Accepted name: pyruvate dehydrogenase (NADP+)
Reaction: pyruvate + CoA + NADP+ = acetyl-CoA + CO2 + NADPH
Other name(s): pyruvate dehydrogenase (NADP)
Systematic name: pyruvate:NADP+ 2-oxidoreductase (CoA-acetylating)
Comments: The Euglena enzyme can also use FAD or methyl viologen as acceptor, more slowly. The enzyme is inhibited by oxygen.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 93389-35-6
References:
1. Inui, H., Miyatake, K., Nakano, Y. and Kitaoka, S. Occurrence of oxygen-sensitive, NADP+-dependent pyruvate dehydrogenase in mitochondria of Euglena gracilis. J. Biochem. (Tokyo) 96 (1984) 931-934. [PMID: 6438078]
2. Inui, H., Ono, K., Miyatake, K., Nakano, Y. and Kitaoka, S. Purification and characterization of pyruvate:NADP+ oxidoreductase in Euglena gracilis. J. Biol. Chem. 262 (1987) 9130-9135. [PMID: 3110154]
Accepted name: oxoglutarate dehydrogenase (NADP+)
Reaction: 2-oxoglutarate + CoA + NADP+ = succinyl-CoA + CO2 + NADPH
Other name(s): oxoglutarate dehydrogenase (NADP)
Systematic name: 2-oxoglutarate:NADP+ 2-oxidoreductase (CoA-succinylating)
Comments: The Euglena enzyme can also use NAD+ as acceptor, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 126469-85-0
References:
1. Inui, H., Miyatake, K., Nakano, Y. and Kitaoka, S. Occurrence of oxygen-sensitive, NADP+-dependent pyruvate dehydrogenase in mitochondria of Euglena gracilis. J. Biochem. (Tokyo) 96 (1984) 931-934. [PMID: 6438078]
Accepted name: 4-hydroxyphenylacetaldehyde dehydrogenase
Reaction: 4-hydroxyphenylacetaldehyde + NAD+ + H2O = 4-hydroxyphenylacetate + NADH + 2 H+
Other name(s): 4-HPAL dehydrogenase
Systematic name: 4-hydroxyphenylacetaldehyde:NAD+ oxidoreductase
Comments: With EC 4.2.1.87 octopamine dehydratase, brings about the metabolism of octopamine in Pseudomonas.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 109456-56-6
References:
1. Cuskey, S.M., Peccoraro, V. and Olsen, R.H. Initial catabolism of aromatic biogenic amines by Pseudomonas aeruginosa PAO: pathway description, mapping of mutations, and cloning of essential genes. J. Bacteriol. 169 (1987) 2398-2404. [PMID: 3034855]
Accepted name: γ-guanidinobutyraldehyde dehydrogenase
Reaction: 4-guanidinobutanal + NAD+ + H2O = 4-guanidinobutanoate + NADH + 2 H+
For diagram, click here
Other name(s): α-guanidinobutyraldehyde dehydrogenase; 4-guanidinobutyraldehyde dehydrogenase; GBAL dehydrogenase
Systematic name: 4-guanidinobutanal:NAD+ 1-oxidoreductase
Comments: Involved in the degradation of arginine in Pseudomonas putida (cf. EC 1.2.1.19 aminobutyraldehyde dehydrogenase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 56831-75-5
References:
1. Yorifuji, T., Koike, K., Sakurai, T. and Yokoyama, K. 4-Aminobutyraldehyde and 4-guanidinobutyraldehyde dehydrogenases for arginine degradation in Pseudomonas putida. Agric. Biol. Chem. 50 (1986) 2009-2016.
[EC 1.2.1.55 Transferred entry: now EC 1.1.1.279 (R)-3-hydroxyacid ester dehydrogenase. (EC 1.2.1.55 created 1990, deleted 2003)]
[EC 1.2.1.56 Transferred entry: now EC 1.1.1.280 (S)-3-hydroxyacid ester dehydrogenase. (EC 1.2.1.56 created 1990, deleted 2003)]
Accepted name: butanal dehydrogenase
Reaction: butanal + CoA + NAD(P)+ = butanoyl-CoA + NAD(P)H + H+
Systematic name: butanal:NAD(P)+ oxidoreductase (CoA-acylating)
Comments: Also acts on acetaldehyde, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 116412-25-0
References:
1. Palosaari, N.R. and Rogers, P. Purification and properties of the inducible coenzyme A-linked butyraldehyde dehydrogenase from Clostridium acetobutylicum. J. Bacteriol. 170 (1988) 2971-2976.
