomyces cerevisiae. Belongs to peptidase family M48. Sterol-regulatory element-binding proteins intramembrane protease Membrane-bound transcription factor site 2 protease Site-2 protease S2P endopeptidase Zinc Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site 477-DRSRILL-|-CVLTFLCLSFNPLTSLLQWGGA-505. The residues Asn-Pro, 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced. Belongs to peptidase family M50. The transcription factors SREBP-1 and -2 are synthesized as precursor proteins that are attached to the membranes of the endoplasmic reticulum and two cleavages are needed to release the active factor so that it can move to the nucleus. This enzyme cleaves the second of these, and is thus the 'site 2 protease', S2P. Tumor necrosis factor alpha-converting enzyme TACE ADAM 17 endopeptidase Zinc Belongs to peptidase family M12. Narrow endopeptidase specificity. Cleaves Pro-Leu-Ala-Gln-Ala-|-Val-Arg-Ser-Ser-Ser in the membrane-bound, 26-kDa form of tumor necrosis factor alpha (TNF-alpha). Similarly cleaves other membrane-anchored, cell-surface proteins to 'shed' the extracellular domains. In vivo, the cleavage of tumor necrosis factor alpha precursor releases the soluble, 17-kDa TNF-alpha, which induces inflammation. Threonine endopeptidases Proteasome endopeptidase complex Prosome Multicatalytic proteinase (complex) Multicatalytic endopeptidase complex Proteasome Ingensin Macropain Lens neutral proteinase Inhibited by mercurial reagents and some inhibitors of serine endopeptidases. Cleavage of peptide bonds with very broad specificity. A 20-S protein composed of 28 subunits arranged in four rings of seven. The molecule is barrel-shaped, and the active sites are on the inner surfaces. Terminal apertures restrict access of substrates to the active sites. Belongs to peptidase family T1. In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity. Endopeptidases of unknown catalytic mechanism Acting on carbon-nitrogen bonds, other than peptide bonds In linear amides L-asparaginase L-asparagine amidohydrolase Asparaginase L-asparagine + H(2)O = L-aspartate + NH(3). Formyltetrahydrofolate deformylase Formyltetrahydrofolate hydrolase Formyl-FH(4) hydrolase 10-formyltetrahydrofolate + H(2)O = formate + tetrahydrofolate. Penicillin amidase Penicillin acylase Penicillin + H(2)O = a carboxylate + 6-aminopenicillanate. Biotinidase Also acts on biotin esters. http://purl.uniprot.org/mim/253260 Biotin amide + H(2)O = biotin + NH(3). Aryl-acylamidase An anilide + H(2)O = a carboxylate + aniline. Also acts on 4-substituted anilides. Dehydropeptidase II Histozyme Aminoacylase Aminoacylase I Benzamidase Acylase I Hippuricase An N-acyl-L-amino acid + H(2)O = a carboxylate + an L-amino acid. Used in separating D-and L-amino acids. Wide specificity; also hydrolyzes dehydropeptides. http://purl.uniprot.org/mim/609924 Aspartoacylase Aminoacylase II http://purl.uniprot.org/mim/271900 N-acyl-L-aspartate + H(2)O = a carboxylate + L-aspartate. Acetylornithinase N-acetylornithinase Acetylornithine deacetylase Also hydrolyzes N-acetylmethionine. N(2)-acetyl-L-ornithine + H(2)O = acetate + L-ornithine. Acyl-lysine deacylase Epsilon-lysine acylase N(6)-acyl-L-lysine + H(2)O = a carboxylate + L-lysine. Succinyl-diaminopimelate desuccinylase N-succinyl-LL-2,6-diaminoheptanedioate + H(2)O = succinate + LL-2,6-diaminoheptanedioate. NAMase Nicotine deamidase Nicotinamidase Nicotinamide + H(2)O = nicotinate + NH(3). Glutaminase L-glutamine amidohydrolase L-glutamine + H(2)O = L-glutamate + NH(3). Citrullinase L-citrulline + H(2)O = L-ornithine + CO(2) + NH(3). N-acetyl-beta-alanine deacetylase N-acetyl-beta-alanine + H(2)O = acetate + beta-alanine. Pantothenase (R)-pantothenate + H(2)O = (R)-pantoate + beta-alanine. Ceramidase Acylsphingosine deacylase N-acylsphingosine + H(2)O = a carboxylate + sphingosine. http://purl.uniprot.org/mim/228000 Bile salt hydrolase Glycocholase Choloylglycine hydrolase Also acts on the 3-alpha,12-alpha-dihydroxy-derivative, and on choloyl-taurine. 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholan-24-oylglycine + H(2)O = 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + glycine. N-acetylglucosamine-6-phosphate deacetylase N-acetyl-D-glucosamine 6-phosphate + H(2)O = D-glucosamine 6-phosphate + acetate. Aspartylglucosaminidase Aspartylglucosylaminidase Aspartylglucosylaminase Glycosylasparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase Aspartylglycosylamine amidohydrolase Aspartylglucosylamine deaspartylase Beta-aspartylglucosylamine amidohydrolase Glucosylamidase N-aspartyl-beta-glucosaminidase http://purl.uniprot.org/mim/208400 Acts only on asparagine-oligosaccharides containing one amino acid, i.e. the asparagine has free alpha-amino and alpha-carboxyl groups (cf. EC 3.5.1.52). N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H(2)O = N-acetyl-beta-D-glucosaminylamine + L-aspartate. N-formylmethionylaminoacyl-tRNA deformylase N-formyl-L-methionylaminoacyl-tRNA + H(2)O = formate + L-methionylaminoacyl-tRNA. N-acetylmuramoyl-L-alanine amidase Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. 2-(acetamidomethylene)succinate hydrolase 2-(acetamidomethylene)succinate + 2 H(2)O = acetate + succinate semialdehyde + NH(3) + CO(2). Involved in the degradation of pyridoxin in Pseudomonas. Omega-amidase A monoamide of a dicarboxylic acid + H(2)O = a dicarboxylate + NH(3). Acts on glutaramate, succinamate and their 2-oxo derivatives. 5-aminovaleramidase 5-aminopentanamidase The enzyme from Pseudomonas putida also acts on 4-aminobutanamide and, more slowly, on 6-aminohexanamide. 5-aminopentanamide + H(2)O = 5-aminopentanoate + NH(3). Formylmethionine deformylase N-formyl-L-methionine + H(2)O = formate + L-methionine. Hippuricase Benzoylglycine amidohydrolase Hippurate hydrolase Hippurate + H(2)O = benzoate + glycine. Acts on various N-benzoylamino acids. N-acetylglucosamine deacetylase N-acetyl-D-glucosamine + H(2)O = D-glucosamine + acetate. D-glutaminase D-glutamine + H(2)O = D-glutamate + NH(3). N-methyl-2-oxoglutaramate hydrolase 5-hydroxy-N-methylpyroglutamate synthase In the reverse reaction, the product cyclizes non-enzymically to 2-hydroxy-N-methyl-5-oxoproline. N-methyl-2-oxoglutaramate + H(2)O = 2-oxoglutarate + methylamine. L-asparagine/L-glutamine amidohydrolase Glutamin-(asparagin-)ase Glutaminase-asparaginase L-ASNase/L-GLNase The D-isomers are also hydrolyzed, more slowly. L-asparagine is hydrolyzed at 0.8 of the rate of L-glutamine. (2) L-asparagine + H(2)O = L-aspartate + NH(3). (1) L-glutamine + H(2)O = L-glutamate + NH(3). Alkylamidase It has little or no activity toward short-chain substrates. The enzyme hydrolyzes N-monosubstituted and N,N-disubstituted amides, and there is some activity toward primary amides. N-methylhexanamide + H(2)O = hexanoate + methylamine. Amidase Acylamidase Acylase A monocarboxylic acid amide + H(2)O = a monocarboxylate + NH(3). Acylagmatine amidase Also acts on acetylagmatine, propanoylagmatine and bleomycin B(2). Benzoylagmatine + H(2)O = benzoate + agmatine. Chitin deacetylase Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin. Chitin + H(2)O = chitosan + acetate. Nicotinamide-nucleotide amidase Also acts more slowly on beta-nicotinamide D-ribonucleoside. Beta-nicotinamide D-ribonucleotide + H(2)O = beta-nicotinate D-ribonucleotide + NH(3). Peptidoglutaminase I Peptidyl-glutaminase Specific for the hydrolysis of the gamma-amide of glutamine substituted at the alpha-amino group, e.g., glycyl-L-glutamine, N-acetyl-L-glutamine and L-leucylglycyl-L-glutamine. Alpha-N-peptidyl-L-glutamine + H(2)O = alpha-N-peptidyl-L-glutamate + NH(3). Glutaminylpeptide glutaminase Protein-glutamine glutaminase Peptidoglutaminase II Protein L-glutamine + H(2)O = protein L-glutamate + NH(3). Specific for the hydrolysis of the gamma-amide of glutamine substituted at the carboxyl position or both the alpha-amino and carboxyl positions, e.g., L-glutaminylglycine and L-phenylalanyl-L-glutaminylglycine. 6-aminohexanoate-dimer hydrolase 6-aminohexanoic acid oligomer hydrolase The residues are removed sequentially from the N-terminus. Also hydrolyzes, more slowly, oligomers of 6-aminohexanoate containing up to 6 residues. N-(6-aminohexanoyl)-6-aminohexanoate + H(2)O = 2 6-aminohexanoate. N-acetyldiaminopimelate deacetylase N-acetyl-LL-2,6-diaminoheptanedioate + H(2)O = acetate + LL-2,6-diaminoheptanedioate. N(8)-monoacetylspermidine deacetylase N(8)-acetylspermidine amidohydrolase Acetylspermidine deacetylase N-acetylspermidine deacetylase N(8)-acetylspermidine deacetylase N(1)-acetylspermidine amidohydrolase N(8)-acetylspermidine + H(2)O = acetate + spermidine. It was initially thought that N(1)-acetylspermidine was the substrate for this deacetylase reaction but this has since been disproved. Formamidase Formamide amidohydrolase Formamide + H(2)O = formate + NH(3). Also acts, more slowly, on acetamide, propanamide and butanamide. Urease Nickel Urea + H(2)O = CO(2) + 2 NH(3). Valeramidase Pentanamidase Different from EC 3.5.1.49. Pentanamide + H(2)O = pentanoate + NH(3). Also acts, more slowly, on other short-chain aliphatic amides. Aminobutyryl-CoA thiolesterase 4-acetamidobutyryl-CoA deacetylase The enzyme also hydrolyzes 4-aminobutanoyl-CoA to aminobutanoate and coenzyme A. 4-acetamidobutanoyl + H(2)O = acetate + 4-aminobutanoyl-CoA. Glycopeptidase Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase N-oligosaccharide glycopeptidase Glycopeptide N-glycosidase N-glycanase Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. Does not act on (GlcNAc)-Asn, because it requires the presence of more than two amino-acid residues in the substrate (cf. EC 3.5.1.26). N-carbamoylputrescine amidase N-carbamoylputrescine + H(2)O = putrescine + CO(2) + NH(3). Allophanate hydrolase Urea-1-carboxylate + H(2)O = 2 CO(2) + 2 NH(3). The Saccharomyces cerevisiae enzyme (but not that from green algae) also catalyzes the reaction of EC 6.3.4.6, thus bringing about the hydrolysis of urea to CO(2) and NH(3) in the presence of ATP and bicarbonate. Long-chain aminoacylase Long-chain-fatty-acyl-glutamate deacylase Optimum chain length of acyl residue is 12 to 16. N-long-chain-fatty-acyl-L-glutamate + H(2)O = a long-chain carboxylate + L-glutamate. Does not act on acyl derivatives of other amino acids. N,N-dimethylformamidase Iron Also acts on N-ethylformamide and N-methylformamide and, more slowly, on N,N-diethylformamide, N,N-dimethylacetamide and unsubstituted acyl amides. N,N-dimethylformamide + H(2)O = dimethylamine + formate. Tryptophanamidase L-tryptophanamide + H(2)O = L-tryptophan + NH(3). Manganese Also acts on N-ethylformamide and L-tyrosinamide, and on some tryptophan dipeptides. N-benzyloxycarbonylglycine hydrolase Cobalt Zinc Also acts, more slowly, on N-benzyloxycarbonylalanine, but not on the corresponding derivatives of other amino acids or on N-benzyloxycarbonylpeptides (cf. EC 3.5.1.64). N-benzyloxycarbonylglycine + H(2)O = benzyl alcohol + CO(2) + glycine. N-carbamoylsarcosine amidase CSHase N-carbamoylsarcosine amidohydrolase N-carbamoylsarcosine + H(2)O = sarcosine + CO(2) + NH(3). Beta-ureidopropionase N-carbamoyl-beta-alanine + H(2)O = beta-alanine + CO(2) + NH(3). The animal enzyme also acts on beta-ureidoisobutyrate. http://purl.uniprot.org/mim/606673 N-(long-chain-acyl)ethanolamine deacylase N-acylethanolamine amidohydrolase N-(long-chain-acyl)ethanolamine + H(2)O = a long-chain carboxylate + ethanolamine. Does not act on N-acylsphingosine or N,O-diacylethanolamine. Mimosine amidohydrolase Mimosinase (S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H(2)O = 3-hydroxy-4H-pyrid-4-one + L-serine. An enzyme from Leucaena leucocephala leaf, which also contains the toxic amino acid, mimosine. Acetylputrescine deacetylase The enzyme from Micrococcus luteus also acts on N(8)-acetylspermidine and acetylcadaverine, but more slowly. N-acetylputrescine + H(2)O = acetate + putrescine. 4-acetamidobutyrate deacetylase Also acts on N-acetyl-beta-alanine and 5-acetamidopentanoate. 4-acetamidobutanoate + H(2)O = acetate + 4-aminobutanoate. N(alpha)-benzyloxycarbonylleucine hydrolase N(alpha)-benzyloxycarbonyl-L-leucine + H(2)O = benzyl alcohol + CO(2) + L-leucine. Also acts on N(alpha)-t-butoxycarbonyl-L-leucine, and, more slowly, on the corresponding derivatives of L-aspartate, L-methionine, L-glutamate and L-alanine (cf. EC 3.5.1.58). Theanine hydrolase N(5)-ethyl-L-glutamine + H(2)O = L-glutamate + ethylamine. Also acts on other N-alkyl-L-glutamines. 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase Involved in the degradation of pyridoxin by Pseudomonas and Arthrobacter. 2-(hydroxymethyl)-3-(acetamidomethylene)succinate + 2 H(2)O = acetate + 2-(hydroxymethyl)-4-oxobutanoate + NH(3) + CO(2). 4-methyleneglutaminase 4-methyleneglutamine deamidase 4-methylene-L-glutamine + H(2)O = 4-methylene-L-glutamate + NH(3). N-formylglutamate deformylase Beta-citryl-L-glutamate hydrolase N-formyl-L-glutamate + H(2)O = formate + L-glutamate. The animal enzyme also acts on beta-citryl-L-glutamate and beta-citryl-L-glutamine. Glycosphingolipid deacylase Glycosphingolipid ceramide deacylase Does not act on sphingolipids such as ceramide. Not identical with EC 3.5.1.23. Hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives. Ureidosuccinase N-carbamoyl-L-aspartate + H(2)O = L-aspartate + CO(2) + NH(3). Aculeacin-A deacylase Hydrolysis of the amide bond in aculeacin A and related neutral lipopeptide antibiotics, releasing the long-chain fatty acid side-chain. N-feruloylglycine deacylase N-feruloylglycine + H(2)O = ferulate + glycine. Hydrolyzes a range of L-amino acids from the cinnamoyl and substituted cinnamoyl series. Not identical with EC 3.5.1.14. D-benzoylarginine-4-nitroanilide amidase N-benzoyl-D-arginine-4-nitroanilide + H(2)O = N-benzoyl-D-arginine + 4-nitroaniline. Carnitinamidase L-carnitinamide + H(2)O = L-carnitine + NH(3). Does not act on D-carnitinamide. Chenodeoxycholoyltaurine hydrolase Some other taurine conjugates are hydrolyzed, but not glycine conjugates of bile acids. Chenodeoxycholoyltaurine + H(2)O = chenodeoxycholate + taurine. Urethanase Urethane hydrolase Urethane + H(2)O = ethanol + CO(2) + NH(3). Aralkyl acylamidase Arylalkyl acylamidase It also accepts arylalkyl acetates but not acetanilide derivatives, which are common substrates of EC 3.5.1.13. Strict specificity for N-acetyl arylalkylamines, including N-acetyl-2-phenylethylamine, N-acetyl-3-phenylpropylamine, N-acetyldopamine, N-acetyl-serotonin and melatonin. N-acetylarylalkylamine + H(2)O = arylalkylamine + acetate. N-carbamoyl-D-amino acid hydrolase Has strict stereospecificity for N-carbamoyl-D-amino acids and does not act upon the corresponding L-amino acids or N-formyl amino acids, N-carbamoyl-sarcosine, -citrulline, -allantoin and -ureidopropionate, which are substrates for other amidohydrolases. N-carbamoyl-D-amino acid + H(2)O = D-amino acid + NH(3) + CO(2). GSP amidase Glutathionylspermidine amidohydrolase (spermidine-forming) Glutathionylspermidine amidase Transforms glutathionylspermidine into glutathione and spermidine. The enzyme from Escherichia coli is bifunctional and also catalyzes the reaction of EC 6.3.1.8, resulting in a net hydrolysis of ATP. N(1)-(gamma-L-glutamyl-L-cysteinyl-glycyl)-spermidine + H(2)O = gamma-L-glutamyl-L-cysteinyl-glycine + spermidine. Phthalyl amidase o-phthalyl amidase The substituent on nitrogen may be an alkyl group, but may also be complex, giving an amino acid or peptide derivative. The enzyme from Xanthobacter agilis hydrolyzes phthalylated amino acids, peptides, beta-lactams, aromatic and aliphatic amines. Phthalyl is used to mean 2-carboxybenzoyl. A phthalylamide + H(2)O = phthalic acid + a substituted amine. Substitutions on the phthalyl ring include 6-F, 6-NH(2), 3-OH, and a nitrogen in the aromatic ring ortho to the carboxy group attached to the amine. Formylaspartate deformylase N-formyl-L-aspartate + H(2)O = formate + L-aspartate. D-aminoacylase N-acyl-D-amino-acid deacylase Used in separating D-and L-amino acids. Zinc N-acyl-D-amino acid + H(2)O = an acid + D-amino acid. Has a wide specificity; hydrolyzes N-acyl derivative of neutral D-amino acids. N-acyl-D-glutamate amidohydrolase N-acyl-D-glutamate deacylase N-acyl-D-glutamate + H(2)O = a carboxylate + D-glutamate. Zinc N-acyl-D-aspartate deacylase N-acyl-D-aspartate amidohydrolase N-acyl-D-aspartate + H(2)O = a carboxylate + D-aspartate. Zinc Biuret amidohydrolase Biuret + H(2)O = urea + CO(2) + NH(3). Involved in a pathway by which the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, is degraded in bacteria. (S)-N-acetyl-1-phenylethylamine hydrolase (S)-N-acetyl-1-phenylethylamine amidohydrolase Some related acetylated compounds are hydrolyzed with variable enantiomeric selectivities. Inhibited by phenylmethanesulfonyl fluoride. N-acetylphenylethylamine + H(2)O = phenylethylamine + acetate. Mandelamide hydrolase Mandelamide amidase (R)-mandelamide + H(2)O = (R)-mandelate + NH(3). N-carbamoyl-L-amino-acid hydrolase L-carbamoylase Carbamoyl-L-valine is the best substrate. The enzyme has broad specificity for carbamoyl-L-amino acids, although it is inactive on the carbamoyl derivatives of glutamate, aspartate, arginine, tyrosine or tryptophan. The enzyme hydrolyzes formyl derivatives rapidly, and acetyl derivatives very slowly. It is inactive on derivatives of D-amino acids, the substrates of EC 3.5.1.77, or on N-carbamoyl-beta-alanine, the substrate of EC 3.5.1.6. N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H(2)O = L-2-amino acid + NH(3) + CO(2). Manganese or nickel or cobalt PDF Polypeptide deformylase Peptide deformylase Iron(2+) N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Differs in substrate specificity from EC 3.5.1.27 and EC 3.5.1.31. Requires at least a dipeptide for an efficient rate of reaction. Formyl-L-methionyl peptide + H(2)O = formate + methionyl peptide. N-acetylglucosaminylphosphatidylinositol deacetylase GlcNAc-PI de-N-acetylase GlcNAc-PI deacetylase N-acetyl-D-glucosaminylphosphatidylinositol acetylhydrolase N-acetylglucosaminylphosphatidylinositol de-N-acetylase Acetylglucosaminylphosphatidylinositol deacetylase The enzyme appears to be composed of a single subunit (PIG-L in mammalian cells and GPI12 in Saccharomyces cerevisiae). In some species, the long-chain sn-1-acyl group of the phosphatidyl group is replaced by a long-chain alkyl or alk-1-enyl group. Involved in the second step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. 6-(N-acetyl-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H(2)O = 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate. Formylkynureninase Arylformamidase Kynurenine formamidase Formylase Also acts on other aromatic formylamines. N-formyl-L-kynurenine + H(2)O = formate + L-kynurenine. AdoCbi amidohydrolase Adenosylcobinamide hydrolase AdoCbi hydrolase Adenosylcobinamide + H(2)O = adenosylcobyric acid + (R)-1-aminopropan-2-ol. Involved in the salvage pathway of cobinamide in archaea. Archaea convert adenosylcobinamide (AdoCbi) into adenosylcobinamide phosphate (AdoCbi-P) in two steps. First, the amidohydrolase activity of cbiZ cleaves off the aminopropanol moiety of AdoCbi yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted into AdoCbi-P by the action of EC 6.3.1.10 (CbiB). N-substituted formamide deformylase While N-benzylformamide is the best substrate, the enzyme from Arthrobacter pascens can also act on the N-substituted formamides N-butylformamide, N-allylformamide, N-(2-(cyclohex-1-enyl)ethyl)formamide and N-(1-phenylethyl)formamide, but much more slowly. Amides of other acids do not act as substrates. Zinc N-benzylformamide + H(2)O = formate + benzylamine. Pantetheinase Pantetheine hydrolase Vanin-1 The enzyme recycles pantothenate (vitamin B(5)) and produces cysteamine, a potent anti-oxidant. The enzyme hydrolyzes only one of the amide bonds of pantetheine. The substrate analogs phosphopantetheine and CoA are not substrates. (R)-pantetheine + H(2)O = (R)-pantothenate + 2-aminoethanethiol. CA Glutaryl-7-ACA acylase Glutaryl-7-aminocephalosporanic-acid acylase Cephalosporin C acylase GCA GL-7-ACA acylase Cephalosporin acylase GA Glutaryl-7-aminocephalosporanic acid acylase 7-beta-(4-carboxybutanamido)cephalosporanic acid acylase It reacts only weakly with cephalosporin C. Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics. (7R)-7-(4-carboxybutanamido)cephalosporanate + H(2)O = (7R)-7-aminocephalosporanate + glutarate. Gamma-glutamyl-gamma-aminobutyrate hydrolase Gamma-glutamyl-GABA hydrolase Also can catalyze the reactions of EC 3.5.1.35 and EC 3.5.1.65. Forms part of a novel putrescine-utilizing pathway in Escherichia coli, in which it has been hypothesized that putrescine is first glutamylated to form gamma-glutamylputrescine, which is oxidized to 4-(glutamylamino)butanal and then to 4-(glutamylamino)butanoate. 4-(glutamylamino)butanoate + H(2)O = 4-aminobutanoate + L-glutamate. N-malonylurea hydrolase Ureidomalonase Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 and EC 3.5.2.1. 3-oxo-3-ureidopropanoate + H(2)O = malonate + urea. SGDS Succinylglutamate desuccinylase N(2)-succinylglutamate desuccinylase This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109, EC 3.5.3.23, EC 2.6.1.11, EC 1.2.1.71 and EC 3.5.1.96. N-succinyl-L-glutamate + H(2)O = succinate + L-glutamate. N(2)-acetylglutamate is not a substrate. Cobalt The final enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine. In cyclic amides Barbiturase Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 and EC 3.5.1.95. Specific for barbiturate as substrate. Barbiturate + H(2)O = 3-oxo-3-ureidopropanoate. May be involved in the regulation of pyrimidine metabolism, along with EC 2.4.2.9. It was previously thought that the end-products of the reaction were malonate and urea. Zinc Creatininase Creatinine amidohydrolase Creatinine + H(2)O = creatine. L-lysinamidase L-alpha-aminocaprolactam hydrolase L-lysine-lactamase L-lysine 1,6-lactam + H(2)O = L-lysine. Also hydrolyzes L-lysinamide. 6-aminohexanoate-cyclic-dimer hydrolase 1,8-diazacyclotetradecane-2,9-dione + H(2)O = N-(6-aminohexanoyl)-6-aminohexanoate. The cyclic dimer of 6-aminohexanoate is converted to the linear dimer. 2,5-dioxopiperazine hydrolase Cyclo(Gly-Gly) hydrolase 2,5-dioxopiperazine + H(2)O = glycylglycine. Highly specific; does not hydrolyze other dioxopiperazines, glycylglycine, proteins or barbiturates. N-methylhydantoinase (ATP-hydrolyzing) N-methylhydantoin amidohydrolase ATP + N-methylimidazolidine-2,4-dione + 2 H(2)O = ADP + phosphate + N-carbamoylsarcosine. Cyanuric acid amidohydrolase Involved in a pathway by which the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, is degraded in bacteria. Cyanuric acid + H(2)O = biuret + CO(2). Maleimide hydrolase Imidase Cyclic imide hydrolase It has lower activity toward cyclic ureides, which are the substrates of EC 3.5.2.2. The reverse, cyclization, reaction is also catalyzed, but much more slowly. Succinimide and glutarimide, and sulfur-containing cyclic imides, such as rhodanine, can also act as substrates for the enzyme from Blastobacter sp. A17p-4. Maleimide + H(2)O = maleamic acid. HIUHase Hydroxyisourate hydrolase 5-hydroxyisourate hydrolase 5-hydroxyisourate + H(2)O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate. The reaction is the first stage in the conversion of 5-hydroxyisourate into (S)-allantoin. This reaction will also occur spontaneously, but more slowly. Enamidase Zinc 6-oxo-1,4,5,6-tetrahydronicotinate + 2 H(2)O = 2-formylglutarate + NH(3). Other enzymes involved in this pathway are EC 1.17.1.5, EC 1.3.7.1, EC 1.1.1.291, EC 5.4.99.4, EC 5.3.3.6, EC 4.2.1.85 and EC 4.1.3.32. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Iron Hydantoinase Dihydropyrimidinase http://purl.uniprot.org/mim/222748 Also acts on dihydrothymine and hydantoin. 5,6-dihydrouracil + H(2)O = 3-ureidopropanoate. Carbamoylaspartic dehydrase Dihydroorotase DHOase (S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate. Carboxymethylhydantoinase L-5-carboxymethylhydantoin + H(2)O = N-carbamoyl-L-aspartate. Allantoinase (S)-allantoin + H(2)O = allantoate. Penicillinase Cephalosporinase Beta-lactamase A beta-lactam + H(2)O = a substituted beta-amino acid. Zinc is only requires in class-B enzymes. Zinc A group of enzymes of varying specificity hydrolyzing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. Imidazolone-5-propionate hydrolase 4(5)-imidazolone-5(4)-propionic acid hydrolase Imidazolonepropionase Imidazolone propionic acid hydrolase (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H(2)O = N-formimidoyl-L-glutamate + H(+). 5-OPase 5-oxo-L-prolinase 5-oxoprolinase (ATP-hydrolyzing) Pyroglutamase (ATP-hydrolyzing) ATP + 5-oxo-L-proline + 2 H(2)O = ADP + phosphate + L-glutamate. In linear amidines Canavanase Arginine amidinase Arginase Also hydrolyzes alpha-N-substituted L-arginines and canavanine. Manganese http://purl.uniprot.org/mim/207800 L-arginine + H(2)O = L-ornithine + urea. D-arginase D-arginine + H(2)O = D-ornithine + urea. Agmatine ureohydrolase Agmatinase Agmatine + H(2)O = putrescine + urea. Agmatine deiminase Agmatine + H(2)O = N-carbamoylputrescine + NH(3). The plant enzyme also catalyzes the reactions of EC 2.1.3.3, EC 2.1.3.6 and EC 2.7.2.2, thus functioning as a putrescine synthase, converting agmatine and ornithine into putrescine and citrulline, respectively. Formiminoglutamate deiminase Formimidoylglutamate deiminase N-formimidoyl-L-glutamate + H(2)O = N-formyl-L-glutamate + NH(3). Amidinoaspartase Also acts slowly on N-amidino-L-glutamate. N-amidino-L-aspartate + H(2)O = L-aspartate + urea. Protein-arginine deiminase Also acts on N-acyl-L-arginine and, more slowly, on L-arginine esters. Protein L-arginine + H(2)O = protein L-citrulline + NH(3). http://purl.uniprot.org/mim/180300 Methylguanidinase Methylguanidine + H(2)O = methylamine + urea. Acts on other alkylguanidines, very slowly. Guanidinopropionase Manganese Also acts, more slowly, on taurocyamine and 4-guanidinobutanoate. 3-guanidinopropanoate + H(2)O = beta-alanine + urea. Dimethylarginine dimethylaminohydrolase N(G),N(G)-dimethylarginine dimethylaminohydrolase Dimethylargininase N(omega),N(omega)-dimethyl-L-arginine + H(2)O = dimethylamine + L-citrulline. Also acts on N(omega)-monomethyl-L-arginine. Ureidoglycolate hydrolase (S)-ureidoglycolate + H(2)O = glyoxylate + 2 NH(3) + CO(2). Guanidinoacetase Glycocyaminase Manganese Guanidinoacetate + H(2)O = glycine + urea. Diguanidinobutanase 1,4-diguanidinobutane + H(2)O = agmatine + urea. Other diguanidinoalkanes with 3 to 10 methylene groups can act, more slowly. Methylenediurea deaminase Methylenediurease NH(2)-CO-NH-CH(2)-NH-CO-NH(2) + 2 H(2)O = N-(hydroxymethyl)urea + 2 NH(3) + CO(2). The methylenediurea is hydrolyzed and decarboxylated to give an aminated methylurea, which then spontaneously hydrolyzes to hydroxymethylurea. The enzyme from Ochrobactrum anthropi also hydrolyzes dimethylenetriurea and trimethylenetetraurea as well as ureidoglycolate, which is hydrolyzed to urea and glyoxylate, and allantoate, which is hydrolyzed to ureidoglycolate, ammonia and carbon dioxide. Proclavaminate amidino hydrolase PAH Proclavaminic acid amidino hydrolase Proclavaminate amidinohydrolase Manganese Amidinoproclavaminate + H(2)O = proclavaminate + urea. It carries out an intermediary reaction between the first reaction of EC 1.14.11.21, and the second and third reactions of that enzyme. Forms part of the pathway for the biosythesis of the beta-lactamase inhibitor clavulanate in Streptomyces clavuligerus. N-succinylarginine dihydrolase N(2)-succinylarginine dihydrolase SADH Arginine succinylhydrolase N(2)-succinyl-L-arginine + 2 H(2)O = N(2)-succinyl-L-ornithine + 2 NH(3) + CO(2). The five enzymes involved in this pathway are EC 2.3.1.109, EC 3.5.3.23, EC 2.6.1.11, EC 1.2.1.71 and EC 3.5.1.96. The second enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. Arginine, N(2)-acetylarginine and N(2)-glutamylarginine do not act as substrates. Creatine amidinohydrolase Creatinase Creatine + H(2)O = sarcosine + urea. Allantoate amidinohydrolase Allantoicase Also hydrolyzes (R)-ureidoglycolate to glyoxylate and urea. Allantoate + H(2)O = (S)-ureidoglycolate + urea. Formimidoylaspartate deiminase Formiminoaspartate deiminase N-formimidoyl-L-aspartate + H(2)O = N-formyl-L-aspartate + NH(3). Arginine dihydrolase Arginine deiminase Also acts on canavanine. L-arginine + H(2)O = L-citrulline + NH(3). Guanidinobutyrase Also acts, very slowly, on 5-guanidinopentanoate and 6-guanidino-hexanoate. Manganese 4-guanidinobutanoate + H(2)O = 4-aminobutanoate + urea. Formiminoglutamase Formimidoylglutamase Formiminoglutamate hydrolase N-formimidoyl-L-glutamate + H(2)O = L-glutamate + formamide. Allantoate deiminase Allantoate + H(2)O = ureidoglycine + NH(3) + CO(2). In cyclic amidines Cytosine aminohydrolase Cytosine deaminase Also acts on 5-methylcytosine. Cytosine + H(2)O = uracil + NH(3). IMP synthetase IMP cyclohydrolase Inosinicase IMP + H(2)O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. Pterin deaminase The animal enzyme is specific for pterin, isoxanthopterin and tetrahydropterin. 2-amino-4-hydroxypteridine + H(2)O = 2,4-dihydroxypteridine + NH(3). Deoxycytidylate deaminase dCMP deaminase Also acts on some 5-substituted dCMPs. dCMP + H(2)O = dUMP + NH(3). dCTP deaminase Deoxycytidine triphosphate deaminase dCTP + H(2)O = dUTP + NH(3). Deoxycytidine deaminase Deoxycytidine + H(2)O = deoxyuridine + NH(3). Guanosine deaminase Guanosine aminase Guanosine + H(2)O = xanthosine + NH(3). GTP cyclohydrolase I The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic. http://purl.uniprot.org/mim/233910 http://purl.uniprot.org/mim/128230 GTP + H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. Adenosine-phosphate deaminase Acts on 5'-AMP, ADP, ATP, NAD(+) and adenosine, in decreasing order of activity. 