An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.

EC 1.1.1.255

Recommended name: mannitol dehydrogenase

Reaction: D-mannitol + NAD = D-mannose + NADH₂

Other name(s): MTD; NAD-dependent mannitol dehydrogenase

Systematic name: mannitol:NAD 1-oxidoreductase

Comments: The enzyme from Apium graveolens (celery) oxidises alditols with a minimum requirement of 2R chirality at the carbon adjacent to the primary carbon undergoing the oxidation. The enzyme is specific for NAD and does not use NADP.

References:

1. Stoop, J.M.H. and Pharr, D.M. Partial purification and characterization of mannitol: mannose 1-oxidoreductase from celeriac (Apium graveolens var. rapaceum) roots. Arch. Biochem. Biophys. 298 (1992) 612-619. [Medline UI: 93037501]

2. Stoop, J.M.H., Williamson, J.D., Conkling, M.A. and Pharr, D.M. Purification of NAD-dependent mannitol dehydrogenase from celery suspension cultures. Plant Physiol. (1995) 108 (1995) 1219-1225. [Medline UI: 95357413]

3. Williamson, J.D., Stoop, J.M.H., Massel, M.O., Conkling, M.A. and Pharr, D.M. Sequence analysis of a mannitol dehydrogenase cDNA from plants reveals a function for the pathogenesis-related protein ELI3. Proc. Natl. Acad. Sci. USA 92 (1995) 7148-7152. [Medline UI: 95365325]

4. Stoop, J.M.H., Chilton, W.S. and Pharr, D.M. Substrate specificity of the NAD-dependent mannitol dehydrogenase from celery. Phytochemistry 43 (1996) 1145-1150.

EC 1.1.1.256

Recommended name: fluoren-9-ol dehydrogenase

Reaction: fluoren-9-ol + 2 NAD(P) = fluoren-9-one + 2 NADPH₂

Systematic name: fluoren-9-ol:NAD(P) oxidoreductase

Comments: Involved in the pathway for fluorene metabolism in Arthrobacter sp.

References:

1. Casellas, M., Grifoll, M., Bayona, J.M. and Solanas, A.M. New metabolites in the degradation of fluorene by Arthrobacter sp. strain F101. Appl. Environ. Microbiol. 63 (1997) 819-826. [Medline UI: 97208201]

2. Grifoll, M., Casellas, M., Bayona, J.M. and Solanas, A.M. Isolation and characterization of a fluorene-degrading bacterium: identification of ring oxidation and ring fission products. Appl. Environ. Microbiol. 58 (1992) 2910-2917. [Medline UI: 93073895]

EC 1.1.1.257

Recommended name: 4-(hydroxymethyl)benzenesulfonate dehydrogenase

Reaction: 4-(hydroxymethyl)benzenesulfonate + NAD = 4-formylbenzenesulfonate + NADH₂

Systematic name: 4-(hydroxymethyl)benzenesulfonate:NAD oxidoreductase

Comments: Involved in the toluene-4-sulfonate degradation pathway in Comamonas testosteroni.

References:

1. Junker, F., Saller, E., Schläfli Oppenberg, H.R., Kroneck, P.M., Leisinger, T. and Cook, A.M. Degradative pathways for p-toluenecarboxylate and p-toluenesulfonate and their multicomponent oxygenases in Comamonas testosteroni strains PSB-4 and T-2. Microbiology 142 (1996) 2419-2427. [Medline UI: 96425866]

EC 1.1.1.258

Recommended name: 6-hydroxyhexanoate dehydrogenase

Reaction: 6-hydroxyhexanoate + NAD = 6-oxohexanoate + NADH₂

Systematic name: 6-hydroxyhexanoate:NAD oxidoreductase

Comments: Involved in the cyclohexanol degradation pathway in Acinetobacter NCIB 9871.

References:

1. Donoghue, N.A. and Trudgill, P.W. The metabolism of cyclohexanol by Acinetobacter NCIB 9871. Eur. J. Biochem. 60 (1975) 1-7. [Medline UI: 76091952]

2. Hecker, L.I., Tondeur, Y. and Farrelly, J.G. Formation of ε-hydroxycaproate and ε-aminocaproate from N-nitrosohexamethyleneimine: evidence that microsomal α-hydroxylation of cyclic nitrosamines may not always involve the insertion of molecular oxygen into the substrate. Chem. Biol. Interact. 49 (1984) 235-248. [Medline UI: 84205831]

EC 1.1.1.259

Recommended name: 3-hydroxypimeloyl-CoA dehydrogenase

Reaction: 3-hydroxypimeloyl-CoA + NAD = 3-oxopimeloyl-CoA + NADH₂

Systematic name: 3-hydroxypimeloyl-CoA:NAD oxidoreductase

Comments: Involved in the anaerobic pathway of benzoate degradation in bacteria.

References:

1. Harwood, C.S. and Gibson, J. Shedding light on anaerobic benzene ring degradation: a process unique to prokaryotes? J. Bacteriol. 179 (1997) 301-309. [Medline UI: 97144512]

EC 1.2.1.60

Recommended name: 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase

Reaction: 5-carboxymethyl-2-hydroxymuconate semialdehyde + H₂O + NAD = 5-carboxymethyl-2-hydroxymuconate + NADH₂

Other name(s): carboxymethylhydroxymuconic semialdehyde dehydrogenase

Systematic name: 5-carboxymethyl-2-hydroxymuconic-semialdehyde:NAD oxidoreductase

Comments: Involved in the tyrosine degradation pathway in Arthrobacter sp.

References:

1. Blakley, E.R. The catabolism of L-tyrosine by an Arthrobacter sp. Can. J. Microbiol. 23 (1977) 1128-1139. [Medline UI: 78001412]

2. Alonso, J.M. and Garrido-Pertierra, A. Carboxymethylhydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli. Biochim. Biophys. Acta 719 (1982) 165-167. [Medline UI: 83075498]

3. Cooper R.A. and Skinner M.A. Catabolism of 3- and 4-hydroxyphenylacetate by the 3,4-dihydroxyphenylacetate pathway in Escherichia coli. J. Bacteriol. 143 (1980) 302-306. [Medline UI: 80249373] 4. Garrido-Pertierra, A. and Cooper, R.A. Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4-hydroxyphenylacetate pathway of Escherichia coli. Eur. J. Biochem. 117 (1981) 581-584.

EC 1.2.1.61

Recommended name: 4-hydroxymuconic semialdehyde dehydrogenase

Reaction: 4-hydroxymuconic semialdehyde + NAD + H₂O = maleylacetate + NADH₂

Systematic name: 4-hydroxymuconic-semialdehyde:NAD oxidoreductase

Comments: Involved in the 4-nitrophenol degradation pathway.

References:

1. Spain, J.C. and Gibson, D.T. Pathway for bioremediation of p-nitrophenol in a Moraxella sp. Appl. Environ. Microbiol. 57 (1991) 812-819.

EC 1.2.1.62

Recommended name: 4-formylbenzenesulfonate dehydrogenase

Reaction: 4-formylbenzenesulfonate + NAD + H₂O = 4-sulfobenzoate + NADH₂

Systematic name: 4-formylbenzenesulfonate:NAD oxidoreductase

Comments: Involved in the toluene-4-sulfonate degradation pathway.

References:

1. Junker, F., Saller, E., Schläfli Oppenberg, H.R., Kroneck, P.M., Leisinger, T. and Cook, A.M. Degradative pathways for p-toluenecarboxylate and p-toluenesulfonate and their multicomponent oxygenases in Comamonas testosteroni strains PSB-4 and T-2. Microbiology 142 (1996) 2419-2427. [Medline UI: 96425866]

2. Junker, F., Kiewitz, R. and Cook, A.M. Characterization of the p-toluenesulfonate operon tsaMBCD and tsaR in Comamonas testosteroni T-2. J. Bacteriol. 179 (1997) 919-927. [Medline UI: 97158690]

EC 1.2.1.63

Recommended name: 6-oxohexanoate dehydrogenase

Reaction: 6-oxohexanoate + NADP + H₂O= adipate + NADPH₂

Systematic name: 6-oxohexanoate:NADP oxidoreductase

Comments: Last step in the cyclohexanol degradation pathway in Acinetobacter sp.

References:

1. Davey, J.F. and Trudgill, P.W. The metabolism of trans-cyclohexan-1,2-diol by an Acinetobacter species. Eur. J. Biochem. 74 (1977) 115-127. [Medline UI: 77161994]

2. Donoghue, N.A. and Trudgill P.W. The metabolism of cyclohexanol by Acinetobacter NCIB 9871. Eur. J. Biochem. 60 (1975) 1-7. [Medline UI: 76091952]

EC 1.2.1.64

Recommended name: 4-hydroxybenzaldehyde dehydrogenase

Reaction: 4-hydroxybenzaldehyde + NAD + H₂O = 4-hydroxybenzoate + NADH₂

Other name(s): p-hydroxybenzaldehyde dehydrogenase

Systematic name: 3-hydroxybenzaldehyde:NAD oxidoreductase

Comments: Involved in the toluene degradation pathway in Pseudomonas mendocina.