Accepted name: phenylglyoxylate dehydrogenase (acylating)
Reaction: phenylglyoxylate + NAD+ + CoA = benzoyl-S-CoA + CO2 + NADH
Glossary: thiamine diphosphate
Systematic name: phenylglyoxylate:NAD+ oxidoreductase
Comments: requires thiamine diphosphate as cofactor. The enzyme from the denitrifying bacterium Azoarcus evansii is specific for phenylglyoxylate. 2-Oxoisovalerate is oxidized at 15% of the rate for phenylglyoxylate. Also reduces viologen dyes. Contains iron-sulfur centres and FAD.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 205510-78-7
References:
1. Hirsch, W., Schägger, H. and Fuchs, G. Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new enzyme of anaerobic phenylalanine metabolism in the denitrifying bacterium Axoarcus evansii. Eur. J. Biochem. 251 (1998) 907-915. [PMID: 9490067]
Accepted name: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)
Reaction: D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ = 3-phospho-D-glyceroyl phosphate + NAD(P)H + H+
Other name(s): triosephosphate dehydrogenase (NAD(P)); glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating)
Systematic name: D-glyceraldehyde 3-phosphate:NAD(P)+ oxidoreductase (phosphorylating)
Comments: NAD+ and NADP+ can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and EC 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating), which are NAD+- and NADP+-dependent, respectively.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 39369-25-0
References:
1. Valverde, F., Losada, M. and Serrano, A. Cloning by functional complementation in E. coli of the gap2 gene of Synechocystis PCC 6803 supports an amphibolic role for cyanobacterial NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase. In: Photosynthesis: From Light to Biosphere (P. Mathis, ed.), Vol. 1 (1995) pp. 959-962. Kluwer Academic Publishers.
2. Valverde, F., Losada, M. and Serrano, A. Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803. J. Bacteriol. 179 (1997) 4513-4522. [PMID: 9226260]
Accepted name: 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase
Reaction: 5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+ = 5-carboxymethyl-2-hydroxymuconate + NADH + 2 H+
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.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 63241-20-3
References:
1. Blakley, E.R. The catabolism of L-tyrosine by an Arthrobacter sp. Can. J. Microbiol. 23 (1977) 1128-1139. [PMID: 20216]
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. [PMID: 6756482]
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. [PMID: 6995433]
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.
Accepted name: 4-hydroxymuconic-semialdehyde dehydrogenase
Reaction: 4-hydroxymuconic semialdehyde + NAD+ + H2O = maleylacetate + NADH + 2 H+
For diagram of reaction click here.
Systematic name: 4-hydroxymuconic-semialdehyde:NAD+ oxidoreductase
Comments: Involved in the 4-nitrophenol degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:
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.
