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, PDB, 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, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, 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, EAWAG-BBD, EXPASY, KEGG, Metacyc, 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, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, 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, EAWAG-BBD, EXPASY, KEGG, Metacyc, 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 (NAD+)
Reaction: 4-hydroxybenzaldehyde + NAD+ + H2O = 4-hydroxybenzoate + NADH + 2 H+
Other name(s): p-hydroxybenzaldehyde dehydrogenase (ambiguous); 4-hydroxybenzaldehyde dehydrogenase (ambiguous)
Systematic name: 4-hydroxybenzaldehyde:NAD+ oxidoreductase
Comments: The bacterial enzyme (characterized from an unidentified denitrifying bacterium) is involved in an anaerobic toluene degradation pathway. The plant enzyme is involved in formation of 4-hydroxybenzoate, a cell wall-bound phenolic acid that plays a major role in plant defense against pathogens. cf. EC 1.2.1.96, 4-hydroxybenzaldehyde dehydrogenase (NADP+).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, 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. Sircar, D. and Mitra, A. Evidence for p-hydroxybenzoate formation involving enzymatic phenylpropanoid side-chain cleavage in hairy roots of Daucus carota. J. Plant Physiol. 165 (2008) 407-414. [PMID: 17658659]
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, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, 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, EAWAG-BBD, EXPASY, KEGG, Metacyc, 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+
For diagram of reaction click here (another example).
Other name(s): NADP-dependent malonyl CoA reductase; malonyl CoA reductase (NADP); malonyl CoA reductase (malonate semialdehyde-forming)
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-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutanoate 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, PDB, 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+
For diagram of reaction click here.
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-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [2,3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, 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+
For diagram of reaction click here.
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, EAWAG-BBD, EXPASY, KEGG, Metacyc, 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, PDB, 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 dehydrogenase
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 oxygenase; 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+ + CoA
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: NADPH:long-chain acyl-CoA 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, PDB, 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 = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate
Other name(s): xylG (gene name); praB (gene name)
Systematic name: 2-hydroxymuconate-6-semialdehyde: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, EAWAG-BBD, EXPASY, KEGG, Metacyc, 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]
Accepted name: propanal dehydrogenase (CoA-propanoylating)
Reaction: propanal + CoA + NAD+ = propanoyl-CoA + NADH + H+
Other name(s): BphJ
Systematic name: propanal:NAD+ oxidoreductase (CoA-propanoylating)
Comments: The enzyme forms a bifunctional complex with EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase, with a tight channel connecting the two subunits [1,2,3]. Also acts, more slowly, on glycolaldehyde and butanal. In Pseudomonas species the enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). NADP+ can replace NAD+ with a much slower rate [3].
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, PDB, CAS registry number:
References:
1. Baker, P., Pan, D., Carere, J., Rossi, A., Wang, W. and Seah, S.Y.K. Characterization of an aldolase-dehydrogenase complex that exhibits substrate channeling in the polychlorinated biphenyls degradation pathway. Biochemistry 48 (2009) 6551-6558. [PMID: 19476337]
2. Carere, J., Baker, P. and Seah, S.Y.K. Investigating the molecular determinants for substrate channeling in BphI-BphJ, an aldolase-dehydrogenase complex from the polychlorinated biphenyls degradation pathway. Biochemistry 50 (2011) 8407-8416. [PMID: 21838275]
3. Baker, P., Hillis, C., Carere, J. and Seah, S.Y.K. Protein-protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes. Biochemistry 51 (2012) 1942-1952. [PMID: 22316175]
Accepted name: L-glutamate γ-semialdehyde dehydrogenase
Reaction: L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
For diagram of reaction click here.