5'-AMP + H(2)O = 5'-IMP + NH(3). The bacterial enzyme also acts on the deoxy derivatives (cf. EC 3.5.4.6). ATP deaminase ATP + H(2)O = ITP + NH(3). Phosphoribosyl-AMP cyclohydrolase 1-(5-phosphoribosyl)-AMP + H(2)O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. The Neurospora crassa enzyme also catalyzes the reactions of EC 1.1.1.23 and EC 3.6.1.31. Adenase Adenine aminase Adenine deaminase Adenine + H(2)O = hypoxanthine + NH(3). Pyrithiamine deaminase 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-methylpyridinium bromide + H(2)O = 1-(4-hydroxy-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-methylpyridinium bromide + NH(3). Creatinine deaminase Creatinine + H(2)O = N-methylhydantoin + NH(3). 1-pyrroline-4-hydroxy-2-carboxylate deaminase 1-pyrroline-4-hydroxy-2-carboxylate + H(2)O = 2,5-dioxopentanoate + NH(3). Blasticidin-S deaminase Catalyzes the deamination of the cytosine group of the antibiotics blasticidin S, cytomycin and acetylblasticidin S. Blasticidin S + H(2)O = deaminohydroxyblasticidin S + NH(3). Sepiapterin deaminase Sepiapterin + H(2)O = xanthopterin-B(2) + NH(3). Also acts on isosepiapterin, more slowly. GTP cyclohydrolase II Two C-N bonds are hydrolyzed, releasing formate, with simultaneous removal of the terminal diphosphate. GTP + 3 H(2)O = formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate. Diaminohydroxyphosphoribosylaminopyrimidine deaminase 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + H(2)O = 5-amino-6-(5-phosphoribosylamino)uracil + NH(3). The substrate is the product of EC 3.5.4.25. Methenyl-H(4)MPT cyclohydrolase Methenyltetrahydromethanopterin cyclohydrolase 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H(2)O = 5-formyl-5,6,7,8-tetrahydromethanopterin. Methanopterin is a pterin analog. Involved in the formation of methane from CO(2) in Methanobacterium thermoautotrophicum. S-adenosylhomocysteine deaminase S-adenosyl-L-homocysteine + H(2)O = S-inosyl-L-homocysteine + NH(3). GTP cyclohydrolase III GTP cyclohydrolase IIa This enzyme catalyzes the hydrolysis of the imidazole ring of guanosine 5'-triphosphate, N(7)-methylguanosine 5'-triphosphate or inosine 5'-triphosphate. Magnesium It also catalyzes the hydrolysis of diphosphate to form two equivalents of phosphate. Xanthosine 5'-triphosphate and ATP are not substrates. GTP + 3 H(2)O = 2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one + 2 phosphate. Unlike EC 3.5.4.25, this enzyme does not release formate, but does hydrolyze the diphosphate from GTP to phosphate. Guanine deaminase Guanase GAH Guanine aminase Guanine + H(2)O = xanthine + NH(3). dCTP deaminase (dUMP-forming) While most bacteria require two enzymes to form dUMP from dCTP (EC 3.5.4.13 and EC 3.6.1.23), the archaeon Methanocaldococcus jannaschii uses a single enzyme to carry out both functions. Is highly specific for dCTP as substrate as dCMP, CTP, CDP, CMP, cytosine or deoxycytosine are not deaminated. This enzyme can also act as a dUTP diphosphatase, but more slowly. dCTP + 2 H(2)O = dUMP + diphosphate + NH(3). Magnesium Adenosine aminohydrolase Adenosine deaminase Adenosine + H(2)O = inosine + NH(3). http://purl.uniprot.org/mim/102700 Cytosine nucleoside deaminase Cytidine deaminase Cytidine aminohydrolase http://purl.uniprot.org/mim/605258 Cytidine + H(2)O = uridine + NH(3). 5-AMP deaminase AMP deaminase Adenylate deaminase Myoadenylate deaminase Adenylic acid deaminase AMP aminase AMP aminohydrolase http://purl.uniprot.org/mim/102770 http://purl.uniprot.org/mim/102772 AMP + H(2)O = IMP + NH(3). Cf. EC 3.5.4.17. ADP deaminase ADP + H(2)O = IDP + NH(3). Aminoimidazolase 4-aminoimidazole + H(2)O = unidentified product + NH(3). Iron The product of the reaction is rapidly converted into formimino-glycine. Methenyltetrahydrofolate cyclohydrolase 5,10-methenyltetrahydrofolate + H(2)O = 10-formyltetrahydrofolate. http://purl.uniprot.org/mim/172460 In nitriles Nitrilase A nitrile + 2 H(2)O = a carboxylate + NH(3). Acts on a wide range of aromatic nitriles including (indol-3-yl)-acetonitrile, and also on some aliphatic nitriles, and on the corresponding acid amides (cf. EC 4.2.1.84). Ricinine nitrilase Ricinine + 2 H(2)O = 3-carboxy-4-methoxy-N-methyl-2-pyridone + NH(3). Cyanoalanine nitrilase 3-cyano-L-alanine + 2 H(2)O = L-aspartate + NH(3). L-asparagine is formed as an intermediate. Arylacetonitrilase Also hydrolyzes other 4-substituted phenylacetonitriles, thien-2-ylacetonitrile, tolylacetonitriles, and, more slowly, benzyl cyanide. Requires thiol compounds. 4-chlorophenylacetonitrile + 2 H(2)O = 4-chlorophenylacetate + NH(3). Bromoxynil nitrilase Highly specific. Involved in the bacterial degradation of the herbicide bromoxynil. 3,5-dibromo-4-hydroxybenzonitrile + 2 H(2)O = 3,5-dibromo-4-hydroxy-benzoate + NH(3). Aliphatic nitrilase Substrates include crotononitrile, acrylonitrile and glutaronitrile. R-CN + 2 H(2)O = R-COOH + NH(3). Preferentially hydrolyzes aliphatic nitriles, some of which are apparently not substrates for other known EC 3.5.5.1. Thiocyanate hydrolase The enzyme from Thiobacillus thioparus catalyzes the first step in the degradation of thiocyanate. Thiocyanate + 2 H(2)O = carbonyl sulfide + NH(3) + HO(-). In other compounds Riboflavinase Riboflavin + H(2)O = ribitol + lumichrome. Thiaminase Thiaminase II Thiamine + H(2)O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole. Hydroxydechloroatrazine ethylaminohydrolase Hydroxyatrazine hydrolase Hydroxyatrazine ethylaminohydrolase Involved in a pathway by which the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, is degraded in bacteria via N-isopropylammelide, 2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine. 4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + H(2)O = N-isopropylammelide + ethylamine. N-isopropylammelide isopropylaminohydrolase Involved in a pathway by which the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopopylamino)-1,3,5-triazine, is degraded in bacteria via N-isopropylammelide, 2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine. N-isopropylammelide + H(2)O = cyanuric acid + isopropylamine. 2-aminomuconate deaminase The reaction is spontaneous in acid conditions. Intermediate in the biodegradation of nitrobenzene by Pseudomonas pseudocaligenes JS45. 2-aminomuconate + H(2)O = 4-oxalocrotonate + NH(3). GlcN6P deaminase Phosphoglucosaminisomerase Phosphoglucosamine isomerase Glucosamine phosphate deaminase Glucosamine-6-phosphate isomerase Glucosamine-6-phosphate deaminase N-acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme. Isomerization of the aldose-ketose type converts the -CH(-NH(2))-CH=O group of glucosamine 6-phosphate into -C(=NH)-CH(2)-OH, forming 2-deoxy-2-imino-D-arabino-hexitol which then hydrolyzes to yield fructose 6-phosphate and ammonia. D-glucosamine 6-phosphate + H(2)O = D-fructose 6-phosphate + NH(3). 1-aminocyclopropane carboxylic acid deaminase 1-aminocyclopropane-1-carboxylate endolyase (deaminating) ACC deaminase 1-aminocyclopropane-1-carboxylate deaminase 1-aminocyclopropane-1-carboxylate + H(2)O = 2-oxobutanoate + NH(3). Pyridoxal-phosphate Its introduction has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation. Acting on acid anhydrides In phosphorous-containing anhydrides Diphosphate phosphohydrolase Pyrophosphate phosphohydrolase Inorganic pyrophosphatase Inorganic diphosphatase Diphosphate + H(2)O = 2 phosphate. The enzyme from some sources may be identical with EC 3.1.3.1 or EC 3.1.3.9. Specificity varies with the source and with the activating metal ion. Polyphosphatase Metaphosphatase Polyphosphate depolymerase Endopolyphosphatase The product contains 4 or 5 phosphate residues. Polyphosphate + n H(2)O = (n+1) oligophosphate. Metaphosphatase Exopolyphosphatase Exopolypase (Polyphosphate)(n) + H(2)O = (polyphosphate)(n-1) + phosphate. Deoxycytidine-triphosphatase dCTPase dCTP diphosphatase Deoxy-CTPase dCTP pyrophosphatase dCTP + H(2)O = dCMP + diphosphate. Also hydrolyzes dCDP to dCMP and phosphate. ADP-ribose diphosphatase Adenosine diphosphoribose pyrophosphatase ADP-ribose pyrophosphatase ADP-ribose phosphohydrolase ADPR-PPase ADP-ribose + H(2)O = AMP + D-ribose 5-phosphate. Adenosine-tetraphosphatase Also acts on inosine tetraphosphate and tripolyphosphate but shows little or no activity with other nucleotides or polyphosphates. Adenosine 5'-tetraphosphate + H(2)O = ATP + phosphate. Nucleoside 5-triphosphatase NTPase Nucleoside triphosphate hydrolase Nucleoside triphosphate phosphohydrolase Nucleoside-5-triphosphate phosphohydrolase Nucleoside-triphosphatase Also hydrolyzes other nucleoside triphosphates, diphosphates, thiamine diphosphate and FAD. NTP + H(2)O = NDP + phosphate. CDP-glycerol pyrophosphatase CDP-glycerol diphosphatase CDP-glycerol + H(2)O = CMP + sn-glycerol 3-phosphate. Ap4Aase Ap4A hydrolase Diguanosinetetraphosphatase (asymmetrical) Diadenosinetetraphosphatase (asymmetrical) Ap(4)A hydrolase Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) Bis(5'-adenosyl)-tetraphosphatase Diadenosine 5',5'''-P(1),P(4)-tetraphosphate asymmetrical hydrolase Dinucleosidetetraphosphatase (asymmetrical) Ap(4)Aase Bis(5'-guanosyl)-tetraphosphatase Also acts on bis(5'-xanthosyl)-tetraphosphate and, more slowly, on bis(5'-adenosyl)-tetraphosphate and bis(5'-uridyl)-tetraphosphate (cf. EC 3.6.1.41). P(1),P(4)-bis(5'-guanosyl) tetraphosphate + H(2)O = GTP + GMP. FAD diphosphatase FAD pyrophosphatase FAD + H(2)O = AMP + FMN. May be identical with EC 3.6.1.9. The plant enzyme also hydrolyzes NAD(+) and NADH; the animal enzyme hydrolyzes NAD(+) and CoA at about half of the rate of hydrolysis of FAD. Nucleoside-triphosphate diphosphatase Nucleoside-triphosphate pyrophosphatase A nucleoside triphosphate + H(2)O = a nucleotide + diphosphate. May be identical with EC 3.6.1.9. http://purl.uniprot.org/mim/147520 Trimetaphosphatase Trimetaphosphate + H(2)O = triphosphate. 5'-acylphosphoadenosine hydrolase 5'-acylphosphoadenosine + H(2)O = AMP + a carboxylate. Also acts on inosine and uridine compounds. ADP-sugar pyrophosphatase ADP-sugar diphosphatase ADP-sugar + H(2)O = AMP + alpha-D-aldose 1-phosphate. Has a distinct specificity from EC 3.6.1.45. NADP pyrophosphatase NAD+ pyrophosphatase NADH pyrophosphatase NAD(+) diphosphatase NAD(+) pyrophosphatase Also acts on NADP(+), 3-acetylpyridine and the thionicotinamide analogs of NAD(+) and NADP(+). NAD(+) + H(2)O = AMP + NMN. Deoxyuridine-triphosphatase dUTPase Desoxyuridine 5'-triphosphate nucleotidohydrolase dUTP pyrophosphatase dUTP diphosphatase Desoxyuridine 5'-triphosphatase dUTP + H(2)O = dUMP + diphosphate. Nucleoside phosphoacylhydrolase Hydrolyzes mixed phospho-anhydride bonds. Attacks ribonucleoside 5'-nitrophenylphosphates, but is inactive against phosphodiesters. Triphosphatase Triphosphate + H(2)O = diphosphate + phosphate. CDP-diacylglycerol phosphatidylhydrolase CDP-diacylglycerol diphosphatase CDP-diacylglycerol pyrophosphatase CDP-diacylglycerol + H(2)O = CMP + phosphatidate. C(55)-isoprenyl pyrophosphatase Isoprenyl pyrophosphatase C(55)-isoprenyl diphosphatase Undecaprenyl-diphosphatase The undecaprenol involved is ditrans,octacis-undecaprenol. Undecaprenyl diphosphate + H(2)O = undecaprenyl phosphate + phosphate. ThTPase Thiamine-triphosphatase Thiamine triphosphate + H(2)O = thiamine diphosphate + phosphate. AP3Aase Bis(5'-adenosyl)-triphosphatase Dinucleosidetriphosphatase Diadenosine 5',5'''-P(1),P(3)-triphosphate hydrolase AP3A hydrolase AP(3)A hydrolase AP(3)Aase P(1)-P(3)-bis(5'-adenosyl) triphosphate + H(2)O = ADP + AMP. ATPase Triphosphatase ATP monophosphatase Adenosinetriphosphatase Adenylpyrophosphatase Many enzymes previously listed under this number are now listed separately as EC 3.6.1.32 to EC 3.6.1.39. The remaining enzymes, not separately listed on the basis of some function coupled with hydrolyzes of ATP, include enzymes dependent on Ca(2+), Mg(2+), anions, H(+) or DNA. ATP + H(2)O = ADP + phosphate. M(7)G(5')pppN diphosphatase M(7)G(5')pppN pyrophosphatase Decapase 7-methylguanosine 5'-triphospho-5'-polynucleotide + H(2)O = 7-methylguanosine 5'-phosphate + polynucleotide. Phosphoribosyl-ATP pyrophosphatase Phosphoribosyl-ATP diphosphatase Phosphoribosyladenosine triphosphate pyrophosphatase The Neurospora crassa enzyme also catalyzes the reactions of EC 1.1.1.23 and EC 3.5.4.19. 1-(5-phosphoribosyl)-ATP + H(2)O = 1-(5-phosphoribosyl)-AMP + diphosphate. Thymidine-triphosphatase dTTP + H(2)O = dTDP + phosphate. Also acts, more slowly, on dUTP and UTP. Guanosine pentaphosphate phosphohydrolase Guanosine-5'-triphosphate,3'-diphosphate diphosphatase pppGpp 5'-phosphohydrolase Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase Guanosine 5'-triphosphate,3'-diphosphate + H(2)O = guanosine 5'-diphosphate,3'-diphosphate + phosphate. Also hydrolyzes other guanosine 5'-triphosphate derivatives with at least one unsubstituted phosphate group on the 3'-position, but not GTP, ATP or adenosine 5'-triphosphate,3'-diphosphate. Diadenosinetetraphosphatase (symmetrical) Bis(5'-nucleosyl)-tetraphosphatase (symmetrical) Ap4A hydrolase Ap(4)A hydrolase Diadenosine 5',5'''-P(1),P(4)-tetraphosphate pyrophosphohydrolase Dinucleosidetetraphosphatase (symmetrical) Also acts on bis(5'-guanosyl) tetraphosphate and bis(5'-adenosyl) pentaphosphate, and, more slowly, on some other polyphosphates, forming a nucleoside bisphosphate as one product in all cases (cf. EC 3.6.1.17). P(1),P(4)-bis(5'-adenosyl) tetraphosphate + H(2)O = 2 ADP. GDPase Guanosine-diphosphatase GDP + H(2)O = GMP + phosphate. Also acts on UDP but not on other nucleoside diphosphates and triphosphates. Dolichyldiphosphatase Dolichyl diphosphate + H(2)O = dolichyl phosphate + phosphate. Oligosaccharide-diphosphodolichol diphosphatase Oligosaccharide-diphosphodolichol pyrophosphatase Oligosaccharide-diphosphodolichol + H(2)O = oligosaccharide phosphate + dolichyl phosphate. UDP-sugar pyrophosphatase Nucleosidediphosphate-sugar pyrophosphatase UDP-sugar hydrolase Nucleosidediphosphate-sugar diphosphatase UDP-sugar diphosphatase Divalent cation Some but not all enzymes of this class also appear to have EC 3.1.3.5 activity. UDP-sugar is the best substrate, although other nucleoside-sugar diphosphates are used as substrates with similar Km values but much lower maximum velocities. UDP-sugar + H(2)O = UMP + alpha-D-aldose 1-phosphate. Thus, this enzyme has a specificity distinct from that of EC 3.6.1.21. ATP-diphosphatase Apyrase ATP-diphosphohydrolase ADPase Adenosine diphosphatase ATP + 2 H(2)O = AMP + 2 phosphate. Also acts on ADP, and on other nucleoside triphosphates and diphosphates. Most of the ecto-ATPases occurring on the cell surface and hydrolyzing extracellular nucleoside triphosphates and diphosphates belong to this enzyme family. Calcium Diphosphoinositol-polyphosphate diphosphatase Diphosphoinositol-polyphosphate phosphohydrolase DIPP This enzyme hydrolyzes the diphosphate bond, leaving a phospho group where a diphospho group had been. It can also act on bis(adenosine) diphosphate. Diphospho-myo-inositol polyphosphate + H(2)O = myo-inositol polyphosphate + phosphate. Nucleoside-diphosphatase Acts on IDP, GDP, UDP and also on D-ribose 5-diphosphate. A nucleoside diphosphate + H(2)O = a nucleotide + phosphate. Acylphosphatase Acylphosphate phosphohydrolase An acylphosphate + H(2)O = a carboxylate + phosphate. ATPase ATP diphosphatase ATP pyrophosphatase ATP + H(2)O = AMP + diphosphate. Also acts on ITP, GTP, CTP and UTP. Nucleotide pyrophosphatase Nucleotide diphosphatase A dinucleotide + H(2)O = 2 mononucleotides. http://purl.uniprot.org/mim/602475 Substrates include NAD(+), NADP(+), FAD, CoA and also ATP and ADP. http://purl.uniprot.org/mim/208000 In sulfonyl-containing anhydrides Adenylylsulfatase Adenylyl sulfate + H(2)O = AMP + sulfate. Phosphoadenylylsulfatase PAPS sulfatase 3-phosphoadenylyl sulfatase Manganese 3'-phosphoadenylyl sulfate + H(2)O = adenosine 3',5'-bisphosphate + sulfate. Acting on acid anhydrides; catalyzing transmembrane movement of substances Flippase Phospholipid-transporting ATPase Mg(2+)-ATPase Magnesium-ATPase Phospholipid-translocating ATPase P-type ATPase that undergoes covalent phosphorylation during the transport cycle. http://purl.uniprot.org/mim/211600 Magnesium http://purl.uniprot.org/mim/147480 ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out). The enzyme apparently has several activities, one of them being the movement of phospholipids from one membrane face to the other. http://purl.uniprot.org/mim/243300 H(+)/K(+)-exchanging ATPase H(+)/K(+)-ATPase Potassium-transporting ATPase Gastric H(+)/K(+) ATPase Hydrogen/potassium-exchanging ATPase Proton pump Hydrolysis of ATP is coupled with the exchange of H(+) and K(+) ions. Magnesium ATP + H(2)O + H(+)(In) + K(+)(Out) = ADP + phosphate + H(+)(Out) + K(+)(In). P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Chloride-motive ATPase Chloride-transporting ATPase Chloride-translocating ATPase Cl(-)-transporting ATPase P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Magnesium ATP + H(2)O + Cl(-)(Out) = ADP + phosphate + Cl(-)(In). K(+)-transporting ATPase K(+)-importing ATPase Potassium-transporting ATPase Potassium-importing ATPase Magnesium P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The probable stoichiometry is one ion per ATP hydrolyzed. A bacterial enzyme of di(heterotetrameric) structure that is involved in K(+) import. ATP + H(2)O + K(+)(Out) = ADP + phosphate + K(+)(In). H(+)-transporting ATPase Mitochondrial ATPase H(+)-transporting two-sector ATPase H(+)-transporting ATP synthase F(o)F(1)-ATPase Chloroplast ATPase F(0)F(1)-ATPase F(1)-ATPase ATP synthase http://purl.uniprot.org/mim/551500 http://purl.uniprot.org/mim/500003 http://purl.uniprot.org/mim/256000 Within this complex, the gamma-and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). This movement is driven by the H(+) electrochemical potential gradient. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha-and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. http://purl.uniprot.org/mim/535000 The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. http://purl.uniprot.org/mim/267300 ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out). Sodium-transporting two-sector ATPase Na(+)-transporting two-sector ATPase Na(+)-translocating ATPase ATP synthase, sodium ion specific ATP + H(2)O = ADP + phosphate. A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. An enzyme found in alkaliphilic bacteria that is similar to EC 3.6.3.14. Arsenical pump-driving ATPase Arsenite-translocating ATPase Arsenical resistance ATPase Arsenite-transporting ATPase ATP + H(2)O + arsenite(In) = ADP + phosphate + arsenite(Out). A bacterial multisubunit non-phosphorylated ATPase that is involved in the export of arsenite and antimonite anions. Monosaccharide-transporting ATPase Family of bacterial enzymes importing ribose, xylose, arabinose, galactose and methylgalactoside. ATP + H(2)O + monosaccharide(Out) = ADP + phosphate + monosaccharide(In). Oligosaccharide-transporting ATPase A bacterial enzyme that imports lactose, melibiose and raffinose. ATP + H(2)O + oligosaccharide(Out) = ADP + phosphate + oligosaccharide(In). Maltose-transporting ATPase ATP + H(2)O + maltose(Out) = ADP + phosphate + maltose(In). Comprises bacterial enzymes that import maltose and maltose oligosaccharides. Magnesium-translocating P-type ATPase Magnesium-importing ATPase Mg(2+)-importing ATPase ATP + H(2)O + Mg(2+)(Out) = ADP + phosphate + Mg(2+)(In). P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Magnesium Glycerol-3-phosphate-transporting ATPase A bacterial enzyme that imports phosphorylated glycerol. ATP + H(2)O + glycerol-3-phosphate(Out) = ADP + phosphate + glycerol-3-phosphate(In). Histidine permease Polar-amino-acid-transporting ATPase Comprises bacterial enzymes that import His, Arg, Lys, Glu, Gln, Asp, ornithine, octopine and nopaline. ATP + H(2)O + polar amino acid(Out) = ADP + phosphate + polar amino acid(In). Nonpolar-amino-acid-transporting ATPase Comprises bacterial enzymes that import Leu, Ile and Val. ATP + H(2)O + nonpolar amino acid(Out) = ADP + phosphate + nonpolar amino acid(In). Oligopeptide permease Oligopeptide-transporting ATPase ATP + H(2)O + oligopeptide(Out) = ADP + phosphate + oligopeptide(In). A bacterial enzyme that imports di-and oligopeptides. Nickel-transporting ATPase ATP + H(2)O + Ni(2+)(Out) = ADP + phosphate + Ni(2+)(In). A bacterial enzyme that imports Ni(2+). Sulfate-transporting ATPase A bacterial enzyme that imports sulfate and thiosulfate anions. ATP + H(2)O + sulfate(Out) = ADP + phosphate + sulfate(In). Nitrate-transporting ATPase A bacterial enzyme that imports NO(3)(-), NO(2)(-) and OCN(-). ATP + H(2)O + nitrate(Out) = ADP + phosphate + nitrate(In). ABC phosphate transporter Phosphate-transporting ATPase A bacterial enzyme that imports phosphate anions. ATP + H(2)O + phosphate(Out) = ADP + phosphate + phosphate(In). Phosphonate-transporting ATPase ATP + H(2)O + phosphonate(Out) = ADP + phosphate + phosphonate(In). A bacterial enzyme that imports phosphonate and organophosphate anions. Molybdate-transporting ATPase ATP + H(2)O + molybdate(Out) = ADP + phosphate + molybdate(In). A bacterial enzyme that imports molybdate anions. Cadmium-translocating P-type ATPase Cd(2+)-exporting ATPase Cadmium-exporting ATPase P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Magnesium ATP + H(2)O + Cd(2+)(In) = ADP + phosphate + Cd(2+)(Out). Fe(3+)-transporting ATPase A bacterial enzyme that imports ferric cations. ATP + H(2)O + Fe(3+)(Out) = ADP + phosphate + Fe(3+)(In). Polyamine-transporting ATPase A bacterial enzyme that imports putrescine and spermidine. ATP + H(2)O + polyamine(Out) = ADP + phosphate + polyamine(In). Quaternary-amine-transporting ATPase A bacterial enzyme that imports betaine and glycine. ATP + H(2)O + quaternary amine(Out) = ADP + phosphate + quaternary amine(In). Vitamin B12-transporting ATPase A bacterial enzyme that imports cobalamin derivatives. ATP + H(2)O + vitamin B12(Out) = ADP + phosphate + vitamin B12(In). Iron-chelate-transporting ATPase ATP + H(2)O + iron chelate(Out) = ADP + phosphate + iron chelate(In). A bacterial enzyme that imports Fe-enterobactin, Fe-dicitrate, Fe-hydroxamate and other siderophores. Manganese-transporting ATPase ABC-type manganese permease complex A bacterial enzyme that imports Mn(2+), Zn(2+) and iron chelates. ATP + H(2)O + Mn(2+)(Out) = ADP + phosphate + Mn(2+)(In). Taurine-transporting ATPase ATP + H(2)O + taurine(Out) = ADP + phosphate + taurine(In). A bacterial enzyme that imports taurine. Guanine-transporting ATPase A eukaryotic enzyme that imports guanine and tryptophan (it contains a single ATP-binding site). ATP + H(2)O + guanine(Out) = ADP + phosphate + guanine(In). Capsular-polysaccharide-transporting ATPase An enzyme that exports capsular polysaccharide from Gram-negative bacteria. ATP + H(2)O + capsular polysaccharide(In) = ADP + phosphate + capsular polysaccharide(Out). Lipopolysaccharide-transporting ATPase Enzymes of Gram-negative bacteria that export lipo-oligosaccharides and lipopolysaccharides. ATP + H(2)O + lipopolysaccharide(In) = ADP + phosphate + lipopolysaccharide(Out). Cu(2+)-exporting ATPase Copper-transporting ATPase Copper-translocating P-type ATPase Copper-exporting ATPase http://purl.uniprot.org/mim/277900 P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Magnesium ATP + H(2)O + Cu(2+)(In) = ADP + phosphate + Cu(2+)(Out). http://purl.uniprot.org/mim/309400 http://purl.uniprot.org/mim/304150 Teichoic-acid-transporting ATPase ATP + H(2)O + teichoic acid(In) = ADP + phosphate + teichoic acid(Out). An enzyme found in Gram-positive bacteria that exports teichoic acid. Heme-transporting ATPase ATP + H(2)O + heme(In) = ADP + phosphate + heme(Out). An enzyme found in Gram-negative bacteria that exports heme. Beta-glucan-transporting ATPase An enzyme found in Gram-negative bacteria that exports beta-glucan. ATP + H(2)O + beta-glucan(In) = ADP + phosphate + beta-glucan(Out). Peptide-transporting ATPase A family of enzymes that exports alpha-hemolysin, cyclolysin, colicin V and siderophores from Gram-negative bacteria, and bacteriocin, subtilin, competence factor and pediocin from Gram-positive bacteria. ATP + H(2)O + peptide(In) = ADP + phosphate + peptide(Out). MDR protein Multidrug-resistance protein P-glycoprotein Pleiotropic-drug-resistance protein Steroid-transporting ATPase ATP phosphohydrolase (steroid-exporting) PDR protein Xenobiotic-transporting ATPase ATP + H(2)O + xenobiotic(In) = ADP + phosphate + xenobiotic(Out). Many of them transport glutathione conjugates with drugs. Several distinct enzymes may be present in a single eukaryotic cell. http://purl.uniprot.org/mim/600803 http://purl.uniprot.org/mim/147480 http://purl.uniprot.org/mim/602347 Enzymes of Gram-positive bacteria and eukaryotic cells that export a number of drugs, with unusual specificity, covering various groups of unrelated substances, while ignoring some that are closely related structurally. Some also show some 'flippase' (EC 3.6.3.1) activity. Cadmium-transporting ATPase Yeast cadmium factor A Saccharomyces cerevisiae enzyme that exports some heavy metals, especially Cd(2+), from the cytosol into the vacuole. ATP + H(2)O = ADP + phosphate. Fatty-acyl-CoA-transporting ATPase An animal and Saccharomyces cerevisiae enzyme that transports fatty acyl CoA into and out of peroxisomes. ATP + H(2)O + fatty acyl CoA(Cis) = ADP + phosphate + fatty acyl CoA(Trans). Alpha-factor-transporting ATPase A Saccharomyces cerevisiae enzyme that exports the alpha-factor sex pheromone. ATP + H(2)O + alpha-factor(In) = ADP + phosphate + alpha-factor(Out). Channel-conductance-controlling ATPase Cystic-fibrosis membrane-conductance-regulating protein ATP + H(2)O = ADP + phosphate. An animal enzyme that is active in forming a chloride channel, the absence of which brings about cystic fibrosis. It is also involved in the functioning of other transmembrane channels. Zinc-exporting ATPase Zn(2+)-exporting ATPase P(1B)-type ATPase Zinc-translocating P-type ATPase ATP + H(2)O + Zn(2+)(In) = ADP + phosphate + Zn(2+)(Out). Magnesium P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme also exports Cd(2+) and Co(2+). Protein-secreting ATPase A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. ATP + H(2)O = ADP + phosphate. There are several families of enzymes included here, e.g. ATP-hydrolyzing enzymes of the general secretory pathway (Sec or Type II), of the virulence-related secretory pathway (Type III) and of the conjugal DNA-protein transfer pathway (Type IV). Type II enzymes occur in bacteria, archaea and eukaryotes, whereas type III and type IV enzymes occur in bacteria where they form components of a multi-subunit complex. Mitochondrial protein-transporting ATPase A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase involved in the transport of proteins or preproteins into mitochondria using the TIM protein complex. ATP + H(2)O = ADP + phosphate. TIM is the protein transport machinery of the inner mitochondrial membrane that contains three essential Tim proteins: Tim17 and Tim23 are thought to build a preprotein translocation channel while Tim44 interacts transiently with the matrix heat-shock protein Hsp70 to form an ATP-driven import motor. Chloroplast protein-transporting ATPase A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. ATP + H(2)O = ADP + phosphate. Involved in the transport of proteins or preproteins into chloroplast stroma (several ATPases may participate in this process). Ag(+)-exporting ATPase ATP + H(2)O + Ag(+)(In) = ADP + phosphate + Ag(+)(Out). P-type ATPase that exports Ag(+) ions from pathogenic microorganisms as well as from some animal tissues. H(+)-transporting ATPase Proton-exporting ATPase Proton transport ATPase Proton-translocating P-type ATPase H(+)-exporting ATPase Magnesium ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out). Generates an electrochemical potential gradient of protons across the plasma membrane. P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Sodium transport ATPase Na(+)-exporting ATPase Sodium-exporting ATPase Na(+)-transporting ATPase Sodium-translocating P-type ATPase Magnesium P-type ATPase that undergoes covalent phosphorylation during the transport cycle. ATP + H(2)O + Na(+)(In) = ADP + phosphate + Na(+)(Out). Involved in the efflux of Na(+), with one ion being exported per ATP hydrolyzed. Calcium pump Calcium-translocating P-type ATPase Calcium-transporting ATPase Ca(2+)-transporting ATPase This enzyme family comprises three types of Ca(2+)-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum and in Saccharomyces cerevisiae. http://purl.uniprot.org/mim/101900 http://purl.uniprot.org/mim/169600 Magnesium http://purl.uniprot.org/mim/601003 ATP + H(2)O + Ca(2+)(Cis) = ADP + phosphate + Ca(2+)(Trans). http://purl.uniprot.org/mim/124200 P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The first and third transport one ion per ATP hydrolyzed, whereas the second transports two ions. Sodium pump Na(+)/K(+)-exchanging ATPase Na,K-activated ATPase Sodium/potassium-exchanging ATPase Sodium/potassium-transporting ATPase Na(+)/K(+)-ATPase Magnesium It is involved in generating the plasma membrane electrical potential. An enzyme from the plasma membrane of animal cells that catalyzes the efflux of three Na(+) and influx of two K(+) per ATP hydrolyzed. P-type ATPase that undergoes covalent phosphorylation during the transport cycle. ATP + H(2)O + Na(+)(In) + K(+)(Out) = ADP + phosphate + Na(+)(Out) + K(+)(In). http://purl.uniprot.org/mim/104290 http://purl.uniprot.org/mim/128235 http://purl.uniprot.org/mim/602481 Acting on acid anhydrides; involved in cellular and subcellular movement Myosin ATPase Actomyosin In the absence of actin, myosin shows only low ATPase activity, which requires Ca(2+). ATP + H(2)O = ADP + phosphate. Involved in muscle contraction. Non-chaperonin molecular chaperone ATPase Molecular chaperone Hsc70 ATPase They comprise a number of heat-shock-cognate proteins. ATP + H(2)O = ADP + phosphate. They are also active in clathrin uncoating and in the oligomerization of actin. This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. Nucleoplasmin ATPase ATP + H(2)O = ADP + phosphate. An acidic nuclear protein that is active in the ATP-dependent assembly of nucleosome cores, in decondensation of sperm chromatin and in other histone-involving processes. Dynein ATPase ATP + H(2)O = ADP + phosphate. Hydrolysis of ATP provides energy for the movement of organelles (endosomes, lysosomes, mitochondria) along microtubules to the centrosome toward the microtubule's minus end. A multisubunit protein complex associated with microtubules. It also functions in the movement of eukaryotic flagella and cilia. Katanin Microtubule-severing ATPase ATP + H(2)O = ADP + phosphate. Another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome. Plus-end-directed kinesin ATPase Kinesin Also hydrolyzes GTP. Microtubular motor protein, involved in organelle movement, in mitosis and meiosis. ATP + H(2)O = ADP + phosphate. In contrast to dynein, it moves along microtubules toward the plus end. Minus-end-directed kinesin ATPase Structurally almost identical to EC 3.6.4.3 but the movement it catalyzes is toward the minus end of microtubules. ATP + H(2)O = ADP + phosphate. Vesicle-fusing ATPase They include peroxin, which apparently is involved in Zellweger's syndrome. ATP + H(2)O = ADP + phosphate. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. A large family of ATP-hydrolyzing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. Peroxisome-assembly ATPase Peroxisome assembly factor-2 An extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle. ATP + H(2)O = ADP + phosphate. Their molecular masses range from 25 to 600 kDa. Proteasome ATPase RP triphosphatase RP triple-A protein Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome. ATP + H(2)O = ADP + phosphate. Belongs to the AAA-type superfamily and, like EC 3.6.4.5, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Chaperonin ATPase Chaperonin Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or to entry into mitochondria and chloroplasts. Molecular masses of subunits ranges from 10-90 kDa. ATP + H(2)O = ADP + phosphate. Acting on GTP; involved in cellular and subcellular movement Heterotrimeric G-protein GTPase G(olf) is instrumental in odor perception, transducin in vision and gustducin in taste recognition. At least 16 different alpha subunits (39-52 kDa), 5 beta subunits (36 kDa) and 12 gamma subunits (6-9 kDa) are known. This group includes stimulatory and inhibitory G-proteins such as G(s), G(i), G(o) and G(olf), targeting adenylate cyclase and/or K(+) and Ca(2+) channels; G(q) stimulating phospholipase C; transducin activating cGMP phosphodiesterase; gustducin activating cAMP phosphodiesterase. This group comprises GTP-hydrolyzing systems, where GTP and GDP alternate in binding. GTP + H(2)O = GDP + phosphate. Small monomeric GTPase A family of about 50 enzymes with a molecular mass of 21 kDa that are distantly related to the alpha-subunit of EC 3.6.1.46. GTP + H(2)O = GDP + phosphate. Involved in cell-growth regulation (Ras subfamily), membrane vesicle traffic and uncoating (Rab and ARF subfamilies), nuclear protein import (Ran subfamily) and organization of the cytoskeleton (Rho and Rac subfamilies). Peptide-release factor (RF) Initiation factor (IF) Peptide-release or termination factor Elongation factor (EF) Protein-synthesizing GTPase In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyzes it in prokaryotes. GTP + H(2)O = GDP + phosphate. In eukaryotes, it is eIF-2 (150 kDa) that binds GTP. In the elongation phase, the GTP-hydrolyzing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1-alpha (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa). GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs. EF-Tu and EF-1-alpha catalyze binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyze the translocation of peptidyl-tRNA from the A-site to the P-site. This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis. Signal-recognition-particle GTPase GTP + H(2)O = GDP + phosphate. Activity is associated with the signal-recognition particle (a protein-and RNA-containing structure involved in endoplasmic-reticulum-associated protein synthesis). Dynamin GTPase http://purl.uniprot.org/mim/160150 http://purl.uniprot.org/mim/606482 An enzyme with a molecular mass of about 100 kDa that is involved in endocytosis and is instrumental in pinching off membrane vesicles. GTP + H(2)O = GDP + phosphate. Tubulin GTPase An intrinsic activity of alpha-tubulin involved in tubulin folding, division plane formation in prokaryotic cells and others. GTP + H(2)O = GDP + phosphate. Acting on carbon-carbon bonds In ketonic substances Oxalacetic hydrolase Oxaloacetase Oxaloacetate + H(2)O = oxalate + acetate. Cyclohexane-1,3-dione hydrolase Cyclohexane-1,3-dione + H(2)O = 5-oxohexanoate. Highly specific; does not act on other dione derivatives of cyclohexane, cyclopentane or cycloheptane. Fumarylacetoacetate hydrolase Fumarylacetoacetase Beta-diketonase 4-fumarylacetoacetate + H(2)O = acetoacetate + fumarate. Also acts on other 3,5-and 2,4-dioxo acids. http://purl.uniprot.org/mim/276700 L-kynurenine hydrolase Kynureninase Pyridoxal-phosphate L-kynurenine + H(2)O = anthranilate + L-alanine. Also acts on 3'-hydroxykynurenine and some other (3-arylcarbonyl)-alanines. Phloretin hydrolase Also hydrolyzes other C-acylated phenols related to phloretin. Phloretin + H(2)O = phloretate + phloroglucinol. Acylpyruvate hydrolase Acts on formylpyruvate, 2,4-dioxopentanoate, 2,4-dioxohexanoate and 2,4-dioxoheptanoate. A 3-acylpyruvate + H(2)O = a carboxylate + pyruvate. Acetylpyruvate hydrolase Acetylpyruvate + H(2)O = acetate + pyruvate. Highly specific; does not act on pyruvate, oxaloacetate, maleylpyruvate, fumarylpyruvate or acetylacetone. Oxidized PVA hydrolase Beta-diketone hydrolase Involved in the bacterial degradation of polyvinyl alcohol. Nonane-4,6-dione + H(2)O = pentan-2-one + butanoate. Also acts on the product of the action of EC 1.1.3.18 on polyvinyl alcohols. HOHPDA hydrolase 2,6-dioxo-6-phenylhexa-3-enoate hydrolase 2,6-dioxo-6-phenylhexa-3-enoate + H(2)O = benzoate + 2-oxopent-4-enoate. Involved in the breakdown of biphenyl-related compounds by Pseudomonas sp. Cleaves the products from biphenol, 3-isopropylcatechol and 3-methylcatechol produced by EC 1.13.11.39 by ring-fission at a -CO-C bond. 2-hydroxymuconate-semialdehyde hydrolase 2-hydroxymuconate semialdehyde + H(2)O = formate + 2-oxopent-4-enoate. Acting on halide bonds In C-halide compounds Alkylhalidase Halogenase Bromochloromethane + H(2)O = formaldehyde + bromide + chloride. 2-haloacid dehalogenase (configuration-inverting) DL-DEXi DL-2-haloacid halidohydrolase (inversion of configuration) DL-2-haloacid dehalogenase 2-haloalkanoid acid halidohydrolase DL-2-haloacid dehalogenase (inversion of configuration) 2-haloalkanoic acid dehalogenase The enzyme from Pseudomonas sp. 113 acts on 2-haloalkanoic acids whose carbon chain lengths are five or less (see also EC 3.8.1.2, EC 3.8.1.9 and EC 3.8.1.11). (2) (R)-2-haloacid + H(2)O = (S)-2-hydroxyacid + halide. (1) (S)-2-haloacid + H(2)O = (R)-2-hydroxyacid + halide. Dehalogenates both (S)-and (R)-2-haloalkanoic acids to the corresponding (R)-and (S)-hydroxyalkanoic acids, respectively, with inversion of configuration at C-2. DL-2-haloacid dehalogenase DL-DEXr 2-haloalkanoic acid dehalogenase 2-haloalkanoid acid halidohydrolase 2-haloacid dehalogenase (configuration-retaining) Dehalogenates both (S)-and (R)-2-haloalkanoic acids to the corresponding (S)-and (R)-hydroxyalkanoic acids, respectively, with retention of configuration at C-2 (see also EC 3.8.1.2, EC 3.8.1.9 and EC 3.8.1.10). (2) (R)-2-haloacid + H(2)O = (R)-2-hydroxyacid + halide. (1) (S)-2-haloacid + H(2)O = (S)-2-hydroxyacid + halide. L-2-haloacid dehalogenase 2-haloalkanoid acid halidohydrolase 2-haloacid dehalogenase DL-2-haloacid dehalogenase 2-haloacid halidohydrolase Halocarboxylic acid halidohydrolase 2-haloalkanoic acid dehalogenase 2-halocarboxylic acid dehalogenase II (S)-2-haloacid dehalogenase L-DEX (S)-2-haloacid + H(2)O = (R)-2-hydroxyacid + halide. Acts on acids of short chain lengths, C(2) to C(4), with inversion of configuration at C-2 (see also EC 3.8.1.9, EC 3.8.1.10 and EC 3.8.1.11). Haloacetate dehalogenase Haloacetate + H(2)O = glycolate + halide. Haloalkane dehalogenase 1-chlorohexane halidohydrolase 1-haloalkane + H(2)O = a primary alcohol + halide. Acts on a wide range of 1-haloalkanes, haloalcohols, haloalkenes and some haloaromatic compounds. 4-chlorobenzoate dehalogenase 4-chlorobenzoate + H(2)O = 4-hydroxybenzoate + chloride. Catalyzes the first step in the degradation of chlorobenzoate in Pseudomonas. In many microorganisms, this activity comprises three separate enzymes, EC 6.2.1.33, EC 3.8.1.7 and EC 3.1.2.23. 4-chlorobenzoyl-CoA dehalogenase This enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway. 4-chlorobenzoyl-CoA + H(2)O = 4-hydroxybenzoyl CoA + chloride. Specific for dehalogenation at the 4-position. Can dehalogenate substrates bearing fluorine, chlorine, bromine and iodine in the 4-position. Atrazine chlorohydrolase Involved in the degradation of the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, in bacteria. Atrazine + H(2)O = 4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl. D-DEX D-2-haloacid dehalogenase (R)-2-haloacid dehalogenase 2-haloalkanoic acid dehalogenase 2-haloalkanoid acid halidohydrolase Acts on acids of short chain lengths, C(2) to C(4), with inversion of configuration at C-2 (see also EC 3.8.1.2, EC 3.8.1.10 and EC 3.8.1.11). (R)-2-haloacid + H(2)O = (S)-2-hydroxyacid + halide. Acting on phosphorus-nitrogen bonds Acting on phosphorus-nitrogen bonds Phosphoamidase Possibly identical with EC 3.1.3.9 or EC 3.1.3.16. Also acts on N-phospho-arginine and other phosphoamides. N-phosphocreatine + H(2)O = creatine + phosphate. Lyases Carbon-carbon lyases Carboxy-lyases 2-oxo-acid carboxy-lyase Pyruvate decarboxylase Alpha-carboxylase Alpha-ketoacid carboxylase Pyruvic decarboxylase Thiamine diphosphate A 2-oxo acid = an aldehyde + CO(2). Also catalyzes acyloin formation. Aspartate alpha-decarboxylase Aspartate 1-decarboxylase L-aspartate 1-carboxy-lyase Pyruvate L-aspartate = beta-alanine + CO(2). Desulfinase Aspartate 4-decarboxylase L-aspartate 4-carboxy-lyase Pyridoxal-phosphate Also catalyzes the decarboxylation of aminomalonate and the desulfination of 3-sulfino-L-alanine to sulfite and alanine. L-aspartate = L-alanine + CO(2). Valine decarboxylase L-valine carboxy-lyase Pyridoxal-phosphate L-valine = 2-methylpropanamine + CO(2). Also acts on L-leucine. Glutamate decarboxylase L-glutamate 1-carboxy-lyase The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. Pyridoxal-phosphate L-glutamate = 4-aminobutanoate + CO(2). http://purl.uniprot.org/mim/603513 3-hydroxy-L-glutamate 1-carboxy-lyase Hydroxyglutamate decarboxylase 3-hydroxy-L-glutamate = 4-amino-3-hydroxybutanoate + CO(2). Pyridoxal-phosphate L-ornithine carboxy-lyase Ornithine decarboxylase Pyridoxal-phosphate L-ornithine = putrescine + CO(2). L-lysine carboxy-lyase Lysine decarboxylase Also acts on 5'-hydroxy-L-lysine. L-lysine = cadaverine + CO(2). Pyridoxal-phosphate Arginine decarboxylase L-arginine carboxy-lyase L-arginine = agmatine + CO(2). Pyridoxal-phosphate Oxalate carboxy-lyase Oxalate decarboxylase Manganese Oxalate = formate + CO(2). DAP decarboxylase Meso-2,6-diaminoheptanedioate carboxy-lyase Diaminopimelate decarboxylase Meso-2,6-diaminoheptanedioate = L-lysine + CO(2). Pyridoxal-phosphate 1-(5-phosphoribosyl)-5-amino-4-imidazolecarboxylate carboxy-lyase 5-phosphoribosyl-5-aminoimidazole carboxylase AIR carboxylase 5-amino-1-ribosylimidazole 5-phosphate carboxylase 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase Phosphoribosylaminoimidazole carboxylase 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole is not a substrate. While this is the reaction that occurs in vertebrates during purine biosynthesis, two enzymes are required to carry out the same reaction in Escherichia coli, rdfs:labelly EC 6.3.4.18 and EC 5.4.99.18. 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO(2). L-histidine carboxy-lyase Histidine decarboxylase Pyridoxal-phosphate or pyruvate L-histidine = histamine + CO(2). Orotidylic decarboxylase Orotidine-5'-phosphate decarboxylase Uridine 5'-monophosphate synthase Orotidine-5'-phosphate carboxy-lyase UMP synthase OMPdcase OMP decarboxylase The enzyme from higher eukaryotes is identical with EC 2.4.2.10. Orotidine 5'-phosphate = UMP + CO(2). http://purl.uniprot.org/mim/258920 Aminobenzoate carboxy-lyase Aminobenzoate decarboxylase Pyridoxal-phosphate 4(or 2)-aminobenzoate = aniline + CO(2). Tyrosine decarboxylase L-tyrosine carboxy-lyase Pyridoxal-phosphate The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine. L-tyrosine = tyramine + CO(2). Aromatic amino acid decarboxylase L-DOPA decarboxylase DOPA decarboxylase 5-hydroxytryptophan decarboxylase Aromatic-L-amino-acid decarboxylase Tryptophan decarboxylase Hydroxytryptophan decarboxylase Aromatic-L-amino-acid carboxy-lyase (2) 5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO(2). Pyridoxal-phosphate (1) 3,4-dihydroxyphenylalanine = dopamine + CO(2). http://purl.uniprot.org/mim/608643 Also acts on L-tryptophan, 5-hydroxy-L-tryptophan and dihydroxy-L-phenylalanine (DOPA). Cysteinesulfinic acid decarboxylase CSADCase 3-sulfino-L-alanine carboxy-lyase Sulfinoalanine decarboxylase Cysteine-sulfinate decarboxylase Pyridoxal-phosphate Also acts on L-cysteate. 3-sulfino-L-alanine = hypotaurine + CO(2). Oxaloacetate carboxy-lyase Oxaloacetate decarboxylase Oxalate beta-decarboxylase Biotin Some animal enzymes require manganese. The process is accompanied by the extrusion of two sodium ions from cells. Oxaloacetate = pyruvate + CO(2). Sodium or manganese The enzyme from Klebsiella aerogenes is a biotinyl protein and also decarboxylates glutaconyl-CoA and methylmalonyl-CoA. Pantothenoylcysteine decarboxylase N-((R)-pantothenoyl)-L-cysteine carboxy-lyase N-((R)-pantothenoyl)-L-cysteine = pantetheine + CO(2). PEP carboxylase Phosphoenolpyruvate carboxylase PEPCase Phosphoenolpyruvic carboxylase Phosphate + oxaloacetate = H(2)O + phosphoenolpyruvate + CO(2). PEPCK PEP carboxykinase Phosphoenolpyruvate carboxykinase Phosphoenolpyruvate carboxylase Phosphoenolpyruvate carboxykinase (GTP) Phosphopyruvate carboxylase http://purl.uniprot.org/mim/261650 GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO(2). http://purl.uniprot.org/mim/261680 ITP can act as phosphate donor. Mevalonate pyrophosphate decarboxylase Diphosphomevalonate decarboxylase Mevalonate diphosphate decarboxylase ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO(2). 3-dehydro-L-gulonate carboxy-lyase Keto-L-gulonate decarboxylase Dehydro-L-gulonate decarboxylase 3-dehydro-L-gulonate = L-xylulose + CO(2). UDP-glucuronate decarboxylase UDP-D-glucuronate carboxy-lyase NAD UDP-D-glucuronate = UDP-D-xylose + CO(2). Phosphopantothenoylcysteine decarboxylase N-((R)-4'-phosphopantothenoyl)-L-cysteine carboxy-lyase Pyruvate N-((R)-4'-phosphopantothenoyl)-L-cysteine = pantotheine 4'-phosphate + CO(2). Uroporphyrinogen decarboxylase Uroporphyrinogen-III carboxy-lyase Uroporphyrinogen III decarboxylase Acts on a number of porphyrinogens. http://purl.uniprot.org/mim/176100 Uroporphyrinogen III = coproporphyrinogen + 4 CO(2). http://purl.uniprot.org/mim/176090 Phosphoenolpyruvate carboxykinase (pyrophosphate) Phosphoenolpyruvate carboxylase PEP carboxyphosphotransferase Phosphoenolpyruvate carboxykinase (diphosphate) Phosphopyruvate carboxylase Also catalyzes the reaction: phosphoenolpyruvate + phosphate = pyruvate + diphosphate. Diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO(2). Ribulose 1,5-diphosphate carboxylase/oxygenase Carboxydismutase RuBisCO Ribulose bisphosphate carboxylase/oxygenase D-ribulose 1,5-diphosphate carboxylase D-ribulose-1,5-bisphosphate carboxylase Diphosphoribulose carboxylase Ribulose 1,5-diphosphate carboxylase RuBP carboxylase Ribulose diphosphate carboxylase/oxygenase Ribulose-bisphosphate carboxylase Ribulose diphosphate carboxylase Ribulose 1,5-bisphosphate carboxylase/oxygenase Ribulose 1,5-bisphosphate carboxylase Will utilize O(2) instead of CO(2), forming 3-phospho-D-glycerate and 2-phosphoglycolate. 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO(2) + H(2)O. Acetoacetate carboxy-lyase Acetoacetate decarboxylase Acetoacetate = acetone + CO(2). Hydroxypyruvate carboxy-lyase Hydroxypyruvate decarboxylase Hydroxypyruvate = glycolaldehyde + CO(2). (S)-methylmalonyl-CoA carboxy-lyase Propionyl-CoA carboxylase Methylmalonyl-coenzyme A decarboxylase Propionyl coenzyme A carboxylase (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase Methylmalonyl-CoA decarboxylase The enzyme from Veillonella alcalescens is a biotinyl-protein, requires sodium and acts as a sodium pump. Biotin (S)-methylmalonyl-CoA = propanoyl-CoA + CO(2). Carnitine decarboxylase Carnitine carboxy-lyase Carnitine = 2-methylcholine + CO(2). Requires ATP. Phenylpyruvate carboxy-lyase Phenylpyruvate decarboxylase Phenylpyruvate = phenylacetaldehyde + CO(2). Also acts on (indol-3-yl)pyruvate. 4-carboxymuconolactone decarboxylase 4-carboxymuconolactone carboxy-lyase 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate = 4,5-dihydro-5-oxofuran-2-acetate + CO(2). Picolinic acid decarboxylase Aminocarboxymuconate-semialdehyde decarboxylase 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate = 2-aminomuconate semialdehyde + CO(2). The product rearranges non-enzymically to picolinate. 2,3-DHBA decarboxylase 2,3-dihydroxybenzoic acid decarboxylase o-pyrocatechuate decarboxylase 2,3-dihydroxybenzoate carboxy-lyase 2,3-dihydroxybenzoate = catechol + CO(2). Tartronate semialdehyde carboxylase Glyoxylate carboligase Tartronate-semialdehyde synthase 2 glyoxylate = tartronate semialdehyde + CO(2). Thiamine diphosphate Indole-3-glycerol-phosphate synthase Indoleglycerol phosphate synthetase In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.3.27, EC 4.2.1.20, and EC 5.3.1.24). 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O. PEP carboxykinase Phosphoenolpyruvate carboxylase Phosphoenolpyruvate carboxykinase (ATP) Phosphopyruvate carboxylase Phosphoenolpyruvate carboxykinase PEPCK ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO(2). Acetolactate decarboxylase (S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase (S)-2-hydroxy-2-methyl-3-oxobutanoate = (R)-2-acetoin + CO(2). S-adenosyl-L-methionine decarboxylase S-adenosyl-L-methionine carboxy-lyase Adenosylmethionine decarboxylase S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2). Pyruvate 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-carboxy-lyase 3-hydroxy-2-methylpyridine-4,5-dicarboxylate = 3-hydroxy-2-methylpyridine-5-carboxylate + CO(2). 6-MSA decarboxylase 6-methylsalicylate decarboxylase 6-methylsalicylate carboxy-lyase 6-methylsalicylate = 3-cresol + CO(2). L-phenylalanine carboxy-lyase Phenylalanine decarboxylase L-phenylalanine decarboxylase Pyridoxal-phosphate L-phenylalanine = phenylethylamine + CO(2). Also acts on tyrosine and other aromatic amino acids. Dihydroxyfumarate carboxy-lyase Dihydroxyfumarate decarboxylase Dihydroxyfumarate = tartronate semialdehyde + CO(2). 4,5-dihydroxyphthalate decarboxylase 4,5-dihydroxyphthalate carboxy-lyase 4,5-dihydroxyphthalate = 3,4-dihydroxybenzoate + CO(2). 3-oxododecanoate carboxy-lyase Beta-ketoacyl decarboxylase Beta-ketolaurate decarboxylase 3-oxolaurate decarboxylase 3-oxododecanoate = 2-undecanone + CO(2). Also decarboxylates other C(14) to C(16) oxo acids. L-methionine decarboxylase L-methionine carboxy-lyase Methionine decarboxylase L-methionine = 3-methylthiopropanamine + CO(2). Orsellinate decarboxylase Orsellinate carboxy-lyase 2,4-dihydroxy-6-methylbenzoate = orcinol + CO(2). Gallate carboxy-lyase Gallate decarboxylase Gallic acid decarboxylase 3,4,5-trihydroxybenzoate = pyrogallol + CO(2). Aconitate decarboxylase Cis-aconitate carboxy-lyase CAD Cis-aconitic decarboxylase Cis-aconitate = itaconate + CO(2). Stipitatonate decarboxylase Stipitatonate = stipitatate + CO(2). 4-hydroxybenzoate decarboxylase p-hydroxybenzoate decarboxylase 4-hydroxybenzoate carboxy-lyase 4-hydroxybenzoate = phenol + CO(2). Gentisate decarboxylase 2,5-dihydroxybenzoate decarboxylase Gentisate carboxy-lyase 2,5-dihydroxybenzoate = hydroquinone + CO(2). Protocatechuate decarboxylase Protocatechuate carboxy-lyase 3,4-dihydroxybenzoate decarboxylase 3,4-dihydroxybenzoate = catechol + CO(2). L-alanine-alpha-ketobutyrate aminotransferase 2,2-dialkylglycine decarboxylase (pyruvate) Pyridoxal-phosphate Acts on 2-amino-2-methylpropanoate (i.e. 2-methylalanine), 2-amino-2-methylbutanoate and 1-aminocyclopentanecarboxylate. 2,2-dialkylglycine + pyruvate = dialkyl ketone + CO(2) + L-alanine. Phosphatidylserine decarboxylase Phosphatidyl-L-serine carboxy-lyase PS decarboxylase Pyridoxal-phosphate or pyruvate Phosphatidyl-L-serine = phosphatidylethanolamine + CO(2). Uracil-5-carboxylic acid decarboxylase Uracil-5-carboxylate carboxy-lyase Uracil-5-carboxylate decarboxylase Uracil 5-carboxylate = uracil + CO(2). UDP-galacturonate decarboxylase UDP-D-galacturonate carboxy-lyase UDP-D-galacturonate = UDP-L-arabinose + CO(2). 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase 5-oxopent-3-ene-1,2,5-tricarboxylate carboxy-lyase 5-oxopent-3-ene-1,2,5-tricarboxylate = 2-oxohept-3-enedioate + CO(2). 3,4-dihydroxyphthalate decarboxylase 3,4-dihydroxyphthalate carboxy-lyase 3,4-dihydroxyphthalate = 3,4-dihydroxybenzoate + CO(2). Benzoylformate carboxy-lyase Benzoylformate decarboxylase Benzoylformate = benzaldehyde + CO(2). Thiamine diphosphate Glutaconyl coenzyme A decarboxylase Glutaconyl-CoA decarboxylase 4-carboxybut-2-enoyl-CoA carboxy-lyase Pent-2-enoyl-CoA carboxy-lyase 4-carboxybut-2-enoyl-CoA = but-2-enoyl-CoA + CO(2). The enzyme from Acidaminococcus fermentans is a biotinyl-protein, requires sodium, and acts as a sodium pump. Biotin Prior to the sodium dependent decarboxylation, the carboxylate is transferred to biotin in a sodium independent manner. Alpha-ketoglutarate decarboxylase 2-oxoglutarate carboxy-lyase 2-oxoglutarate decarboxylase Thiamine diphosphate 2-oxoglutarate = succinate semialdehyde + CO(2). Highly specific. Branched-chain-2-oxoacid decarboxylase (3S)-3-methyl-2-oxopentanoate carboxy-lyase Acts on a number of 2-oxo acids, with a high affinity toward branched-chain substrates. The aldehyde formed may be enzyme-bound, and may be an intermediate in the bacterial system for biosynthesis of branched-chain fatty acids. (3S)-3-methyl-2-oxopentanoate = 2-methylbutanal + CO(2). (R,R)-tartrate carboxy-lyase Tartrate decarboxylase (R,R)-tartrate = D-glycerate + CO(2). Indolepyruvate decarboxylase Indol-3-yl-pyruvate carboxy-lyase 3-(indol-3-yl)pyruvate carboxy-lyase Indole-3-pyruvate decarboxylase Magnesium 3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO(2). Thiamine diphosphate More specific than EC 4.1.1.1. 5-guanidino-2-oxopentanoate decarboxylase 2-oxo-5-guanidinovalerate alpha-ketoarginine decarboxylase 2-oxo-5-guanidinopentanoate decarboxylase 2-oxo-5-guanidinopentanoate carboxy-lyase Thiamine diphosphate 5-guanidino-2-oxo-pentanoate = 4-guanidinobutanal + CO(2). Divalent cation 2-aryl-2-methylmalonate carboxy-lyase Arylmalonate decarboxylase AMDase 2-aryl-2-methylmalonate = 2-arylpropionate + CO(2). 4-oxalocrotonate decarboxylase 4-oxalocrotonate carboxy-lyase 4-oxalocrotonate = 2-oxopent-4-enoate + CO(2). Involved in the meta-cleavage pathway for the degradation of phenols, cresols and catechols. Acetylenedicarboxylate hydratase Acetylenedicarboxylate carboxy-lyase Acetylenedicarboxylate decarboxylase It is thus analogous to EC 4.2.1.71 in its mechanism. The mechanism appears to involve hydration of the acetylene and decarboxylation of the oxaloacetic acid formed, although free oxaloacetate is not an intermediate. Acetylenedicarboxylate + H(2)O = pyruvate + CO(2). Sulfopyruvate decarboxylase Sulfopyruvate carboxy-lyase Thiamine diphosphate Does not decarboxylate pyruvate or phosphonopyruvate. The enzyme appears to be oxygen-sensitive. 3-sulfopyruvate = 2-sulfoacetaldehyde + CO(2). Oxalyl-CoA carboxy-lyase Oxalyl-CoA decarboxylase Thiamine diphosphate Oxalyl-CoA = formyl-CoA + CO(2). 4-hydroxyphenylpyruvate decarboxylase 4-hydroxyphenylpyruvate carboxy-lyase 4-hydroxyphenylpyruvate = 4-hydroxyphenylacetaldehyde + CO(2). Reacts with dopamine to give the benzylisoquinoline alkaloid skeleton. L-threonine O-3-phosphate carboxy-lyase Threonine-phosphate decarboxylase L-threonine-O-3-phosphate decarboxylase L-threonine O-3-phosphate = (R)-1-aminopropan-2-yl phosphate + CO(2). The product of this reaction, (R)-1-aminopropan-2-yl phosphate, is the substrate of EC 6.3.1.10, which converts adenosylcobyric acid into adenosylcobinamide phosphate in the anaerobic cobalamin biosynthesis pathway. Pyridoxal-phosphate Unable to decarboxylate the D-isomer of threonine O-3-phosphate. 3-phosphonopyruvate carboxy-lyase Phosphonopyruvate decarboxylase Thiamine diphosphate Activated by the divalent cations Mg(2+), Ca(2+) and Mn(2+). Pyruvate and sulfopyruvate can also act as substrates, but more slowly. 3-phosphonopyruvate = 2-phosphonoacetaldehyde + CO(2). Magnesium Catalyzes a step in the biosynthetic pathway of 2-aminoethylphosphonate, a component of the capsular polysaccharide complex of Bacteroides fragilis. p-hydroxyphenylacetate decarboxylase 4-hydroxyphenylacetate decarboxylase 4-hydroxyphenylacetate carboxy-lyase p-Hpd 4-Hpd The enzyme, from the strict anaerobe Clostridium difficile, can also use (3,4-dihydroxyphenyl)acetate as a substrate, yielding 4-methylcatechol as a product. (4-hydroxyphenyl)acetate = 4-methylphenol + CO(2). The enzyme is a glycyl radical enzyme. Phenylpyruvate tautomerase II D-tautomerase D-dopachrome decarboxylase D-dopachrome carboxy-lyase D-dopachrome tautomerase L-dopachrome, L-or D-alpha-methyldopachrome and dopaminochrome do not act as substrates (see also EC 5.3.3.12). D-dopachrome = 5,6-dihydroxyindole + CO(2). Specific for D-dopachrome as substrate. 3-dehydro-L-gulonate-6-phosphate carboxy-lyase 3-keto-L-gulonate 6-phosphate decarboxylase 3-dehydro-L-gulonate-6-phosphate decarboxylase KGPDC Along with EC 5.1.3.22, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli. 3-dehydro-L-gulonate 6-phosphate = L-xylulose 5-phosphate + CO(2). Magnesium L-2,4-diaminobutyrate decarboxylase Diaminobutyrate decarboxylase DABA DC L-2,4-diaminobutanoate carboxy-lyase L-2,4-diaminobutanoate = propane-1,3-diamine + CO(2). N(4)-acetyl-L-2,4-diaminobutanoate, 2,3-diaminopropanoate, ornithine and lysine are not substrates. In Acinetobacter baumannii it is cotranscribed with the neighboring dat gene that encodes EC 2.6.1.76, which can supply the substrate for the decarboxylase. Divalent cation Pyridoxal-phosphate Malonyl-CoA carboxy-lyase Malonyl-CoA decarboxylase http://purl.uniprot.org/mim/248360 Specific for malonyl-CoA. Malonyl-CoA = acetyl-CoA + CO(2). The enzyme from Pseudomonas ovalis also catalyzes the reaction of EC 2.8.3.3. Aldehyde-lyases Mandelonitrile benzaldehyde-lyase D-oxynitrilase (R)-oxynitrilase Hydroxynitrile lyase Mandelonitrile lyase A variety of enzymes from different sources and with different properties. Mandelonitrile = cyanide + benzaldehyde. Active toward a number of aromatic and aliphatic hydroxynitriles (cyanohydrins). Some are flavoproteins, others are not. Flavoprotein (S)-4-hydroxymandelonitrile hydroxybenzaldehyde-lyase Hydroxynitrile lyase Hydroxymandelonitrile lyase Does not accept aliphatic hydroxynitriles, unlike EC 4.1.2.10 and EC 4.1.2.37. (S)-4-hydroxymandelonitrile = cyanide + 4-hydroxybenzaldehyde. Ketopantoaldolase 2-dehydropantoate aldolase 2-dehydropantoate formaldehyde-lyase 2-dehydropantoate = 3-methyl-2-oxobutanoate + formaldehyde. Fructose-bisphosphate aldolase Fructose-1,6-bisphosphate triosephosphate-lyase D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase Aldolase Also acts on (3S,4R)-ketose 1-phosphates. Zinc The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. http://purl.uniprot.org/mim/229600 http://purl.uniprot.org/mim/103850 2-dehydro-3-deoxy-D-gluconate-6-phosphate D-glyceraldehyde-3-phosphate-lyase KDPG-aldolase 2-keto-3-deoxy-6-phosphogluconate aldolase Phospho-2-keto-3-deoxygluconate aldolase Phospho-2-dehydro-3-deoxygluconate aldolase 2-dehydro-3-deoxy-phosphogluconate aldolase 2-dehydro-3-deoxy-D-gluconate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate. Also acts on 2-oxobutanoate. L-fuculose-1-phosphate lactaldehyde-lyase Fuculose aldolase L-fuculose-phosphate aldolase L-fuculose 1-phosphate aldolase L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde. 2-keto-3-deoxy-L-arabonate aldolase 2-keto-3-deoxy-L-pentonate aldolase 2-dehydro-3-deoxy-L-pentonate glycolaldehyde-lyase 2-dehydro-3-deoxy-L-pentonate aldolase 2-dehydro-3-deoxy-L-pentonate = pyruvate + glycolaldehyde. L-rhamnulose-1-phosphate lactaldehyde-lyase L-rhamnulose 1-phosphate aldolase L-rhamnulose-phosphate aldolase Rhamnulose-1-phosphate aldolase L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde. Erythrulose-1-phosphate synthetase Erythrulose-1-phosphate formaldehyde-lyase Ketotetrose-phosphate aldolase Phosphoketotetrose aldolase Erythrulose 1-phosphate = glycerone phosphate + formaldehyde. Alpha-keto-beta-deoxy-D-glucarate aldolase 2-keto-3-deoxyglucarate aldolase 2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase 2-dehydro-3-deoxyglucarate aldolase 2-dehydro-3-deoxy-D-glucarate = pyruvate + tartronate semialdehyde. 