Accepted name: 4-formylbenzenesulfonate dehydrogenase
Reaction: 4-formylbenzenesulfonate + NAD+ + H2O = 4-sulfobenzoate + NADH + 2 H+
Systematic name: 4-formylbenzenesulfonate:NAD+ oxidoreductase
Comments: Involved in the toluene-4-sulfonate degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 167973-68-4
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. [PMID: 8828208]
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. [PMID: 9006050]
Accepted name: 6-oxohexanoate dehydrogenase
Reaction: 6-oxohexanoate + NADP+ + H2O = adipate + NADPH + 2 H+
Systematic name: 6-oxohexanoate:NADP+ oxidoreductase
Comments: Last step in the cyclohexanol degradation pathway in Acinetobacter sp.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 62628-29-9
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. [PMID: 856571]
2. Donoghue, N.A. and Trudgill P.W. The metabolism of cyclohexanol by Acinetobacter NCIB 9871. Eur. J. Biochem. 60 (1975) 1-7. [PMID: 1261]
Accepted name: 4-hydroxybenzaldehyde dehydrogenase
Reaction: 4-hydroxybenzaldehyde + NAD+ + H2O = 4-hydroxybenzoate + NADH + 2 H+
Other name(s): p-hydroxybenzaldehyde dehydrogenase
Systematic name: 3-hydroxybenzaldehyde:NAD+ oxidoreductase
Comments: Involved in the toluene degradation pathway in Pseudomonas mendocina.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 61229-72-9
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. [PMID: 2722739]
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. [PMID: 2019564]
Accepted name: salicylaldehyde dehydrogenase
Reaction: salicylaldehyde + NAD+ + H2O = salicylate + NADH + 2 H+
Glossary: salicylaldehyde = 2-hydroxybenzaldehyde
Systematic name: salicylaldehyde:NAD+ oxidoreductase
Comments: Involved in the naphthalene degradation pathway in some bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 55354-34-2
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. [PMID: 1447127]
[EC 1.2.1.66 Transferred entry: mycothiol-dependent formaldehyde dehydrogenase. Now EC 1.1.1.306, S-(hydroxymethyl)mycothiol dehydrogenase (EC 1.2.1.66 created 2000, deleted 2010)]
Accepted name: vanillin dehydrogenase
Reaction: vanillin + NAD+ + H2O = vanillate + NADH + 2 H+
Glossary entries:
Vanillate: 4-hydroxy-3-methoxybenzoate
Vanillin: 4-hydroxy-3-methoxybenzaldehyde
Systematic name: vanillin:NAD+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 189767-93-9
References:
1. Pometto, A.L. and Crawford, D.L. Whole-cell bioconversion of vanillin to vanillic acid by Streptomyces viridosporus. Appl. Environ. Microbiol. 45 (1983) 1582-1585. [PMID: 6870241]
Accepted name: coniferyl-aldehyde dehydrogenase
Reaction: coniferyl aldehyde + H2O + NAD(P)+ = ferulate + NAD(P)H + 2 H+
For reaction pathway click here.
Systematic name: coniferyl aldehyde:NAD(P)+ oxidoreductase
Comments: Also oxidizes other aromatic aldehydes, but not aliphatic aldehydes.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 208540-41-4
References:
1. Achterholt, S., Priefert, H. and Steinbuchel, A. Purification and characterization of the coniferyl 2-hydroxy-1,4-benzoquinonealdehyde dehydrogenase from Pseudomonas sp. Strain HR199 and molecular characterization of the gene. J. Bacteriol. 180 (1998) 4387-4391. [PMID: 9721273]
Accepted name: fluoroacetaldehyde dehydrogenase
Reaction: fluoroacetaldehyde + NAD+ + H2O = fluoroacetate + NADH + 2 H+
Systematic name: fluoroacetaldehyde:NAD+ oxidoreductase
Comments: The enzyme from Streptomyces cattleya has a high affinity for fluoroacetate and glycolaldehyde but not for acetaldehyde.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 387336-50-7
References:
1. Murphy, C.D., Moss, S.J. and O'Hagan, D. Isolation of an aldehyde dehydrogenase involved in the oxidation of fluoroacetaldehyde to fluoroacetate in Streptomyces cattleya. Appl. Environ. Microbiol. 67 (2001) 4919-4921. [PMID: 11571203]
2. Murphy, C.D., Schaffrath, C. and O'Hagan, D. Fluorinated natural products: the biosynthesis of fluoroacetate and 4-fluorothreonine in Streptomyces cattleya. Chemosphere 52 (2003) 455-461. [PMID: 12738270]
Accepted name: glutamyl-tRNA reductase
Reaction: L-glutamate 1-semialdehyde + NADP+ + tRNAGlu = L-glutamyl-tRNAGlu + NADPH + H+
For diagram click here.