Glossary: L-glutamate 5-semialdehyde = L-glutamate γ-semialdehyde = (S)-2-amino-5-oxopentanoate
Other name(s): 1-pyrroline-5-carboxylate dehydrogenase; Δ1-pyrroline-5-carboxylate dehydrogenase; 1-pyrroline dehydrogenase; pyrroline-5-carboxylate dehydrogenase; pyrroline-5-carboxylic acid dehydrogenase; L-pyrroline-5-carboxylate-NAD+ oxidoreductase; 1-pyrroline-5-carboxylate:NAD+ oxidoreductase; Δ1-pyrroline-5-carboxylic acid dehydrogenase
Systematic name: L-glutamate γ-semialdehyde:NAD+ oxidoreductase
Comments: This enzyme catalyses the irreversible oxidation of glutamate-γ-semialdehyde to glutamate as part of the proline degradation pathway. (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2, proline dehydrogenase) is in spontaneous equilibrium with its tautomer L-glutamate γ-semialdehyde. In many bacterial species, both activities are carried out by a single bifunctional enzyme [3,4].The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1-pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)-1-pyrroline-5-carboxylate is converted into D-glutamate. NADP+ can also act as acceptor, but with lower activity [5].
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number: 9054-82-4
References:
1. Adams, E. and Goldstone, A. Hydroxyproline metabolism. IV. Enzymatic synthesis of γ-hydroxyglutamate from Δ1-pyrroline-3-hydroxy-5-carboxylate. J. Biol. Chem. 235 (1960) 3504-3512. [PMID: 13681370]
2. Strecker, H.J. The interconversion of glutamic acid and proline. III. Δ1-Pyrroline-5-carboxylic acid dehydrogenase. J. Biol. Chem. 235 (1960) 3218-3223.
3. Forlani, G., Scainelli, D. and Nielsen, E. Δ1-Pyrroline-5-carboxylate dehydrogenase from cultured cells of potato (purification and properties). Plant Physiol. 113 (1997) 1413-1418. [PMID: 12223682]
4. Brown, E.D. and Wood, J.M. Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli. J. Biol. Chem. 267 (1992) 13086-13092. [PMID: 1618807]
5. Inagaki, E., Ohshima, N., Sakamoto, K., Babayeva, N.D., Kato, H., Yokoyama, S. and Tahirov, T.H. New insights into the binding mode of coenzymes: structure of Thermus thermophilus Δ1-pyrroline-5-carboxylate dehydrogenase complexed with NADP+. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 (2007) 462-465. [PMID: 17554163]
Accepted name: D-glyceraldehyde dehydrogenase (NADP+)
Reaction: D-glyceraldehyde + NADP+ + H2O = D-glycerate + NADPH + H+
Other name(s): glyceraldehyde dehydrogenase; GADH
Systematic name: D-glyceraldehyde:NADP+ oxidoreductase
Comments: The enzyme from the archaea Thermoplasma acidophilum and Picrophilus torridus is involved in the non-phosphorylative Entner-Doudoroff pathway. cf. EC 1.2.99.8, glyceraldehyde dehydrogenase (FAD-containing).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Jung, J.H. and Lee, S.B. Identification and characterization of Thermoplasma acidophilum glyceraldehyde dehydrogenase: a new class of NADP+-specific aldehyde dehydrogenase. Biochem. J. 397 (2006) 131-138. [PMID: 16566751]
2. Reher, M. and Schonheit, P. Glyceraldehyde dehydrogenases from the thermoacidophilic euryarchaeota Picrophilus torridus and Thermoplasma acidophilum, key enzymes of the non-phosphorylative Entner-Doudoroff pathway, constitute a novel enzyme family within the aldehyde dehydrogenase superfamily. FEBS Lett 580 (2006) 1198-1204. [PMID: 16458304]
Accepted name: glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+]
Reaction: D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O = 3-phospho-D-glycerate + NAD(P)H + 2 H+
Other name(s): non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (ambiguous); GAPN
Systematic name: D-glyceraldehyde-3-phosphate:NAD(P)+ oxidoreductase
Comments: The enzyme is part of the modified Embden-Meyerhof-Parnas pathway of the archaeon Thermoproteus tenax. cf. EC 1.2.1.9 [glyceraldehyde-3-phosphate dehydrogenase (NADP+)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Brunner, N.A., Brinkmann, H., Siebers, B. and Hensel, R. NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties. J. Biol. Chem. 273 (1998) 6149-6156. [PMID: 9497334]
2. Brunner, N.A., Siebers, B. and Hensel, R. Role of two different glyceraldehyde-3-phosphate dehydrogenases in controlling the reversible Embden-Meyerhof-Parnas pathway in Thermoproteus tenax: regulation on protein and transcript level. Extremophiles 5 (2001) 101-109. [PMID: 11354453]
3. Pohl, E., Brunner, N., Wilmanns, M. and Hensel, R. The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax. J. Biol. Chem. 277 (2002) 19938-19945. [PMID: 11842090]
4. Lorentzen, E., Hensel, R., Knura, T., Ahmed, H. and Pohl, E. Structural basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase from Thermoproteus tenax. J. Mol. Biol. 341 (2004) 815-828. [PMID: 15288789]
Accepted name: 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase
Reaction: 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + NADP+ + H2O = 3-oxo-5,6-dehydrosuberyl-CoA + NADPH + H+
For diagram of reaction click here.