2-dehydro-3-deoxy-6-phosphogalactonate aldolase 6-phospho-2-dehydro-3-deoxygalactonate aldolase 2-dehydro-3-deoxy-D-galactonate-6-phosphate D-glyceraldehyde-3-phosphate-lyase 6-phospho-2-keto-3-deoxygalactonate aldolase 2-dehydro-3-deoxyphosphogalactonate aldolase 2-oxo-3-deoxygalactonate 6-phosphate aldolase 2-dehydro-3-deoxy-D-galactonate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate. D-fructose-6-phosphate D-erythrose-4-phosphate-lyase (phosphate-acetylating) Fructose-6-phosphate phosphoketolase Thiamine diphosphate D-fructose 6-phosphate + phosphate = acetyl phosphate + D-erythrose 4-phosphate + H(2)O. Also acts on D-xylulose 5-phosphate. 3-deoxy-D-manno-octulosonate D-arabinose-lyase 3-deoxy-D-manno-octulosonate aldolase 3-deoxy-D-manno-octulosonate = pyruvate + D-arabinose. N,N-dimethylaniline-N-oxide formaldehyde-lyase Dimethylaniline-N-oxide aldolase Acts on various N,N-dialkylarylamides. N,N-dimethylaniline N-oxide = N-methylaniline + formaldehyde. Dihydroneopterin aldolase 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine glycolaldehyde-lyase 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde. Phenylserine aldolase L-threo-3-phenylserine benzaldehyde-lyase Pyridoxal-phosphate L-threo-3-phenylserine = glycine + benzaldehyde. Sphingosine-1-phosphate aldolase Sphinganine-1-phosphate aldolase Sphingosine-1-phosphate lyase Sphinganine-1-phosphate palmitaldehyde-lyase Pyridoxal-phosphate Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde. 2-keto-3-deoxy-D-pentonate aldolase 2-dehydro-3-deoxy-D-pentonate aldolase 2-dehydro-3-deoxy-D-pentonate = pyruvate + glycolaldehyde. Phospho-5-dehydro-2-deoxygluconate aldolase Phospho-5-keto-2-deoxygluconate aldolase 5-dehydro-2-deoxyphosphogluconate aldolase 5-dehydro-2-deoxy-D-gluconate-6-phosphate malonate-semialdehyde-lyase 5-dehydro-2-deoxy-D-gluconate 6-phosphate = glycerone phosphate + malonate semialdehyde. 17-alpha-hydroxyprogesterone aldolase 17-alpha-hydroxyprogesterone acetaldehyde-lyase 17-alpha-hydroxyprogesterone = 4-androstene-3,17-dione + acetaldehyde. Trimethylamine-oxide aldolase Trimethylamine-N-oxide formaldehyde-lyase (CH(3))(3)NO = (CH(3))(2)NH + formaldehyde. (24R,24'R)-fucosterol-epoxide acetaldehyde-lyase Fucosterol-epoxide lyase The insect enzyme is involved in the conversion of sitosterol into cholesterol. (24R,24'R)-fucosterol epoxide = desmosterol + acetaldehyde. (3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate 2-carboxybenzaldehyde-lyase (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate 2-carboxybenzaldehyde-lyase 4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase 2'-carboxybenzalpyruvate aldolase Involved, with EC 1.13.11.38, in the metabolism of phenanthrene in bacteria. (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate + H(2)O = 2-formylbenzoate + pyruvate. 4-hydroxy-3-hexanone aldolase 4-hydroxy-3-hexanone propanal-lyase Propioin synthase 4-hydroxy-3-hexanone = 2 propanal. Lactate aldolase Lactate synthase (S)-lactate acetaldehyde-lyase (S)-lactate = formate + acetaldehyde. Oxynitrilase Acetone-cyanohydrin acetone-lyase Hydroxynitrilase Alpha-hydroxynitrile lyase Hydroxynitrile lyase 2-hydroxyisobutyronitrile acetone-lyase Acetone-cyanohydrin lyase Acetone cyanohydrin = cyanide + acetone. Accepts aliphatic and aromatic hydroxynitriles, unlike EC 4.1.2.11 which does not act on aliphatic hydroxynitriles. 2-hydroxyisobutyronitrile (acetone cyanohydrin) is liberated by glycosidase action on linamarin. Benzoin aldolase Benzaldehyde lyase 2-hydroxy-1,2-diphenylethanone benzaldehyde-lyase 2-hydroxy-1,2-diphenylethanone benzaldehyde-lyase 2-hydroxy-1,2-diphenylethanone = 2 benzaldehyde. Thiamine diphosphate Transfered to EC 4.1.2.37 Deoxyribose-phosphate aldolase Phosphodeoxyriboaldolase Deoxyriboaldolase 2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. Tagatose 1,6-diphosphate aldolase Tagatose-bisphosphate aldolase D-tagatose-1,6-bisphosphate aldolase D-tagatose-1,6-bisphosphate triosephosphate lyase Involved in the tagatose 6-phosphate pathway of lactose catabolism in bacteria. D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Enzyme activity is stimulated by certain divalent cations. Vanillin synthase Vanillin is converted to vanillate by EC 1.2.1.67. 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA = vanillin + acetyl-CoA. Involved, together with EC 4.2.1.101 in the production of vanillin from trans-ferulic acid. Threonine aldolase L-threonine acetaldehyde-lyase Pyridoxal-phosphate L-threonine = glycine + acetaldehyde. Tryptophan synthase alpha TSA (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate D-glyceraldehyde-3-phosphate-lyase Indole-3-glycerolphosphate D-glyceraldehyde-3-phosphate-lyase Indole-3-glycerol phosphate lyase Indoleglycerolphosphate aldolase Indole-3-glycerol-phosphate lyase Indole synthase Indole glycerol phosphate hydrolase Resembles the alpha-subunit of EC 4.2.1.20 but, unlike tryptophan synthase, its activity is independent of the beta-subunit and free indole is released. Forms part of the defense mechanism against insects and microbial pathogens in the grass family, Gramineae, where it catalyzes one of the steps in the formation of the cyclic hydroxamic acids 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one (DIBOA) and 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one (DIMBOA). (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate. Phosphoketolase D-xylulose-5-phosphate D-glyceraldehyde-3-phosphate-lyase (phosphate-acetylating) Xylulose-5-phosphate phosphoketolase D-xylulose 5-phosphate + phosphate = acetyl phosphate + D-glyceraldehyde 3-phosphate + H(2)O. Thiamine diphosphate Oxo-acid-lyases Isocitrate glyoxylate-lyase Isocitrate lyase Isocitratase ICL Isocitritase Isocitrase Isocitrate = succinate + glyoxylate. The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate. Oxalomalate lyase 3-oxalomalate glyoxylate-lyase 3-oxalomalate = oxaloacetate + glyoxylate. Erythro-3-hydroxy-L(s)-aspartate glyoxylate-lyase 3-hydroxyaspartate aldolase Erythro-3-hydroxy-L(s)-aspartate = glycine + glyoxylate. KHG-aldolase 4-hydroxy-2-oxoglutarate aldolase 2-oxo-4-hydroxyglutarate aldolase 4-hydroxy-2-oxoglutarate glyoxylate-lyase 2-keto-4-hydroxyglutarate aldolase 4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate. Acts on both stereoisomers. 4-hydroxy-4-methyl-2-oxoglutarate aldolase 4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase Also acts on 4-hydroxy-4-methyl-2-oxoadipate and 4-carboxy-4-hydroxy-2-oxohexadioate. 4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate. (3S)-citramalate pyruvate-lyase Citramalate lyase (3S)-citramalate = acetate + pyruvate. Can be dissociated into components, two of which are identical with EC 2.8.3.11 and EC 4.1.3.25. (3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase Malyl-CoA lyase Malyl-coenzyme A lyase (3S)-3-carboxy-3-hydroxypropanoyl-CoA = acetyl-CoA + glyoxylate. Citramalyl-CoA lyase (3S)-citramalyl-CoA pyruvate-lyase Also acts on (3S)-citramalyl thioacyl-carrier protein. (3S)-citramalyl-CoA = acetyl-CoA + pyruvate. Component of EC 4.1.3.22. 3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA acetate-lyase 3-hydroxy-3-isohexenylglutaryl-CoA lyase Also acts on the hydroxy derivative of farnesoyl-CoA. 3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA = 7-methyl-3-oxooct-6-enoyl-CoA + acetate. Anthranilate synthase The enzyme separated from the complex uses NH(3) only. The native enzyme in the complex with uses either glutamine or (less efficiently) NH(3). Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate. In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.1.48, EC 4.2.1.20, and EC 5.3.1.24). N-acetylneuraminate pyruvate-lyase N-acetylneuraminic acid aldolase N-acetylneuraminate lyase N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate. Also acts on N-glycoloylneuraminate, and on O-acetylated sialic acids, other than 4-O-acetylated derivatives. (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase Methylisocitrate lyase (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate. Acts on threo-D(s)-2-methylisocitrate, but not on threo-D(s)-isocitrate, threo-DL-isocitrate or erythro-L(s)-isocitrate. 2,3-dimethylmalate lyase (2R,3S)-2,3-dimethylmalate pyruvate-lyase Other enzymes involved in this pathway are EC 1.17.5.1, EC 1.3.7.1, EC 3.5.2.18, EC 1.1.1.291, EC 5.4.99.4, EC 5.3.3.6 and EC 4.2.1.85. (2R,3S)-2,3-dimethylmalate = propanoate + pyruvate. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Citryl-CoA lyase (3S)-citryl-CoA oxaloacetate-lyase (3S)-citryl-CoA = acetyl-CoA + oxaloacetate. Component of EC 4.1.3.6 and EC 4.1.3.8. Also acts on (3S)-citryl thioacyl-carrier protein. (1-hydroxycyclohexan-1-yl)acetyl-CoA cyclohexanone-lyase (1-hydroxycyclohexan-1-yl)acetyl-CoA lyase (1-hydroxycyclohexan-1-yl)acetyl-CoA = acetyl-CoA + cyclohexanone. Naphthoate synthase Dihydroxynaphthoic acid synthetase DHNA synthetase o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing) o-succinylbenzoyl-CoA = 1,4-dihydroxy-2-naphthoate + CoA. Highly specific. 4-amino-4-deoxychorismate pyruvate-lyase 4-amino-4-deoxychorismate lyase Enzyme X ADC lyase Aminodeoxychorismate lyase 4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate. Pyridoxal-phosphate Forms part of the folate biosynthesis pathway. Acts on 4-amino-4-deoxychorismate, the product of EC 6.3.5.8, to form p-aminobenzoate. 4-hydroxy-2-oxovalerate pyruvate-lyase HOA 4-hydroxy-2-ketovalerate aldolase 4-hydroxy-2-oxovalerate aldolase 4-hydroxy-2-oxopentanoate pyruvate-lyase 4-hydroxy-2-oxopentanoate = pyruvate + acetaldehyde. In Pseudomonas species, this enzyme forms part of a bifunctional enzyme with EC 1.2.1.10. Manganese Catalyzes the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. Hydroxymethylglutaryl-CoA lyase (S)-3-hydroxy-3-methylglutaryl-CoA acetoacetate-lyase HMG-CoA lyase 3-hydroxy-3-methylglutarate-CoA lyase http://purl.uniprot.org/mim/246450 (S)-3-hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate. CL CPL Chorismate lyase Chorismate = 4-hydroxybenzoate + pyruvate. Catalyzes the first step in the biosynthesis of ubiquinone in Escherichia coli and other Gram-negative bacteria. The yeast Saccharomyces cerevisiae can synthesize ubiquinone from either chorismate or tyrosine. Citritase Citrate (pro-3S)-lyase Citratase Citrase Citrate aldolase Citrate lyase Citridesmolase Can be dissociated into components, two of which are identical with EC 2.8.3.10 and EC 4.1.3.34. Citrate = acetate + oxaloacetate. EC 3.1.2.16 deacetylates and inactivates the enzyme. Other carbon-carbon lyases L-tryptophan indole-lyase Tryptophanase TNase L-tryptophan + H(2)O = indole + pyruvate + NH(3). Potassium Pyridoxal-phosphate Also catalyzes 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogs of L-cysteine, L-serine and other 3-substituted amino acids. Benzylsuccinate synthase Toluene + fumarate = benzylsuccinate. A glycyl radical enzyme that is inhibited by benzyl alcohol, benzaldehyde, phenylhydrazine and is inactivated by oxygen. Tyrosine phenol-lyase Beta-tyrosinase L-tyrosine + H(2)O = phenol + pyruvate + NH(3). Pyridoxal-phosphate Also slowly catalyzes pyruvate formation from D-tyrosine, S-methyl-L-cysteine, L-cysteine, L-serine and D-serine. Photoreactivating enzyme DNA photolyase Deoxyribodipyrimidine photo-lyase Cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA). Catalyzes the reactivation by light of irradiated DNA. A similar reactivation of irradiated RNA is probably due to a separate enzyme. FAD A flavoprotein containing a second chromophore group. 5,10-methenyltetrahydrofolate Octadecanal decarbonylase Inhibited by metal-chelating agents. Octadecanal = heptadecane + CO. Involved in the biosynthesis of alkanes in pea from fatty acids of chain length C(18) to C(32). Carbon-oxygen lyases Hydro-lyases Carbonic anhydrase Carbonate dehydratase Carbonate hydro-lyase Carbonic dehydratase H(2)CO(3) = CO(2) + H(2)O. Zinc http://purl.uniprot.org/mim/259730 http://purl.uniprot.org/mim/600852 3-dehydroquinate dehydratase 3-dehydroquinate = 3-dehydroshikimate + H(2)O. Cyclohexa-1,5-dienecarbonyl-CoA hydratase Dienoyl-CoA hydratase Cyclohexa-1,5-diene-1-carboxyl-CoA hydratase Cyclohexa-1,5-diene-1-carbonyl-CoA hydratase Cyclohexa-1,5-dienecarbonyl-CoA + H(2)O = 6-hydroxycyclohex-1-enecarbonyl-CoA. Forms part of the anaerobic benzoate degradation pathway, which also includes EC 1.3.99.7, EC 1.3.99.15 and EC 4.2.1.55. Trans-feruloyl-CoA hydratase Trans-feruloyl-CoA + H(2)O = 4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA. Cyclohexyl-isocyanide hydratase Isonitrile hydratase N-cyclohexylformamide = cyclohexyl isocyanide + H(2)O. The enzyme from Pseudomonas putida strain N19-2 can also catalyze the hydration of other isonitriles to the corresponding N-substituted formamides. The enzyme has no metal requirements. Cyanate hydratase Cyanate lyase Cyanate C-N-lyase Cyanase Cyanate aminohydrolase Cyanate hydrolase Bicarbonate functions as a recycling substrate. Cyanate + HCO(3)(-) + 2 H(+) = NH(3) + 2 CO(2). This enzyme, which is found in bacteria and plants, is used to decompose cyanate, which can be used as the sole source of nitrogen. The reaction can be considered as the reverse of 'carbamate = cyanate + H(2)O', where this is assisted by reaction with bicarbonate and carbon dioxide, and hence is classified in sub-subclass 4.2.1. 2-hydroxyisoflavanone dehydratase The reaction also occurs spontaneously. Catalyzes the final step in the formation of the isoflavonoid skeleton. 2,7,4'-trihydroxyisoflavanone = daidzein + H(2)O. Bile-acid 7-alpha-dehydratase BA7 alpha dehydratase 7-alpha,12-alpha-dihydroxy-3-oxochol-4-enoate = 12-alpha-hydroxy-3-oxochola-4,6-dienoate + H(2)O. The enzyme from Eubacterium sp. strain VPI 12708 can also use 7-alpha-hydroxy-3-oxochol-4-enoate as a substrate but not 7-alpha,12-alpha-dihydroxy-3-oxochol-5-beta-anoate, 3-alpha,7-alpha,12-alpha-trihydroxychol-5-beta-anoate or 7-beta-hydroxy-3-oxochol-4-enoate. 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase D-3-hydroxyacyl-CoA dehydratase http://purl.uniprot.org/mim/261515 Involved in the beta-oxidation of the cholesterol side chain in the cholic-acid biosynthesis pathway. (24R,25R)-3-alpha,7-alpha,12-alpha,24-tetrahydroxy-5-beta-cholestanoyl-CoA = (24E)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA + H(2)O. Forms part of the rat peroxisomal multifunctional enzyme perMFE-2, which also exhibits a dehydrogenase activity. N-acetyldiaminobutyrate dehydratase N-acetyldiaminobutanoate dehydratase L-ectoine synthase Ectoine synthase This is the third enzyme in the ectoine biosynthesis pathway, the other enzymes involved being EC 2.6.1.76 and EC 2.3.1.178. Ectoine is an osmoprotectant that is found in halophilic eubacteria. N(4)-acetyl-L-2,4-diaminobutanoate = L-ectoine + H(2)O. Methylthioribulose 1-phosphate dehydratase 1-PMT-ribulose dehydratase S-methyl-5-thio-D-ribulose 1-phosphate = 5-(methylthio)-2,3-dioxopentyl phosphate + H(2)O. This enzyme forms part of the methionine salvage pathway. 2-phosphoglycerate dehydratase Phosphopyruvate hydratase Enolase http://purl.uniprot.org/mim/131370 Also acts on 3-phospho-D-erythronate. 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. Magnesium AUDH Aldos-2-ulose dehydratase Pyranosone dehydratase 1,5-anhydro-D-fructose dehydratase (microthecin-forming) Catalyzes two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. The other enzymes involved in this pathway are EC 4.2.1.111, EC 4.2.2.13 and EC 5.3.3.15. Aldose-2-uloses such as 2-dehydroglucose can also act as substrates, but more slowly. Differs from EC 4.2.1.111, which can carry out only reaction 1 and requires a cofactor for activity. (2) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. A bifunctional enzyme that acts as both a lyase and as an isomerase. (1) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H(2)O. AFDH 1,5-anhydro-D-fructose 4-dehydratase 1,5-anhydro-D-arabino-hex-2-ulose dehydratase AF dehydratase 1,5-anhydro-D-fructose dehydratase 1,5-anhydro-D-fructose hydrolyase The other enzymes involved in this pathway are EC 4.2.1.110, EC 4.2.2.13 and EC 5.3.3.15. Calcium or magnesium or sodium 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H(2)O. Unlike EC 4.2.1.110 the enzyme is specific for 1,5-anhydro-D-fructose as substrate and shows no activity toward aldose-2-uloses such as 2-dehydroglucose; in addition, it is inhibited by its end-product ascopyrone M and it cannot convert the end-product ascopyrone M into microthecin, as can EC 4.2.1.110. Catalyzes one of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. AHy Acetylene hydratase Acetaldehyde = acetylene + H(2)O. Ethylene cannot act as a substrate. The tungsten center binds a water molecule that is activated by an adjacent aspartate residue, enabling it to attack acetylene bound in a distinct hydrophobic pocket. Bis(molybdopterin guanine dinucleotide)molybdenum cofactor Tungsten Iron-sulfur Phosphogluconate dehydratase 6-phospho-D-gluconate = 2-dehydro-3-deoxy-6-phospho-D-gluconate + H(2)O. Enoyl-CoA hydratase Unsaturated acyl-CoA hydratase Enoyl hydrase With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74). Acts in the reverse direction. (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O. http://purl.uniprot.org/mim/609016 http://purl.uniprot.org/mim/609015 Methylglutaconyl-CoA hydratase (S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H(2)O. http://purl.uniprot.org/mim/250950 Imidazoleglycerol-phosphate dehydratase D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H(2)O. Fumarate hydratase Fumarase http://purl.uniprot.org/mim/150800 http://purl.uniprot.org/mim/606812 (S)-malate = fumarate + H(2)O. http://purl.uniprot.org/mim/605839 L-tryptophan synthetase Tryptophan synthase Tryptophan desmolase Tryptophan synthetase Indoleglycerol phosphate aldolase L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H(2)O. The indole then migrates to the beta-subunit where, with serine in the presence of pyridoxal 5'-phosphate, it is converted to tryptophan. Pyridoxal-phosphate The alpha-subunit catalyzes the conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and glyceraldehyde 3-phosphate. Also catalyzes the conversion of serine and indole into tryptophan and water, and of 1-C-(indol-3-yl)glycerol 3-phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.1.2.8). In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27 and EC 5.3.1.24). Beta-thionase Cystathionine beta-synthase Serine sulfhydrase Methylcysteine synthase A multifunctional enzyme: catalyzes beta-replacement reaction between L-serine, L-cysteine, cysteine thioethers or some other beta-substituted alpha-L-amino acids and a variety of mercaptans. Pyridoxal-phosphate http://purl.uniprot.org/mim/236200 L-serine + L-homocysteine = L-cystathionine + H(2)O. Aminolevulinate dehydratase Delta-aminolevulinic acid dehydratase Porphobilinogen synthase Zinc 2 5-aminolevulinate = porphobilinogen + 2 H(2)O. http://purl.uniprot.org/mim/125270 L-arabinonate dehydratase L-arabinonate hydro-lyase L-arabinonate = 2-dehydro-3-deoxy-L-arabinonate + H(2)O. Acetylenecarboxylate hydratase Alkynoate hydratase Malonate-semialdehyde dehydratase Acetylenemonocarboxylate hydratase The reaction is effectively irreversible, favoring oxopropanoate (malonic semialdehyde) and its tautomers. 3-oxopropanoate = propynoate + H(2)O. The mechanism appears to involve hydration of the acetylene to 3-hydroxypropenoate, which will spontaneously tautomerize to 3-oxopropanoate. Also acts on but-3-ynoate forming acetoacetate. It is thus analogous to EC 4.1.1.78 in its mechanism. Propanediol dehydratase Cobalamin Propane-1,2-diol = propanal + H(2)O. Also dehydrates ethylene glycol to acetaldehyde. Citrate(isocitrate) hydro-lyase Cis-aconitase Aconitate hydratase Aconitase Citrate hydro-lyase Cis-aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. Citrate = isocitrate. The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. Iron-sulfur Glycerol dehydratase Glycerol = 3-hydroxypropanal + H(2)O. Cobalamin Maleate hydratase (R)-malate = maleate + H(2)O. L(+)-tartrate dehydratase Exists in an inactive low-molecular form, which is converted into active enzyme in the presence of Fe(2+) and thiol (cf. EC 4.2.1.81). Iron (R,R)-tartrate = oxaloacetate + H(2)O. Isopropylmalate isomerase 3-isopropylmalate dehydratase (2R,3S)-3-isopropylmalate hydro-lyase Alpha-IPM isomerase (2) (2S)-2-isopropylmaleate + H(2)O = (2S)-2-isopropylmalate. Catalyzes the isomerization between (2R,3S)-3-isopropylmalate and (2S)-2-isopropylmalate, via the formation of (2S)-2-isopropylmaleate. (1) (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmaleate + H(2)O. Mesaconate hydratase (S)-2-methylmalate dehydratase (S)-2-methylmalate = 2-methylfumarate + H(2)O. Also hydrates fumarate to (S)-malate. (R)-2-methylmalate dehydratase Citraconate hydratase Iron (R)-2-methylmalate = 2-methylmaleate + H(2)O. Cis-homoaconitase 2-hydroxybutane-1,2,4-tricarboxylate hydro-lyase HACN Homoaconitase Homoaconitate hydratase (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate = (Z)-but-1-ene-1,2,4-tricarboxylate + H(2)O. The enzyme responsible for the conversion of cis-homoaconitate into homocitrate in T.thermophilus is unknown at present but the reaction can be catalyzed in vitro using EC 4.2.1.3 from pig. The enzyme from the hyperthermophilic eubacterium Thermus thermophilus can catalyze the reaction shown above but cannot catalyze the previously described reaction, i.e. formation of homocitrate by hydration of cis-homoaconitate. Iron-sulfur Gluconate dehydratase D-gluconate = 2-dehydro-3-deoxy-D-gluconate + H(2)O. Citrate dehydratase Citrate hydro-lyase Cis-aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. Does not act on isocitrate. Citrate = cis-aconitate + H(2)O. Glucarate dehydratase D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H(2)O. D-4-deoxy-5-ketoglucarate hydro-lyase 5-dehydro-4-deoxyglucarate dehydratase 5-keto-4-deoxy-glucarate dehydratase 5-dehydro-4-deoxy-D-glucarate = 2,5-dioxopentanoate + H(2)O + CO(2). Galactarate dehydratase D-galactarate = 5-dehydro-4-deoxy-D-glucarate + H(2)O. 2-dehydro-3-deoxy-L-arabinonate dehydratase 2-keto-3-deoxy-L-arabinonate dehydratase 2-dehydro-3-deoxy-L-arabinonate = 2,5-dioxopentanoate + H(2)O. Myo-inosose-2 dehydratase 2,4,6/3,5-pentahydroxycyclohexanone = 3,5/4-trihydroxycyclohexa-1,2-dione + H(2)O. Cobalt or manganese CDP-glucose 4,6-dehydratase NAD CDP-glucose = CDP-4-dehydro-6-deoxy-D-glucose + H(2)O. dTDP-glucose 4,6-dehydratase NAD dTDP-glucose = dTDP-4-dehydro-6-deoxy-D-glucose + H(2)O. GDP-mannose 4,6-dehydratase Guanosine diphosphomannose 4,6-dehydratase GDP-D-mannose dehydratase Guanosine diphosphomannose oxidoreductase Guanosine 5'-diphosphate-D-mannose oxidoreductase GDP-D-mannose 4,6-dehydratase NAD GDP-mannose = GDP-4-dehydro-6-deoxy-D-mannose + H(2)O. In Aneurinibacillus thermoaerophilus L420-91T, this enzyme acts as a bifunctional enzyme, catalyzing the above reaction as well as the reaction catalyzed by EC 1.1.1.281. Forms the first step in the biosynthesis of GDP-D-rhamnose and GDP-L-fucose. D-glutamate cyclase D-glutamate = 5-oxo-D-proline + H(2)O. Also acts on various derivatives of D-glutamate. Urocanase Imidazolonepropionate hydrolase Urocanate hydratase NAD 3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H(2)O. http://purl.uniprot.org/mim/276880 Arabinonate dehydratase D-arabinonate hydro-lyase D-arabinonate = 2-dehydro-3-deoxy-D-arabinonate + H(2)O. Pyrazolylalanine synthase Pyridoxal-phosphate L-serine + pyrazole = 3-(pyrazol-1-yl)-L-alanine + H(2)O. Prephenate dehydratase This enzyme in the enteric bacteria also possesses EC 5.4.99.5 activity and converts chorismate into prephenate. Prephenate = phenylpyruvate + H(2)O + CO(2). Dihydrodipicolinate synthase DHDPS Dihydrodipicolinate synthetase L-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + 2 H(2)O. Oleate hydratase Acts on a number of 10-hydroxy acids. (R)-10-hydroxystearate = oleate + H(2)O. Lactoyl-CoA dehydratase Lactoyl-CoA = acryloyl-CoA + H(2)O. 3-hydroxybutyryl-CoA dehydratase Crotonase (3R)-3-hydroxybutanoyl-CoA = crotonoyl-CoA + H(2)O. Also acts on crotonoyl thioesters of pantetheine and acyl-carrier protein. Itaconyl-CoA hydratase Citramalyl-CoA = itaconyl-CoA + H(2)O. Isohexenylglutaconyl-CoA hydratase Also acts on dimethylacryloyl-CoA and farnesoyl-CoA. 3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA = 3-(4-methylpent-3-en-1-yl)-pent-2-enedioyl-CoA + H(2)O. Crotonyl acyl carrier protein hydratase Enoyl acyl carrier protein hydrase Crotonoyl-[acyl-carrier-protein] hydratase 3-hydroxybutyryl acyl carrier protein dehydratase Beta-hydroxybutyryl acyl carrier protein (ACP) dehydrase Beta-hydroxybutyryl acyl carrier protein dehydrase (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydro-lyase (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] = but-2-enoyl-[acyl-carrier-protein] + H(2)O. Specific for short-chain length 3-hydroxyacyl-[acyl-carrier-protein] derivatives C(4) to C(8). 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase Beta-hydroxyoctanoyl thioester dehydratase D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase Beta-hydroxyoctanoyl-acyl carrier protein dehydrase D-3-hydroxyoctanoyl-acyl carrier protein dehydratase (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase Beta-hydroxyoctanoyl-ACP-dehydrase Specific for 3-hydroxyacyl-[acyl-carrier-protein] derivatives C(6) to C(12). (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] = oct-2-enoyl-[acyl-carrier-protein] + H(2)O. Galactonate dehydratase D-galactonate = 2-dehydro-3-deoxy-D-galactonate + H(2)O. D-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase Beta-hydroxydecanoyl thioester dehydrase Beta-hydroxyacyl-acyl carrier protein dehydratase Beta-hydroxydecanoyl thiol ester dehydrase Beta-hydroxyacyl-ACP dehydrase 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase 3-hydroxydecanoyl-acyl carrier protein dehydrase 3-hydroxydecanoyl-acyl carrier protein dehydratase HDDase Beta-hydroxydecanoate dehydrase Specific for C(10) chain length. (2) (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] = cis-dec-3-enoyl-[acyl-carrier-protein] + H(2)O. (1) (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] = trans-dec-2-enoyl-[acyl-carrier-protein] + H(2)O. Beta-hydroxypalmityl-ACP dehydrase (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] hydro-lyase Beta-hydroxypalmitoyl thioester dehydratase 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase D-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase Beta-hydroxypalmitoyl-acyl carrier protein dehydrase (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] = hexadec-2-enoyl-[acyl-carrier-protein] + H(2)O. Specific for 3-hydroxyacyl-[acyl-carrier-protein] derivatives C(12) to C(16) and has the highest activity on the C(16) derivative. 5-alpha-hydroxysteroid dehydratase 5-alpha-ergosta-7,22-diene-3-beta,5-diol = ergosterol + H(2)O. 3-cyanoalanine hydratase L-asparagine = 3-cyanoalanine + H(2)O. Formamide hydro-lyase Cyanide hydratase Formamide = cyanide + H(2)O. D-fuconate dehydratase Also acts on L-arabinonate. D-fuconate = 2-dehydro-3-deoxy-D-fuconate + H(2)O. L-fuconate dehydratase L-fuconate = 2-dehydro-3-deoxy-L-fuconate + H(2)O. Also acts, slowly, on D-arabinonate. Cyanamide hydratase Urea = cyanamide + H(2)O. Altronate dehydratase D-altronate = 2-dehydro-3-deoxy-D-gluconate + H(2)O. Uracil hydrolyase Pseudouridine synthase Pseudouridylate synthase Uracil + D-ribose 5-phosphate = pseudouridine 5'-phosphate + H(2)O. Families of enzymes that forms pseudouridine in all kinds of RNA from eubacteria, archaea and eukaryotes. Protoaphin-aglucone dehydratase (cyclizing) Protoaphin aglucone = xanthoaphin + H(2)O. The product is converted non-enzymically to erythroaphin, an aphid pigment. Long-chain-enoyl-CoA hydratase Unlike EC 4.2.1.17 does not act on crotonoyl-CoA. The best substrate is oct-3-enoyl-CoA. (3S)-3-hydroxyacyl-CoA = trans-2-enoyl-CoA + H(2)O. Acts in the reverse direction. Uroporphyrinogen-III cosynthetase Uroporphyrinogen-III cosynthase Hydroxymethylbilane hydro-lyase (cyclizing) Uroporphyrinogen-III synthase In the presence of EC 2.5.1.61, forms uroporphyrinogen III from porphobilinogen. Hydroxymethylbilane = uroporphyrinogen III + H(2)O. http://purl.uniprot.org/mim/263700 UDP-glucose 4,6-dehydratase UDP-glucose = UDP-4-dehydro-6-deoxy-D-glucose + H(2)O. Trans-L-3-hydroxyproline dehydratase Highly specific. Trans-L-3-hydroxyproline = Delta(1)-pyrroline 2-carboxylate + H(2)O. 2,3-dehydroproline is an intermediate. (S)-norcoclaurine synthase (S)-norlaudanosoline synthase 4-(2-aminoethyl)benzene-1,2-diol + 4-hydroxyphenylacetaldehyde = (S)-norcoclaurine + H(2)O. Will also catalyze the reaction of 4-(2-aminoethyl)benzene-1,2-diol + (3,4-dihydroxyphenyl)acetaldehyde to form (S)-norlaudanosoline, but this alkaloid has not been found to occur in plants. The reaction makes a 6-membered ring by forming a bond between C-6 of the 3,4-dihydroxyphenyl group of the dopamine and C-1 of the aldehyde in the imine formed between the substrates. The product is the precursor of the benzylisoquinoline alkaloids in plants. 2-methylcitrate dehydratase 2-methylcitrate hydro-lyase 2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase Both this enzyme and EC 4.2.1.3 are required to complete the isomerization of (2S,3S)-methylcitrate to (2R,3S)-2-methylisocitrate. (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H(2)O. Not identical with EC 4.2.1.4. Can also use cis-aconitate as a substrate but more slowly. Specific for (2S,3S)-methylcitrate, showing no activity with (2R,3S)-methylcitrate. Mannonic hydrolase Altronate hydrolase D-mannonate hydro-lyase Mannonate dehydratase D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H(2)O. 2-oxopent-4-enoate hydratase OEH 2-keto-4-pentenoate hydratase Also acts, more slowly, on cis-2-oxohex-4-enoate, but not on the trans-isomer. 