Systematic name: L-glutamate-semialdehyde: NADP+ oxidoreductase (L-glutamyl-tRNAGlu-forming)
Comments: This enzyme forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway. The route shown in the diagram is used in most eubacteria, and in all archaebacteria, algae and plants. However, in the α-proteobacteria, EC 2.3.1.37, 5-aminolevulinate synthase, is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic α-proteobacterium. 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.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 119940-26-0
References:
1. von Wettstein, D., Gough, S. and Kannangara, C.G. Chlorophyll biosynthesis. Plant Cell 7 (1995) 1039-1057. [PMID: 12242396]
2. Pontoppidan, B. and Kannangara, C.G. Purification and partial characterisation of barley glutamyl-tRNAGlu reductase, the enzyme that directs glutamate to chlorophyll biosynthesis. Eur. J. Biochem. 225 (1994) 529-537. [PMID: 7957167]
3. Schauer, S., Chaturvedi, S., Randau, L., Moser, J., Kitabatake, M., Lorenz, S., Verkamp, E., Schubert, W.D., Nakayashiki, T., Murai, M., Wall, K., Thomann, H.-U., Heinz, D.W., Inokuchi, H, Söll, D. and Jahn, D. Escherichia coli glutamyl-tRNA reductase. Trapping the thioester intermediate. J. Biol. Chem. 277 (2002) 48657-48663. [PMID: 12370189]
Accepted name: succinylglutamate-semialdehyde dehydrogenase
Reaction: N-succinyl-L-glutamate 5-semialdehyde + NAD+ + H2O = N-succinyl-L-glutamate + NADH + 2 H+
For diagram, click here or click here.
Other name(s): succinylglutamic semialdehyde dehydrogenase; N-succinylglutamate 5-semialdehyde dehydrogenase; SGSD; AruD; AstD
Systematic name: N-succinyl-L-glutamate 5-semialdehyde:NAD+ oxidoreductase
Comments: This is the fourth enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. 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 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.11 (acetylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase) [3,6].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Vander Wauven, C., Jann, A., Haas, D., Leisinger, T. and Stalon, V. N2-succinylornithine in ornithine catabolism of Pseudomonas aeruginosa. Arch. Microbiol. 150 (1988) 400-404. [PMID: 3144259]
2. Vander Wauven, C. and Stalon, V. Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia. J. Bacteriol. 164 (1985) 882-886. [PMID: 2865249]
3. Tricot, C., Vander Wauven, C., Wattiez, R., Falmagne, P. and Stalon, V. Purification and properties of a succinyltransferase from Pseudomonas aeruginosa specific for both arginine and ornithine. Eur. J. Biochem. 224 (1994) 853-861. [PMID: 7523119]
4. Itoh, Y. Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa. J. Bacteriol. 179 (1997) 7280-7290. [PMID: 9393691]
5. Schneider, B.L., Kiupakis, A.K. and Reitzer, L.J. Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. J. Bacteriol. 180 (1998) 4278-4286. [PMID: 9696779]
6. Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V. Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev. 50 (1986) 314-352. [PMID: 3534538]
Accepted name: erythrose-4-phosphate dehydrogenase
Reaction: D-erythrose 4-phosphate + NAD+ + H2O = 4-phosphoerythronate + NADH + 2 H+
For diagram, click here
Other name(s): erythrose 4-phosphate dehydrogenase; E4PDH; GapB; Epd dehydrogenase; E4P dehydrogenase
Systematic name: D-erythrose 4-phosphate:NAD+ oxidoreductase
Comments: This enzyme was originally thought to be a glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), but this has since been disproved, as glyceraldehyde 3-phosphate is not a substrate [1,2]. Forms part of the pyridoxal-5'-phosphate coenzyme biosynthesis pathway in Escherichia coli, along with EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (pyridoxamine-phosphate oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 131554-04-6
References:
1. Zhao, G., Pease, A.J., Bharani, N. and Winkler, M.E. Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis. J. Bacteriol. 177 (1995) 2804-2812. [PMID: 7751290]
2. Boschi-Muller, S., Azza, S., Pollastro, D., Corbier, C. and Branlant, G. Comparative enzymatic properties of GapB-encoded erythrose-4-phosphate dehydrogenase of Escherichia coli and phosphorylating glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 272 (1997) 15106-15112. [PMID: 9182530]
3. Yang, Y., Zhao, G., Man, T.K. and Winkler, M.E. Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12. J. Bacteriol. 180 (1998) 4294-4299. [PMID: 9696782]
Accepted name: sulfoacetaldehyde dehydrogenase
Reaction: 2-sulfoacetaldehyde + H2O + NAD+ = sulfoacetate + NADH + 2 H+
Glossary: 2-sulfoacetaldehyde = 2-oxoethanesulfonate
taurine = 2-aminoethanesulfonate
Other name(s): SafD
Systematic name: 2-sulfoacetaldehyde:NAD+ oxidoreductase
Comments: This reaction is part of a bacterial pathway that can utilize the amino group of taurine as a sole source of nitrogen for growth. At physiological concentrations, NAD+ cannot be replaced by NADP+. The enzyme is specific for sulfoacetaldehyde, as formaldehyde, acetaldehyde, betaine aldehyde, propanal, glyceraldehyde, phosphonoacetaldehyde, glyoxylate, glycolaldehyde and 2-oxobutyrate are not substrates.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Krejčík, Z., Denger, K., Weinitschke, S., Hollemeyer, K., Pačes, V., Cook, A.M. and Smits, T.H.M. Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: purification of sulfoacetaldehyde dehydrogenase. Arch. Microbiol. 190 (2008) 159-168. [PMID: 18506422]
Note For the reference an accent may not be seen. č is c-hacek.