Glossary: 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde = 3,8-dioxooct-5-enoyl-CoA
Other name(s): paaZ (gene name)
Systematic name: 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde:NADP+ oxidoreductase
Comments: The enzyme from Escherichia coli is a bifunctional fusion protein that also catalyses EC 3.3.2.12, oxepin-CoA hydrolase. Combined the two activities result in a two-step conversion of oxepin-CoA to 3-oxo-5,6-dehydrosuberyl-CoA, part of an aerobic phenylacetate degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Ferrandez, A., Minambres, B., Garcia, B., Olivera, E.R., Luengo, J.M., Garcia, J.L. and Diaz, E. Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. J. Biol. Chem. 273 (1998) 25974-25986. [PMID: 9748275]
2. Ismail, W., El-Said Mohamed, M., Wanner, B.L., Datsenko, K.A., Eisenreich, W., Rohdich, F., Bacher, A. and Fuchs, G. Functional genomics by NMR spectroscopy. Phenylacetate catabolism in Escherichia coli. Eur. J. Biochem. 270 (2003) 3047-3054. [PMID: 12846838]
3. Teufel, R., Mascaraque, V., Ismail, W., Voss, M., Perera, J., Eisenreich, W., Haehnel, W. and Fuchs, G. Bacterial phenylalanine and phenylacetate catabolic pathway revealed. Proc. Natl. Acad. Sci. USA 107 (2010) 14390-14395. [PMID: 20660314]
Accepted name: 3,6-anhydro-α-L-galactose dehydrogenase
Reaction: 3,6-anhydro-α-L-galactopyranose + NAD(P)+ + H2O = 3,6-anhydro-L-galactonate + NAD(P)H + H+
Systematic name: 3,6-anhydro-α-L-galactopyranose:NAD(P)+ 1-oxidoredutase
Comments: The enzyme, characterized from the marine bacterium Vibrio sp. EJY3, is involved in a degradation pathway for 3,6-anhydro-α-L-galactose, a major component of the polysaccharides produced by red macroalgae, such as agarose and porphyran.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Yun, E.J., Lee, S., Kim, H.T., Pelton, J.G., Kim, S., Ko, H.J., Choi, I.G. and Kim, K.H. The novel catabolic pathway of 3,6-anhydro-L-galactose, the main component of red macroalgae, in a marine bacterium. Environ Microbiol 17 (2014) 1677-1688. [PMID: 25156229]
[EC 1.2.1.93 Transferred entry: formate dehydrogenase (NAD+, ferredoxin). Now EC 1.17.1.11, formate dehydrogenase (NAD+, ferredoxin) (EC 1.2.1.93 created 2015, deleted 2017)]
Accepted name: farnesal dehydrogenase
Reaction: (2E,6E)-farnesal + NAD+ + H2O = (2E,6E)-farnesoate + NADH + 2 H+
For diagram of reaction click here.