4-hydroxy-2-oxopentanoate = 2-oxopent-4-enoate + H(2)O. D(-)-tartrate dehydratase Iron (S,S)-tartrate = oxaloacetate + H(2)O. Xylonate dehydratase D-xylo-aldonate dehydratase D-xylonate = 2-dehydro-3-deoxy-D-xylonate + H(2)O. 4-carboxy-2-oxohexenedioate hydratase 4-oxalmesaconate hydratase 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = (E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(2)O. Nitrile hydratase Nitrilase Nitrile hydro-lyase An aliphatic amide = a nitrile + H(2)O. Does not act on these amides or on aromatic nitriles (cf. EC 3.5.5.1). Acts on short-chain aliphatic nitriles, converting them into the corresponding acid amides. Dimethylmaleate hydratase Inhibited by oxygen. Iron Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.17.5.1, EC 1.3.7.1, EC 3.5.2.18, EC 1.1.1.291, EC 5.4.99.4, EC 5.3.3.6 and EC 4.1.3.32. (2R,3S)-2,3-dimethylmalate = dimethylmaleate + H(2)O. Octopamine dehydratase 1-(4-hydroxyphenyl)-2-aminoethanol = (4-hydroxyphenyl)acetaldehyde + NH(3). The enzyme-catalyzed reaction is believed to be dehydration to an enamine, which is spontaneously hydrolyzed to an aldehyde and ammonia. Synephrine dehydratase 1-(4-hydroxyphenyl)-2-(methylamino)ethanol = (4-hydroxyphenyl)acetaldehyde + methylamine. The enzyme from Arthrobacter synephrinum is highly specific. Removal of H(2)O from (+-)-synephrine produces a 2,3-enamine, which hydrolyzes to the products shown in the reaction above. L-carnitine dehydratase Carnitine dehydratase L-carnitine = 4-(trimethylammonio)but-2-enoate + H(2)O. Dihydroxy-acid dehydratase 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H(2)O. L-rhamnonate dehydratase L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H(2)O. Carboxycyclohexadienyl dehydratase Arogenate dehydratase Also acts on prephenate and D-prephenyllactate. L-arogenate = L-phenylalanine + H(2)O + CO(2). Cf. EC 4.2.1.51. Allene oxide synthase Hydroperoxide isomerase Hydroperoxide dehydratase Acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides. Heme-thiolate (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate = (9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate + H(2)O. ATP-dependent NAD(P)H-hydrate dehydratase ATP-dependent H(4)NAD(P)OH dehydratase Hence EC 4.2.1.93 can convert the whole mixture into NADH. ATP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = ADP + phosphate + NADH. Also acts on hydrated NADPH. NADH spontaneously hydrates to both (6S)-and (6R)-compounds, and these spontaneously interconvert. Scytalone dehydratase Involved with EC 1.1.1.252 in the biosynthesis of melanin in pathogenic fungi. Scytalone = 1,3,8-trihydroxynaphthalene + H(2)O. Kievitone hydratase The enzyme from Fusarium sp. hydrates the methylbutenyl side chain of the isoflavonoid phytoalexins, thus reducing their toxicity. Kievitone hydrate = kievitone + H(2)O. 4-alpha-hydroxy-tetrahydropterin dehydratase Tetrahydrobiopterin dehydratase Pterin-4-alpha-carbinolamine dehydratase 4a-hydroxytetrahydrobiopterin dehydratase http://purl.uniprot.org/mim/264070 Catalyzes the dehydration of 4a-hydroxytetrahydrobiopterins. (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H(2)O. Phaseollidin hydratase Phaseollidin hydrate = phaseollidin + H(2)O. The enzyme from Fusarium solani, which is distinct from EC 4.2.1.95, hydrates the methylbutenyl side-chain of the isoflavonoid phytoalexin, phaseollidin. 16-alpha-dehydroxylase 16-dehydroprogesterone hydratase 16-alpha-hydroxyprogesterone dehydratase Hydroxyprogesterone dehydroxylase 16-alpha-hydroxyprogesterone dehydroxylase 16-alpha-hydroxypregnenolone is also a substrate. 16-alpha-hydroxyprogesterone = 16,17-didehydroprogesterone + H(2)O. 2-methylisocitrate dehydratase (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase The enzyme from the fungus Yarrowia lipolytica does not act on isocitrate. (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H(2)O. Acting on polysaccharides Spreading factor Hyaluronidase Hyaluronate lyase Mucinase Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine. The product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose. Also acts on chondroitin. Pectolyase Endo-pectin lyase Pectin methyltranseliminase Polymethylgalacturonic transeliminase PMGL PL Pectin trans-eliminase Pectin lyase PNL Favors pectin, the methyl ester, over pectate, the anion (which is the preferred substrate of EC 4.2.2.2). Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosyl groups at their non-reducing ends. Poly(alpha-L-guluronate) lyase Alginase II Eliminative cleavage of polysaccharides containing a terminal alpha-L-guluronate group, to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends. Xanthan lyase Eliminative cleavage of the terminal beta-D-mannosyl-beta-D-1,4-glucuronosyl linkage of the side-chain of the polysaccharide xanthan, leaving a 4-deoxy-alpha-L-threo-hex-4-enuronosyl group at the terminus of the side-chain. Alpha-1,4-glucan lyase Exo-(1->4)-alpha-D-glucan lyase Alpha-1,4-glucan exo-lyase Alpha-1,4-glucan 1,5-anhydro-D-fructose eliminase Exo-(1,4)-alpha-D-glucan lyase Exo-alpha-1,4-glucan lyase The enzyme catalyzes the sequential degradation of (1->4)-alpha-D-glucans from the non-reducing end with the release of 1,5-anhydro-D-fructose. Does not degrade (1->6)-alpha-gucosidic bonds and thus the degradation of a branched glucan, such as amylopectin or glycogen, will result in the formation of 1,5-anhydro-D-fructose plus a limit dextrin. Thus, for an alpha-glucan containing n (1->4)-linked glucose units, the final products are 1 glucose plus (n-1) 1,5-anhydro-D-fructose. Linear alpha-glucan = (n-1) 1,5-anhydro-D-fructose + D-glucose. Maltose, maltosaccharides and amylose are all completely degraded. Other enzymes involved in the anhydrofructose pathway are EC 4.2.1.110, EC 4.2.1.111 and EC 5.3.3.15. Glucuronan lyase Eliminative cleavage of (1->4)-beta-D-glucuronans to give oligosaccharides with 4-deoxy-beta-D-gluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides. Anhydroneuraminidase Anhydrosialidase Sialglycoconjugate N-acylneuraminylhydrolase (2,7-cyclizing) Sialidase L Cf. EC 3.2.1.18 and EC 3.2.1.129. Also acts on N-glycolylneuraminate glycosides. Elimination of alpha-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-alpha-N-acetylneuraminate. 2,6-beta-D-fructan D-fructosyl-D-fructosyltransferase (forming di-beta-D-fructofuranose 2,6':2',6-dianhydride) Levan fructotransferase Levan fructotransferase (DFA-IV-forming) These enzymes have long been known as fructotransferases, so this is retained in the description (official rdfs:label). Since the transfer is intramolecular, the reaction is an elimination and, hence, the enzyme is a lyase, belonging in enzyme class 4.-.-.-. Produces di-beta-D-fructofuranose 2,6':2',6-dianhydride (DFA IV) by successively eliminating the diminishing (2->6)-beta-D-fructan (levan) chain from the terminal D-fructosyl-D-fructosyl disaccharide. This enzyme, like EC 4.2.2.17 and EC 4.2.2.18 eliminates the fructan chain from the terminal disaccharide leaving a difructose dianhydride. Inulin fructotransferase (DFA-I-forming) Inulin D-fructosyl-D-fructosyltransferase (forming alpha-D-fructofuranose beta-D-fructofuranose 1,2':1',2-dianhydride) Inulin D-fructosyl-D-fructosyltransferase (1,2':1',2-dianhydride-forming) Inulin fructotransferase (depolymerizing, difructofuranose-1,2':2',1-dianhydride-forming) Inulin fructotransferase (DFA-I-producing) This enzyme, like EC 4.2.2.16 and EC 4.2.2.18 eliminates the fructan chain from the terminal disaccharide leaving a difructose dianhydride. These enzymes have long been known as fructotransferases, so this is retained in the description (official rdfs:label). Produces alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,1'-dianhydride (DFA I) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide. Since the transfer is intramolecular, the reaction is an elimination and, hence, the enzyme is a lyase, belonging in enzyme class 4.-.-.-. Inulin D-fructosyl-D-fructosyltransferase (1,2':2,3'-dianhydride-forming) Inulinase II Inulin fructotransferase (DFA-III-producing) Inulin fructotransferase (depolymerizing) Inulase II Inulin fructotransferase (DFA-III-forming) Inulin D-fructosyl-D-fructosyltransferase (forming alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride) Inulin fructotransferase (depolymerizing, difructofuranose-1,2':2,3'-dianhydride-forming) Produces alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide. This enzyme, like EC 4.2.2.16 and EC 4.2.2.17 eliminates the fructan chain from the terminal disaccharide leaving a difructose dianhydride. Since the transfer is intramolecular, the reaction is an elimination and, hence, the enzyme is a lyase, belonging in enzyme class 4.-.-.-. These enzymes have long been known as fructotransferases, so this is retained in the description (official rdfs:label). Chondroitinase B ChonB Chondroitin B lyase Eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (Delta-UA-GalNAc-4S). In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha-1-3)GalNAc(beta-1-](n) of DS. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source. The minimum substrate length required for catalysis is a tetrasaccharide. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta-1-3)GalNAc(beta-1-](n), which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. This is the only lyase that is known to be specific for dermatan sulfate as substrate. Alpha-1,4-D-endopolygalacturonic acid lyase Pectic lyase PPase-N Endo-alpha-1,4-polygalacturonic acid lyase Polygalacturonic acid lyase Polygalacturonic transeliminase Endopectin methyltranseliminase PGA lyase Pectic acid transeliminase Pectic acid lyase Polygalacturonic acid trans-eliminase Pectate lyase Pectate transeliminase Polygalacturonate lyase Endogalacturonate transeliminase Pectin trans-eliminase Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends. Favors pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10). Chondroitinase ABC Chondroitin sulfate ABC endoeliminase Chondroitin-sulfate-ABC endolyase ChS ABC lyase Chondroitin sulfate ABC endolyase Chondroitin sulfate ABC lyase Chondroitin ABC lyase Chondroitin ABC eliminase Chondroitinase ChS ABC lyase I The related enzyme EC 4.2.2.21 has the same substrate specificity but removes disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments produced by EC 4.2.2.20. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source. Endolytic cleavage of beta-1,4-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta(4)-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta(4)-unsaturated tetra- and disaccharides. In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. Keratan sulfate, heparan sulfate and heparin are not substrates. Degrades a variety of glycosaminoglycans of the chondroitin-sulfate-and dermatan-sulfate type. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta-1-3)GalNAc(beta-1-](n), which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha-1-3)GalNAc(beta-1-](n) of DS. Chondroitin sulfate, chondroitin-sulfate proteoglycan and dermatan sulfate are the best substrates but the enzyme can also act on hyaluronan at a much lower rate. Chondroitin sulfate ABC exoeliminase Chondroitin ABC eliminase Chondroitinase ABC Chondroitin sulfate ABC exolyase ChS ABC lyase II ChS ABC lyase Chondroitin-sulfate-ABC exolyase Chondroitin sulfate ABC lyase Chondroitin ABC lyase Chondroitinase The related enzyme EC 4.2.2.20 has the same substrate specificity but produces a mixture of Delta(4)-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta(4)-unsaturated tetra-and disaccharides. Exolytic cleavage of disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha-1-3)GalNAc(beta-1-](n) of DS. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta-1-3)GalNAc(beta-1-](n), which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. Chondroitin sulfate, chondroitin-sulfate proteoglycan and dermatan sulfate are the best substrates but the enzyme can also act on hyaluronan at a much lower rate. In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. Degrades a variety of glycosaminoglycans of the chondroitin-sulfate-and dermatan-sulfate type. Keratan sulfate, heparan sulfate and heparin are not substrates. Alginate lyase I Poly(beta-D-mannuronate) lyase Poly(mana) alginate lyase Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their ends. Chondroitin AC eliminase Chondroitin sulfate lyase Chondroitinase Chondroitin AC lyase Acts on chondroitin 4-sulfate and chondroitin 6-sulfate, but less well on hyaluronate. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha-1-3)GalNAc(beta-1-](n) of DS. In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta-1-3)GalNAc(beta-1-](n), which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source. Oligogalacturonide lyase Catalyzes eliminative removal of unsaturated terminal residues also from oligosaccharides of D-galacturonate. 4-(4-deoxy-beta-D-gluc-4-enuronosyl)-D-galacturonate = 2 5-dehydro-4-deoxy-D-glucuronate. Heparin lyase Heparinase Heparin eliminase Eliminative cleavage of polysaccharides containing 1,4-linked D-glucuronate or L-iduronate residues and 1,4-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends. Heparin-sulfate eliminase Heparitin-sulfate lyase Heparin-sulfate lyase Elimination of sulfate; appears to act on linkages between N-acetyl-D-glucosamine and uronate. Product is an unsaturated sugar. Does not act on N,O-desulfated glucosamine or N-acetyl-O-sulfated glucosamine linkages. Pectate exo-lyase PATE Exo-PATE Exopectate lyase Exopolygalacturonic acid-trans-eliminase Exopectic acid transeliminase Exo-PGL Pectate disaccharide-lyase Exopolygalacturonate lyase Eliminative cleavage of 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate from the reducing end of pectate, i.e. de-esterified pectin. Acting on phosphates Threonine synthase Pyridoxal-phosphate O-phospho-L-homoserine + H(2)O = L-threonine + phosphate. (-)-endo-fenchol synthase (3R)-linalyl diphosphate is an intermediate in the reaction. Geranyl diphosphate = (-)-endo-fenchol + diphosphate. Sabinene-hydrate synthase Sabinene hydrate cyclase Both cis-and trans-isomers of sabinene hydrate are formed. Geranyl diphosphate = sabinene hydrate + diphosphate. (3R)-linalyl diphosphate is an intermediate in the reaction. 6-pyruvoyl tetrahydrobiopterin synthase PTPS 6-pyruvoyltetrahydropterin synthase http://purl.uniprot.org/mim/261640 Magnesium 6-((1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl)-7,8-dihydropterin = 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate. Catalyzes triphosphate elimination and an intramolecular redox reaction. The product is 6-pyruvoyltetrahydrobiopterin. (+)-delta-cadinene synthase D-cadinene synthase Magnesium 2-trans,6-trans-farnesyl diphosphate = (+)-delta-cadinene + diphosphate. The sesquiterpenoid (+)-delta-cadinene is an intermediate in phytoalexin biosynthesis. Beta-geraniolene synthase (-)-(1S,5S)-pinene synthase Pinene synthase Geranyl diphosphate = pinene + diphosphate. A mixture of alpha and beta-pinene is produced. Mg(2+) is essentially ineffective as the divalent metal ion cofactor. Manganese Potassium Myrcene synthase Potassium Geranyl diphosphate = myrcene + diphosphate. Mg(2+) is essentially ineffective as the divalent metal ion cofactor. Manganese (-)-(4S)-limonene synthase (4S)-limonene synthase 4S-(-)-limonene synthase Geranyl diphosphate = (-)-(4S)-limonene + diphosphate. Mg(2+) is essentially ineffective as the divalent metal ion cofactor. Manganese Potassium Taxa-4(5),11(12)-diene synthase Taxadiene synthase The cyclization involves a 1,5-hydride shift. Geranylgeranyl diphosphate = taxa-4,11-diene + diphosphate. Abietadiene cyclase Abietadiene synthase Magnesium (+)-copalyl diphosphate = (-)-abietadiene + diphosphate. Part of a bifunctional enzyme involved in the biosynthesis of abietadiene. See also EC 5.5.1.12. Ent-kaurene synthetase B Ent-kaurene synthase B Ent-kaurene synthase Part of a bifunctional enzyme involved in the biosynthesis of ent-kaurene. Ent-copalyl diphosphate = ent-kaurene + diphosphate. See also EC 5.5.1.13. O-phosphoethanolamine-phospholyase O-phosphorylethanol-amine phospho-lyase Ethanolamine-phosphate phospho-lyase Amino alcohol O-phosphate phospholyase Ethanolamine phosphate + H(2)O = acetaldehyde + NH(3) + phosphate. Also acts on D-(or L)-1-aminopropan-2-ol O-phosphate. Pyridoxal-phosphate (+)-limonene synthase (R)-limonene synthase Forms the first step of carvone biosynthesis in caraway. Manganese Geranyl diphosphate = (+)-(4R)-limonene + diphosphate. Vetispiradiene cyclase Vetispiradiene synthase Pemnaspirodiene synthase Vetispiradiene-forming farnesyl pyrophosphate cyclase HVS Trans,trans-farnesyl diphosphate = vetispiradiene + diphosphate. The initial internal cyclization produces the monocyclic intermediate germacrene A. Germacradienol/germacrene-D synthase Germacradienol synthase H-1si of farnesyl diphosphate is lost in the formation of (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol. (2) 2-trans,6-trans-farnesyl diphosphate = (-)-(7S)-germacrene-D + diphosphate. The enzyme mediates a key step in the biosynthesis of geosmin, a widely occurring metabolite of many streptomycetes, bacteria and fungi. Formation of (-)-germacrene-D involves a stereospecific 1,3-hydride shift of H-1si of farnesyl diphosphate. (1) 2-trans,6-trans-farnesyl diphosphate + H(2)O = (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + diphosphate. Magnesium Both products are formed from a common intermediate. (+)-(10R)-germacrene A synthase GAS (+)-germacrene A synthase Germacrene A synthase Germacrene-A synthase While germacrene-A is an enzyme-bound intermediate in the biosynthesis of a number of phytoalexins, e.g. EC 4.2.3.9 from some species and EC 4.2.3.21, it is the sole sesquiterpenoid product formed in chicory. 2-trans,6-trans-farnesyl diphosphate = (+)-(R)-germacrene-A + diphosphate. Magnesium Amorphadiene synthase Amorpha-4,11-diene synthase Catalyzes the formation of both olefinic and oxygenated sesquiterpenes, with amorpha-4,11-diene being the major product. Manganese A key enzyme in the biosynthesis of the antimalarial endoperoxide artemisinin. 2-trans,6-trans-farnesyl diphosphate = amorpha-4,11-diene + diphosphate. Magnesium When geranyl diphosphate is used as a substrate, no monoterpenes are produced. S-linalool synthase LIS 3S-linalool synthase Neither (S)-nor (R)-linalyl diphosphate can act as substrate for the enzyme from Clarkia breweri. Manganese or magnesium Geranyl diphosphate + H(2)O = (3S)-linalool + diphosphate. Unlike many other monoterpene synthases, only a single product, (3S)-linalool, is formed. (3R)-linalool synthase R-linalool synthase (-)-3R-linalool synthase Unlike many other monoterpene synthases, only a single product, (3R)-linalool, is formed. Geranyl diphosphate cannot be replaced by isopentenyl diphosphate, dimethylallyl diphosphate, farnesyl diphosphate or geranylgeranyl diphosphate as substrate. Geranyl diphosphate + H(2)O = (3R)-linalool + diphosphate. Manganese or magnesium Isoprene synthase ISPC ISPS Located in the chloroplast of isoprene-emitting plants, such as poplar and aspen, and may be activitated by light-dependent changes in chloroplast pH and Mg(2+) concentration. Dimethylallyl diphosphate = isoprene + diphosphate. Magnesium or manganese Methylglyoxal synthase Does not act on D-glyceraldehyde 3-phosphate. Glycerone phosphate = methylglyoxal + phosphate. 3-dehydroquinate synthase 3-dehydroquinate synthetase 5-dehydroquinic acid synthetase Dehydroquinate synthase 5-dehydroquinate synthase 3-deoxy-arabino-heptulonate 7-phosphate = 3-dehydroquinate + phosphate. NAD The hydrogen atoms on C-7 of the substrate are retained on C-2 of the products. Cobalt Chorismate synthase 5-enolpyruvylshikimate-3-phosphate phospholyase The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH.). FMN 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate. Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction. Sesquiterpene cyclase Trichodiene synthase Trichodiene synthetase Trans,trans-farnesyl diphosphate = trichodiene + diphosphate. Pentalenene synthetase Pentalenene synthase The initial step in the reaction is probably a cyclization of farnesyl diphosphate to form humulene. 2-trans,6-trans-farnesyl diphosphate = pentalenene + diphosphate. Involved in the biosynthesis of pentalenolactone and related antibiotics. Casbene synthetase Casbene synthase Geranylgeranyl diphosphate = casbene + diphosphate. The enzyme from castor bean (Ricinus communis) produces the antifungal diterpene casbene. 5-epi-aristolochene synthase Trans,trans-farnesyl diphosphate aristolochene-lyase Aristolochene synthase Sesquiterpene cyclase While in some species germacrene A remains as an enzyme-bound intermediate, it has been shown to be a minor product of the reaction in Penicillium roqueforti (see also EC 4.2.3.23). Magnesium Manganese Aristolochene is the likely parent compound for a number of sesquiterpenes produced by filamentous fungi. The initial internal cyclization produces the monocyclic intermediate germacrene A; further cyclization and methyl transfer converts the intermediate into aristolochene. 2-trans,6-trans-farnesyl diphosphate = aristolochene + diphosphate. Other carbon-oxygen lyases Carboxymethyloxysuccinate lyase Carboxymethyloxysuccinate = fumarate + glycolate. Phage-T4 UV endonuclease AP endonuclease class I Deoxyribonuclease (apurinic or apyrimidinic) E.coli endonuclease III AP lyase DNA-(apurinic or apyrimidinic site) lyase Phage-T(4) UV endonuclease Micrococcus luteus UV endonuclease Endodeoxyribonuclease (apurinic or apyrimidinic) The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. 'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. This group of enzymes was previously listed as endonucleases, under the number EC 3.1.25.2. Carbon-nitrogen lyases Ammonia-lyases Aspartase Aspartate ammonia-lyase Fumaric aminase L-aspartate = fumarate + NH(3). Serine-sulfate ammonia-lyase L-serine O-sulfate + H(2)O = pyruvate + NH(3) + sulfate. Dihydroxyphenylalanine ammonia-lyase 3,4-dihydroxy-L-phenylalanine = trans-caffeate + NH(3). Ornithine cyclase (deaminating) Ornithine cyclase Ornithine cyclodeaminase OCD The enzyme is a member of the mu-crystallin protein family. NAD The reaction is stimulated by the presence of ADP or ATP and is inhibited by O(2). L-ornithine = L-proline + NH(3). O-carbamoyl-L-serine deaminase Carbamoyl-serine ammonia-lyase Pyridoxal-phosphate O-carbamoyl-L-serine + H(2)O = pyruvate + 2 NH(3) + CO(2). 3-aminobutyryl-CoA ammonia-lyase L-3-aminobutyryl-CoA deaminase Crotonoyl-pantetheine can replace crotonoyl-CoA but it is a poorer substrate. Hydroxylamine can replace ammonia as a substrate. L-3-aminobutyryl-CoA = crotonoyl-CoA + NH(3). Alpha,beta-diaminopropionate ammonia-lyase Diaminopropionate ammonia-lyase Diaminopropionatase Active toward both D-and L-diaminopropionate. 2,3-diaminopropionate + H(2)O = pyruvate + 2 NH(3). D-and L-serine are poor substrates. Pyridoxal-phosphate Threo-3-hydroxyaspartate dehydratase L-threo-3-hydroxyaspartate dehydratase Threo-3-hydroxyaspartate ammonia-lyase Pyridoxal-phosphate Threo-3-hydroxy-L-aspartate = oxaloacetate + NH(3). Serine deaminase L-serine ammonia-lyase L-serine deaminase L-serine dehydratase L-hydroxyaminoacid dehydratase L-serine hydro-lyase (deaminating) Pyridoxal-phosphate This reaction is also carried out by EC 4.3.1.19 from a number of sources. The reaction catalyzed probably involves initial elimination of water (hence the enzyme's original classification as EC 4.2.1.13), followed by isomerization and hydrolysis of the product with C-N bond breakage. L-serine = pyruvate + NH(3). D-serine hydro-lyase (deaminating) D-serine deaminase D-serine dehydratase (deaminating) D-serine hydrolase D-serine dehydrase D-serine ammonia-lyase D-hydroxy amino acid dehydratase D-serine dehydratase Also acts, slowly, on D-threonine. Pyridoxal-phosphate D-serine = pyruvate + NH(3). The reaction catalyzed probably involves initial elimination of water (hence the enzyme's original classification as EC 4.2.1.14), followed by isomerization and hydrolysis of the product with C-N bond breakage. L-serine dehydratase L-threonine dehydratase Threonine dehydratase Threonine ammonia-lyase L-threonine deaminase L-threonine hydro-lyase (deaminating) Threonine deaminase Threonine dehydrase Serine deaminase The enzyme from a number of sources also acts on L-serine, cf. EC 4.3.1.17. The protein from Pseudomonas putida does not require pyridoxal-phosphate. The reaction catalyzed probably involves initial elimination of water (hence the enzyme's original classification as EC 4.2.1.16), followed by isomerization and hydrolysis of the product with C-N bond breakage. Pyridoxal-phosphate L-threonine = 2-oxobutanoate + NH(3). Methylaspartate ammonia-lyase Beta-methylaspartase L-threo-3-methylaspartate = mesaconate + NH(3). Cobalamin Erythro-3-hydroxyaspartate ammonia-lyase Erythro-3-hydroxy-L(s)-aspartate hydro-lyase (deaminating) Erythro-3-hydroxyaspartate dehydratase 3-hydroxyaspartate dehydratase Erythro-beta-hydroxyaspartate dehydratase Erythro-3-hydroxy-L-aspartate = oxaloacetate + NH(3). The reaction catalyzed probably involves initial elimination of water (hence the enzyme's original classification as EC 4.2.1.38) followed by isomerization and hydrolysis of the product with C-N bond breakage. Pyridoxal-phosphate Histidine alpha-deaminase Histidine ammonia-lyase Histidinase Histidase http://purl.uniprot.org/mim/235800 L-histidine = urocanate + NH(3). Formimidoyltetrahydrofolate cyclodeaminase Formiminotetrahydrofolate cyclodeaminase In eukaroytes, occurs as a bifunctional enzyme that also has EC 2.1.2.5 activity. 5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH(3). Phenylalanine ammonia-lyase L-phenylalanine = trans-cinnamate + NH(3). May also act on L-tyrosine. Beta-alanyl-CoA ammonia-lyase Beta-alanyl-CoA = acryloyl-CoA + NH(3). Ethanolamine ammonia-lyase Ethanolamine = acetaldehyde + NH(3). Cobalamin Glucosaminate ammonia-lyase D-glucosaminate dehydratase Glucosaminic dehydrase D-glucosaminic acid dehydrase 2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating) Acetylenemonocarboxylic acid hydrase 2-amino-2-deoxy-D-gluconate ammonia-lyase Aminodeoxygluconate ammonia-lyase Aminodeoxygluconate dehydratase D-glucosaminate = 2-dehydro-3-deoxy-D-gluconate + NH(3). Pyridoxal-phosphate Lyases acting on amides, amidines, etc Arginosuccinase N-(L-argininosuccinate) arginine-lyase Omega-N-(L-arginino)succinate arginine-lyase Argininosuccinate lyase 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. http://purl.uniprot.org/mim/207900 Adenylosuccinate lyase Succino AMP-lyase Adenylosuccinase http://purl.uniprot.org/mim/103050 (1) N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. Also acts on 1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole. (2) (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. Ureidoglycolatase Ureidoglycolate hydrolase Ureidoglycolate lyase Ureidoglycolase (S)-ureidoglycolate = glyoxylate + urea. Purine imidazole-ring cyclase Also acts on 2,6-diamino-5-formamido-3,4-dihydro-4-oxopyrimidine residues. DNA 4,6-diamino-5-formamidopyrimidine = DNA adenine + H(2)O. Brings about the reclosure of the imidazole rings of purine residues damaged by gamma-rays. Alpha-hydroxyglycine amidating dealkylase Peptidylamidoglycolate lyase Peptidylamidoglycolate = peptidyl amide + glyoxylate. Acts on the product of the reaction catalyzed by EC 1.14.17.3, thus removing a terminal glycine residue and leaving a des-glycine peptide amide. Amine-lyases 3-ketovalidoxylamine C-N-lyase 4-nitrophenyl-3-ketovalidamine = 4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one. Involved in the degradation of the fungicide validamycin A by Flavobacterium saccharophilum. Calcium Eliminates 4-nitroaniline from 4-nitrophenyl-3-ketovalidamine or 4-nitrophenol from 4-nitrophenyl-alpha-D-3-dehydroglucoside. Strictosidine synthetase Strictosidine synthase STR Catalyzes a a Pictet-Spengler reaction between the aldehyde group of secologanin and the amino group of tryptamine. 