References:

1. Bossert, I.D., Whited, G., Gibson, D.T. and Young, L.Y. Anaerobic oxidation of p-cresol mediated by a partially purified methylhydroxylase from a denitrifying bacterium. J. Bacteriol. 171 (1989) 2956-2962. [Medline UI: 89255047]

2. Whited, G.M. and Gibson, D.T. Separation and partial characterization of the enzymes of the toluene-4-monooxygenase catabolic pathway in Pseudomonas mendocina KR1. J. Bacteriol. 173 (1991) 3017-3020. [Medline UI: 91210195]

EC 1.2.1.65

Recommended name: salicylaldehyde dehydrogenase

Reaction: salicylaldehyde + NAD + H₂O = salicylate + NADH₂

Systematic name: salicylaldehyde:NAD oxidoreductase

Comments: Involved in the naphthalene degradation pathway in some bacteria.

References:

1. Eaton, R. and Chapman, P.J. Bacterial metabolism of naphthalene: construction and use of recombinant bacteria to study ring cleavage of 1,2-dihydroxynaphthalene and subsequent reactions. J. Bacteriol. 174 (1992) 7542-7554. [Medline UI: 93077433]

EC 1.2.1.66

Recommended name: mycothiol-dependent formaldehyde dehydrogenase

Reaction: formaldehyde + mycothiol + NAD = S -formylmycothiol + NADH₂

Other name(s) NAD/factor-dependent formaldehyde dehydrogenase

Systematic name: formaldehyde:NAD oxidoreductase (mycothiol-formylating)

Comments: A similar reaction to that of EC 1.2.1.1 [formaldehyde dehydrogenase (glutathione)], except that mycothiol {1-O-[2-(N-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-D-myo-inositol} replaces glutathione. The S-formylmycothiol formed hydrolyses to mycothiol and formate.

References:

1. Misset-Smits, M., Van Ophem, P.W., Sakuda, S. and Duine, J.A. Mycothiol, 1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-α-D-glucopyranosyl)-D-myo-inositol, is the factor of NAD/factor-dependent formaldehyde dehydrogenase. FEBS Lett. 409 (1997) 221-222. [Medline UI: 97345657]

2. Norin, A., Van Ophem, P.W., Piersma, S.R., Person, B., Duine, J.A. and Jornvall, H. Mycothiol-dependent formaldehyde dehydrogenase, a prokaryotic medium-chain dehydrogenase/reductase, phylogenetically links different eukaryotic alcohol dehydrogenase's - primary structure, conformational modelling and functional correlations. Eur. J. Biochem. 248 (1997) 282-289. [Medline UI: 98004265]

EC 1.2.3.12

Recommended name: vanillate demethylase

Reaction: vanillate + O₂ + NADH₂ = 3,4-dihydroxybenzoate + NAD + H₂O + formaldehyde

Other name(s): 4-hydroxy-3-methoxybenzoate demethylase

Systematic name: vanillate:oxygen oxidoreductase (demethylating)

Comments: Forms part of the vanillin degradation pathway in Arthrobacter sp.

References:

1. Brunel, F. and Davison, J. Cloning and sequencing of Pseudomonas genes encoding vanillate demethylase. J. Bacteriol. 170 (1988) 4924-4930. [ Medline UI: 89008117]

2. Priefert, H., Rabenhorst, J. and Steinbuchel, A. Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate. J. Bacteriol. 179 (1997) 2595-2607. [Medline UI: 97252489]

EC 1.2.3.13

Recommended name: 4-hydroxyphenylpyruvate oxidase

Reaction: 4-hydroxyphenylpyruvate + 1/2 O₂ = 4-hydroxyphenylacetate + CO₂

Systematic name: 4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating)

Comments: Involved in tyrosine degradation pathway in Arthrobacter sp.

References:

1. Blakley, E.R. The catabolism of L-tyrosine by an Arthrobacter sp. Can. J. Microbiol. 23 (1977) 1128-1139. [Medline UI: 78001412]

EC 1.3.1.56

Recommended name: cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase

Reaction: cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD = biphenyl-2,3-diol + NADH₂

Other name(s): 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase

Systematic name: cis-3-phenylcyclohexa-3,5-diene-1,2-diol:NAD oxidoreductase

Comments: Catalyses the second step in the biphenyl degradation pathway in bacteria.

References:

1. Sylvestre, M., Hurtubise, Y., Barriault, D., Bergeron, J. and Ahmad, D. Characterization of active recombinant 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase from Comamonas testosteroni B-356 and sequence of the encoding gene (bphB). Appl. Environ. Microbiol. 62 (1996) 2710-2715. [Medline UI: 96316386]

2. Fukuda, M., Yasukochi, Y., Kikuchi, Y., Nagata, Y., Kimbara, K., Horiuchi, H., Takagi, M. and Yano, K. Identification of the bphA and bphB genes of Pseudomonas sp. strains KKS102 involved in degradation of biphenyl and polychlorinated biphenyls. Biochem. Biophys. Res. Commun. 202 (1994) 850-856. [Medline UI: 94324977]

3. Hofer, B., Eltis, L.D., Dowling, D.N. and Timmis, K.N. Genetic analysis of a Pseudomonas locus encoding a pathway for biphenyl/polychlorinated biphenyl degradation. Gene 130 (1993) 47-55. [Medline UI: 93345822]

EC 1.3.1.57

Recommended name: phloroglucinol reductase

Reaction: dihydrophloroglucinol + NADP = phloroglucinol + NADPH₂

Systematic name: dihydrophloroglucinol:NADP oxidoreductase

Comments: Involved in the gallate anaerobic degradation pathway in bacteria.

References:

1. Haddock, J.D. and Ferry, J.G. Purification and properties of phloroglucinol reductase from Eubacterium oxidoreducens G-41. J. Biol. Chem. 264 (1989) 4423-4427. [Medline UI: 89174692]

EC 1.3.1.58

Recommended name: 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase

Reaction: cis-5,6-dihydroxy-4-isopropylcyclohexa-1,3-dienecarboxylate + NAD = 2,3-dihydroxy-p-cumate + NADH₂

Systematic name: cis-2,3-dihydroxy-2,3-dihydro-p-cumate:NAD oxidoreductase

Comments: Involved in the p-cymene degradation pathway in Pseudomonas putida.

References:

1. Eaton, R.W. p-Cumate catabolic pathway in Pseudomonas putida Fl: cloning and characterization of DNA carrying the cmt operon. J. Bacteriol. 178 (1996) 1351-1362. [Medline UI: 96200106]

EC 1.3.1.59

Recommended name: 1,6-dihydroxy-5-methylcyclohexa-2,4-dienecarboxylate dehydrogenase

Reaction: 1,6-dihydroxy-5-methylcyclohexa-2,4-dienecarboxylate + NAD = 3-methylcatechol + CO₂ + NADH₂

Systematic name: 1,6-dihydroxy-5-methylcyclohexa-2,4-dienecarboxylate:NAD oxidoreductase (decarboxylating)

Comments: Involved in the m-xylene degradation pathway in bacteria.

References:

1. Neidle, E., Hartnett, C., Ornston, L.N., Bairoch, A., Rekik, M. and Harayama, S. cis-Diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. Eur. J. Biochem. 204 (1992) 113-120. [Medline UI: 92155191]

EC 1.3.1.60

Recommended name: dibenzothiophene dihydrodiol dehydrogenase

Reaction: cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene + NAD = 1,2-dihydroxydibenzothiophene + NADH₂

Systematic name: cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene:NAD oxidoreductase

Comments: Involved in the dibenzothiophene degradation pathway in bacteria.

References:

1. Laborde, A.L. and Gibson, D.T. Metabolism of dibenzothiophene by a Beijerinckia species. Appl. Environ. Microbiol. 34 (1977) 783-790. [Medline UI: 78079253]

2. Denome, S.A., Stanley, D.C., Olson, E.S. and Young, K.D. Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: complete DNA sequence of an upper naphthalene catabolic pathway. J. Bacteriol. 175 (1993) 6890-6901. [Medline UI: 94042852]

EC 1.3.1.61

Recommended name: terephthalate 1,2-cis-dihydrodiol dehydrogenase

Reaction: cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate + NAD = 3,4-dihydroxybenzoate + CO₂ + NADH₂

Systematic name: cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate:NAD oxidoreductase (decarboxylating)

Comments: Involved in the terephthalate degradation pathway in bacteria.