Accepted name: abieta-7,13-dien-18-al dehydrogenase
Reaction: abieta-7,13-dien-18-al + H2O + NAD+ = abieta-7,13-dien-18-oate + NADH + H+
For diagram of reaction click here
Glossary: abieta-7,13-dien-18-al = (1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene-1-carbaldehyde
abieta-7,13-dien-18-oate = (1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene-1-carboxylate
Other name(s): abietadienal dehydrogenase (ambiguous)
Systematic name: abieta-7,13-dien-18-al:NAD+ oxidoreductase
Comments: Abietic acid is the principle component of conifer resin. This enzyme catalyses the last step of the pathway of abietic acid biosynthesis in Abies grandis (grand fir). The activity has been demonstrated in cell-free stem extracts of A. grandis, was present in the cytoplasm, and required NAD+ as cofactor [1]. The enzyme is expressed constitutively at a high level, and is not inducible by wounding of the plant tissue [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Funk, C. and Croteau, R. Diterpenoid resin acid biosynthesis in conifers: characterization of two cytochrome P450-dependent monooxygenases and an aldehyde dehydrogenase involved in abietic acid biosynthesis. Arch. Biochem. Biophys. 308 (1994) 258-266. [PMID: 8311462]
2. Funk, C., Lewinsohn, E., Vogel, B.S., Steele, C.L. and Croteau, R. Regulation of oleoresinosis in grand fir (Abies grandis) (coordinate induction of monoterpene and diterpene cyclases and two cytochrome P450-dependent diterpenoid hydroxylases by stem wounding). Plant Physiol. 106 (1994) 999-1005. [PMID: 12232380]
Accepted name: malonyl CoA reductase (malonate semialdehyde-forming)
Reaction: malonate semialdehyde + CoA + NADP+ = malonyl-CoA + NADPH + H+
Other name(s): NADP-dependent malonyl CoA reductase; malonyl CoA reductase (NADP)
Systematic name: malonate semialdehyde:NADP+ oxidoreductase (malonate semialdehyde-forming)
Comments: Requires Mg2+. Catalyses the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropionate and the 3-hydroxypropionate/4-hydroxybutyrate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and some thermoacidophilic archaea, respectively [1,2]. The enzyme from Sulfolobus tokodaii has been purified, and found to contain one RNA molecule per two subunits [3]. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the next reaction in the pathway, EC 1.1.1.298 [3-hydroxypropionate dehydrogenase (NADP+)] [4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Strauss, G. and Fuchs, G. Enzymes of a novel autotrophic CO2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle. Eur. J. Biochem. 215 (1993) 633-643. [PMID: 8354269]
2. Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782-1786. [PMID: 18079405]
3. Alber, B., Olinger, M., Rieder, A., Kockelkorn, D., Jobst, B., Hugler, M. and Fuchs, G. Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp. J. Bacteriol. 188 (2006) 8551-8559. [PMID: 17041055]
4. Hugler, M., Menendez, C., Schagger, H. and Fuchs, G. Malonyl-coenzyme A reductase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO2 fixation. J. Bacteriol. 184 (2002) 2404-2410. [PMID: 11948153]