Glossary: farnesal = 3,7,11-trimethyldodeca-2,6,10-trienal
farnesoate = 3,7,11-trimethyldodeca-2,6,10-trienoate
Other name(s): AaALDH3
Systematic name: farnesal:NAD+ oxidoreductase
Comments: Invoved in juvenile hormone production in insects. The enzyme was described from the corpora allata of Drosophila melanogaster (fruit fly), Manduca sexta (tobacco hornworm) and Aedes aegypti (dengue mosquito).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Madhavan, K., Conscience-Egli, M., Sieber, F. and Ursprung, H. Farnesol metabolism in Drosophila melanogaster: ontogeny and tissue distribution of octanol dehydrogenase and aldehyde oxidase. J Insect Physiol 19 (1973) 235-241. [PMID: 4631837]
2. Baker, F.C., Mauchamp, B., Tsai, L.W. and Schooley, D.A. Farnesol and farnesal dehydrogenase(s) in corpora allata of the tobacco hornworm moth, Manduca sexta. J. Lipid Res. 24 (1983) 1586-1594. [PMID: 6366103]
3. Rivera-Perez, C., Nouzova, M., Clifton, M.E., Garcia, E.M., LeBlanc, E. and Noriega, F.G. Aldehyde dehydrogenase 3 converts farnesal into farnesoic acid in the corpora allata of mosquitoes. Insect Biochem. Mol. Biol. 43 (2013) 675-682. [PMID: 23639754]
Accepted name: L-2-aminoadipate reductase
Reaction: (S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate = L-2-aminoadipate + NADPH + H+ + ATP (overall reaction)
(1a) L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein] + AMP + diphosphate = L-2-aminoadipate + holo-[LYS2 peptidyl-carrier-protein] + ATP
(1b) (S)-2-amino-6-oxohexanoate + holo-[LYS2 peptidyl-carrier-protein] + NADP+ = L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein] + NADPH + H+
Glossary: L-2-aminoadipate = (2S)-2-aminohexanedioate
Other name(s): LYS2; α-aminoadipate reductase
Systematic name: (S)-2-amino-6-oxohexanoate:NADP+ oxidoreductase (ATP-forming)
Comments: This enzyme, characterized from the yeast Saccharomyces cerevisiae, catalyses the reduction of L-2-aminoadipate to (S)-2-amino-6-oxohexanoate during L-lysine biosynthesis. An adenylation domain activates the substrate at the expense of ATP hydrolysis, and forms L-2-aminoadipate adenylate, which is attached to a peptidyl-carrier protein (PCP) domain. Binding of NADPH results in reductive cleavage of the acyl-S-enzyme intermediate, releasing (S)-2-amino-6-oxohexanoate. Different from EC 1.2.1.31, L-aminoadipate-semialdehyde dehydrogenase, which catalyses a similar transformation in the opposite direction without ATP hydrolysis.
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References:
1. Ehmann, D.E., Gehring, A.M. and Walsh, C.T. Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of α-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5. Biochemistry 38 (1999) 6171-6177. [PMID: 10320345]
Accepted name: 4-hydroxybenzaldehyde dehydrogenase (NADP+)
Reaction: 4-hydroxybenzaldehyde + NADP+ + H2O = 4-hydroxybenzoate + NADPH + 2 H+
Other name(s): p-hydroxybenzaldehyde dehydrogenase (ambiguous); pchA (gene name)
Systematic name: 4-hydroxybenzaldehyde:NADP+ oxidoreductase
Comments: Involved in the aerobic pathway for degradation of toluene, 4-methylphenol, and 2,4-xylenol by several Pseudomonas strains. The enzyme is also active with 4-hydroxy-3-methylbenzaldehyde. cf. EC 1.2.1.64, 4-hydroxybenzaldehyde dehydrogenase (NAD+).
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References:
1. 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]
2. Chen, Y.F., Chao, H. and Zhou, N.Y. The catabolism of 2,4-xylenol and p-cresol share the enzymes for the oxidation of para-methyl group in Pseudomonas putida NCIMB 9866. Appl. Microbiol. Biotechnol. 98 (2014) 1349-1356. [PMID: 23736872]
Accepted name: 3-sulfolactaldehyde dehydrogenase
Reaction: (2S)-3-sulfolactaldehyde + NAD(P)+ + H2O = (2S)-3-sulfolactate + NAD(P)H + H+
For diagram of reaction click here.