References:

1. Laborde, A.L. and Gibson, D.T. Metabolism of dibenzothiophene by a Beijerinckia species. Appl. Environ. Microbiol. 34 (1977) 783-790. [Medline UI: 78079253]

EC 1.3.1.62

Recommended name: pimeloyl-CoA dehydrogenase

Reaction: pimeloyl-CoA + NAD = 6-carboxyhex-2-enoyl-CoA + NADH₂

Systematic name: pimeloyl-CoA:NAD oxidoreductase

Comments: Involved in the benzoate degradation (anaerobic) pathway in bacteria.

References:

1. Wang, Y.Z., Zhou, Y. and Zylstra, G.J. Molecular analysis of isophthalate and terephthalate degradation by Comamonas testosteroni YZW-D. Environ. Health Perspect. 103 Suppl. 5 (1995) 9-12. [Medline UI: 96127609]

EC 1.3.1.63

Recommended name: 2,4-dichlorobenzoyl-CoA reductase

Reaction: 4-chlorobenzoyl-CoA + NADP + HCl = 2,4-dichlorobenzoyl-CoA + NADPH₂

Systematic name: 4-chlorobenzoyl-CoA:NADP oxidoreductase (halogenating)

Comments: Acts in the reverse direction to form part of the 2,4-dichlorobenzoate degradation pathway in bacteria.

References:

1. Romanov, V. and Hausinger, R.P. NADPH-dependent reductive ortho dehalogenation of 2,4-dichlorobenzoic acid in Corynebacterium sepedonicum KZ-4 and Coryneform bacterium strain NTB-1 via 2,4-dichlorobenzoyl coenzyme A. J. Bacteriol. 178 (1996) 2656-2661. [Medline UI: 96196174]

EC 1.3.1.64

Recommended name: phthalate 4,5-cis-dihydrodiol dehydrogenase

Reaction: cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD = 4,5-dihydroxyphthalate + NADH₂

Systematic name: cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate:NAD oxidoreductase

Comments: Involved in the phthalate degradation pathway in bacteria.

References:

1. Batie, C.J., LaHaie, E. and Ballou, D.P. Purification and characterization of phthalate oxygenase and phthalate oxygenase reductase from Pseudomonas cepacia. J. Biol. Chem. 262 (1987) 1510-1518. [Medline UI: 87109290]

EC 1.3.1.65

Recommended name: 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline dehydrogenase

Reaction: 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline + NAD = 5,6-dihydroxy-3-methyl-2-oxo-1,2-dihydroquinoline + NADH₂

Systematic name: 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline:NAD oxidoreductase

Comments: Acts in the reverse direction to form part of the 3-methylquinoline degradation pathway in bacteria.

References:

1. Schach, S., Schwarz, G., Fetzner, S. and Lingens, F. Microbial metabolism of quinoline and related compounds. XVII. Degradation of 3-methylquinoline by Comamonas testosteroni 63. Biol. Chem. Hoppe Seyler 374 (1993) 175-181. [Medline UI: 93257093]

EC 1.3.1.66

Recommended name: cis-dihydroethylcatechol dehydrogenase

Reaction: cis-1,2-dihydro-3-ethylcatechol + NAD = 3-ethylcatechol + NADH₂

Systematic name: cis-1,2-dihydro-3-ethylcatechol:NAD oxidoreductase

Comments: Involved in the ethylbenzene degradation pathway in bacteria.

References:

1. Gibson, D.T., Gschwendt, B., Yeh, W.K. and Kobal, V.M. Initial reactions in the oxidation of ethylbenzene by Pseudomonas putida. Biochemistry 12 (1973) 1520-1528. [Medline UI: 73165367]

EC 1.3.1.67

Recommended name: cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate dehydrogenase

Reaction: cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate + NAD(P) = 4-methylcatechol + NAD(P)H₂ + CO₂

Systematic name: cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate:NAD(P) oxidoreductase (decarboxylating)

Comments: Involved in the p-xylene degradation pathway in bacteria.

References:

1. Whited, G.M., McCombie, W.R., Kwart, L.D. and Gibson, D.T. Identification of cis-diols as intermediates in the oxidation of aromatic acids by a strain of Pseudomonas putida that contains a TOL plasmid. J. Bacteriol. 166 (1986) 1028-1039. [Medline UI: 86223762]

EC 1.3.1.68

Recommended name: 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate dehydrogenase

Reaction: 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate + NAD = 3-methylcatechol + NADH₂ + CO₂

Systematic name: 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate:NAD oxidoreductase (decarboxylating)

Comments: Involved in the o-xylene degradation pathway in bacteria.

References:

1. Higson, F.K. and Focht, D.D. Degradation of 2-methylbenzoic acid by Pseudomonas cepacia MB2. Appl. Environ. Microbiol. 58 (1992) 194-200. [Medline UI: 92171487]

EC 1.3.99.20

Recommended name: 4-hydroxybenzoyl-CoA reductase

Reaction: 4-hydroxybenzoyl-CoA + acceptor = benzoyl-CoA + reduced acceptor

Systematic name: 4-hydroxybenzoyl-CoA:(acceptor) oxidoreductase

Comments: Involved in the anaerobic pathway of phenol metabolism in bacteria.

References:

1. Glockler, R., Tschech, A. and Fuchs, G. Reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA in a denitrifying, phenol-degrading Pseudomonas species. FEBS Lett. 251 (1989) 237-240. [Medline UI: 89325672]

2. Heider, J., Boll, M., Breese, K., Breinig, S., Ebenau-Jehle, C., Feil, U., Gad'on, N., Laempe, D., Leuthner, B., Mohamed, M.E.S., Schneider, S., Burchhardt, G. and Fuchs, G. Differential induction of enzymes involved in anaerobic metabolism of aromatic compounds in the denitrifying bacterium Thauera aromatica. Arch. Microbiol. 170 (1998) 120-131. [Medline UI: 98350021]

3. Breese, K. and Fuchs, G. 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica - prosthetic groups, electron donor, and genes of a member of the molybdenum-flavin-iron-sulfur proteins. Eur. J. Biochem. 251 (1998) 916-923. [Medline UI: 98149712]

4. Brackmann, R. and Fuchs, G. Enzymes of anaerobic metabolism of phenolic compounds. 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from a denitrifying Pseudomonas species. Eur. J. Biochem. 213 (1993) 563-571. [Medline UI: 93238735]

EC 1.4.3.17

Recommended name: tryptophan α,β-oxidase

Reaction: L-tryptophan + O₂ = α,β-didehydrotryptophan + H₂O₂

Other name(s): L-tryptophan α,β-dehydrogenase

Systematic name: L-tryptophan:oxygen α,β-oxidoreductase

Comments: Requires heme. 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. Also catalyses the α,β dehydrogenation of L-tryptophan side chains in peptides.

References:

1. Genet, R., Denoyelle, C. and Menez, A. Purification and partial characterization of an amino acid α,β-dehydrogenase, L-tryptophan 2',3'-oxidase from Chromobacterium violaceum. J. Biol. Chem. 269 (1994) 18177-18184. [Medline UI: 94299537]

2. Genet, R., Benetti, P.H., Hammadi, A. and Menez, A. L-Tryptophan 2',3'-oxidase from Chromobacterium violaceum. Substrate specificity and mechanistic implications. J. Biol. Chem. 270 (1995) 23540-23545. [Medline UI: 96007498]

EC 1.5.99.11

Recommended name: coenzyme F₄₂₀-dependent N⁵,N¹⁰-methenyltetrahydromethanopterin reductase

Reaction: N⁵,N¹⁰-methylenetetrahydromethanopterin + reduced coenzyme F₄₂₀ = 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F₄₂₀

Other names: methylene-H₄MPT reductase

Systematic name: N⁵,N¹⁰-methylenetetrahydromethanopterin:coenzyme-F₄₂₀ oxidoreductase

Comments: Catalyses an intermediate step in methanogenesis from CO₂ and H₂ in bacteria.

References:

1. Ma, K. and Thauer, R.K. Purification and properties of N⁵,N¹⁰-methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum (strain Marburg). Eur. J. Biochem. 191 (1990) 187-193. [Medline UI: 90336628]

2. te Brommelstroet, B.W., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F₄₂₀-dependent enzymes, from Methanosarcina barkeri. Biochim. Biophys. Acta 1079 (1991) 293-302. [Medline UI: 92002148]

EC 1.6.5.6

Recommended name: p-benzoquinone reductase (NADPH)

Reaction: NADPH₂ + p-benzoquinone = NADP + hydroquinone

Systematic name: NADPH₂:p-benzoquinone oxidoreductase

Comments: Involved in the 4-nitrophenol degradation pathway in bacteria..

References:

1. Spain, J.C. and Gibson, D.T. Pathway for bioremediation of p-nitrophenol in a Moraxella sp. Appl. Environ. Microbiol. 57 (1991) 812-819.