Accepted name: succinate-semialdehyde dehydrogenase (acetylating)
Reaction: succinate semialdehyde + CoA + NADP+ = succinyl-CoA + NADPH + H+
Other name(s): succinyl-coA reductase; coenzyme-A-dependent succinate-semialdehyde dehydrogenase
Systematic name: succinate semialdehyde:NADP+ oxidoreductase (CoA-acetylating)
Comments: Catalyses the NADPH-dependent reduction of succinyl-CoA to succinate semialdehyde. The enzyme has been described in Clostridium kluyveri, where it participates in succinate fermentation [1]), and in Metallosphaera sedula, where it participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [2,3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Sohling, B. and Gottschalk, G. Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri. Eur. J. Biochem. 212 (1993) 121-127. [PMID: 8444151]
2. Alber, B., Olinger, M., Rieder, A., Kockelkorn, D., Jobst, B., Hugler, M. and Fuchs, G. Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp. J. Bacteriol. 188 (2006) 8551-8559. [PMID: 17041055]
3. Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782-1786. [PMID: 18079405]
Accepted name: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)
Reaction: 3,4-didehydroadipyl-CoA semialdehyde + NADP+ + H2O = 3,4-didehydroadipyl-CoA + NADPH + H+
Other name(s): BoxD; 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase
Systematic name: 3,4-didehydroadipyl-CoA semialdehyde:NADP+ oxidoreductase
Comments: This enzyme catalyses a step in the aerobic benzoyl-coenzyme A catabolic pathway in Azoarcus evansii and Burkholderia xenovorans.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:
References:
1. Gescher, J., Ismail, W., Olgeschlager, E., Eisenreich, W., Worth, J. and Fuchs, G. Aerobic benzoyl-coenzyme A (CoA) catabolic pathway in Azoarcus evansii: conversion of ring cleavage product by 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase. J. Bacteriol. 188 (2006) 2919-2927. [PMID: 16585753]
2. Bains, J. and Boulanger, M.J. Structural and biochemical characterization of a novel aldehyde dehydrogenase encoded by the benzoate oxidation pathway in Burkholderia xenovorans LB400. J. Mol. Biol. 379 (2008) 597-608. [PMID: 18462753]
Accepted name: 2-formylbenzoate dehydrogenase
Reaction: 2-formylbenzoate + NAD+ + H2O = o-phthalic acid + NADH + H+
Glossary: o-phthalic acid = benzene-1,2-dicarboxylic acid
2-formylbenzoate = 2-carboxybenzaldehyde
Other name(s): 2-carboxybenzaldehyde dehydrogenase; 2CBAL dehydrogenase; PhdK
Systematic name: 2-formylbenzoate:NAD+ oxidoreductase
Comments: The enzyme is involved in phenanthrene degradation.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Iwabuchi, T. and Harayama, S. Biochemical and genetic characterization of 2-carboxybenzaldehyde dehydrogenase, an enzyme involved in phenanthrene degradation by Nocardioides sp. strain KP7. J. Bacteriol. 179 (1997) 6488-6494. [PMID: 9335300]
2. Kiyohara, H., Nagao, K. and Yano, K. Isolation and some properties of NAD-linked 2-carboxybenzaldehyde dehydrogenase in Alcaligenes faecalis AFK 2 grown on phenanthrene. J. Gen. Appl. Microbiol. 27 (1981) 443-455.