Glossary: (2S)-3-sulfolactaldehyde = (2
Other name(s): SLA dehydrogenase
Systematic name: (2S)-3-sulfolactaldehyde:NAD(P)+ oxidoreductase
Comments: The enzyme, characterized from the bacterium Pseudomonas putida SQ1, participates in a sulfoquinovose degradation pathway. Also acts on succinate semialdehyde.
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References:
1. Felux, A.K., Spiteller, D., Klebensberger, J. and Schleheck, D. Entner-Doudoroff pathway for sulfoquinovose degradation in Pseudomonas putida SQ1. Proc. Natl. Acad. Sci. USA 112 (2015) E4298-E4305. [PMID: 26195800]
Accepted name: 2-hydroxy-2-methylpropanal dehydrogenase
Reaction: 2-hydroxy-2-methylpropanal + NAD+ + H2O = 2-hydroxyisobutanoate + NADH + H+
Other name(s): mpdC (gene name)
Systematic name: 2-hydroxy-2-methylpropanal:NAD+ oxidoreductase
Comments: This bacterial enzyme is involved in the degradation pathways of the alkene 2-methylpropene and the fuel oxygenate methyl tert-butyl ether (MTBE), a widely occurring groundwater contaminant.
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References:
1. Lopes Ferreira, N., Labbe, D., Monot, F., Fayolle-Guichard, F. and Greer, C.W. Genes involved in the methyl tert-butyl ether (MTBE) metabolic pathway of Mycobacterium austroafricanum IFP 2012. Microbiology 152 (2006) 1361-1374. [PMID: 16622053]
Accepted name: 4-(γ-glutamylamino)butanal dehydrogenase
Reaction: 4-(γ-L-glutamylamino)butanal + NAD(P)+ + H2O = 4-(γ-L-glutamylamino)butanoate + NAD(P)H + H+
Other name(s): puuC (gene name)
Systematic name: 4-(γ-L-glutamylamino)butanal:NAD(P)+ oxidoreductase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is involved in a putrescine catabolic pathway. It has a broad substrate range, and can also catalyse the activities of EC 1.2.1.19, aminobutyraldehyde dehydrogenase, and EC 1.2.1.24, succinate-semialdehyde dehydrogenase (NAD+).
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References:
1. Kurihara, S., Oda, S., Kato, K., Kim, H.G., Koyanagi, T., Kumagai, H. and Suzuki, H. A novel putrescine utilization pathway involves γ-glutamylated intermediates of Escherichia coli K-12. J. Biol. Chem. 280 (2005) 4602-4608. [PMID: 15590624]
2. Jo, J.E., Mohan Raj, S., Rathnasingh, C., Selvakumar, E., Jung, W.C. and Park, S. Cloning, expression, and characterization of an aldehyde dehydrogenase from Escherichia coli K-12 that utilizes 3-hydroxypropionaldehyde as a substrate. Appl. Microbiol. Biotechnol. 81 (2008) 51-60. [PMID: 18668238]
3. Schneider, B.L. and Reitzer, L. Pathway and enzyme redundancy in putrescine catabolism in Escherichia coli. J. Bacteriol. 194 (2012) 4080-4088. [PMID: 22636776]
Accepted name: 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase
Reaction: 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NAD+ + H2O = 3-hydroxy-2-methylpyridine-4,5-dicarboxylate + NADH + H+
For diagram of reaction click here.
Other name(s): mlr6793 (locus name)
Systematic name: 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate:NAD+ 5-oxidoreductase
Comments: The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6).