*EC 1.6.99.3

Recommended name: NADH₂ dehydrogenase

Reaction: NADH₂ + acceptor = NAD + reduced acceptor

Other name(s): cytochrome c reductase; type 1 dehydrogenase; b-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyri3633se; DPNH diaphorase; NADH diaphorase; NADH hydrogenase; NADH oxidoreductase; NADH-menadione oxidoreductase; reduced diphosphopyridine nucleotide diaphorase; NADH:cytochrome c oxidoreductase

Systematic name: NADH₂:(acceptor) oxidoreductase

Comments: A flavoprotein containing iron-sulfur centres. After preparations have been subjected to certain treatments, cytochrome c may act as an acceptor. Under normal conditions, two protons are extruded from the cytoplasm or the intramitochondrial or stromal compartment. Formerly EC 1.6.2.1; present in a mitochondrial complex as EC 1.6.5.3.

References:

1. Adachi, K. and Okuyama, T. Study on the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes. I. Crystallization and properties of the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes. Biochim. Biophys. Acta 268 (1972) 629-637. [Medline UI: 72214031]

2. Hatefi, Y., Ragan, C.I. and Galante, Y.M. The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system. In: Martonosi, A.N. (Ed.), The Enzymes of Biological Membranes, 2nd ed., vol. 4, Wiley, New York, 1985, pp. 1-70.

3. Hochstein, L.I. and Dalton, B.P. Studies of a halophilic NADH dehydrogenase. I. Purification and properties of the enzyme. Biochim. Biophys. Acta 302 (1973) 216-228. [Medline UI: 73163219]

4. Kaniuga, Z. The transformation of mitochondrial NADH dehydrogenase into NADH:cytochrome c oxidoreductase. Biochim. Biophys. Acta 73 (1963) 550-564.

*EC 1.9.3.1

Recommended name: cytochrome-c oxidase

Reaction: 4 ferrocytochrome c + O₂ = 4 ferricytochrome c + 2 H₂O

Other name(s): cytochrome oxidase; cytochrome a₃; cytochrome aa₃; Warburg's respiratory enzyme; indophenol oxidase; indophenolase; complex IV (mitochondrial electron transport); ferrocytochrome c oxidase; NADH cytochrome c oxidase

Systematic name: ferrocytochrome-c:oxygen oxidoreductase

Comments: A cytochrome of the a type containing copper. The reduction of O₂ to water is accompanied by the extrusion of four protons from the intramitochondrial compartment. Several bacteria appear to contain analogous oxidases.

References:

1. Keilin, D. and Hartree, E.F. Cytochrome oxidase. Proc. R. Soc. Lond. B Biol. Sci. 125 (1938) 171-186.

2. Keilin, D. and Hartree, E.F. Cytochrome and cytochrome oxidase. Proc. R. Soc. Lond. B Biol. Sci. 127 (1939) 167-191.

3. Wainio, W.W., Eichel, B. and Gould, A. Ion and pH optimum for the oxidation of ferrocytochrome c by cytochrome c oxidase in air. J. Biol. Chem. 235 (1960) 1521-1525.

4. Yonetani, T. Studies on cytochrome oxidase. II. Steady state properties. J. Biol. Chem. 235 (1960) 3138-3243. [NLM CIT. ID: 60107671]

5. Yonetani, T. Studies on cytochrome oxidase. III. Improved purification and some properties. J. Biol. Chem. 236 (1961) 1680-1688. [NLM CIT. ID: 60107672]

*EC 1.10.2.2

Recommended name: ubiquinol-cytochrome-c reductase

Reaction: QH₂ + 2 ferricytochrome c = Q + 2 ferrocytochrome c

Other name(s): coenzyme Q-cytochrome c reductase; dihydrocoenzyme Q-cytochrome c reductase; reduced ubiquinone-cytochrome c reductase, complex III (mitochondrial electron transport); ubiquinone-cytochrome c reductase; ubiquinol-cytochrome c oxidoreductase; reduced coenzyme Q-cytochrome c reductase; ubiquinone-cytochrome c oxidoreductase; reduced ubiquinone-cytochrome c oxidoreductase; mitochondrial electron transport complex III; ubiquinol-cytochrome c-2 oxidoreductase; ubiquinone-cytochrome b-c₁ oxidoreductase; ubiquinol-cytochrome c₂ reductase; ubiquinol-cytochrome c₁ oxidoreductase; CoQH₂-cytochrome c oxidoreductase; ubihydroquinol:cytochrome c oxidoreductase; coenzyme QH₂-cytochrome c reductase; QH₂:cytochrome c oxidoreductase

Systematic name: ubiquinol:ferricytochrome-c oxidoreductase

Comments: Contains cytochromes b-562, b-566 and c₁, and a 2-iron ferredoxin. 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, NADH dehydrogenase).

References:

1. Marres, C.A.M. and Slater, E.C. Polypeptide composition of purified QH₂:cytochrome c oxidoreductase from beef-heart mitochondria. Biochim. Biophys. Acta 462 (1977) 531-548. [Medline UI: 78080802]

2. Rieske, J.S. Composition, structure, and function of complex III of the respiratory chain. Biochim. Biophys. Acta 456 (1976) 195-247. [Medline UI: 77022290]

3. Wikström, M., Krab, K. and Saraste, M. Proton-translocating cytochrome complexes. Annu. Rev. Biochem. 50 (1981) 623-655. [Medline UI: 81280521]

EC 1.13.12.12

Recommended name: apo-β-carotenoid-14',13'-dioxygenase

Reaction: 8'-apo-β-carotenol + O₂ = 14'-apo-β-carotenal + H₂O

Systematic name: 8'-apo-β-carotenol:O₂ oxidoreductase

Comments: A thiol-dependent enzyme. Unlike β-carotene-15,15'-dioxygenase (EC 1.13.11.21), it is not active towards β-carotene.

References:

1. Dmitrovskii, A.A., Gessler, N.N., Gomboeva, S.B., Ershov, Yu.V. and Bykhovsky, V.Ya. Enzymatic oxidation of β-apo-8'-carotenol to β-apo-14'-carotenal by an enzyme different from β-carotene-15,15'-dioxygenase. Biochemistry (Moscow) 62 (1997) 787-792. [Medline UI: 97473086]

EC 1.14.11.17

Recommended name: taurine dioxygenase

Reaction: taurine + 2-oxoglutarate + O₂ = sulfite + aminoacetaldehyde + succinate + CO₂

Other name(s) 2-aminoethanesulfonate dioxygenase; α-ketoglutarate-dependent taurine dioxygenase

Systematic name: taurine, 2-oxoglutarate:O₂ oxidoreductase (sulfite-forming)

Comments: Requires Fe^II. The enzyme from E. coli also acts on pentanesulfonate, 3-(N-morpholino)propanesulfonate and 2-(1,3-dioxoisoindolin-2-yl)ethanesulfonate, but at lower rates.

References:

1. Eichhorn, E., Van Der Poeg, J.R., Kertesz, M.A. and Leisinger, T. Characterization of α-ketoglutarate-dependent taurine dioxygenase from Escherichia coli. J.Biol. Chem. 272 (1997) 23031-23036. [Medline UI: 97435261]

EC 1.14.99.5

Recommended name: stearoyl-CoA 9-desaturase

Reaction: stearoyl-CoA + AH₂ + O₂ = oleoyl-CoA + A + 2 H₂O

Other names: acyl-CoA desaturase; fatty acid desaturase; δ⁹-desaturase

Systematic name: stearoyl-CoA, hydrogen-donor:oxygen oxidoreductase

Comments: An iron protein. The rat liver enzyme is an enzyme system involving cytochrome b₅ and EC 1.6.2.2.

References:

1. Fulco, A.J. and Bloch, K. Cofactor requirements for the formation of δ⁹-unsaturated fatty acids in Mycobacterium phlei. J. Biol. Chem. 239 (1964) 993-997. [NLM CIT. ID: 64125595]

2. Oshino, N., Imai, Y. and Sato, R. Electron-transfer mechanism associated with fatty acid desaturation catalyzed by liver microsomes. Biochim. Biophys. Acta 128 (1966) 13-27. [Medline UI: 67182592]

3. Oshino, N., Imai, Y. and Sato, R. A function of cytochrome b₅ in fatty acid desaturation by rat liver microsomes. J. Biochem. (Tokyo) 69 (1971) 155-167. [Medline UI: 71111382]

4. Strittmatter, P., Sputz, L., Corcoran, D., Rogers, M.J., Setlow, B. and Redline, R. Purification and properties of rat liver microsomal stearyl coenzyme A desaturase. Proc. Natl. Acad. Sci. USA 71 (1974) 4565-4569. [Medline UI: 75065561]

EC 1.14.99.6

Recommended name: acyl-[acyl-carrier-protein] 9-desaturase

Reaction: stearoyl-[acyl-carrier protein] + reduced acceptor + O₂ = oleoyl-[acyl-carrier protein] + acceptor + 2 H₂O

Other names: stearyl acyl carrier protein desaturase; stearyl-ACP desaturase

Systematic name: acyl-[acyl-carrier-protein], hydrogen-donor:oxygen oxidoreductase

Comments: The enzyme from safflower is specific for stearoyl-CoA; that from Euglena acts on derivatives of a number of long-chain fatty acids. Requires ferredoxin.