3-alpha-(S)-strictosidine + H(2)O = tryptamine + secologanin. Involved in the biosynthesis of the monoterpenoid indole alkaloids. Deacetylisoipecoside synthase The product is rapidly converted to demethylisoalangiside. The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 4.3.3.4. Deacetylisoipecoside + H(2)O = dopamine + secologanin. Deacetylipecoside synthase Deacetylipecoside + H(2)O = dopamine + secologanin. The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 4.3.3.3. The product is rapidly converted to demethylalangiside. Carbon-sulfur lyases Carbon-sulfur lyases Cystathionine gamma-lyase Cystathionase Gamma-cystathionase Cysteine desulfhydrase Homoserine deaminase Cystathioninase Homoserine dehydratase Cystine desulfhydrase Also catalyzes elimination reactions of L-homoserine to form H(2)O, NH(3) and 2-oxobutanoate, of L-cystine, producing thiocysteine, pyruvate and NH(3), and of L-cysteine producing pyruvate, NH(3) and H(2)S. L-cystathionine + H(2)O = L-cysteine + NH(3) + 2-oxobutanoate. Pyridoxal-phosphate http://purl.uniprot.org/mim/219500 Cysteine lyase Can use a second molecule of cysteine (producing lanthionine) or other alkyl thiols as replacing agents. L-cysteine + sulfite = L-cysteate + H(2)S. Pyridoxal-phosphate L-methioninase Methionine gamma-lyase Methionine lyase Pyridoxal-phosphate L-methionine = methanethiol + NH(3) + 2-oxobutanoate. L-cysteine-S-conjugate thiol-lyase (deaminating) Cysteine-S-conjugate beta-lyase Pyridoxal-phosphate R may represent aromatic compounds such as 4-bromobenzene and 2,4-dinitrobenzene. RS-CH(2)-CH(NH(3)(+))COO(-) = RSH + NH(3) + pyruvate. Aminocyclopropanecarboxylate synthase S-adenosyl-L-methionine methylthioadenosine-lyase 1-aminocyclopropane-1-carboxylate synthase 1-aminocyclopropane-1-carboxylic acid synthase ACC synthase Pyridoxal-phosphate Catalyzes an alpha,gamma-elimination. S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine. D-cysteine desulfhydrase D-cysteine + H(2)O = H(2)S + NH(3) + pyruvate. Selenocysteine reductase Selenocysteine beta-lyase Selenocysteine lyase L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor. Does not act on cysteine, serine or chloroalanine. Pyridoxal-phosphate Dithiothreitol or 2-mercaptoethanol can act as reducing agent in the reaction. Holocytochrome-c synthase Cytochrome c heme-lyase Cytochrome c synthase In the reverse direction, the enzyme catalyzes the attachment of heme to two cysteine residues in the protein, forming thioether links. Holocytochrome c = apocytochrome c + heme. http://purl.uniprot.org/mim/309801 (2R)-phospho-3-sulfolactate synthase PSL synthase Phosphosulfolactate synthase It specifically requires phosphoenolpyruvate and its broad alkaline pH optimum suggests that it uses sulfite rather than bisulfite. The enzyme from Methanococcus jannaschii catalyzes the Michael addition of sulfite to phosphoenolpyruvate. Magnesium (2R)-O-phospho-3-sulfolactate = phosphoenolpyruvate + hydrogen sulfite. Homocysteine desulfurase Homocysteine desulfhydrase Pyridoxal-phosphate L-homocysteine + H(2)O = H(2)S + NH(3) + 2-oxobutanoate. LTC(4) synthetase Leukotriene-C(4) synthase LTC(4) synthase Leukotriene C(4) synthetase Leukotriene A(4):glutathione S-leukotrienyltransferase Not identical with EC 2.5.1.18. The reaction proceeds in the direction of addition. Leukotriene C(4) = leukotriene A(4) + glutathione. http://purl.uniprot.org/mim/246530 S-ribosylhomocysteinase S-ribosylhomocysteine lyase S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione. Iron(2+) The 4,5-dihydroxypentan-2,3-dione formed spontaneously cyclizes and combines with borate to form an autoinducer (AI-2) in the bacterial quorum-sensing mechanism, which is used by many bacteria to control gene expression in response to cell density. Glutathione-dependent formaldehyde-activating enzyme S-(hydroxymethyl)glutathione synthase S-(hydroxymethyl)glutathione = glutathione + formaldehyde. The enzyme from Paracoccus denitrificans accelerates the spontaneous reaction in which the adduct of formaldehyde and glutathione is formed, i.e. the substrate for EC 1.1.1.284, in the formaldehyde-detoxification pathway. Coenzyme M-epoxyalkane ligase Epoxyalkyl:CoM transferase Epoxyalkane:CoM transferase Epoxyalkane:coenzyme M transferase Epoxyalkane:2-mercaptoethanesulfonate transferase EaCoMT Epoxypropane:coenzyme M transferase Epoxypropyl:CoM transferase 2-hydroxypropyl-CoM lyase This enzyme forms component I of a four-component enzyme system (comprising EC 4.4.1.23 (component I), EC 1.8.1.5 (component II), EC 1.1.1.268 (component III) and EC 1.1.1.269 (component IV)) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2. (1) (R)-2-hydroxypropyl-CoM = (R)-1,2-epoxypropane + HS-CoM. (2) (S)-2-hydroxypropyl-CoM = (S)-1,2-epoxypropane + HS-CoM. The enzyme will function with some other thiols (e.g., 2-sulfanylethanol) as the nucleophile. Acts on both enantiomers of chiral epoxyalkanes to form the corresponding (R)-and (S)-2-hydroxyalkyl-CoM adducts. Zinc Uses short-chain epoxyalkanes from C(2) (epoxyethane) to C(6) (1,2-epoxyhexane). Sulfolactate sulfo-lyase The inducible enzyme from Paracoccus pantotrophus NKNCYSA forms part of the cysteate-degradation pathway. L-cysteate ((2S)2-amino-3-sulfopropanoate) serves as a sole source of carbon and energy for the aerobic growth of P.pantotrophus, as an electron acceptor for several sulfate-reducing bacteria, as an electron donor for some nitrate-reducing bacteria and as a substrate for a fermentation in a sulfate-reducing baterium. Iron(2+) 3-sulfolactate = pyruvate + bisulfite. L-cysteate sulfo-lyase D-cysteine can also act as a substrate, but more slowly. The inducible enzyme from Silicibacter pomeroyi DSS-3 forms part of the cysteate-degradation pathway. L-cysteate + H(2)O = pyruvate + bisulfite + NH(3). It is converted into pyruvate, sulfide and NH(3). Pyridoxal-phosphate Dimethylpropiothetin dethiomethylase S,S-dimethyl-beta-propiothetin = dimethyl sulfide + acrylate. Alliinase Alliin lyase L-cysteine sulfoxide lyase Cysteine sulphoxide lyase Cysteine sulfoxide lyase An S-alkyl-L-cysteine S-oxide = an alkyl sulfenate + 2-aminoacrylate. Pyridoxal-phosphate Methylglyoxalase Glyoxalase I Ketone-aldehyde mutase Aldoketomutase (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing) Lactoylglutathione lyase Also acts on 3-phosphoglycerol-glutathione. (R)-S-lactoylglutathione = glutathione + methylglyoxal. S-alkyl-L-cysteine alkylthiol-lyase (deaminating) S-alkylcysteine lyase S-alkyl-L-cysteine lyase S-alkyl-L-cysteinase S-alkyl-L-cysteine sulfoxide lyase Decomposes S-alkyl-L-cysteines by alpha,beta-elimination. Pyridoxal-phosphate Possibly identical, in Saccharomyces cerevisiae, with EC 4.4.1.8. An S-alkyl-L-cysteine + H(2)O = an alkyl thiol + NH(3) + pyruvate. Beta C-S lyase Cysteine lyase Cystathionine beta-lyase Beta-cystathionase Cystine lyase Pyridoxal-phosphate L-cystathionine + H(2)O = L-homocysteine + NH(3) + pyruvate. The enzyme from some sources also acts on L-cystine, forming pyruvate, ammonia and cysteine persulfide, and a number of related compounds. Possibly identical, in Saccharomyces cerevisiae, with EC 4.4.1.6. Beta-cyanoalanine synthase L-3-cyanoalanine synthase Beta-cyano-L-alanine synthase L-cysteine + HCN = L-3-cyanoalanine + H(2)S. Pyridoxal-phosphate Carbon-halide lyases Carbon-halide lyases DDT-dehydrochlorinase 1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride. 3-chloro-D-alanine dehydrochlorinase Pyridoxal-phosphate Also catalyzes beta-replacement reactions, e.g. converts 3-chloro-D-alanine and H(2)S into D-cysteine and HCl. 3-chloro-D-alanine + H(2)O = pyruvate + HCl + NH(3). Dichloromethane dehalogenase Glutathione Dichloromethane + H(2)O = formaldehyde + 2 HCl. L-2-amino-4-chloropent-4-enoate dehydrochlorinase L-2-amino-4-chloropent-4-enoate + H(2)O = 2-oxopent-4-enoate + HCl + NH(3). S-carboxymethylcysteine synthase 3-chloro-L-alanine + thioglycolate = S-carboxymethyl-L-cysteine + chloride. Pyridoxal-phosphate Phosphorus-oxygen lyases Phosphorus-oxygen lyases Adenyl cyclase 3',5'-cyclic AMP synthetase Adenylate cyclase ATP pyrophosphate-lyase Adenylyl cyclase ATP = 3',5'-cyclic AMP + diphosphate. Also acts on dATP to form 3',5'-cyclic dAMP. Activated by NAD(+) in presence of EC 2.4.2.31. Requires pyruvate. 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase MECDP-synthase 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP. Magnesium or manganese Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. Monophosphatidylinositol phosphodiesterase Phosphatidylinositol phospholipase C 1-phosphatidylinositol phosphodiesterase Phosphatidylinositol diacylglycerol-lyase 1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol. This enzyme is bacterial. Activity is also found in animals, but this activity is due to the presence of EC 3.1.4.11. Variant-surface-glycoprotein phospholipase C GPI-specific phospholipase C Glycosylphosphatidylinositol diacylglycerol-lyase Glycosylphosphatidylinositol-phospholipase C 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase (1,2-cyclic-phosphate-forming) VSG-lipase Glycosyl inositol phospholipid anchor-hydrolyzing enzyme GPI-PLC Glycosylphosphatidylinositol-specific phospholipase C (Glycosyl)phosphatidylinositol-specific phospholipase C In other cases, the diacylglycerol is replaced by ceramide. In some cases, the long-chain acyl group at the sn-1 position of glycerol is replaced by an alkyl or alk-1-enyl group. It therefore cleaves proteins from the lipid part of the glycosylphostphatidylinositol (GPI) anchors. 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol = 6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol. The only characterized enzyme with this specificity is from Trypanosoma brucei, where the acyl groups are myristoyl, but the function of the trypanosome enzyme is unknown. Substitution on O-2 of the inositol blocks action of this enzyme. This enzyme is also active when O-4 of the glucosamine is substituted by carrying the oligosaccharide that can link a protein to the structure. It is not identical with EC 3.1.4.50. FMN cyclase FAD-AMP lyase (cyclizing) While FAD was the best substrate tested the enzyme also splits ribonucleoside diphosphate-X compounds in which X is an acyclic or cyclic monosaccharide or derivative bearing an X-OH group that is able to attack internally the proximal phosphorus with the geometry necessary to form a P=X product; either a five-atom monocyclic phosphodiester or a cis-bicyclic phosphodiester-pyranose fusion. The reaction is strongly inhibited by ADP or ATP but is unaffected by the presence of the product, cFMN. FAD = AMP + riboflavin cyclic-4',5'-phosphate. Manganese or cobalt Guanylyl cyclase Guanyl cyclase Guanylate cyclase http://purl.uniprot.org/mim/204000 http://purl.uniprot.org/mim/601875 Also acts on ITP and dGTP. GTP = 3',5'-cyclic GMP + diphosphate. http://purl.uniprot.org/mim/601777 Cytidylyl cyclase Cytidyl cyclase 3'5'-cyclic-CMP synthase Cytidylate cyclase CTP = 3',5'-cyclic CMP + diphosphate. Other lyases Sole sub-subclass for lyases that do not belong in the other subclasses Ferrochelatase Heme synthetase Iron chelatase Heme synthase Protoheme ferro-lyase Protoheme + 2 H(+) = protoporphyrin + Fe(2+). http://purl.uniprot.org/mim/177000 Organomercurial lyase Alkylmercury lyase Organomercury lyase Acts on CH(3)Hg(+) and a number of other alkylmercury compounds, in the presence of cysteine or other thiols, liberating mercury as a mercaptide. Some arylmercury compounds can also act as substrates. An alkylmercury + H(+) = an alkane + Hg(2+). Sirohydrochlorin cobaltochelatase Anaerobic cobalt chelatase Cobaltochelatase Cobalt-sirohydrochlorin + 2 H(+) = sirohydrochlorin + Co(2+). This enzyme is a type II chelatase, being either a monomer (CbiX) or a homodimer (CibK) and being ATP-independent. The enzyme contains two histidines at the active site that are thought to be involved in the deprotonation of the tetrapyrrole substrate as well as in metal binding. CbiX from Bacillus megaterium inserts cobalt at the level of sirohydrochlorin (factor-II) rather than precorrin-2. CbiK from Salmonella enterica uses precorrin-2 as the substrate to yield cobalt-precorrin-2. Sirohydrochlorin ferrochelatase In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirB being responsible for the above reaction. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107) and the second step involves an NAD(+)-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76). Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. This enzyme catalyzes the third of three steps leading to the formation of siroheme from uroporphyrinogen III. Aliphatic aldoxime dehydratase An aliphatic aldoxime = an aliphatic nitrile + H(2)O. Exhibits a strong preference for aliphatic aldoximes, such as butyraldoxime and acetaldoxime, over aromatic aldoximes, such as pyridine-2-aldoxime, which is a poor substrate. No activity was found with the aromatic aldoximes benzaldoxime and pyridine-4-aldoxime. Protoheme IX Calcium 3-indoleacetaldoxime hydro-lyase Indoleacetaldoxime dehydratase Indoleacetaldoxime hydro-lyase Indole-3-acetaldehyde-oxime hydro-lyase (Indol-3-yl)acetaldehyde oxime = (indol-3-yl)acetonitrile + H(2)O. Arylacetaldoxime dehydratase Phenylacetaldoxime dehydratase PAOx dehydratase However, it is inactive with phenylacetaldoximes that have a substituent group at an alpha-site of an oxime group, for example, with (E/Z)-2-phenylpropionaldoxime and (E/Z)-mandelaldoxime. Heme (Z)-phenylacetaldehyde oxime = phenylacetonitrile + H(2)O. The enzyme is active toward several (Z)-arylacetaldoximes and (E/Z)-alkylaldoximes as well as toward arylalkylaldoximes such as 3-phenylpropionaldoxime and 4-phenylbutyraldoxime. The activity of the enzyme is inhibited completely by the heavy-metal cations Cu(+), Cu(2+), Ag(+) and Hg(+) whereas Fe(2+) and Sn(2+) have an activatory effect. (Z)-phenylacetaldoxime binds to ferric heme (the Fe(3+) form) via the oxygen atom whereas it binds to the active ferrous form via the nitrogen atom. In this way, the oxidation state of the heme controls the coordination stucture of the substrate--heme complex, which regulates enzyme activity. The enzyme from Bacillus sp. OxB-1 contains protoheme IX, the iron of which must be in the form Fe(2+) for activity. Isomerases Racemases and epimerases Acting on amino acids and derivatives Alanine racemase Pyridoxal-phosphate L-alanine = D-alanine. Amino-acid racemase Pyridoxal-phosphate An L-amino acid = a D-amino acid. Phenylalanine racemase (ATP-hydrolyzing) ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine. Ornithine racemase L-ornithine = D-ornithine. Aspartate racemase L-aspartate = D-aspartate. Also acts, at half the rate, on L-alanine. Nocardicin-A epimerase Isonocardicin A = nocardicin A. The (9'S) configuration of isonocardicin A is converted into the (9'R) configuration. Alpha-amino-epsilon-caprolactam racemase 2-amino-hexano-6-lactam racemase 2-aminohexano-6-lactam racemase Also interconverts 2-aminopentano-5-lactam (alpha-amino-delta-valerolactam) and 2-amino-4-thiahexano-6-lactam (where S replaces CH(2) of C-4). L-2-aminohexano-6-lactam = D-2-aminohexano-6-lactam. It does not catalyze the racemisation of alpha-amino acids but has some transaminase activity with them. Pyridoxal-phosphate Protein-serine epimerase Protein-serine racemase [Protein]-L-serine = [protein]-D-serine. The enzyme specifically interconverts the configuration of Ser-46 of the peptide omega-agatoxin-KT, found in the venom of the funnel web spider, Agelenopsis aperta, but not that of the other serine residue, Ser-28. Isopenicillin-N epimerase Epimerization at C-5 of the 5-amino-5-carboxypentanoyl group to form penicillin N is required to make a substrate for EC 1.14.20.1, to produce cephalosporins. Isopenicillin N = penicillin N. Pyridoxal-phosphate Forms part of the penicillin biosynthesis pathway. Methionine racemase Pyridoxal-phosphate L-methionine = D-methionine. Glutamate racemase Pyridoxal-phosphate L-glutamate = D-glutamate. Proline racemase L-proline = D-proline. Lysine racemase L-lysine = D-lysine. Threonine racemase Inverts both chiral centers. L-threonine = D-threonine. Diaminopimelate epimerase LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate. Hydroxyproline epimerase 4-hydroxyproline epimerase Hydroxyproline 2-epimerase Trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline. Also interconverts trans-4-hydroxy-D-proline and cis-4-hydroxy-L-proline. Arginine racemase L-arginine = D-arginine. Pyridoxal-phosphate Acting on hydroxy acids and derivatives Lactic acid racemase Lactate racemase Hydroxyacid racemase Lacticoracemase (S)-lactate = (R)-lactate. Mandelate racemase (S)-mandelate = (R)-mandelate. 3-hydroxybutyryl-CoA epimerase (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. Acetylmethylcarbinol racemase Acetoin racemase (S)-acetoin = (R)-acetoin. Tartrate epimerase (R,R)-tartrate = meso-tartrate. Isocitrate epimerase (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate is the commonly occurring isomer of isocitrate. (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate = (1S,2S)-1-hydroxypropane-1,2,3-tricarboxylate. Acting on carbohydrates and derivatives D-ribulose-5-phosphate epimerase D-ribulose phosphate-3-epimerase Phosphoribulose epimerase D-xylulose-5-phosphate 3-epimerase Pentose-5-phosphate 3-epimerase Erythrose-4-phosphate epimerase Ribulose-phosphate 3-epimerase Xylulose phosphate 3-epimerase Also converts D-erythrose 4-phosphate into D-erythrulose 4-phosphate and D-threose 4-phosphate. D-ribulose 5-phosphate = D-xylulose 5-phosphate. Cytidine diphosphoparatose epimerase Cytidine diphosphoabequose epimerase CDP-abequose epimerase CDP-tyvelose 2-epimerase CDP-paratose 2-epimerase CDP-paratose epimerase Cytidine diphosphate paratose-2-epimerase Cytidine diphosphodideoxyglucose epimerase CDP-D-abequose 2-epimerase CDP-3,6-dideoxy-D-glucose = CDP-3,6-dideoxy-D-mannose. CDP-tyvelose (CDP-3,6-dideoxy-D-mannose) is systematically called CDP-3,6-dideoxy-D-arabino-hexose. CDP-paratose (CDP-3,6-dideoxy-D-glucose), is more systematically called CDP-alpha-3,6-dideoxy-D-ribo-hexose. NAD Cellobiose epimerase Cellobiose = D-glucosyl-D-mannose. UDP-glucuronate 5'-epimerase UDP-glucuronic acid epimerase UDP-glucuronic acid 5'-epimerase NAD UDP-glucuronate = UDP-L-iduronate. Thymidine diphospho-4-ketorhamnose 3,5-epimerase dTDP-4-keto-6-deoxyglucose 3,5-epimerase dTDP-L-rhamnose synthetase dTDP-4-dehydrorhamnose 3,5-epimerase Occurs in a complex with EC 1.1.1.133. dTDP-4-dehydro-6-deoxy-D-glucose = dTDP-4-dehydro-6-deoxy-L-mannose. Uridine diphosphate-N-acetylglucosamine-2'-epimerase Uridine diphosphoacetylglucosamine 2'-epimerase Uridine diphospho-N-acetylglucosamine 2'-epimerase UDP-GlcNAc-2-epimerase UDP-N-acetylglucosamine 2-epimerase http://purl.uniprot.org/mim/269921 UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine. http://purl.uniprot.org/mim/605820 http://purl.uniprot.org/mim/600737 Hydrolyzes the product to UDP and N-acetyl-D-mannosamine. Glucose-6-phosphate 1-epimerase Alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate. UDP-glucosamine 4-epimerase UDP-glucosamine = UDP-galactosamine. Heparosan-N-sulfate-glucuronate 5-epimerase Acts on D-glucuronosyl residues adjacent to sulfated D-glucosamine units in the heparin precursor. Not identical with EC 5.1.3.19. Heparosan-N-sulfate D-glucuronate = heparosan-N-sulfate L-iduronate. GDP-mannose 3,5-epimerase GDP-mannose = GDP-L-galactose. Polyglucuronate 5-epimerase Chondroitin-glucuronate 5-epimerase Dermatan-sulfate 5-epimerase Chondroitin D-glucuronate = dermatan L-iduronate. Not identical with EC 5.1.3.17. Uridine diphosphate galactose 4-epimerase Uridine diphospho-galactose-4-epimerase Galactowaldenase UDP-glucose 4-epimerase UDP-galactose 4-epimerase UDP-glucose = UDP-galactose. NAD Also acts on UDP-2-deoxyglucose. http://purl.uniprot.org/mim/230350 ADP-glyceromanno-heptose 6-epimerase ADP-L-glycero-D-manno-heptose 6-epimerase NAD ADP-D-glycero-D-manno-heptose = ADP-L-glycero-D-manno-heptose. Maltose epimerase Alpha-maltose = beta-maltose. The enzyme catalyzes the interconversion of alpha and beta anomers of maltose more effectively than those of disaccharides such as lactose and cellobiose. L-ribulose-5-phosphate 3-epimerase L-xylulose 5-phosphate 3-epimerase Along with EC 4.1.1.85, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli. L-ribulose 5-phosphate = L-xylulose 5-phosphate. Mutarotase Aldose 1-epimerase Aldose mutarotase Also acts on L-arabinose, D-xylose, D-galactose, maltose and lactose. Alpha-D-glucose = beta-D-glucose. L-ribulose-5-phosphate 4-epimerase L-ribulose 5-phosphate 4-epimerase L-ribulose-phosphate 4-epimerase Phosphoribulose isomerase Ribulose phosphate 4-epimerase L-ru5P Divalent cation L-ribulose 5-phosphate = D-xylulose 5-phosphate. UDP-arabinose 4-epimerase UDP-L-arabinose = UDP-D-xylose. Uridine diphosphoglucuronate epimerase UDP-galacturonate 4-epimerase UDP-glucuronate 4-epimerase UDP glucuronic epimerase UDP-glucuronate = UDP-D-galacturonate. Uridine diphosphoacetylglucosamine epimerase UDP-N-acetylglucosamine 4-epimerase UDP-GlcNAc 4-epimerase UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-galactosamine. N-acylglucosamine 2-epimerase N-acetyl-D-glucosamine 2-epimerase GlcNAc 2-epimerase Requires catalytic amounts of ATP. N-acyl-D-glucosamine = N-acyl-D-mannosamine. N-acetylmannosamine-6-phosphate 2-epimerase Acylglucosamine-6-phosphate 2-epimerase N-acetylglucosmamine 6-phosphate 2-epimerase Acylmannosamine phosphate 2-epimerase Acylglucosamine phosphate 2-epimerase N-acylglucosamine-6-phosphate 2-epimerase N-acyl-D-glucosamine 6-phosphate = N-acyl-D-mannosamine 6-phosphate. Acting on other compounds Methylmalonyl coenzyme A racemase 2-methyl-3-oxopropanoyl-CoA 2-epimerase Methylmalonyl-CoA racemase Methylmalonyl-CoA epimerase DL-methylmalonyl-CoA racemase http://purl.uniprot.org/mim/251120 (R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA. 16-hydroxysteroid epimerase 16-alpha-hydroxysteroid = 16-beta-hydroxysteroid. Allantoin racemase (S)(+)-allantoin = (R)(-)-allantoin. Alpha-methylacyl-CoA racemase Not active toward free acids. (2S)-2-methylacyl-CoA = (2R)-2-methylacyl-CoA. http://purl.uniprot.org/mim/214950 Alpha-methyl-branched acyl-CoA derivatives with chain lengths of more than C(10) are substrates. http://purl.uniprot.org/mim/604489 Also active toward some aromatic compounds (e.g. ibuprofen) and bile acid intermediates, such as trihydroxycoprostanoyl-CoA. Cis-trans-isomerases Cis-trans Isomerases Maleate isomerase Maleate = fumarate. 2-chloro-4-carboxymethylenebut-2-en-1,4-olide isomerase Chlorodienelactone isomerase 2-chlorocarboxymethylenebutenolide isomerase Cis-2-chloro-4-carboxymethylenebut-2-en-1,4-olide = trans-2-chloro-4-carboxymethylenebut-2-en-1,4-olide. Maleylacetoacetate isomerase Maleylacetone isomerase 4-maleylacetoacetate = 4-fumarylacetoacetate. Also acts on maleylpyruvate. Retinene isomerase Retinal isomerase Retinoid isomerase All-trans-retinal = 11-cis-retinal. Light shifts the reaction toward the cis-isomer. Maleylpyruvate isomerase 3-maleylpyruvate = 3-fumarylpyruvate. Linoleate isomerase 9-cis,12-cis-octadecadienoate = 9-cis,11-trans-octadecadienoate. Furylfuramide isomerase NAD (E)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide = (Z)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide. Retinol isomerase All-trans-retinol isomerase All-trans-retinol = 11-cis-retinol. Converts all-trans-retinol to 11-cis-retinol in the dark, thus reversing the effect of EC 5.2.1.3. Peptidyl-prolyl cis-trans isomerase Peptidylprolyl isomerase Peptidylprolyl cis-trans isomerase Rotamase Cyclophilin PPIase http://purl.uniprot.org/mim/194050 The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. Peptidylproline (omega=180) = peptidylproline (omega=0). Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. Farnesol 2-isomerase 2-trans,6-trans-farnesol = 2-cis,6-trans-farnesol. Intramolecular oxidoreductases Interconverting aldoses and ketoses Triosephosphate mutase Triosephosphate isomerase Triose-phosphate isomerase Phosphotriose isomerase Triose phosphoisomerase http://purl.uniprot.org/mim/190450 D-glyceraldehyde 3-phosphate = glycerone phosphate. Glucuronate isomerase D-glucuronate isomerase Uronic acid isomerase Uronate isomerase Uronic isomerase D-glucuronate = D-fructuronate. Also converts D-galacturonate to D-tagaturonate. Arabinose phosphate isomerase Phosphoarabinoisomerase Arabinose-5-phosphate isomerase D-arabinose 5-phosphate = D-ribulose 5-phosphate. Rhamnose isomerase L-rhamnose isomerase L-rhamnose = L-rhamnulose. D-lyxose isomerase D-lyxose ketol-isomerase D-lyxose = D-xylulose. Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase N-(5'-phospho-D-ribosylformimino)-5-amino-1-(5''-phosphoribosyl)-4-imidazolecarboxamide isomerase 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1-deoxyribulos-1-ylamino)methylideneamino)-1-(5-phosphoribosyl)imidazole-4-carboxamide. 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase 5-keto-4-deoxyuronate isomerase 4-deoxy-L-threo-5-hexosulose uronate = 3-deoxy-D-glycero-2,5-hexodiulosonate. D-ribose isomerase Ribose isomerase D-ribose = D-ribulose. Also acts on L-lyxose and L-rhamnose. Corticosteroid side-chain-isomerase An epimerization at C-20 and C-21 is probably catalyzed by the same enzyme. 11-deoxycorticosterone = 20-hydroxy-3-oxopregn-4-en-21-al. Hydroxypyruvate isomerase Hydroxypyruvate = 2-hydroxy-3-oxopropanoate. 1-PMTR isomerase S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate aldose-ketose-isomerase MTR-1-P isomerase S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate ketol-isomerase 5-methylthioribose-1-phosphate isomerase 5-methylthio-5-deoxy-D-ribose-1-phosphate ketol-isomerase S-methyl-5-thioribose-1-phosphate isomerase S-methyl-5-thio-D-ribose-1-phosphate aldose-ketose-isomerase 1-phospho-5'-S-methylthioribose isomerase Methylthioribose 1-phosphate isomerase S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate. PRAI Phosphoribosylanthranilate isomerase N-(5'-phosphoribosyl)anthranilate isomerase In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27, and EC 4.2.1.20). N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. L-fucose isomerase L-fucose = L-fuculose. Galactose-6-phosphate isomerase Involved in the tagatose 6-phosphate pathway of lactose catabolism in bacteria. D-galactose 6-phosphate = D-tagatose 6-phosphate. Arabinose isomerase D-arabinose isomerase L-fucose isomerase D-arabinose = D-ribulose. Also acts on L-fucose and, more slowly, on L-galactose and D-altrose. L-arabinose isomerase L-arabinose = L-ribulose. D-xylose ketoisomerase Xylose isomerase Some enzymes also convert D-glucose to D-fructose. Magnesium D-xylose = D-xylulose. Phosphopentosisomerase D-ribose-5-phosphate ketol-isomerase Ribose phosphate isomerase Ribose-5-phosphate isomerase Ribose 5-phosphate epimerase Phosphoriboisomerase Phosphopentoseisomerase 5-phosphoribose isomerase D-ribose 5-phosphate = D-ribulose 5-phosphate. http://purl.uniprot.org/mim/608611 Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate. D-mannose isomerase Mannose isomerase Also acts on D-lyxose and D-rhamnose. D-mannose = D-fructose. Phosphohexomutase Phosphohexoisomerase Mannose-6-phosphate isomerase Phosphomannose isomerase Phosphomannoisomerase http://purl.uniprot.org/mim/602579 Zinc D-mannose 6-phosphate = D-fructose 6-phosphate. Phosphoglucose isomerase Phosphohexoisomerase Hexosephosphate isomerase Phosphohexose isomerase Oxoisomerase Glucose-6-phosphate isomerase Phosphoglucoisomerase Phosphohexomutase Hexose monophosphate isomerase Phosphosaccharomutase Also catalyzes the anomerization of D-glucose 6-phosphate. http://purl.uniprot.org/mim/172400 D-glucose 6-phosphate = D-fructose 6-phosphate. Interconverting keto- and enol- groups Phenylpyruvic keto--enol isomerase Phenylpyruvate keto--enol tautomerase Phenylpyruvate tautomerase Keto-phenylpyruvate = enol-phenylpyruvate. Also acts on other arylpyruvates. Oxaloacetate tautomerase Oxalacetic keto--enol isomerase Oxaloacetate keto--enol tautomerase Keto-oxaloacetate = enol-oxaloacetate. Transposing C==C bonds Delta(5)-3-oxosteroid isomerase 3-oxosteroid isomerase Steroid Delta-isomerase Delta(5)-3-ketosteroid isomerase Steroid isomerase Hydroxysteroid isomerase Delta(5)-steroid isomerase Delta(5)-3-keto steroid isomerase A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid. 5-carboxymethyl-2-hydroxymuconic acid isomerase 5-carboxymethyl-2-hydroxymuconate Delta-isomerase CHM isomerase 5-carboxymethyl-2-hydroxymuconate = 5-carboxy-2-oxohept-3-enedioate. Isopiperitenone Delta-isomerase Isopiperitenone = piperitenone. Involved in the biosynthesis of menthol and related monoterpenes in peppermint (Mentha piperita) leaves. L-dopachrome isomerase Dopachrome tautomerase Dopachrome conversion factor Dopachrome rearranging enzyme Dopachrome keto-enol isomerase Dopachrome oxidoreductase DCF Tyrosinase-related protein 2 DCT Dopachrome Delta(7),Delta(2)-isomerase L-dopachrome-methyl ester tautomerase TRP Dopachrome Delta-isomerase Dopachrome isomerase Dopachrome methyl ester is a substrate, but dopaminochrome (2,3-dihydroxyindolyl-5,6-quinone) is not (see also EC 4.1.1.84). L-dopachrome = 5,6-dihydroxyindole-2-carboxylate. Stereospecific for L-dopachrome (5,6-dioxo-2,3-5,6-tetrahydroindole-2-carboxylate). Zinc Polyenoic fatty acid isomerase Eicosapentaenoate cis-Delta(5,8,11,14,17)-eicosapentaenoate cis-Delta(5)-trans-Delta(7,9)-cis-Delta(14,17) isomerase PFI The enzyme from the red alga Ptilota filicina catalyzes the isomerization of skip dienes (methylene-interrupted double bonds) in a broad range of fatty acids and fatty-acid analogs, such as arachidonate and gamma-linolenate, to yield a conjugated triene. (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate = (5Z,7E,8E,14Z,17Z)-eicosapentaenoate. Trans-2-decenoyl-ACP isomerase Trans-2,cis-3-decenoyl-ACP isomerase Beta-hydroxydecanoyl thioester dehydrase Trans-2-decenoyl-[acyl-carrier-protein] isomerase The cis-3-enoyl product is required to form unsaturated fatty acids, such as palmitoleic acid and cis-vaccenic acid, in dissociated (or type II) fatty-acid biosynthesis. While the enzyme from Escherichia coli is highly specific for the 10-carbon enoyl-ACP, the enzyme from Streptococcus pneumoniae can also use the 12-carbon enoyl-ACP as substrate in vitro but not 14-or 16-carbon enoyl-ACPs. ACP can be replaced by either CoA or N-acetylcysteamine thioesters. Trans-dec-2-enoyl-[acyl-carrier-protein] = cis-dec-3-enoyl-[acyl-carrier-protein]. Ascopyrone tautomerase APM tautomerase Ascopyrone isomerase Ascopyrone P tautomerase Ascopyrone intramolecular oxidoreductase 1,5-anhydro-D-glycero-hex-3-en-2-ulose tautomerase APTM Catalyzes one of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose. Ascopyrone P is an anti-oxidant. The other enzymes involved in this pathway are EC 4.2.1.110, EC 4.2.1.111 and EC 4.2.2.13. Isopentenylpyrophosphate isomerase Isopentenylpyrophosphate Delta-isomerase Isopentenyl-diphosphate Delta-isomerase IPP isomerase Methylbutenylpyrophosphate isomerase Isopentenyl diphosphate = dimethylallyl diphosphate. Magnesium or manganese or calcium FMN or FAD Vinylacetyl-CoA Delta-isomerase Vinylacetyl coenzyme A isomerase Also acts on 3-methyl-vinylacetyl-CoA. Vinylacetyl-CoA = crotonyl-CoA. Muconolactone Delta-isomerase Muconolactone isomerase (S)-5-oxo-2,5-dihydrofuran-2-acetate = 5-oxo-4,5-dihydrofuran-2-acetate. Cholestenol Delta-isomerase 5-alpha-cholest-7-en-3-beta-ol = 5-alpha-cholest-8-en-3-beta-ol. http://purl.uniprot.org/mim/302960 Methylitaconate Delta-isomerase Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.17.1.5, EC 1.3.7.1, EC 3.5.2.18, EC 1.1.1.291, EC 5.4.99.4, EC 4.2.1.85 