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BRENDA,
EXPASY,
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Metacyc,
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References:
1. Lee, Y.C., Nelson, M.J. and Snell, E.E. Enzymes of vitamin B6 degradation. Purification and properties of isopyridoxal dehydrogenase and 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylic-acid dehydrogenase. J. Biol. Chem 261 (1986) 15106-15111. [PMID: 3533936]
2. Yokochi, N., Yoshikane, Y., Matsumoto, S., Fujisawa, M., Ohnishi, K. and Yagi, T. Gene identification and characterization of 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase, an NAD+-dependent dismutase. J. Biochem. 145 (2009) 493-503. [PMID: 19218190]
3. Mugo, A.N., Kobayashi, J., Mikami, B., Yoshikane, Y., Yagi, T. and Ohnishi, K. Crystal structure of 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase, an NAD(+)-dependent dismutase from Mesorhizobium loti. Biochem. Biophys. Res. Commun. 456 (2015) 35-40. [PMID: 25446130]
Accepted name: L-tyrosine reductase
Reaction: L-tyrosinal + NADP+ + AMP + diphosphate = L-tyrosine + NADPH + H+ + ATP
Glossary: L-tyrosinal = (2S)-2-amino-3-(4-hydroxyphenyl)propanal
Other name(s): lnaA (gene name); lnbA (gene name)
Systematic name: (2S)-2-amino-3-(4-hydroxyphenyl)propanal:NADP+ oxidoreductase (ATP-forming)
Comments: The enzyme, characterized from the ascomycete fungus Aspergillus flavus, is specific for L-tyrosine. It contains three domains - an adenylation domain, a peptidyl-carrier protein (PCP) domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group. The enzyme activates its substrate to an adenylate form, followed by a transfer to the PCP domain. The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to the aldehyde.
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References:
1. Forseth, R.R., Amaike, S., Schwenk, D., Affeldt, K.J., Hoffmeister, D., Schroeder, F.C. and Keller, N.P. Homologous NRPS-like gene clusters mediate redundant small-molecule biosynthesis in Aspergillus flavus. Angew Chem Int Ed Engl 52 (2013) 1590-1594. [PMID: 23281040]
Accepted name: isopyridoxal dehydrogenase (5-pyridoxate-forming)
Reaction: isopyridoxal + NAD+ + H2O = 5-pyridoxate + NADH + H+
Glossary: isopyridoxal = 5-hydroxy-4-(hydroxymethyl)-6-methylpyridine-3-carbaldehyde
Systematic name: isopyridoxal:NAD+ oxidoreductase (5-pyridoxate-forming)
Comments: The enzyme, characterized from the bacterium Arthrobacter sp. Cr-7, participates in the degradation of pyridoxine. The enzyme also catalyses the activity of EC 1.1.1.416, isopyridoxal dehydrogenase (5-pyridoxolactone-forming).
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Lee, Y.C., Nelson, M.J. and Snell, E.E. Enzymes of vitamin B6 degradation. Purification and properties of isopyridoxal dehydrogenase and 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylic-acid dehydrogenase. J. Biol. Chem 261 (1986) 15106-15111. [PMID: 3533936]
Accepted name: [amino group carrier protein]-6-phospho-L-2-aminoadipate reductase
Reaction: an [amino group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + phosphate + NADP+ = an [amino group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + NADPH + H+
Other name(s): lysY (gene name)
Systematic name: [amino group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine:NADP+ 5-oxidoreductase (phosphorylating)
Comments: The enzyme participates in an L-lysine biosynthesis in certain species of archaea and bacteria.
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References:
1. Nishida, H., Nishiyama, M., Kobashi, N., Kosuge, T., Hoshino, T. and Yamane, H. A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: a key to the evolution of amino acid biosynthesis. Genome Res 9 (1999) 1175-1183. [PMID: 10613839]
2. Horie, A., Tomita, T., Saiki, A., Kono, H., Taka, H., Mineki, R., Fujimura, T., Nishiyama, C., Kuzuyama, T. and Nishiyama, M. Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus. Nat. Chem. Biol. 5 (2009) 673-679. [PMID: 19620981]
3. Shimizu, T., Tomita, T., Kuzuyama, T. and Nishiyama, M. Crystal Structure of the LysY.LysW Complex from Thermus thermophilus. J. Biol. Chem 291 (2016) 9948-9959. [PMID: 26966182]
Accepted name: pyruvate dehydrogenase system
Reaction: pyruvate + CoA + NAD+ = acetyl-CoA + CO2 + NADH
Other name(s): pyruvate dehydrogenase complex; PDH
Systematic name: pyruvate:NAD+ 2-oxidoreductase (CoA-acetylating)
Comments: The pyruvate dehydrogenase system (PDH) is a large enzyme complex that belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.25, branched-chain α-keto acid dehydrogenase system, EC 1.2.1.105, 2-oxoglutarate dehydrogenase system, EC 1.4.1.27, glycine cleavage system, and EC 2.3.1.190, acetoin dehydrogenase system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and a dihydrolipoamide dehydrogenase (E3). The reaction catalysed by this system is the sum of three activities: EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring) (E1), EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase (E2), and EC 1.8.1.4, dihydrolipoyl dehydrogenase (E3). The mammalian system also includes E3 binding protein, which is involved in the interaction between the E2 and E3 subunits.