References:

1. Jaworski, J.G. and Stumpf, P.K. Fat metabolism in higher plants. Properties of a soluble stearyl-acyl carrier protein desaturase from maturing Carthamus tinctorius. Arch. Biochem. Biophys. 162 (1974) 158-165. [Medline UI: 74173330]

2. Nagai, J. and Bloch, K. Enzymatic desaturation of stearyl acyl carrier protein. J. Biol. Chem. 243 (1968) 4626-4633. [Medline UI: 69012765]

EC 1.14.99.31

Recommended name: myristoyl-CoA 11-(E) desaturase

Reaction: myristoyl-CoA + NAD(P)H₂ + O₂ = (E)-11-tetradecenoyl-CoA + NAD(P) + 2 H₂O

Systematic name: n-tetradecanoyl-CoA, NADPH₂:O₂ oxidoreductase [11-(E) desaturating]

Comments: 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. EC 1.14.99.32 forms the (Z) isomer by stereospecific cleavage of pro-(R) H at C-11 and C-12.

References:

1. Navaro, I., Font, I., Fabrias, G. and Camps, F. Stereospecificity of the (E)- and (Z)-11 myristoyl desaturases in the biosynthesis of Spodoptera littoralis sex pheromone. J. Am. Chem. Soc. 119 (1997) 11335-11336.

EC 1.14.99.32

Recommended name: myristoyl-CoA 11-(Z) desaturase

Reaction: myristoyl-CoA + NAD(P)H₂ + O₂ = (Z)-11-tetradecenoyl-CoA + NAD(P) + 2 H₂O

Systematic name: n-tetradecanoyl-CoA, NADPH₂:O₂ oxidoreductase [11-(Z) desaturating]

Comments: Involved in sex pheromone synthesis in Spodoptera littoralis. (Z)-11-Tetradecenoyl-CoA is formed by stereospecific removal of H from the pro-(R) positions at C-11 and C-12. EC 1.14.99.32 forms the (E)-isomer by removing the pro-(R) H group at C-11 and the pro-(S) H group at C-12.

References:

1. Navaro, I., Font, I., Fabrias, G. and Camps, F. Stereospecificity of the (E)- and (Z)-11 myristoyl desaturases in the biosynthesis of Spodoptera littoralis sex pheromone. J. Am. Chem. Soc. 119 (1997) 11335-11336.

*EC 2.1.1.86

Recommended name: tetrahydromethanopterin S-methyltransferase

Reaction: 5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate = 5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate

Other name(s): tetrahydromethanopterin methyltransferase

Systematic name: 5-methyl-5,6,7,8-tetrahydromethanopterin:2-mercaptoethanesulfonate 2-methyltransferase

Comments: Involved in the formation of methane from CO in Methanobacterium thermoautotrophicum. Methanopterin is a pterin analogue. The reaction involves the export of one or two sodium ions in Archaea.

References:

1. Sauer, F.D. Tetrahydromethanopterin methyltransferase, a component of the methane synthesizing complex of Methanobacterium thermoautotrophicum. Biochem. Biophys. Res. Commun. 136 (1986) 542-547. [Medline UI: 86215234].

EC 2.4.1.209

Recommended name: cis-p-coumarate glucosyltransferase

Reaction: UDP-glucose + cis-p-coumarate = 4'-O-β-D-glucosyl-cis-p-coumarate + UDP

Systematic name: UDP-glucose:cis-p-coumarate β-D-glucosyltransferase

Comments: cis-Caffeic acid also serves as a glucosyl acceptor with the enzyme from Sphagnum fallax kinggr. The corresponding trans-isomers are not substrates.

References:

1. Rasmussen, S. and Rudolph, H. Isolation, purification and characterization of UDP-glucose:cis-p-coumaric acid-β-D-glucosyltransferase from Sphagnum fallax. Phytochemistry 46 (1997) 449-453. [Agricola: 450 P5622]

EC 2.4.1.210

Recommended name: limonoid glucosyltransferase

Reaction: UDP-glucose + limonin = glucosyl-limonin + UDP

Systematic name: uridine diphosphoglucose-limonoid glucosyltransferase

Comments: The enzyme purified from navel orange albedo tissue also acts on the related tetranortriterpenoid nomilin.

References:

1. Sim, M.K. and Lim, B.C. Purification of limonoid glucosyltransferase from navel orange albedo tissue. Phytochemistry 46 (1997) 33-37.

*EC 2.6.1.16

Recommended name: glutamine-fructose-6-phosphate transaminase (isomerizing)

Reaction: L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate

Other names: hexosephosphate aminotransferase; glucosamine-6-phosphate isomerase (glutamine-forming); glutamine-fructose-6-phosphate transaminase (isomerizing); D-fructose-6-phosphate amidotransferase; glucosaminephosphate isomerase; glucosamine 6-phosphate synthase; GlcN6P synthase

Systematic name: L-glutamine:D-fructose-6-phosphate isomerase (deaminating)

Comments: 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). Formerly EC 5.3.1.19.

References:

1. Ghosh, S., Blumenthal, H.J., Davidson, E., Roseman, S. Glucosamine metabolism. V. Enzymatic synthesis of glucosamine 6-phosphate. J. Biol. Chem. 235 (1960) 1265-1273. [NLM CIT. ID: 60148268]

2. Gryder, R.M., Pogell, B.M. Further studies on glucosamine 6-phosphate synthesis by rat liver enzymes. J. Biol. Chem. 235 (1960) 558-562. [NLM CIT. ID: 60150386]

3. Leloir, L.F., Cardini, C.E. The biosynthesis of glucosamine. Biochim. Biophys. Acta 12 (1953) 15-22.

4. Teplyakov, A., Obmolova, G., Badet-Denisot, M.A. and Badet, B. The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate synthase. Protein Sci. 8 (1999) 596-602. [Medline UI: 99190083]

EC 2.6.1.76

Recommended name: diaminobutyrate-2-oxoglutarate transaminase

Reaction: L-2,4-diaminobutyrate + 2-oxoglutarate = L-glutamate + L-aspartic 4-semialdehyde

Other name(s): L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase; 2,4-diaminobutyrate 4-aminotransferase

Systematic name: L-2,4-diaminobutyrate:2-oxoglutarate 4-aminotransferase

Comments: Involved in the formation of 1,3-diaminopropane in Haemophilus influenzae and Acinetobacter baumannii. A product of the ddc gene that also encodes L-2,4-diaminobutyrate decarboxylase in Acinetobacter baumannii. Differs from EC 2.6.1.46, diaminobutyrate-pyruvate transaminase, which has pyruvate as the amino-group acceptor.

References:

1. Ikai, H.and Yamamoto, S. Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane production pathway in Acinetobacter baumannii. J. Bacteriol. 179 (1997) 5118-5125. [Medline UI: 97405910]

2. Ikai, H. and Yamamoto, S. Two genes involved in the 1,3-diaminopropane production pathway in Haemophilus influenzae. Biol. Pharm. Bull. 21 (1998) 170-173. [Medline UI: 98173550]

*EC 2.7.1.69

Recommended name: protein-N^π-phosphohistidine-sugar phosphotransferase

Reaction: protein N^π-phosphohistidine + sugar = protein histidine + sugar phosphate

Other name(s): enzyme II of the phosphotransferase system (cf. EC 2.7.3.9); glucose permease; PTS permease; phosphotransferase, phosphohistidinoprotein-hexose; enzyme IIl4ac; gene glC proteins; gene bglC RNA formation factors; PEP-dependent phosphotransferase enzyme II; PEP-sugar phosphotransferase enzyme II; phosphoenolpyruvate-sugar phosphotransferase enzyme II; phosphohistidinoprotein-hexose phosphotransferase; phosphohistidinoprotein-hexose phosphoribosyltransferase; phosphoprotein factor-hexose phosophotransferase; protein, specific or class, gene bglC; ribonucleic acid formation factor, gene glC; sucrose phosphotransferase system II

Systematic name: Protein-N^π-phosphohistidine:sugar N-pros-phosphotransferase

Comments: Comprises a group of related enzymes. The protein substrate is a phosphocarrier protein of low molecular mass (9.5 kDa). The protein is phosphorylated in a reaction catalysed by EC 2.7.3.9 (phosphoenolpyruvate-protein phosphotransferase) and this acts as the phosphate donor for the above reaction. The enzyme translocates the sugar it phosphorylates into bacteria. Aldohexoses, and their glycosides and alditols, are phosphorylated on O-6, whereas fructose and sorbose are phosphorylated on O-1. Glycerone and disaccharides are also substrates.