Accepted name: succinate-semialdehyde dehydrogenase (NADP+)
Reaction: succinate semialdehyde + NADP+ + H2O = succinate + NADPH + 2 H+
Other name(s): succinic semialdehyde dehydrogenase (NADP+); succinyl semialdehyde dehydrogenase (NADP+); succinate semialdehyde:NADP+ oxidoreductase; NADP-dependent succinate-semialdehyde dehydrogenase; GabD
Systematic name: succinate-semialdehyde:NADP+ oxidoreductase
Comments: This enzyme participates in the degradation of glutamate and 4-aminobutyrate. It is similar to EC 1.2.1.24 [succinate-semialdehyde dehydrogenase (NAD+)], and EC 1.2.1.16 [succinate-semialdehyde dehydrogenase (NAD(P)+)], but is specific for NADP+. The enzyme from Escherichia coli is 20-fold more active with NADP+ than NAD+ [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Bartsch, K., von Johnn-Marteville, A. and Schulz, A. Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD). J. Bacteriol. 172 (1990) 7035-7042. [PMID: 2254272]
2. Jaeger, M., Rothacker, B. and Ilg, T. Saturation transfer difference NMR studies on substrates and inhibitors of succinic semialdehyde dehydrogenases. Biochem. Biophys. Res. Commun. 372 (2008) 400-406. [PMID: 18474219]
Accepted name: long-chain acyl-[acyl-carrier-protein] reductase
Reaction: a long-chain aldehyde + an [acyl-carrier protein] + NAD(P)+ = a long-chain acyl-[acyl-carrier protein] + NAD(P)H + H+
Glossary: a long-chain aldehyde = a fatty aldehyde
acyl-carrier protein = ACP = [acp]
Other name(s): long-chain acyl-[acp] reductase; fatty acyl-[acyl-carrier-protein] reductase; acyl-[acp] reductase
Systematic name: long-chain-aldehyde:NAD(P)+ oxidoreductase (acyl-[acyl-carrier protein]-forming)
Comments: Catalyses the reaction in the opposite direction. This enzyme, purified from the cyanobacterium Synechococcus elongatus PCC 7942, catalyses the NAD(P)HÐdependent reduction of an activated fatty acid (acyl-[acp]) to the corresponding aldehyde. Together with EC 4.1.99.5, octadecanal decarbonylase, it is involved in alkane biosynthesis. The natural substrates of the enzyme are C16 to C18 activated fatty acids. Requires Mg2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Schirmer, A., Rude, M.A., Li, X., Popova, E. and del Cardayre, S.B. Microbial biosynthesis of alkanes. Science 329 (2010) 559-562. [PMID: 20671186]
Accepted name: sulfoacetaldehyde dehydrogenase (acylating)
Reaction: 2-sulfoacetaldehyde + CoA + NADP+ = sulfoacetyl-CoA + NADPH + H+
Glossary: 2-sulfoacetaldehyde = 2-oxoethanesulfonate
Other name(s): SauS
Systematic name: 2-sulfoacetaldehyde:NADP+ oxidoreductase (CoA-acetylating)
Comments: The enzyme is involved in degradation of sulfoacetate. In this pathway the reaction is catalysed in the reverse direction. The enzyme is specific for sulfoacetaldehyde and NADP+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Weinitschke, S., Hollemeyer, K., Kusian, B., Bowien, B., Smits, T.H. and Cook, A.M. Sulfoacetate is degraded via a novel pathway involving sulfoacetyl-CoA and sulfoacetaldehyde in Cupriavidus necator H16. J. Biol. Chem. 285 (2010) 35249-35254. [PMID: 20693281]
Accepted name: β-apo-4'-carotenal oxygenase
Reaction: 4'-apo-β,ψ-caroten-4'-al + NAD+ + H2O = neurosporaxanthin + NADH + 2 H+
For diagram of reaction click here
Glossary: neurosporaxanthin = 4'-apo-β,ψ-caroten-4'-oic acid
Other name(s): β-apo-4'-carotenal dehydrogenase; YLO-1; carD (gene name)
Systematic name: 4'-apo-β,ψ-carotenal:NAD+ oxidoreductase
Comments: Neurosporaxanthin is responsible for the orange color of of Neurospora.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Estrada, A.F., Youssar, L., Scherzinger, D., Al-Babili, S. and Avalos, J. The ylo-1 gene encodes an aldehyde dehydrogenase responsible for the last reaction in the Neurospora carotenoid pathway. Mol. Microbiol. 69 (2008) 1207-1220. [PMID: 18627463]
2. Diaz-Sanchez, V., Estrada, A.F., Trautmann, D., Al-Babili, S. and Avalos, J. The gene carD encodes the aldehyde dehydrogenase responsible for neurosporaxanthin biosynthesis in Fusarium fujikuroi. FEBS J. 278 (2011) 3164-3176. [PMID: 21749649]
Accepted name: 3-succinoylsemialdehyde-pyridine dehydrogenase
Reaction: 4-oxo-4-(pyridin-3-yl)butanal + NADP+ + H2O = 4-oxo-4-(pyridin-3-yl)butanoate + NADPH + H+
Glossary: 4-oxo-4-(pyridin-3-yl)butanal = 3-succinoylsemialdehyde-pyridine
4-oxo-4-(3-pyridyl)-butanoate = 3-succinoyl-pyridine
Systematic name: 4-oxo-4-(pyridin-3-yl)butanal:NADP+ oxidoreductase
Comments: The enzyme has been characterized from the soil bacterium Pseudomonas sp. HZN6. It participates in the nicotine degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Qiu, J., Ma, Y., Wen, Y., Chen, L., Wu, L. and Liu, W. Functional identification of two novel genes from Pseudomonas sp. strain HZN6 involved in the catabolism of nicotine. Appl. Environ. Microbiol. 78 (2012) 2154-2160. [PMID: 22267672]
Accepted name: alcohol-forming fatty acyl-CoA reductase
Reaction: a long-chain acyl-CoA + 2 NADPH + 2 H+ = a long-chain alcohol + 2 NADP+ + coenzyme A
Glossary: a long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 13 to 22 carbon atoms.