and EC 4.1.3.32. Methylitaconate = 2,3-dimethylmaleate. Aconitate Delta-isomerase Aconitate isomerase Cis-aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. Trans-aconitate = cis-aconitate. This isomerization could take place either in a direct cis-trans interconversion or by an allelic rearrangement; the enzyme has been shown to catalyze the latter change. Dodecenoyl-CoA Delta-isomerase Delta(3),Delta(2)-enoyl-CoA isomerase Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase 3,2-trans-enoyl-CoA isomerase Acetylene-allene isomerase Dodecenoyl-CoA isomerase Also catalyzes the interconversion of 3-acetylenic fatty acyl thioesters and (+)-2,3-dienoyl fatty acyl thioesters, with fatty acid chain lengths C(6) to C(12). (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. Prostaglandin A isomerase Prostaglandin-A(1) Delta-isomerase (13E)-(15S)-15-hydroxy-9-oxoprosta-10,13-dienoate = (13E)-(15S)-15-hydroxy-9-oxoprosta-11,13-dienoate. Interconverts prostaglandin A(1) and prostaglandin C(1). Transposing S-S bonds Protein disulfide-isomerase S-S rearrangase Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange. Catalyzes the rearrangement of -S-S- bonds in proteins. Other intramolecular oxidoreductases PGD2 synthase PGH-PGD isomerase Prostaglandin-H2 D-isomerase Prostaglandin D2 synthase Prostaglandin-D synthase (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate. Brings about the opening of the epidioxy bridge. Glutathione Prostaglandin-H(2) E-isomerase Endoperoxide isomerase Prostaglandin-E synthase PGE isomerase PGH-PGE isomerase Glutathione Brings about the opening of the epidioxy bridge. (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate. PGI(2) synthetase Prostacyclin synthase PGI(2) synthase Prostaglandin-I synthase Heme-thiolate (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-6,9-alpha-epoxy-11-alpha,15-dihydroxyprosta-5,13-dienoate. Converts prostaglandin H(2) into prostaglandin I(2) (prostacyclin). Thromboxane-A synthase Thromboxane synthetase Thromboxane synthase http://purl.uniprot.org/mim/274180 Converts prostaglandin H(2) into thromboxane A(2). (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-9-alpha,11-alpha-epoxy-15-hydroxythromboxa-5,13-dienoate. Heme-thiolate Allene-oxide cyclase Allene oxides formed by the action of EC 4.2.1.92 are converted into cyclopentenone derivatives. (9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate = (15Z)-12-oxophyto-10,15-dienoate. Styrene-oxide isomerase SOI Highly specific. Styrene oxide = phenylacetaldehyde. CCS Capsanthin/capsorubin synthase Ketoxanthophyll synthase Capsanthin-capsorubin synthase (1) Violaxanthin = capsorubin. (2) Antheraxanthin = capsanthin. Isomerization of the epoxide ring of violaxanthin gives the cyclopentyl-ketone of capsorubin or capsanthin. Induced during chromoplast differentiation in plants. Neoxanthin synthase NSY The opening of the epoxide ring of violaxanthin generates a chiral allene. Violaxanthin = neoxanthin. Neoxanthin is a precursor of the plant hormone abscisic acid and the last product of carotenoid synthesis in green plants. Intramolecular transferases (mutases) Transferring acyl groups Lysolecithin migratase Lysolecithin acylmutase 2-lysolecithin = 3-lysolecithin. Precorrin-8X methylmutase Precorrin isomerase Hydrogenobyrinic acid-binding protein HBA synthase Precorrin-8X = hydrogenobyrinate. Phosphotransferases (phosphomutases) Phosphoglycerate phosphomutase Phosphoglycerate mutase Phosphoglyceromutase PGAM Also catalyze, slowly, the reactions of EC 5.4.2.4. The enzymes from mammals and from Saccharomyces cerevisiae are phosphorylated by (2R)-2,3-diphosphoglycerate, which is also an intermediate. With the rabbit muscle enzyme, dissociation of bisphosphate from the enzyme is much slower that the overall isomerization. http://purl.uniprot.org/mim/222800 2-phospho-D-glycerate = 3-phospho-D-glycerate. http://purl.uniprot.org/mim/261670 Enzymes from wheat, rice, insects and some fungi, however, have maximum activity in the absence of 2,3-diphosphophosphoglycerate, and were formerly listed under the present number as phosphoglycerate phosphomutase. Phosphoglucosamine mutase Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6-bisphosphate, which is an intermediate in the reaction, alpha-D-glucose 1,6-bisphosphate or ATP. The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate. Phosphoglucomutase Phosphoglucose mutase Glucose phosphomutase Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. Also, more slowly, catalyzes the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. Phosphoacetylglucosamine mutase Acetylglucosamine phosphomutase N-acetylglucosamine-phosphate mutase N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate. Activated by N-acetyl-alpha-D-glucosamine 1,6-bisphosphate. Bisphosphoglycerate synthase 2,3-bisphosphoglycerate synthase Diphosphoglyceromutase 2,3-diphosphoglycerate mutase 2,3-bisphosphoglycerate mutase Bisphosphoglycerate mutase BPGM Glycerate phosphomutase Diphosphoglycerate mutase http://purl.uniprot.org/mim/222800 The latter is rephosphorylated by the enzyme to yield 2,3-diphosphoglycerate, but this reaction is slowed down by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate. In the direction shown, the enzyme is phosphorylated by 3-phosphoglyceroyl phosphate to give phosphoenzyme and 3-phosphoglycerate. 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate. http://purl.uniprot.org/mim/261670 Also catalyzes, slowly, the reactions of EC 3.1.3.13 and EC 5.4.2.1. Glucose-1-phosphate phosphotransferase Phosphoglucomutase (glucose-cofactor) Glucose phosphomutase Activated by D-glucose, which probably acts as an acceptor for a phosphate residue from the substrate, thus being itself converted into the product. Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. Beta-phosphoglucomutase Beta-D-glucose 1-phosphate = beta-D-glucose 6-phosphate. Phosphodeoxyribomutase Deoxyribose phosphomutase Phosphopentomutase Deoxyribomutase Alpha-D-ribose 1,5-bisphosphate, 2-deoxy-alpha-D-ribose 1,5-bisphosphate, or alpha-D-glucose 1,6-bisphosphate can act as cofactor. Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate. Also converts 2-deoxy-alpha-D-ribose 1-phosphate into 2-deoxy-alpha-D-ribose 5-phosphate. Phosphomannomutase Phosphomannose mutase Alpha-D-mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor. http://purl.uniprot.org/mim/212065 Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate. PEP phosphomutase PEP mutase Phosphoenolpyruvate mutase Phosphoenolpyruvate phosphomutase Phosphoenolpyruvate = 3-phosphonopyruvate. Involved in the biosynthesis of the C-P bond, although the equilibrium greatly favors phosphoenolpyruvate. Transferring amino groups Lysine 2,3-aminomutase Activity is stimulated by S-adenosyl-L-methionine and pyridoxal phosphate. L-lysine = (3S)-3,6-diaminohexanoate. Beta-lysine mutase Beta-lysine 5,6-aminomutase (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate. Cobalamin Adenosylcobalamin-dependent D-lysine 5,6-aminomutase D-lysine 5,6-aminomutase D-alpha-lysine mutase D-lysine = 2,5-diaminohexanoate. Cobalamin D-alpha-ornithine 5,4-aminomutase D-ornithine 4,5-aminomutase D-ornithine aminomutase D-ornithine = (2R,4S)-2,4-diaminopentanoate. Pyridoxal-phosphate Cobalamin Dithiothreitol Tyrosine 2,3-aminomutase Tyrosine alpha,beta-mutase ATP L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate. Leucine 2,3-aminomutase (2S)-alpha-leucine = (3R)-beta-leucine. Cobalamin Glutamate-1-semialdehyde aminotransferase Glutamate-1-semialdehyde 2,1-aminomutase (S)-4-amino-5-oxopentanoate = 5-aminolevulinate. Transferring hydroxy groups (Hydroxyamino)benzene mutase Hydroxylaminobenzene hydroxymutase Hydroxylaminobenzene mutase HAB mutase (Hydroxyamino)benzene = 2-aminophenol. Isochorismate mutase Isochorismate synthetase Isochorismate synthase The reaction is reversible. Magnesium Chorismate = isochorismate. 3-(hydroxyamino)phenol mutase 3HAP mutase 3-hydroxylaminophenol mutase 3-hydroxyaminophenol = aminohydroquinone. Transferring other groups Glutamic mutase Beta-methylaspartate-glutamate mutase Methylaspartate mutase Glutamate isomerase Glutamic isomerase Glutamate mutase Methylaspartic acid mutase Cobalamin L-threo-3-methylaspartate = L-glutamate. Isomaltulose synthase Isomaltulose synthetase Sucrose glucosylmutase Sucrose = 6-O-alpha-D-glucopyranosyl-D-fructofuranose. Simultaneously produces isomaltulose (6-O-alpha-D-glucopyranosyl-D-fructose) and smaller amounts of trehalulose (1-O-alpha-D-glucopyranosyl-beta-D-fructose) from sucrose. tRNA-uridine isomerase tRNA-pseudouridine synthase I tRNA pseudouridylate synthase I The uridylate residues at positions 38, 39 and 40 of nearly all tRNAs are isomerized to pseudouridine. http://purl.uniprot.org/mim/600462 tRNA uridine = tRNA pseudouridine. Isobutyryl-CoA mutase Cobalt 2-methylpropanoyl-CoA = butanoyl-CoA. 4-methyl-2-enelactone methyl-isomerase 4-carboxymethyl-4-methylbutenolide mutase 4-methylmuconolactone methylisomerase 4-methyl-3-enelactone methyl isomerase 4-carboxymethyl-4-methylbut-2-en-1,4-olide = 4-carboxymethyl-3-methylbut-2-en-1,4-olide. (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase Maltodextrin alpha-D-glucosyltransferase (1,4)-alpha-D-glucan 1-alpha-D-glucosylmutase Malto-oligosyltrehalose synthase 4-((1->4)-alpha-D-glucosyl)(n-1)-D-glucose = 1-alpha-D-((1->4)-alpha-D-glucosyl)(n-1)-alpha-D-glucopyranoside. Not active toward maltose. Acts on (1->4)-alpha-D-glucans containing three or more (1->4)-alpha-linked D-glucose units. Trehalose synthase Maltose glucosylmutase Maltose alpha-D-glucosyltransferase Maltose = alpha,alpha-trehalose. Squalene--hopene cyclase The enzyme produces a constant ratio of about 5:1 hopene:hopanol. (2) Squalene + H(2)O = hopan-22-ol. (1) Squalene = hop-22(29)-ene. 5-(carboxyamino)imidazole ribonucleotide mutase N(5)-carboxyaminoimidazole ribonucleotide mutase N(5)-CAIR mutase 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate. The substrate is readily converted into 5-amino-1-(5-phospho-D-ribosyl)imidazole by non-enzymic decarboxylation. In eubacteria, fungi and plants, this enzyme, along with EC 6.3.4.18, is required to carry out the single reaction catalyzed by EC 4.1.1.21 in vertebrates. In the absence of EC 6.3.2.6, the reaction is reversible. (S)-methylmalonyl-CoA mutase Methylmalonyl coenzyme A mutase Methylmalonyl-CoA CoA-carbonyl mutase Methylmalonyl-CoA mutase (R)-2-methyl-3-oxopropanoyl-CoA CoA-carbonylmutase Methylmalonyl coenzyme A carbonylmutase (R)-methylmalonyl-CoA = succinyl-CoA. Cobalamin http://purl.uniprot.org/mim/251000 2-acetolactate mutase Acetohydroxy acid isomerase 2-acetolactate = 3-hydroxy-3-methyl-2-oxobutanoate. Ascorbate Also converts 2-aceto-2-hydroxybutanoate to 3-hydroxy-3-methyl-2-oxopentanoate. Alpha-methyleneglutarate mutase 2-methyleneglutarate mutase Cobalamin Other enzymes involved in this pathway are EC 1.17.1.5, EC 1.3.7.1, EC 3.5.2.18, EC 1.1.1.291, EC 5.3.3.6, EC 4.2.1.85 and EC 4.1.3.32. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. 2-methyleneglutarate = 2-methylene-3-methylsuccinate. Chorismate mutase Hydroxyphenylpyruvate synthase Chorismate = prephenate. Lanosterol synthase 2,3-epoxysqualene--lanosterol cyclase Squalene-2,3-oxide-lanosterol cyclase Oxidosqualene--lanosterol cyclase (S)-2,3-epoxysqualene = lanosterol. Cycloartenol synthase 2,3-epoxysqualene--cycloartenol cyclase (S)-2,3-epoxysqualene = cycloartenol. UDP-galactopyranose mutase UDP-D-galactopyranose = UDP-D-galacto-1,4-furanose. Intramolecular lyases Intramolecular lyases Cis,cis-muconate lactonizing enzyme I Muconate cycloisomerase Muconate lactonizing enzyme Muconate cycloisomerase I Manganese 2,5-dihydro-5-oxofuran-2-acetate = cis,cis-hexadienedioate. Not identical with EC 5.5.1.7 or EC 5.5.1.11. Also acts, in the reverse reaction, on 3-methyl-cis,cis-hexa-dienedioate and, very slowly, on cis,trans-hexadienedioate. Alpha-pinene-oxide decyclase Alpha-pinene oxide lyase Alpha-pinene oxide = (Z)-2-methyl-5-isopropylhexa-2,5-dienal. Both rings of pinene are cleaved in the reaction. Dichloromuconate cycloisomerase Also acts, in the reverse direction, on cis,cis-muconate and its monochloro-derivatives, but with lower affinity. Not identical with EC 5.5.1.1 or EC 5.5.1.7. 2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate = 2,4-dichloro-cis,cis-muconate. Manganese The product of cyclisomerization of dichloro-cis,cis-muconate spontaneously eliminates chloride to produce cis-4-carboxymethylene-3-chlorobut-2-en-4-olide. Copalyl diphosphate synthase Geranylgeranyl diphosphate = (+)-copalyl diphosphate. Part of a bifunctional enzyme involved in the biosynthesis of abietadiene. See also EC 4.2.3.18. Ent-copalyl diphosphate synthase Ent-kaurene synthase A Ent-kaurene synthetase A Geranylgeranyl diphosphate = ent-copalyl diphosphate. Part of a bifunctional enzyme involved in the biosynthesis of kaurene. See also EC 4.2.3.19. 3-carboxy-cis,cis-muconate cycloisomerase CMLE Beta-carboxymuconate lactonizing enzyme 3-carboxymuconate lactonizing enzyme 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate = cis,cis-butadiene-1,2,4-tricarboxylate. Tetrahydroxypteridine cycloisomerase Tetrahydroxypteridine = xanthine-8-carboxylate. Inositol 1-phosphate synthetase Myo-inositol-1-phosphate synthase Inositol-3-phosphate synthase Glucose 6-phosphate cyclase Glucocycloaldolase D-glucose 6-phosphate cycloaldolase D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate. NAD The NAD(+) dehydrogenates the -CHOH-group to -CO-at C-5 of the glucose 6-phosphate, making C-6 into an active methylene, able to condense with the -CHO at C-1; finally, the enzyme-bound NADH reconverts C-5 into the -CHOH-form. Carboxy-cis,cis-muconate cyclase 3-carboxy-cis,cis-muconate lactonizing enzyme 3-carboxymuconate cyclase 3-carboxy-2,5-dihydro-5-oxofuran-2-acetate = 3-carboxy-cis,cis-muconate. Chalcone isomerase Chalcone--flavonone isomerase A chalcone = a flavanone. Chloromuconate cycloisomerase Muconate cycloisomerase II 2-chloro-2,5-dihydro-5-oxofuran-2-acetate = 3-chloro-cis,cis-muconate. Not identical with EC 5.5.1.1 or EC 5.5.1.11. Spontaneous elimination of HCl produces cis-4-carboxymethylenebut-2-en-4-olide. Also acts in reverse direction on 2-chloro-cis,cis-muconate. Manganese Bornyl diphosphate synthase Bornyl pyrophosphate synthase Bornyl pyrophosphate synthetase Geranyl-diphosphate cyclase Geranyl diphosphate = (+)-bornyl diphosphate. Cycloeucalenol cycloisomerase Cycloeucalenol--obtusifoliol isomerase Opens the cyclopropane ring of a number of related 4-alpha-methyl-9-beta-19-cyclosterols, but not those with a 4-beta-methyl group, with formation of an 8(9) double bond. Cycloeucalenol = obtusifoliol. Involved in the synthesis of plant sterols. Other isomerases Sole sub-subclass for isomerases that do not belong in the other subclasses Isothiocyanate isomerase Thiocyanate isomerase Benzyl isothiocyanate = benzyl thiocyanate. Nicking-closing enzyme Swivelase DNA topoisomerase Type I DNA topoisomerase Relaxing enzyme DNA topoisomerase I Omega-protein Untwisting enzyme ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. Brings about the conversion of one topological isomer of DNA into another, e.g. the relaxation of superhelical turns in DNA, the interconversion of simple and knotted rings of single-stranded DNA, and the intertwisting of single-stranded rings of complementary sequences (cf. EC 5.99.1.3). DNA topoisomerase (ATP-hydrolyzing) DNA topoisomerase II DNA gyrase Type II DNA topoisomerase http://purl.uniprot.org/mim/208900 Can introduce negative superhelical turns into double-stranded circular DNA. One unit has nicking-closing activity, and another catalyzes super-twisting and hydrolysis of ATP (cf. EC 5.99.1.2). ATP-dependent breakage, passage and rejoining of double-stranded DNA. Ligases Forming carbon-oxygen bonds Ligases forming aminoacyl-tRNA and related compounds Tyrosine-transfer RNA ligase Tyrosine tRNA synthetase Tyrosyl-tRNA synthetase Tyrosine-transfer ribonucleate synthetase Tyrosyl-transfer RNA synthetase Tyrosyl-tRNA ligase Tyrosyl-transfer ribonucleate synthetase Tyrosine translase Tyrosyl-transfer ribonucleic acid synthetase Tyrosine--tRNA ligase L-tyrosine-tRNA(Tyr) ligase (AMP-forming) http://purl.uniprot.org/mim/608323 ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). Methionyl-transfer ribonucleate synthetase MetRS Methionine translase Methionine--tRNA ligase Methionyl-transfer RNA synthetase Methionyl-transfer ribonucleic acid synthetase Methionyl-tRNA synthetase In those organisms producing N-formylmethionyl-tRNA(fMet) for translation initiation, this enzyme also recognizes the initiator tRNA(fMet) and catalyzes the formation of L-methionyl-tRNA(fMet), the substrate for EC 2.1.2.9. ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met). Seryl-transfer RNA synthetase Seryl-transfer ribonucleate synthetase Seryl-transfer ribonucleic acid synthetase Seryl-tRNA synthetase SerRS Serine--tRNA ligase Serine translase ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). This enzyme also recognizes tRNA(Sec), the special tRNA for selenocysteine, and catalyzes the formation of L-seryl-tRNA(Sec), the substrate for EC 2.9.1.1. Aspartate--tRNA ligase Aspartyl-tRNA synthetase Aspartic acid translase ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). D-alanine--poly(phosphoribitol) ligase D-alanine: membrane acceptor ligase D-alanine-activating enzyme D-alanine-D-alanyl carrier protein ligase D-alanyl-poly(phosphoribitol) synthetase D-alanine-membrane acceptor ligase Involved in the synthesis of teichoic acids. A thioester bond is formed transiently between D-alanine and the sulfhydryl group of the 4'-phosphopantetheine prosthetic group of D-alanyl carrier protein during the activation of the alanine. ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate). Glycine--tRNA ligase Glycyl-tRNA synthetase Glycyl translase ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly). http://purl.uniprot.org/mim/601472 http://purl.uniprot.org/mim/600794 Prolyl-tRNA synthetase Proline translase Proline--tRNA ligase ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). Cysteine translase Cysteinyl-tRNA synthetase Cysteine--tRNA ligase ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). Glutamic acid translase Glutamyl-tRNA synthetase Glutamate--tRNA ligase ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). Glutamine--tRNA ligase Glutamine translase Glutaminyl-tRNA synthetase ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln). Arginyl-tRNA synthetase Arginine translase Arginine--tRNA ligase ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). Tryptophanyl-transfer ribonucleate synthetase Tryptophanyl-tRNA synthetase L-tryptophan-tRNA(Trp) ligase (AMP-forming) Tryptophan translase Tryptophanyl-transfer RNA synthetase Tryptophanyl ribonucleic synthetase Tryptophan--tRNA ligase Tryptophanyl-transfer ribonucleic synthetase Tryptophanyl-tRNA synthase Tryptophanyl-transfer ribonucleic acid synthetase TrpRS ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp). Phenylalanine translase Phenylalanine--tRNA ligase Phenylalanyl-tRNA synthetase ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). Histidyl-tRNA synthetase Histidine translase Histidine--tRNA ligase ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His). Asparagine translase Asparagine--tRNA ligase Asparaginyl-tRNA synthetase ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn). Aspartate--tRNA(Asn) ligase Nondiscriminating aspartyl-tRNA synthetase It has, however, diminished discrimination, so that it can also form aspartyl-tRNA(Asn). This accounts for the ability of this enzyme in, for example, Thermus thermophilus, to recognize both tRNA(Asp) (GUC anticodon) and tRNA(Asn) (GUU anticodon). This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon. When this enzyme acts on tRNA(Asp), it catalyzes the same reaction as EC 6.1.1.12. The aspartate-tRNA(Asn) is not used in protein synthesis until it is converted by EC 6.3.5.6 into asparaginyl-tRNA(Asn). ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + aspartyl-tRNA(Asx). Nondiscriminating glutamyl-tRNA synthetase Glutamate--tRNA(Gln) ligase The ability of this enzyme to recognize both tRNA(Glu) and one of the tRNA(Gln) isoacceptors derives from their sharing a major identity element, a hypermodified derivative of U34 (5-methylaminomethyl-2-thiouridine). The glutamyl-tRNA(Gln) is not used in protein synthesis until it is converted by EC 6.3.5.7 into glutaminyl-tRNA(Gln). This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon. This accounts for the ability of this enzyme in, for example, Bacillus subtilis, to recognize both tRNA(1)(Gln) (UUG anticodon) and tRNA(Glu) (UUC anticodon) but not tRNA(2)(Gln) (CUG anticodon). It has, however, diminished discrimination, so that it can also form glutamate-tRNA(Gln). When this enzyme acts on tRNA(Glu), it catalyzes the same reaction as EC 6.1.1.17. ATP + L-glutamate + tRNA(Glx) = AMP + diphosphate + glutamyl-tRNA(Glx). Lysine--tRNA(Pyl) ligase The tRNA and the ligase are encoded within the same gene cluster, and the ligase does not appear to be closely related to EC 6.1.1.6. ATP + L-lysine + tRNA(Pyl) = AMP + diphosphate + L-lysyl-tRNA(Pyl). In organisms such as Methanosarcina barkeri that incorporate the modified amino acid pyrrolysine (Pyl) into certain methylamine methyltransferases, an unusual tRNA(Pyl), with a CUA anticodon, is charged directly with pyrrolysine by this class II aminoacyl--tRNA ligase. Threonine--tRNA ligase Threonine translase Threonyl-tRNA synthetase ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). Leucine--tRNA ligase Leucine translase Leucyl-tRNA synthetase ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). Isoleucine translase Isoleucyl-tRNA synthetase Isoleucine--tRNA ligase ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). Lysine translase Lysyl-tRNA synthetase Lysine--tRNA ligase ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). Alanyl-tRNA synthetase Alanine--tRNA ligase Alanine translase ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). Valine translase Valine--tRNA ligase Valyl-tRNA synthetase ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). Forming carbon-sulfur bonds Acid--thiol ligases Acetate thiokinase Acetyl-activating enzyme Acyl-activating enzyme Acetyl-CoA synthetase Acetate--CoA ligase Acetyl-CoA synthase Also acts on propanoate and propenoate. ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. Acid--CoA ligase (GDP-forming) Acyl-CoA synthetase (GDP-forming) GTP + an acid + CoA = GDP + phosphate + acyl-CoA. Biotin--CoA ligase Biotinyl-CoA synthetase ATP + biotin + CoA = AMP + diphosphate + biotinyl-CoA. 4-coumaroyl-CoA synthase 4-coumarate--CoA ligase 4-coumaryl-CoA synthetase ATP + 4-coumarate + CoA = AMP + diphosphate + 4-coumaroyl-CoA. Acetate--CoA ligase (ADP-forming) Acetyl-CoA synthetase (ADP-forming) Acetate thiokinase Also acts on propanoate and, very slowly, on butanoate. ATP + acetate + CoA = ADP + phosphate + acetyl-CoA. 6-carboxyhexanoate--CoA ligase 6-carboxyhexanoyl-CoA synthetase Pimeloyl-CoA synthetase ATP + 6-carboxyhexanoate + CoA = AMP + diphosphate + 6-carboxyhexanoyl-CoA. Arachidonate--CoA ligase Arachidonoyl-CoA synthetase ATP + arachidonate + CoA = AMP + diphosphate + arachidonoyl-CoA. 8,11,14-icosatrienoate, but not the other long-chain fatty acids, can act in place of arachidonate. Not identical with EC 6.2.1.3. Acetoacetyl-CoA synthetase Acetoacetate--CoA ligase ATP + acetoacetate + CoA = AMP + diphosphate + acetoacetyl-CoA. Also acts, more slowly, on L-3-hydroxybutanoate. Propionate--CoA ligase Propionyl-CoA synthetase Not identical with EC 6.2.1.1 or EC 6.2.1.2. Propenoate can act instead of propanoate. ATP + propanoate + CoA = AMP + diphosphate + propanoyl-CoA. Citrate--CoA ligase Component of EC 4.1.3.8. ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA. Acyl-protein synthetase Long-chain-fatty-acid--luciferin-component ligase Together with EC 1.2.1.50 forms a fatty acid reductase system which produces the substrate of EC 1.14.14.3, thus being a component of the bacterial luciferase system. ATP + an acid + protein = AMP + diphosphate + an acyl-protein thioester. Fatty acid thiokinase (medium chain) Butyryl-CoA synthetase Acyl-activating enzyme Butyrate--CoA ligase ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA. Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy-and 2,3-or 3,4-unsaturated acids. Acyl-[acyl-carrier-protein] synthetase Long-chain-fatty-acid--[acyl-carrier-protein] ligase Not identical with EC 6.2.1.3. ATP + an acid + [acyl-carrier-protein] = AMP + diphosphate + acyl-[acyl-carrier-protein]. Citrate lyase ligase [Citrate (pro-3S)-lyase] ligase Citrate lyase synthetase Converts the inactive thiol form of EC 4.1.3.6 into the active form. ATP + acetate + [citrate (pro-3S)-lyase](thiol form) = AMP + diphosphate + [citrate (pro-3S)-lyase](acetyl form). Dicarboxylate--CoA ligase Acts on dicarboxylic acids of chain length C(5) to C(16); the best substrate is dodecanedioic acid. ATP + an alpha-omega-dicarboxylic acid = AMP + diphosphate + an omega-carboxyacyl-CoA. Phytanate--CoA ligase Not identical with EC 6.2.1.20. ATP + phytanate + CoA = AMP + diphosphate + phytanoyl-CoA. Benzoate--CoA ligase Also acts on 2-, 3-and 4-fluorobenzoate, but only very slowly on the corresponding chlorobenzoates. ATP + benzoate + CoA = AMP + diphosphate + benzoyl-CoA. o-succinylbenzoyl-CoA synthetase OSB-CoA synthetase o-succinylbenzoate--CoA ligase ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 2-succinylbenzoyl-CoA. 4-hydroxybenzoyl-CoA ligase 4-hydroxybenzoate-CoA synthetase 4-hydroxybenzoate--CoA ligase ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate + 4-hydroxybenzoyl-CoA. 3-alpha,7-alpha-dihydroxy-5-beta-cholestanate--CoA ligase DHCA-CoA ligase ATP + 3-alpha,7-alpha-dihydroxy-5-beta-cholestanate + CoA = AMP + diphosphate + 3-alpha,7-alpha-dihydroxy-5-beta-cholestanoyl-CoA. Acyl-CoA synthetase Fatty acid thiokinase (long chain) Acyl-activating enzyme Lignoceroyl-CoA synthase Long-chain-fatty-acid--CoA ligase Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA. The liver enzyme acts on acids from C(6) to C(20); that from brain shows high activity up to C(24). http://purl.uniprot.org/mim/300194 http://purl.uniprot.org/mim/300387 Phenylacetate--CoA ligase ATP + phenylacetate + CoA = AMP + diphosphate + phenylacetyl-CoA. Also acts, more slowly, on acetate, propanoate and butanoate, but not on hydroxy derivatives of phenylacetate and related compounds. 2-furoate--CoA ligase ATP + 2-furoate + CoA = AMP + diphosphate + 2-furoyl-CoA. Anthranilate--CoA ligase ATP + anthranilate + CoA = AMP + diphosphate + anthranilyl-CoA. 4-chlorobenzoate--CoA ligase 4-chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate. Magnesium Part of the bacterial 2,4-dichlorobenzoate degradation pathway. Trans-feruloyl--CoA synthase Trans-feruloyl-CoA synthetase Magnesium Ferulic acid + CoASH + ATP = trans-feruloyl-CoA + products of ATP breakdown. It has not yet been established whether AMP + diphosphate or ADP + phosphate are formed in this reaction. Succinyl-CoA synthetase (GDP-forming) Succinate--CoA ligase (GDP-forming) Itaconate can act instead of succinate and ITP instead of GTP. GTP + succinate + CoA = GDP + phosphate + succinyl-CoA. Succinyl-CoA synthetase (ADP-forming) Succinate thiokinase Succinate--CoA ligase (ADP-forming) ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. Glutaryl-CoA synthetase Glutarate--CoA ligase ATP + glutarate + CoA = ADP + phosphate + glutaryl-CoA. GTP or ITP can act instead of ATP. Choloyl-CoA synthetase Bile acid coenzyme A ligase BAL 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate--CoA ligase Cholate thiokinase 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoate-CoA ligase Trihydroxycoprostanoyl-CoA synthetase Cholate--CoA ligase 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate:CoA ligase (AMP-forming) 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoate-CoA synthetase Choloyl coenzyme A synthetase Cholic thiokinase 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl coenzyme A synthetase Cholic acid:CoA ligase THCA-CoA ligase Cholyl-CoA synthetase Bile acid CoA ligase Magnesium (2) ATP + (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate + CoA = AMP + diphosphate + (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA. This membrane-bound enzyme catalyzes the first step in the conjugation of bile acids with amino acids, converting bile acids into their acyl-CoA thioesters. Chenodeoxycholate, deoxycholate, lithocholate and trihydroxycoprostanoate can also act as substrates. The second step involves EC 2.3.1.65 and converts the acyl-CoA thioester into the corresponding N-acyl amidate by conjugation with glycine or taurine. (1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA. Oxalyl-CoA synthetase Oxalate--CoA ligase ATP + oxalate + CoA = AMP + diphosphate + oxalyl-CoA. Malate thiokinase Malyl-CoA synthetase Malate--CoA ligase ATP + malate + CoA = ADP + phosphate + malyl-CoA. Forming carbon-nitrogen bonds Acid--ammonia (or amide) ligases (amide synthases) Asparagine synthetase Aspartate--ammonia ligase ATP + L-aspartate + NH(3) = AMP + diphosphate + L-asparagine. Adenosylcobinamide-phosphate synthase (1) ATP + adenosylcobyric acid + (R)-1-aminopropan-2-yl phosphate = ADP + phosphate + adenosylcobinamide phosphate. (2) ATP + adenosylcobyric acid + (R)-1-aminopropan-2-ol = ADP + phosphate + adenosylcobinamide. One of the substrates for this reaction, (R)-1-aminopropan-2-yl phosphate, is produced by CobD (EC 4.1.1.81). This enzyme forms part of the anaerobic cobalamin biosynthesis pathway. Gamma-glutamylputrescine synthetase Glutamate--putrescine ligase Forms part of a bacterial putrescine utilization pathway. ATP + L-glutamate + putrescine = ADP + phosphate + gamma-L-glutamylputrescine. Asl(fm) D-aspartic acid-activating enzyme D-aspartate ligase In Enterococcus faecium, the substrate D-aspartate is produced by EC 5.1.1.13. Normally, the side chains the acylate the 6-amino group of the L-lysine residue contain L-Ala-L-Ala but these amino acids are replaced by D-Asp when D-Asp is included in the medium. ATP + D-aspartate + (beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n) = (beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala))(n) + ADP + phosphate. Forms part of the peptidoglycan assembly pathway of Gram-positive bacteria grown in medium containing D-Asp. Highly specific for D-aspartate, as L-aspartate, D-glutamate, D-alanine, D-iso-asparagine and D-malic acid are not substrates. Hybrid chains containing L-Ala-D-Asp, L-Ala-L-Ala-D-Asp or D-Asp-L-Ala are not formed. Glutamate--ammonia ligase Glutamine synthetase http://purl.uniprot.org/mim/610015 ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine. Also acts, more slowly, on 4-methylene-L-glutamate (cf. EC 6.3.1.7). Asparagine synthetase (ADP-forming) Aspartate--ammonia ligase (ADP-forming) ATP + L-aspartate + NH(3) = ADP + phosphate + L-asparagine. NAD(+) synthase NAD(+) synthetase ATP + deamido-NAD(+) + NH(3) = AMP + diphosphate + NAD(+). L-glutamine also acts, more slowly, as amido-donor (cf. EC 6.3.5.1). Theanine synthetase Glutamate--ethylamine ligase N(5)-ethyl-L-glutamine synthetase ATP + L-glutamate + ethylamine = ADP + phosphate + N(5)-ethyl-L-glutamine. 