References:

1. Kornberg, H.L. and Riordan, C. Uptake of galactose into Escherichia coli by facilitated diffusion. J. Gen. Microbiol. 94 (1976) 75-89. [Medline UI: 76216538]

2. Postma, P.W. and Roseman, S. The bacterial phosphoenolpyruvate: sugar phosphotransferase system. Biochim. Biophys. Acta 457 (1976) 213-257. [Medline UI: 77065789]

EC 3.1.1.73

Recommended name: feruloyl esterase

Reaction: feruloyl-polysaccharide + H₂O = ferulate + polysaccharide

Other name(s): ferulic acid esterase, hydroxycinnamoyl esterase, hemicellulase accessory enzymes; FAE-III, cinnamoyl ester hydrolase, FAEA, cinnAE, FAE-I, FAE-II

Sytematic name: 4-hydroxy-3-methoxycinnamoyl-sugar hydrolase

Comments: Catalyses the hydrolysis of the 4-hydroxy-3-methoxycinnamoyl (feruloyl) group from an esterified sugar, which is usually arabinose in "natural" substrates. p-Nitrophenol acetate and methyl ferulate are poorer substrates. All microbial ferulate esterases are secreted into the culture medium. They are sometimes called hemicellulase accessory enzymes, since they help xylanases and pectinases to break down plant cell wall hemicellulose.

References:

1. Faulds, C.B. and Williamson, G. The purification and characterisation of 4-hydroxy-3-methoxy-cinnamic (ferulic) acid esterase from Streptomyces olivochromogenes (3232). J. Gen. Microbiol. 137 (1991) 2339-2345. [Medline UI: 92121885]

2. Faulds, C.B. and Williamson, G. Purification and characterisation of a ferulic acid esterase (FAE-III) from Aspergillus niger. Specificity for the phenolic moiety and binding to microcrystalline cellulose. Microbiology 140 (1994) 779-787.

3. Kroon, P.A., Faulds, C.B. and Williamson, G. Purification and characterisation of a novel ferulic acid esterase induced by growth of Aspergillus niger on sugarbeet pulp. Biotechnol. Appl. Biochem. 23 (1996) 255-262. [Medline UI: 96260178]

4. deVries, R.P., Michelsen,B., Poulsen, C.H., Kroon, P.A., van den Heuvel, R.H.H., Faulds, C.B., Williamson, G., van den Homberg, J.P.T.W. and Visser, J. The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharides. Appl. Environ. Microbiol. 63 (1997) 4638-4644. [Medline UI: 98069455]

5. Castanares, A., Mccrae, S.I. and Wood, T.M. Purification and properties of a feruloyl/p-coumaroyl esterase from the fungus Penicillium pinophilum. Enzyme Microbiol. Technol. 14 (1992) 875-884.

EC 3.1.2.24

Recommended name: 2-(2-hydroxyphenyl)benzenesulfinate hydrolase

Reaction: 2-(2-hydroxyphenyl)benzenesulfinate + H₂O = 2-hydroxybiphenyl + sulfite

Other name(s): gene dszB-encoded hydrolase

Systematic name: 2-(2-hydroxyphenyl) benzenesulfinate:H₂O hydrolase

Comments: The enzyme from Rhodococcus sp. strain IGTS8 is encoded by the plasmid-encoded dibenzothiophene-desulfurization (dsz) operon.

References:

1. Oldfield, C., Pogrebinsky, O., Simmonds, J., Ölson, E.S. and Kulpa, C.F. Elucidation of the metabolic pathway for dibenzothiophene desulfurization by Rhodococcus sp. strain IGTS8 (ATCC 53968) Microbiology 143 (1997) 2961-2973. [Medline UI: 97453480]

*EC 3.2.1.10

Recommended name: oligo-1,6-glucosidase

Reaction: Hydrolysis of 1,6-α-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (α-amylase), and in isomaltose

Other name(s): limit dextrinase (erroneous); isomaltase; sucrase-isomaltase

Systematic name: oligosaccharide α-1,6-glucohydrolase

Comments: This enzyme, like EC 3.2.1.33 (amylo-α-1,6-glucosidase), can release an α-16-linked glucose, whereas the shortest chain that can be released by EC 3.2.1.41 (pullulanase), EC 3.2.1.142 (limit dextrinase), and EC 3.2.1.68 (isoamylase) is maltose. It also hydrolyses 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 catalyses the reaction of EC 3.2.1.48 (sucrose α-glucosidase). Differs from EC 3.2.1.33 (amylo-α-1,6-glucosidase) 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.

References:

1. Hauri, H.-P., Quaroni, A. and Isselbacher, K.J. Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase. Proc. Natl. Acad. Sci. USA 76 (1979) 5183-5186. [Medline UI: 80056658]

2. Sjöström, H., Norén, O., Christiansen, L., Wacker, H. and Semenza, G. A fully active, two-active-site, single-chain sucrase.isomaltase from pig small intestine. Implications for the biosynthesis of a mammalian integral stalked membrane protein. J. Biol. Chem. 255 (1980) 11332-11338. [Medline UI: 81069795]

3. Rodriguez, I.R., Taravel, F.R. and Whelan, W.J. Characterization and function of pig intestinal sucrase-isomaltase and its separate subunits. Eur J Biochem. 143 (1984) 575-582. [Medline UI: 85003633]

*EC 3.2.1.33

Recommended name: amylo-α-1,6-glucosidase

Reaction: Hydrolysis of (16)-α-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin

Other name(s): amylo-1,6-glucosidase; dextrin 6-α-D-glucosidase

Systematic name: glycogen phosphorylase-limit dextrin α-1,6-glucohydrolase

Comments: This enzyme hydrolyses an unsubstituted (16)-α-glucose residue that forms a branch point on an α-(14)-linked glucose chain. The enzyme activity found in mammals and yeast is in a polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25 (4-α-glucanotransferase), which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-α-glucosidase activity can then hydrolyse. Together, these two activities constitute the glycogen debranching system.

References:

1. Brown, B.H. and Brown, D.I. Enzymes of glcogen debranching: Amylo-1,6-glucosidase (I) and oligo-1,41,4-glucanotransferase (II). Methods Enzymol. 8 (1966) 515-524

2. Lee, E.Y.C., Carter, J.H., Nielsen, L.D. and Fischer, E.H. Purification and properties of yeast amylo-1,6-glucosidase-oligo-1,41,4-glucantransferase. Biochemistry 9 (1970) 2347-2355.

3. Nelson, T.E., Kolb, E. and Larner, J. Purification and properties of rabbit muscle amylo-1,6-glucosidase-oligo-1,41,4-transferase. Biochemistry 8 (1969) 1419-1428.

*EC 3.2.1.41

Recommended name: pullulanase

Reaction: Hydrolysis of (16)-α-D-glucosidic linkages in pullulan [a linear polymer of α-(16)-linked maltotriose units] and in amylopectin and glycogen, and the α- and β-limit dextrins of amylopectin and glycogen.

Other name(s): limit dextrinase (erroneous); amylopectin 6-glucanohydrolase; bacterial debranching enzyme; debranching enzyme; α-dextrin endo-1,6-α-glucosidase

Systematic name: pullulan α-1,6-glucanohydrolase

Comments: Different from EC 3.2.1.142 (limit dextrinase) in its action on glycogen, and its rate of hydrolysis of limit dextrins. Its action on amylopectin is complete. Maltose is the smallest sugar that it can release from an α-(16)-linkage.

References:

1. Abdullah, M., Catley, B.J., Lee, E.Y.C., Robyt, J., Wallenfels, K. and Whelan, W.J. The mechanism of carbohydrate action. XI. Pullulanase, an enzyme specific for the hydrolysis of α-16-bonds in amylaceous oligo- and polysaccharides. Cereal Chemistry 43 (1966) 111-118.

2. Bender, H. and Wallenfels, K. Pullulanase (an amylopectin and glycogen debranching enzyme) from Aerobacter aerogenes. Methods Enzymol. 8 (1966) 555-559.

3. Manners, D.J. Observations on the specificity and nomenclature of starch debranching enzymes. J. Appl. Glycosci. 44 (1997) 83-85.

*EC 3.2.1.68

Recommended name: isoamylase

Reaction: Hydrolysis of (16)-α-D-glucosidic branch linkages in glycogen, amylopectin and their β-limit dextrins

Other name(s): debranching enzyme

Systematic name: glycogen α-1,6-glucanohydrolase

Comments: Also readily hydrolyses amylopectin. Differs from EC 3.2.1.41 (pullulanase) and EC 3.2.1.142 (limit dextrinase) by its inability to hydrolyse pullulan, and by limited action on α-limit dextrins. Maltose is the smallest sugar it can release from an α-(16)-linkage.