Other name(s): FAR (gene name)
Systematic name: long-chain acyl-CoA:NADPH reductase
Comments: The enzyme has been characterized from the plant Simmondsia chinensis (jojoba). The alcohol is formed by a four-electron reduction of fatty acyl-CoA. Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released. The recombinant enzyme was shown to accept saturated and mono-unsaturated fatty acyl-CoAs of 16 to 22 carbons.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Metz, J.G., Pollard, M.R., Anderson, L., Hayes, T.R. and Lassner, M.W. Purification of a jojoba embryo fatty acyl-coenzyme A reductase and expression of its cDNA in high erucic acid rapeseed. Plant Physiol. 122 (2000) 635-644. [PMID: 10712526]
Accepted name: 2-hydroxymuconate-6-semialdehyde dehydrogenase
Reaction: 2-hydroxymuconate-6-semialdehyde + NAD+ + H2O = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
For diagram of reaction click here.
Glossary: 2-hydroxymuconate-6-semialdehyde = (2E,4Z)-2-hydroxy-6-oxohexa-2,4-dienoate
Other name(s): xylG (gene name); praB (gene name)
Systematic name: (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate:NAD+ oxidoreductase
Comments: This substrate for this enzyme is formed by meta ring cleavage of catechol (EC 1.13.11.2, catechol 2,3-dioxygenase), and is an intermediate in the bacterial degradation of several aromatic compounds. Has lower activity with benzaldehyde [1]. Activity with NAD+ is more than 10-fold higher than with NADP+ [3]. cf. EC 1.2.1.32, aminomuconate-semialdehyde dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Inoue, J., Shaw, J.P., Rekik, M. and Harayama, S. Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida. J. Bacteriol. 177 (1995) 1196-1201. [PMID: 7868591]
2. Orii, C., Takenaka, S., Murakami, S. and Aoki, K. Metabolism of 4-amino-3-hydroxybenzoic acid by Bordetella sp. strain 10d: A different modified meta-cleavage pathway for 2-aminophenols. Biosci. Biotechnol. Biochem. 70 (2006) 2653-2661. [PMID: 17090920]
3. Kasai, D., Fujinami, T., Abe, T., Mase, K., Katayama, Y., Fukuda, M. and Masai, E. Uncovering the protocatechuate 2,3-cleavage pathway genes. J. Bacteriol. 191 (2009) 6758-6768. [PMID: 19717587]
Accepted name: geranial dehydrogenase
Reaction: geranial + H2O + NAD+ = geranate + NADH + H+
For diagram of reaction click here.
Other name(s): GaDH; geoB (gene name)
Systematic name: geranial:NAD+ oxidoreductase
Comments: Does not act on neral.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:
References:
1. Wolken, W.A. and van der Werf, M.J. Geraniol biotransformation-pathway in spores of Penicillium digitatum. Appl. Microbiol. Biotechnol. 57 (2001) 731-737. [PMID: 11778886]
2. Lüddeke, F., Wülfing, A., Timke, M., Germer, F., Weber, J., Dikfidan, A., Rahnfeld, T., Linder, D., Meyerdierks, A. and Harder, J. Geraniol and geranial dehydrogenases induced in anaerobic monoterpene degradation by Castellaniella defragrans. Appl. Environ. Microbiol. 78 (2012) 2128-2136. [PMID: 22286981]