4-methyleneglutamate--ammonia ligase 4-methyleneglutamine synthetase ATP + 4-methylene-L-glutamate + NH(3) = AMP + diphosphate + 4-methylene-L-glutamine. Glutamine can act instead of NH(3), more slowly. Glutathione:spermidine ligase (ADP-forming) Glutathionylspermidine synthetase Gamma-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming) Glutathionylspermidine synthase GSP synthetase The enzyme from Escherichia coli is bifunctional and also catalyzes the EC 3.5.1.78 reaction, resulting in a net hydrolysis of ATP. Magnesium Gamma-L-glutamyl-L-cysteinyl-glycine + spermidine + ATP = N(1)-(gamma-L-glutamyl-L-cysteinyl-glycyl)-spermidine + ADP + phosphate. Involved in the synthesis of trypanothione in trypanosomatids. Trypanothione synthase TSR synthetase Involved in the synthesis of trypanothione in trypanosomatids. Gamma-L-glutamyl-L-cysteinyl-glycine + N(1)-(gamma-L-glutamyl-L-cysteinyl-glycyl)-spermidine + ATP = N(1),N(8)-bis-(gamma-L-glutamyl-L-cysteinyl-glycyl)-spermidine + ADP + phosphate. Magnesium Acid--D-amino-acid ligases (peptide synthases) Pantoate--beta-alanine ligase Pantothenate synthetase Pantoic-activating enzyme Pantoate-activating enzyme ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF synthetase UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine synthetase UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine synthetase UDP-MurNAc-pentapeptide synthetase UDP-MurNAc-L-Ala-D-Glu-L-Lys:D-Ala-D-Ala ligase UDP-N-acetylmuramoylalanine-D-glutamyl-lysine--D-alanyl-D-alanine ligase Uridine diphosphoacetylmuramoylpentapeptide synthetase UDPacetylmuramoylpentapeptide synthetase UDP-N-acetylmuramoylalanyl-D-glutamyl-lysine-D-alanyl-D-alanine ligase UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase Also catalyzes the reaction when the C-terminal residue of the tripeptide is meso-2,4-diaminoheptanedioate (acylated at its L-center), linking the D-Ala--D-Ala to the carboxy group of the L-center. ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine. Involved with EC 6.3.2.4, EC 6.3.2.7 or EC 6.3.2.13, EC 6.3.2.8 and EC 6.3.2.9 in the synthesis of a cell-wall peptide. Carnosine synthetase Carnosine synthase ATP + L-histidine + beta-alanine = AMP + diphosphate + carnosine. H(2)-folate synthetase FHFS 7,8-dihydropteroate:L-glutamate ligase (ADP) Dihydropteroate:L-glutamate ligase (ADP-forming) 7,8-dihydrofolate synthetase Folylpoly-(gamma-glutamate) synthetase-dihydrofolate synthase DHFS Dihydrofolate synthase FHFS/FPGS Dihydrofolate synthetase-folylpolyglutamate synthetase Dihydrofolate synthetase ATP + 7,8-dihydropteroate + L-glutamate = ADP + phosphate + 7,8-dihydropteroylglutamate. In contrast, the activities are located on separate proteins in most eukaryotes studied to date. In bacteria, a single protein catalyzes both this activity and that of EC 6.3.2.17, the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H(4)PteGlu(n)), i.e. various tetrahydrofolates. This enzyme is reponsible for attaching the first glutamate residue to dihydropteroate to form dihydrofolate and is present only in those organisms that have the ability to synthesize tetrahydrofolate de novo, e.g. plants, most bacteria, fungi and protozoa. UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase UDP-N-acetylmuramyl-tripeptide synthetase MurE synthetase UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelate synthetase UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diamino-heptanedioate ligase (ADP-forming) ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate. Involved with EC 6.3.2.4, EC 6.3.2.8, EC 6.3.2.9 and EC 6.3.2.10 in the synthesis of a cell-wall peptide. This enzyme adds diaminopimelate in Gram-negative organisms and in some Gram-positive organisms; in others EC 6.3.2.7 adds lysine instead. It is the amino group of the L-center of the diaminopimelate that is acylated. 2,3-dihydroxybenzoate--serine ligase N-(2,3-dihydroxybenzoyl)-serine synthetase ATP + 2,3-dihydroxybenzoate + L-serine = products of ATP breakdown + N-(2,3-dihydroxybenzoyl)-L-serine. D-alanyl-alanyl-poly(glycerolphosphate) synthetase D-alanine:membrane-acceptor ligase D-alanine--alanyl-poly(glycerolphosphate) ligase ATP + D-alanine + alanyl-poly(glycerolphosphate) = ADP + phosphate + D-alanyl-alanyl-poly(glycerolphosphate). Involved in the synthesis of teichoic acids. N(10)-formyltetrahydropteroyldiglutamate synthetase Tetrahydrofolate:L-glutamate gamma-ligase (ADP-forming) Tetrahydrofolate synthase Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase Folylpolyglutamate synthetase Folate polyglutamate synthetase Folylpolyglutamyl synthetase FPGS Formyltetrahydropteroyldiglutamate synthetase Folylpoly(gamma-glutamate) synthase Folylpolyglutamate synthase Tetrahydrofolylpolyglutamate synthase Folylpoly-gamma-glutamate synthase As the affinity of folate-dependent enzymes increases markedly with the number of glutamic residues, the tetrahydropteroyl polyglutamates are the preferred coenzymes of C(1) metabolism. In Arabidopsis thaliana, this enzyme is present as distinct isoforms in the mitochondria, the cytosol and the chloroplast. In contrast, the activities are located on separate proteins in most eukaryotes studied to date. ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1). In bacteria, a single protein catalyzes both this activity and that of EC 6.3.2.12, the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H(4)PteGlu(n)), i.e. various tetrahydrofolates (H(4)folate). Each isoform is encoded by a separate gene, a situation that is unique among eukaryotes. The enzymes from different sources (particularly eukaryotes versus prokaryotes) have different substrate specificities with regard to one-carbon substituents and the number of glutamate residues present on the tetrahydrofolates. Gamma-GHA synthetase Gamma-glutamylhistamine synthase ATP + L-glutamate + histamine = products of ATP breakdown + N(alpha)-gamma-L-glutamylhistamine. Ubiquitin--protein ligase Ubiquitin-conjugating enzyme Ubiquitin-activating enzyme Ubiquitin is coupled to protein by a peptide bond between the C-terminal glycine of ubiquitin and epsilon-amino groups of lysine residues in the protein. ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine. An intermediate in the reaction contains one ubiquitin residue bound as a thioester to the enzyme, and a residue of ubiquitin adenylate non-covalently bound to the enzyme. Gamma-glutamylcysteine synthetase Glutamate--cysteine ligase Gamma-glutamyl-L-cysteine synthetase ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine. Can use L-aminohexanoate in place of glutamate. http://purl.uniprot.org/mim/230450 IAA-lysine synthetase N-(indole-3-acetyl)-L-lysine synthetase Indoleacetate--lysine synthetase ATP + (indol-3-yl)acetate + L-lysine = ADP + phosphate + N(6)-((indol-3-yl)acetyl)-L-lysine. Ubiquitin--calmodulin ligase Ubiquityl-calmodulin synthetase Ubiquityl-calmodulin synthase n ATP + calmodulin + n ubiquitin = n AMP + n diphosphate + (ubiquitin)(n)-calmodulin. Specific for Ca(2+)-calmodulin from vertebrates. At least 3 ubiquitin molecules can be coupled to lysine residues in calmodulin. Diphthamide synthase Diphthine--ammonia ligase Diphthamide synthetase ATP + diphthine + NH(3) = ADP + phosphate + diphthamide. Homoglutathione synthase Homoglutathione synthetase Beta-alanine specific hGSH synthetase ATP + gamma-L-glutamyl-L-cysteine + beta-alanine = ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine. Not identical with EC 6.3.2.3. Kyotorphin synthase Kyotorphin-synthesizing enzyme Tyrosine--arginine ligase Tyrosyl-arginine synthase ATP + L-tyrosine + L-arginine = AMP + diphosphate + L-tyrosyl-L-arginine. TTL Tubulin--tyrosine ligase L-phenylalanine and 3,4-dihydroxy-L-phenylalanine are transferred but with higher Km values. The enzyme is highly specific for alpha-tubulin and moderately specific for ATP and L-tyrosine. L-tyrosine is linked via a peptide bond to the C-terminus of de-tyrosinated alpha-tubulin (des-Tyr(omega)-alpha-tubulin). ATP + detyrosinated alpha-tubulin + L-tyrosine = alpha-tubulin + ADP + phosphate. ACV synthetase L-alpha-aminoadipyl-cysteinyl-valine synthetase N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase L-2-aminohexanedioate + L-cysteine + L-valine + 3 ATP + H(2)O = N-(L-5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + 3 AMP + 3 diphosphate. The enzyme contains 4'-phosphopantetheine, which may be involved in the mechanism of the reaction. Forms part of the penicillin biosynthesis pathway. Magnesium Aerobactin synthase 4 ATP + citrate + 2 N(6)-acetyl-N(6)-hydroxy-L-lysine + 2 H(2)O = 4 ADP + 4 phosphate + aerobactin. Magnesium Aerobactin is one of a group of high-affinity iron chelators known as siderophores and is produced under conditions of iron deprivation. This is the last of the three enzymes involved in its synthesis, the others being EC 1.14.13.59 and EC 2.3.1.102. It is a dihydroxamate comprising two molecules of N(6)-acetyl-N(6)-hydroxylysine and one molecule of citric acid. L-amino-acid alpha-ligase Bacilysin synthetase L-amino acid alpha-ligase L-amino acid ligase ATP + an L-amino acid + an L-amino acid = ADP + phosphate + L-aminoacyl-L-amino acid. Magnesium or manganese While the enzyme has extremely broad substrate specificity, it does not accept highly charged amino acids, such as Lys, Arg, Glu and Asp, nor does it react with secondary amines such as Pro. The N-terminal residue of the alpha-dipeptide formed seems to be limited to Ala, Gly, Ser, Thr and Met (with Ala and Ser being the most preferred), whereas the C-terminal residue seems to allow for a wider variety of amino acids (but with a preference for Met and Phe). D-Ala, D-Ser and D-Phe are not substrates. However, not all combinations or dipeptides are formed; for example, while Ser is acceptable for the N-terminus and Thr for the C-terminus, a Ser-Thr dipeptide is not formed. Glutathione synthase GSH synthetase Glutathione synthetase http://purl.uniprot.org/mim/266130 ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione. http://purl.uniprot.org/mim/231900 D-alanyl-D-alanine synthetase D-alanine--D-alanine ligase D-Ala-D-Ala synthetase D-alanylalanine synthetase Alanine:alanine ligase (ADP-forming) Alanylalanine synthetase ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine. Involved with EC 6.3.2.7 or EC 6.3.2.13, EC 6.3.2.8, EC 6.3.2.9 and EC 6.3.2.10 in the synthesis of a cell-wall peptide. Phosphopantothenoylcysteine synthetase Phosphopantothenate--cysteine ligase Cysteine can be replaced by some of its derivatives. CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + PPi + N-((R)-4'-phosphopantothenoyl)-L-cysteine. 4-((N-succinylamino)carbonyl)-5-aminoimidazole ribonucleotide synthetase Phosphoribosylaminoimidazole-succinocarboxamide synthase Phosphoribosylaminoimidazolesuccinocarboxamide synthase Phosphoribosylaminoimidazole-succinocarboxamide synthetase Phosphoribosylaminoimidazolesuccinocarboxamide synthetase SAICAR synthase 4-(N-succinocarboxamide)-5-aminoimidazole synthetase 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase SAICARs SAICAR synthetase ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate. Forms part of the purine biosynthesis pathway. UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase L-lysine-adding enzyme Uridine diphospho-N-acetylmuramoylalanyl-D-glutamyllysine synthetase UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine synthetase UPD-MurNAc-L-Ala-D-Glu:L-Lys ligase MurE synthetase This enzyme adds lysine in some Gram-positive organisms; in others and in Gram-negative organisms EC 6.3.2.13 adds 2,6-diaminopimelate instead. Involved with EC 6.3.2.4, EC 6.3.2.8, EC 6.3.2.9 and EC 6.3.2.10 in the synthesis of a cell-wall peptide. ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine. Uridine 5'-diphosphate-N-acetylmuramyl-L-alanine synthetase UDP-N-acetylmuramoyl-L-alanine synthetase Uridine-diphosphate-N-acetylmuramate:L-alanine ligase Uridine diphosphate N-acetylmuramate:L-alanine ligase UDP-N-acetylmuramate--L-alanine ligase MurC synthetase Uridine diphospho-N-acetylmuramoylalanine synthetase L-alanine-adding enzyme UDP-acetylmuramyl-L-alanine synthetase UDPMurNAc-L-alanine synthetase UDP-N-acetylmuramyl:L-alanine ligase UDP-N-acetylmuramoylalanine synthetase Alanine-adding enzyme UDP-MurNAc:L-alanine ligase L-Ala ligase Involved with EC 6.3.2.4, EC 6.3.2.7 or EC 6.3.2.13, EC 6.3.2.9 and EC 6.3.2.10 in the synthesis of a cell-wall peptide. ATP + UDP-N-acetylmuramate + L-alanine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine. UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase D-glutamate-adding enzyme UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase UDP-N-acetylmuramoylalanine--D-glutamate ligase MurD synthetase UDP-Mur-NAC-L-Ala:D-Glu ligase D-glutamate ligase Uridine diphospho-N-acetylmuramoylalanyl-D-glutamate synthetase ATP + UDP-N-acetylmuramoyl-L-alanine + glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate. Involved with EC 6.3.2.4, EC 6.3.2.7 or EC 6.3.2.13, EC 6.3.2.8 and EC 6.3.2.10 in the synthesis of a cell-wall peptide. Cyclo-ligases AIR synthetase Phosphoribosylformylglycinamidine cyclo-ligase Phosphoribosyl-aminoimidazole synthetase AIR synthase AIRS Phosphoribosylaminoimidazole synthetase ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. Methenyl-THF synthetase 5,10-methenyltetrahydrofolate synthetase 5-Formyltetrahydrofolate cyclodehydrase 5-formyltetrahydrofolate cyclo-ligase ATP + 5-formyltetrahydrofolate = ADP + phosphate + 5,10-methenyltetrahydrofolate. DTB synthetase Dethiobiotin synthase ATP + 7,8-diaminononanoate + CO(2) = ADP + phosphate + dethiobiotin. CTP has half the activity of ATP. Beta-lactam synthetase (Carboxyethyl)arginine beta-lactam-synthase It has been proposed that L-N(2)-(2-carboxyethyl)arginine is first converted into an acyl-AMP by reaction with ATP and loss of diphosphate, and that the beta-lactam ring is then formed by the intramolecular attack of the beta-nitrogen on the activated carboxy group. ATP + L-N(2)-(2-carboxyethyl)arginine = AMP + diphosphate + deoxyamidinoproclavaminate. Forms part of the pathway for the biosythesis of the beta-lactamase inhibitor clavulanate in Streptomyces clavuligerus. Other carbon--nitrogen ligases GMP synthase Xanthosine-5'-phosphate--ammonia ligase XMP aminase ATP + xanthosine 5'-phosphate + NH(3) = AMP + diphosphate + GMP. Propionyl-CoA holocarboxylase synthetase Biotin--[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase Holocarboxylase synthetase Biotin-[propionyl-CoA-carboxylase (ATP-hydrolyzing)] synthetase http://purl.uniprot.org/mim/253270 ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]. Biotin--[methylcrotonoyl-CoA-carboxylase] synthetase Biotin--[methylcrotonoyl-CoA-carboxylase] ligase ATP + biotin + apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]. http://purl.uniprot.org/mim/253270 Gamma-glutamylmethylamide synthetase Glutamate--methylamine ligase ATP + L-glutamate + methylamine = ADP + phosphate + N(5)-methyl-L-glutamine. GAR synthetase Phosphoribosylglycinamide synthetase GARS Phosphoribosylamine--glycine ligase Glycinamide ribonucleotide synthetase ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. Biotin carboxylase ATP + biotin-carboxyl-carrier protein + CO(2) = ADP + phosphate + carboxybiotin-carboxyl-carrier protein. Biotin--protein ligase Biotin--[acetyl-CoA carboxylase] synthetase Acetyl-CoA carboxylase biotin holoenzyme synthetase Biotin--[acetyl-CoA-carboxylase] ligase http://purl.uniprot.org/mim/253270 ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]. Carbamoyl-phosphate synthase (ammonia) CPS I Carbamoyl-phosphate synthetase I Carbon-dioxide--ammonia ligase Carbamoylphosphate synthetase (ammonia) Carbamoyl-phosphate synthetase (ammonia) http://purl.uniprot.org/mim/265380 http://purl.uniprot.org/mim/237300 2 ATP + NH(3) + CO(2) + H(2)O = 2 ADP + phosphate + carbamoyl phosphate. Dihydrofolate formyltransferase Formyl dihydrofolate synthase Formate--dihydrofolate ligase ATP + formate + dihydrofolate = ADP + phosphate + 10-formyldihydrofolate. N(5)-CAIR synthetase N(5)-carboxyaminoimidazole ribonucleotide synthetase 5-(carboxyamino)imidazole ribonucleotide synthase Carboxyphosphate is the putative acyl phosphate intermediate. ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole + HCO(3)(-) = ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole. Involved in the late stages of purine biosynthesis. In Escherichia coli, this enzyme, along with EC 5.4.99.18, is required to carry out the single reaction catalyzed by EC 4.1.1.21 in vertebrates. UTP--ammonia ligase CTP synthetase CTP synthase Glutamine can replace NH(3). ATP + UTP + NH(3) = ADP + phosphate + CTP. Tetrahydrofolate formylase Formyltetrahydrofolate synthetase Tetrahydrofolic formylase Formate--tetrahydrofolate ligase In eukaryotes occurs as a trifunctional enzyme also having EC 1.5.1.5 and EC 3.5.4.9 activity. ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate. Adenylosuccinate synthase IMP--aspartate ligase Adenylosuccinate synthetase Succinoadenylic kinosynthetase GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. Argininosuccinate synthetase Arginine succinate synthetase Argininosuccinate synthase Citrulline--aspartate ligase ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. http://purl.uniprot.org/mim/215700 UALase ATP--urea amidolyase Urea carboxylase UCA Urease (ATP-hydrolyzing) Urea amidolyase Urea carboxylase (hydrolyzing) Biotin ATP + urea + HCO(3)(-) = ADP + phosphate + urea-1-carboxylate. The enzyme from the prokaryotic bacterium Oleomonas sagaranensis can also use acetamide and formamide as substrates. The Saccharomyces cerevisiae enzyme (but not that from green algae) also catalyzes the reaction of EC 3.5.1.54, thus bringing about the hydrolysis of urea to CO(2) and NH(3). Ribose-5-phosphate--ammonia ligase Ribose 5-phosphate aminotransferase 5-phosphoribosylamine synthetase ATP + ribose 5-phosphate + NH(3) = ADP + phosphate + 5-phosphoribosylamine. 5-phosphoribosylimidazoleacetate synthetase Imidazoleacetate--phosphoribosyldiphosphate ligase ATP + imidazole-4-acetate + 5-phosphoribosyl diphosphate = ADP + phosphate + 1-(5-phosphoribosyl)imidazole-4-acetate + diphosphate. Biotin-transcarboxylase synthetase Biotin--[methylmalonyl-CoA-carboxyltransferase] ligase Biotin--[methylmalonyl-CoA-carboxyltransferase] synthetase Biotin--[methylmalonyl-CoA-carboxytransferase] synthetase Biotin--[methylmalonyl-CoA-carboxytransferase] ligase http://purl.uniprot.org/mim/253270 ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] = AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxytransferase]. Carbon--nitrogen ligases with glutamine as amido-N-donor NAD(+) synthase (glutamine-hydrolyzing) Nicotinamide adenine dinucleotide synthetase (glutamine) NAD(+) synthetase (glutamine-hydrolyzing) NH(3) can act instead of glutamine (cf. EC 6.3.1.5). ATP + deamido-NAD(+) + L-glutamine + H(2)O = AMP + diphosphate + NAD(+) + L-glutamate. Adenosylcobyric acid synthase (glutamine-hydrolyzing) Cobyric acid synthase Ado-cobyric acid synthase (glutamine hydrolyzing) 5'-deoxy-5'-adenosylcobyrinic-acid-a,c-diamide:L-glutamine amido-ligase NH(3) can act instead of glutamine. Magnesium 4 ATP + adenosylcobyrinic acid a,c-diamide + 4 L-glutamine + 4 H(2)O = 4 ADP + 4 phosphate + adenosylcobyric acid + 4 L-glutamate. This enzyme catalyzes the four-step amidation sequence from cobyrinic acid a,c-diamide to cobyric acid via the formation of cobyrinic acid triamide, tetraamide and pentaamide intermediates. GMP synthetase (glutamine-hydrolyzing) GMP synthase (glutamine-hydrolyzing) Glutamine amidotransferase ATP + xanthosine 5'-phosphate + L-glutamine + H(2)O = AMP + diphosphate + GMP + L-glutamate. FGAM synthetase FGAR amidotransferase Formylglycinamide ribotide amidotransferase FGARAT FGAM synthase Phosphoribosylformylglycinamidine synthetase Phosphoribosylformylglycinamidine synthase ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate. Asparagine synthase (glutamine-hydrolyzing) Glutamine-dependent asparagine synthetase AS-B Asparagine synthetase B Asparagine synthetase (glutamine-hydrolyzing) The ammonia released is channeled to the other active site to yield asparagine. The enzyme catalyzes three distinct chemical reactions: glutamine hydrolysis to yield ammonia takes place in the N-terminal domain. ATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate. The enzyme from Escherichia coli has two active sites that are connected by an intramolecular ammonia tunnel. The C-terminal active site mediates both the synthesis of a beta-aspartyl-AMP intermediate and its subsequent reaction with ammonia. Carbamoyl-phosphate synthase (glutamine-hydrolyzing) Carbamoyl phosphate synthetase Carbamoyl-phosphate synthetase (glutamine-hydrolyzing) Carbamyl phosphate synthetase (glutamine) Glutamine-dependent carbamoyl-phosphate synthase Carbamoylphosphate synthetase II CPS Glutamine-dependent carbamyl phosphate synthetase GD-CPSase The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. The carboxy-phosphate intermediate is formed by the phosphorylation of bicarbonate by ATP at a site contained within the N-terminal half of the large subunit. 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. The ammonia migrates through the interior of the protein, where it reacts with carboxy phosphate to produce the carbamate intermediate. The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate. The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length. The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate. Asparaginyl-tRNA synthase (glutamine-hydrolyzing) Aspartyl-tRNA(Asn) amidotransferase Asp-tRNA(Asn) amidotransferase Asp-AdT The aspartyl-tRNA(Asn) is not used in protein synthesis until the present enzyme converts it into asparaginyl-tRNA(Asn) (aspartyl-tRNA(Asp) is not a substrate for this reaction). This reaction forms part of a two-reaction system for producing asparaginyl-tRNA in Deinococcus radiodurans and other organisms lacking a specific enzyme for asparagine synthesis. In the first step, a non-discriminating ligase (EC 6.1.1.23) mischarges tRNA(Asn) with aspartate, leading to the formation of aspartyl-tRNA(Asn). Ammonia or asparagine can substitute for the preferred substrate glutamine. ATP + aspartyl-tRNA(Asn) + L-glutamine = ADP + phosphate + asparaginyl-tRNA(Asn) + L-glutamate. Glutamyl-tRNA(Gln) amidotransferase Glutaminyl-tRNA synthase (glutamine-hydrolyzing) Glu-tRNA(Gln) amidotransferase Glu-AdT The glutamyl-tRNA(Gln) is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNA(Gln) (glutamyl-tRNA(Glu) is not a substrate for this reaction). In systems lacking discernible EC 6.1.1.18, glutaminyl-tRNA(Gln) is formed by a two-enzyme system. Ammonia or asparagine can substitute for the preferred substrate glutamine. In the first step, a nondiscriminating ligase (EC 6.1.1.24) mischarges tRNA(Gln) with glutamate, forming glutamyl-tRNA(Gln). ATP + glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + glutaminyl-tRNA(Gln) + L-glutamate. PabB ADC synthase 4-amino-4-deoxychorismate synthase Aminodeoxychorismate synthase The enzyme is composed of two parts, PabA and PabB. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. Chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate. In the absence of PabA and glutamine, PabB converts ammonia and chorismate into 4-amino-4-deoxychorismate (in the presence of Mg(2+)). This enzyme is coupled with EC 4.1.3.38, to form p-aminobenzoate. Hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolyzing) 2 ATP + hydrogenobyrinic acid + 2 L-glutamine + 2 H(2)O = 2 ADP + 2 phosphate + hydrogenobyrinic acid a,c-diamide + 2 L-glutamate. This step in the aerobic biosynthesis of cobalamin generates hydrogenobyrinic acid a,c-diamide, the substrate required by EC 6.6.1.2, which adds cobalt to the macrocycle. Forming carbon-carbon bonds Ligases that form carbon-carbon bonds Pyruvic carboxylase Pyruvate carboxylase Biotin The animal enzyme requires acetyl-CoA. http://purl.uniprot.org/mim/266150 Manganese or zinc ATP + pyruvate + HCO(3)(-) = ADP + phosphate + oxaloacetate. Acetyl-CoA carboxylase Also catalyzes transcarboxylation; the plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA. http://purl.uniprot.org/mim/200350 ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA. Biotin Propionyl-CoA carboxylase PCCase Biotin http://purl.uniprot.org/mim/606054 ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl-CoA. Also carboxylates butanoyl-CoA and catalyzes transcarboxylation. Methylcrotonoyl-CoA carboxylase Methylcrotonyl-CoA carboxylase Beta-methylcrotonyl-CoA carboxylase ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA. Biotin http://purl.uniprot.org/mim/210210 http://purl.uniprot.org/mim/210200 Geranoyl-CoA carboxylase Geranyl-CoA carboxylase Biotin ATP + geranoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA. Also carboxylates dimethylpropenoyl-CoA and farnesoyl-CoA. Acetone carboxylase The enzyme from Xanthobacter sp. strain Py2 also carboxylates butan-2-one to 3-oxopentanoate. Acetone + CO(2) + ATP + 2 H(2)O = acetoacetate + AMP + 2 phosphate. Magnesium 2-oxoglutarate carboxylase CFI OGC Oxalosuccinate synthetase Carboxylating factor for ICDH The product of the reaction is unstable and is quickly converted into isocitrate by the action of EC 1.1.1.41. It was originally thought that this enzyme was a promoting factor for the carboxylation of 2-oxoglutarate by EC 1.1.1.41, but this has since been disproved. Magnesium Biotin ATP + 2-oxoglutarate + HCO(3)(-) = ADP + phosphate + oxalosuccinate. Forming phosphoric ester bonds Ligases that form phosphoric-ester bonds Polynucleotide ligase (ATP) DNA repair enzyme Sealase DNA ligase (ATP) DNA joinase Polydeoxyribonucleotide synthase (ATP) http://purl.uniprot.org/mim/606593 ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m). Catalyzes the formation of a phosphodiester at the site of a single-strand break in duplex DNA. RNA can also act as substrate, to some extent. DNA repair enzyme Polynucleotide ligase (NAD+) Polydeoxyribonucleotide synthase (NAD+) DNA joinase DNA ligase (NAD(+)) Polynucleotide ligase (NAD(+)) Polydeoxyribonucleotide synthase (NAD(+)) Catalyzes the formation of a phosphodiester at the site of a single-strand break in duplex DNA. NAD(+) + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide + (deoxyribonucleotide)(n+m). RNA can also act as substrate, to some extent. Polyribonucleotide synthase (ATP) RNA ligase (ATP) Ribonucleic ligase Converts linear RNA to a circular form by transfer of the 5'-phosphate to the 3'-hydroxy terminus. ATP + (ribonucleotide)(n) + (ribonucleotide)(m) = AMP + diphosphate + (ribonucleotide)(n+m). RNA-3'-phosphate cyclase RNA 3'-terminal phosphate cyclase RNA cyclase ATP + RNA 3'-terminal-phosphate = AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate. Adenosine 5'-(gamma-thio)triphosphate can act instead of ATP. Forming nitrogen-metal bonds Forming coordination complexes Magnesium-protoporphyrin chelatase Protoporphyrin IX Mg-chelatase Mg-chelatase Magnesium-protoporphyrin IX chelatase Mg-protoporphyrin IX magnesio-lyase Magnesium chelatase Mg-protoporphyrin IX chelatase Protoporphyrin IX magnesium-chelatase Magnesium-chelatase This is the first committed step of chlorophyll biosynthesis and is a branchpoint of two major routes in the tetrapyrrole pathway. ATP + protoporphyrin IX + Mg(2+) + H(2)O = ADP + phosphate + Mg-protoporphyrin IX + 2 H(+). Cobaltochelatase Hydrogenobyrinic acid a,c-diamide cobaltochelatase ATP + hydrogenobyrinic acid a,c-diamide + Co(2+) = ADP + phosphate + cob(II)yrinic acid a,c-diamide + H(+). This enzyme, which forms part of the aerobic cobalamin biosynthesis pathway, is a type I chelatase, being heterotrimeric and ATP-dependent. ATP can be replaced by dATP or CTP but the reaction proceeds more slowly. Hydrogenobyrinic acid is a very poor substrate. The oligomeric protein CobST possesses at least one sulfhydryl group that is essential for ATP-binding. CobN exhibits a high affinity for hydrogenobyrinic acid a,c-diamide. It comprises two components, one of which corresponds to CobN and the other is composed of two polypeptides, specified by cobS and cobT in Pseudomonas denitrificans, and rdfs:labeld CobST. Once the Co(2+) is inserted, the next step in the pathway ensures that the cobalt is ligated securely by reducing Co(II) to Co(I); this step is carried out by EC 1.16.8.1.