References:

1. Yokobayashi, K., Misaki, A. and Harada, T. Purification and properties of Pseudomonas isoamylase. Biochim. Biophys. Acta 212 (1970) 458-469. [Medline UI: 70285889]

EC 3.2.1.142

Recommended name: limit dextrinase

Reaction: Hydrolysis of (16)-α-D-glucosidic linkages in α- and β-limit dextrins of amylopectin and glycogen, and in amylopectin and pullulan

Other name(s): R-enzyme; amylopectin-1,6-glucosidase

Systematic name: dextrin α-1,6-glucanohydrolase

Comments: Plant enzymes with little or no action on glycogen. Action on amylopectin is incomplete, but action on α-limit dextrins is complete. Maltose is the smallest sugar it can release from an α-(16)-linkage.

References:

1. Gordon, R.W., Manners, D.J. and Stark, J.R. The limit dextrinase of the broad bean (Vicia faba). Carbohydrate Res. 42 (1975) 125-134.

2. Manners, D.J. Observations on the specificity and nomenclature of starch debranching enzymes. J. Appl. Glycosci. 44 (1997) 83-85.

EC 3.2.1.143

Recommended name: poly(ADP-ribose) glycohydrolase

Reaction: hydrolyses poly(ADP-ribose) at glycosidic (1"-2') linkage of ribose-ribose bond to produce free ADP-ribose

Comments: Specific to (1"-2') linkage of ribose-ribose bond of poly(ADP-ribose).

References:

1. Miwa, M. and Sugimura, T. Splitting of the ribose-ribose linkage of poly(adenosine diphosphate-ribose) by a calf thymus extract. J. Biol. Chem. 246 (1971) 6362-6364. [Medline UI: 72063535]

2. Lin, W., Ame, J.C., Aboul-Ela, N., Jacobson, E.L. and Jacobson, M.K. Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase. J. Biol. Chem. 272 (1997) 11895-11901. [Medline UI: 97277328]

EC 3.2.1.144

Recommended name: 3-deoxyoctulosonase

Reaction: 3-deoxyoctulosonyl-lipopolysaccharide+ H₂O = 3-deoxyoctulosonic acid + lipopolysaccharide

Other name(s): α-Kdo-ase

Systematic name: 3-deoxyoctulosonyl-lipopolysaccharide hydrolase

Comments: Releases Kdo (α- and β-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-α-Kdo (α-Kdo-OMec) is also a substrate.

References:

1. Li, Y.T., Wang, L.X., Pavlova, N.V., Li, S.C. and Lee, Y.C. α-KDOase activity in oyster and synthesis of α- and β-4-methylumbelliferyl ketosides of 3-deoxy-D-manno-octulosonic acid (KDO) J. Biol. Chem. 272 (1997) 26419-26424. [Medline UI: 97476241]

*EC 3.2.2.15

Recommended name: DNA-deoxyinosine glycosylase

Reaction: hydrolyses DNA and polynucleotides, releasing free hypoxanthine

Other names: DNA(hypoxanthine) glycohydrolase

Systematic name: DNA-deoxyinosine deoxyribohydrolase

References:

1. Karran, P. and Lindahl, T. Enzymatic excision of free hypoxanthine from polydeoxynucleotides and DNA containing deoxyinosine monophosphate residues. J. Biol. Chem. 253 (1978) 5877-5879. [Medline UI: 78242253]

*EC 3.2.2.20

Recommended name: DNA-3-methyladenine glycosylase I

Reaction: Hydrolysis of alkylated DNA, releasing 3-methyladenine

Systematic name: alkylated-DNA glycohydrolase (releasing methyladenine and methylguanine)

Comments: Involved in the removal of alkylated bases from DNA in Escherichia coli (cf. EC 2.1.1.63).

References:

1. Evensen, G. and Seeberg, E. Adaptation to alkylation resistance involves the induction of a DNA glycosylase. Nature (Lond.) 296 (1982) 773-775. [Medline UI: 82173208]

2. Karran, P., Hjelmgren, T. and Lindahl, T. Induction of a DNA glycosylase for N-methylated purines is part of the adaptive response to alkylating agents. Nature (Lond.) 296 (1982) 770-773. [Medline UI: 82173207]

3. Thomas, L., Yang, C.-H. and Goldthwait, D.A. Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine. Biochemistry 21 (1982) 1162-1169. [Medline UI: 82173207]

*EC 3.2.2.21

Recommended name: DNA-3-methyladenine glycosylase II

Reaction: Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine

Systematic name: alkylated-DNA glycohydrolase (releasing methyladenine and methylguanine)

Comments: Involved in the removal of alkylated bases from DNA in Escherichia coli (cf. EC 2.1.1.63).

References:

1. Evensen, G. and Seeberg, E. Adaptation to alkylation resistance involves the induction of a DNA glycosylase. Nature (Lond.) 296 (1982) 773-775. [Medline UI: 82173208]

2. Karran, P., Hjelmgren, T. and Lindahl, T. Induction of a DNA glycosylase for N-methylated purines is part of the adaptive response to alkylating agents. Nature (Lond.) 296 (1982) 770-773. [Medline UI: 82173207]

3. Riazuddin, S. and Lindahl, T. Properties of 3-methyladenine-DNA glycosylase from Escherichia coli. Biochemistry 17 (1978) 2110-2118. [Medline UI: 78211041]

4. Thomas, L., Yang, C.-H. and Goldthwait, D.A. Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine. Biochemistry 21 (1982) 1162-1169. [Medline UI: 82182923]

*EC 3.2.2.22

Recommended name: rRNA N-glycosylase

Reaction: Hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes

Systematic name: rRNA N-glycohydrolase

Comments: Ricin A-chain and related toxins show this activity. Naked rRNA is attacked more slowly than rRNA in intact ribosomes. Naked rRNA from Escherichia coli is cleaved at a corresponding position.

References:

1. Endo, Y. and Tsurugi, K. The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA. J. Biol. Chem. 263 (1988) 8735-8739. [Medline UI: 88243729]

*EC 3.2.2.23

Recommended name: DNA-formamidopyrimidine glycosylase

Reaction: Hydrolysis of DNA containing ring-opened N⁷-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimide

Other name(s): fapy-DNA glycosylase

Systematic name: DNA glycohydrolase [2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimide releasing]

References:

1. Boiteux, S., O'Connor, T.R. and Laval, J. Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein. EMBO J. 6 (1987) 3177-3183. [Medline UI: 88082692]

EC 3.5.1.84

Recommended name: biuret amidohydrolase

Reaction: biuret + H₂O = urea + CO₂ + NH₃

Systematic name: biuret amidohydrolase

Comments: Involved in a pathway by which the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, is degraded in bacteria.

References:

1. Cook, A.M., Beilstein, P., Grossenbacher, H. and Hutter, R. Ring cleavage and degradative pathway of cyanuric acid in bacteria. Biochem. J. 231 (1985) 25-30. [Medline UI: 86050491]

EC 3.5.1.85

Recommended name: (S)-N-acetyl-1-phenylethylamine hydrolase

Reaction: N-acetylphenylethylamine = phenylethylamine + acetate

Other name: (S)-N-acetyl-1-phenylethylamine amidohydrolase

Systematic name: (S)-N-acetylphenylethylamine:H₂O hydrolase

Comments: Inhibited by phenylmethanesulfonyl fluoride. Some related acetylated compounds are hydrolysed with variable enantiomeric selectivities.

References:

1. Brunella, A., Graf, M., Kittelmann, M., Lauma, K. and Ghisalba, O. Production, purification, and characterization of a highly enantioselective (S)-N-acetyl-1-phenylethyl amidohydrolase from Rhodococcus. Appl. Microbiol. Biotechnol. 47 (1997) 515-520.

EC 3.5.2.15

Recommended name: cyanuric acid amidohydrolase

Reaction: cyanuric acid + H₂O = biuret + CO₂

Systematic name: cyanuric acid amidohydrolase

Comments: Involved in a pathway by which the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, is degraded in bacteria.

References:

1. Eaton, R.W. and Karns, J.S. Cloning and comparison of the DNA encoding ammelide aminohydrolase and cyanuric acid amidohydrolase from three s-triazine-degrading bacterial strains. J. Bacteriol. 173 (1991) 1363-1366. [Medline UI: 91123219]

2. Eaton, R.W. and Karns, J.S. Cloning and analysis of s-triazine catabolic genes from Pseudomonas sp. strain NRRLB-12227. J. Bacteriol. 173 (1991) 1215-1222. [Medline UI: 91123197]

EC 3.5.99.3

Recommended name: hydroxydechloroatrazine ethylaminohydrolase

Reaction: 4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + H₂O = N-isopropylammelide + ethylamine

Other name(s): AtzB; hydroxyatrazine ethylaminohydrolase

Systematic name: 4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine ethylaminohydrolase

Comments: 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.

References:

1. Boundy-Mills, K.L., de Souza, M.L., Mandelbaum, R.T., Wackett, L.P. and Sadowsky, M.J. The atzB gene of Pseudomonas sp. strain ADP encodes the second enzyme of a novel atrazine degradation pathway. Appl. Environ. Microbiol. 63 (1997) 916-923. [Medline UI: 97208208]

EC 3.5.99.4

Recommended name: N-isopropylammelide isopropylaminohydrolase

Reaction: N-isopropylammelide + H₂O = cyanuric acid + isopropylamine

Other name(s): AtzC

Systematic name: N-isopropylammelide isopropylaminohydrolase

Comments: 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.

References:

1. Sadowsky, M.J., Tong, Z., de Souza, M. and Wackett, L.P. AtzC is a new member of the amidohydrolase protein superfamily and is homologous to other atrazine-metabolizing enzymes. J. Bacteriol. 180 (1998) 152-158. [Medline UI: 98083068]

EC 3.5.99.5

Recommended name: 2-aminomuconate deaminase

Reaction: 2-aminomuconate + H₂O = 4-oxalocrotonate + NH₃

Systematic name: 2-aminomuconate aminohydrolase

Comments: Intermediate in the biodegradation of nitrobenzene by Pseudomonas pseudocaligenes JS45. The reaction is spontaneous in acid conditions.

References:

1. He, Z. and Spain, J.C. A novel 2-aminomuconate deaminase in the nitrobenzene degradation pathway of Pseudomonas pseudoalcaligenes JS45. J. Bacteriol. 180 (1998) 2502-2506. [Medline UI: 98233748]

2. He, Z, and Spain, J.C. Studies of the catabolic pathway of degradation of nitrobenzene by Pseudomonas pseudoalcaligenes JS45: removal of the amino group from 2-aminomuconic semialdehyde. Appl. Environ. Microbiol. 63 (1997) 4839-4843. [Medline UI: 98129121]

EC 3.5.99.6

Recommended name: glucosamine-6-phosphate deaminase

Reaction: D-glucosamine 6-phosphate + H₂O = D-fructose 6-phosphate + NH₃

Other name(s): glucosaminephosphate isomerase, glucosamine-6-phosphate isomerase

Systematic name: 2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol isomerizing)

Comments: Formerly EC 5.3.1.10. Isomerization of the aldose-ketose type converts the -CH(-NH₂)-CH=O group of glucosamine 6-phosphate into -C(=NH)-CH₂-OH, forming 2-deoxy-2-imino-D-arabino-hexitol, which then hydrolyses to yield fructose 6-phosphate and ammonia. N-Acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme.

References:

1. Comb, D.G., Roseman, S. Glucosamine metabolism. IV. Glucosamine-6-phoshate deaminase. J. Biol. Chem. 232 (1958) 807-827

2. Pattabiraman, T.N., Bachhawat, B.K. Purification of glucosamine 6-phosphate deaminase from human brain. Biochim. Biophys. Acta 54 (1961) 273-283. [NLM CIT. ID: 62005528]

3. Wolfe, J.G., Britton, B.B., Nakada, H.I. Glucosamine degradation by Escherischia coli. III. Isolation and studies of "phosphoglucosaminisomerase". Arch. Biochem Biophys. 66 (1957) 333-339

EC 3.8.1.8

Recommended name: atrazine chlorohydrolase

Reaction: atrazine + H₂O = 4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl

Other name(s): AtzA

Systematic name: atrazine chlorohydrolase

Comments: Involved in the degradation of the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, in bacteria.

References:

1. de Souza, M.L., Wackett, L.P., Boundy-Mills, K.L., Mandelbaum, R.T. and Sadowsky, M.J. Cloning, characterization, and expression of a gene region from Pseudomonas sp. strain ADP involved in the dechlorination of atrazine. Appl. Environ. Microbiol. 61 (1995) 3373-3378. [Medline UI: 96035669]

2. de Souza, M,L,, Sadowsky, M.J. and Wackett, L.P. Atrazine chlorohydrolase from Pseudomonas sp. strain ADP: gene sequence, enzyme purification, and protein characterization. J. Bacteriol. 178 (1996) 4894-4900. [Medline UI: 96326334]

*EC 4.1.1.3

Recommended name: oxaloacetate decarboxylase

Reaction: oxalate = pyruvate + CO₂

Other name(s): oxaloacetate β-decarboxylase

Systematic name: oxaloacetate carboxy-lyase

Comments: The enzyme from Klebsiella aerogenes is a.biotinyl protein and also decarboxylates glutaconyl-CoA and methylmalonyl-CoA. The process is accompanied by the extrusion of two sodium ions from cells. Some animal enzymes require Mn²⁺.

References:

1. Dimroth, P. Characterization of a membrane-bound biotin-containing enzyme: oxaloacetate decarboxylase from Klebsiella aerogenes. Eur. J. Biochem. 115 (1981) 353-358. [Medline UI: 81212142]

2. Dimroth, P. The role of biotin and sodium in the decarboxylation of oxaloacetate by the membrane-bound oxaloacetate decarboxylase from Klebsiella aerogenes. Eur. J. Biochem. 121 (1982) 435-441. [Medline UI: 82138806]

3. Herbert, D. Oxalacetic Carboxylase of Micrococcus lysodeikticus. Methods Enzymol. 1 (1955) 753-757.

4. Horton, A.A. and Kornberg, H.L. Oxaloacetate 4-carboxy-lyase from Pseudomonas ovalis Chester. Biochim. Biophys. Acta 89 (1964) 381-383.

5. Schmitt, A., Bottke, I. and Siebert, G. Properties of oxaloacetate decarboxylase from codfish musclesHoppe-Seyler's Z. Physiol. Chem. 347 (1966) 18-34. [Medline UI: 67200360]

EC 4.2.1.100

Recommended name: cyclohexa-1,5-dienecarbonyl-CoA hydratase

Reaction: cyclohexa-1,5-dienecarbonyl-CoA + H₂O = 6-hydroxycyclohex-1-enecarbonyl-CoA

Other names: cyclohexa-1,5-diene-1-carbonyl-CoA hydratase; dienoyl-CoA hydratase

Systematic name: cyclohexa-1,5-dienecarbonyl-CoA hydro-lyase

Comments: The second enzyme of the central benzoyl-CoA pathway of anaerobic metabolism in Thauera aromatica.

References:

1. Laempe, D., Eisenreich, W., Bacher, A. and Fuchs, G. Cyclohexa-1,5-diene-1-carboxyl-CoA hydratase, an enzyme involved in anaerobic metabolism of benzoyl-CoA in the denitrifying bacterium Thauera aromatica. Eur. J. Biochem. 255 (1998) 618-627. [Medline UI: 98409281]

EC 4.2.2.14

Recommended name: glucuronan lyase

Reaction: Eliminative cleavage of (1, 4)-β-D-glucuronans to give oligosaccharides with 4-deoxy-β-Dgluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides.

Systematic name: (1, 4)-β-D-glucuronan lyase

References:

1. Michaud, P., Pheulpin, P., Petit, E., Seguin, J.P., Barbotin, J.N., Heyraud, A., Courtois, B. and Courtois, J. Identification of glucuronan lyase from a mutant strain of Rhizobium meliloti. Int. J. Biol. Macromol. 21 (1997) 3-9. [Medline UI: 97426305]

EC 4.4.1.18

Recommended name: prenylcysteine lyase

Reaction: a prenyl-L-cysteine + H₂O = a prenol + L-cysteine

Systematic name: prenyl-L-cysteine:L-cysteine-lyase

Comments: Cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine. N-Acetyl-prenylcysteine and prenylcysteinyl peptides are not substrates. May represent the final step in the degradation of prenylated proteins in mammalian tissues. In contrast to the monooxygenases (EC 1.14.13.-), neither O₂ nor NADPH are required.

References:

1. Zhang, L., Tschantz, W.R. and Casey, P.J. Isolation and characterization of a prenylcysteine lyase from bovine brain. J. Biol. Chem. 272 (1997) 23354-23359. [Medline UI: 97435309]

[EC 5.3.1.10 transferred entry: now EC 3.5.99.6 Glucosamine-6-phosphate deaminase]

Glossary:

Biuret imidodicarbonic diamide

Cumate 4-isopropylbenzoate

Cyanuric acid 1,3,5-triazine-2,4,6(1H,3H,5H)-trione

Ferulate 4-hydroxy-3-methoxycinnamate

Fluorene cyclopenta[1,2:3,4]dibenzene

Palatinose isomaltulose

Phloroglucinol 1,3,5-trihydroxybenzene

Pimelic acid heptanedioic acid

Pullulan A linear polymer of 1,6-linked maltotriose units.

Vanillate 4-hydroxy-3-methoxybenzoate