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References:
1. Reed, L.J., Pettit, F.H., Eley, M.H., Hamilton, L., Collins, J.H. and Oliver, R.M. Reconstitution of the Escherichia coli pyruvate dehydrogenase complex. Proc. Natl. Acad. Sci. USA 72 (1975) 3068-3072. [PMID: 1103138]
2. Bates, D.L., Danson, M.J., Hale, G., Hooper, E.A. and Perham, R.N. Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Nature 268 (1977) 313-316. [PMID: 329143]
3. Stanley, C.J., Packman, L.C., Danson, M.J., Henderson, C.E. and Perham, R.N. Intramolecular coupling of active sites in the pyruvate dehydrogenase multienzyme complexes from bacterial and mammalian sources. Biochem. J. 195 (1981) 715-721. [PMID: 7032507]
4. Yang, H.C., Hainfeld, J.F., Wall, J.S. and Frey, P.A. Quaternary structure of pyruvate dehydrogenase complex from Escherichia coli. J. Biol. Chem. 260 (1985) 16049-16051. [PMID: 3905803]
5. Patel, M.S. and Roche, T.E. Molecular biology and biochemistry of pyruvate dehydrogenase complexes. FASEB J. 4 (1990) 3224-3233. [PMID: 2227213]
Accepted name: 2-oxoglutarate dehydrogenase system
Reaction: 2-oxoglutarate + CoA + NAD+ = succinyl-CoA + CO2 + NADH
Other name(s): 2-oxoglutarate dehydrogenase complex
Systematic name: 2-oxoglutarate:NAD+ 2-oxidoreductase (CoA-succinylating)
Comments: The 2-oxoglutarate dehydrogenase system is a large enzyme complex that belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.25, branched-chain α-keto acid dehydrogenase system, EC 1.2.1.104, pyruvate dehydrogenase system, EC 1.4.1.27, glycine cleavage system, and EC 2.3.1.190, acetoin dehydrogenase system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and a dihydrolipoamide dehydrogenase (E3). This enzyme system converts 2-oxoglutarate to succinyl-CoA and produces NADH and CO2 in a complicated series of irreversible reactions. The reaction catalysed by this system is the sum of three activities: EC 1.2.4.2, oxoglutarate dehydrogenase (succinyl-transferring) (E1), EC 2.3.1.61, dihydrolipoyllysine-residue succinyltransferase (E2) and EC 1.8.1.4, dihydrolipoyl dehydrogenase (E3).
Links to other databases:
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References:
1. Robien, M.A., Clore, G.M., Omichinski, J.G., Perham, R.N., Appella, E., Sakaguchi, K. and Gronenborn, A.M. Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli. Biochemistry 31 (1992) 3463-3471. [PMID: 1554728]
2. Knapp, J.E., Mitchell, D.T., Yazdi, M.A., Ernst, S.R., Reed, L.J. and Hackert, M.L. Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J. Mol. Biol. 280 (1998) 655-668. [PMID: 9677295]
3. Reed, L.J. A trail of research from lipoic acid to α-keto acid dehydrogenase complexes. J. Biol. Chem. 276 (2001) 38329-38336. [PMID: 11477096]
4. Murphy, G.E. and Jensen, G.J. Electron cryotomography of the E. coli pyruvate and 2-oxoglutarate dehydrogenase complexes. Structure 13 (2005) 1765-1773. [PMID: 16338405]
5. Frank, R.A., Price, A.J., Northrop, F.D., Perham, R.N. and Luisi, B.F. Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J. Mol. Biol. 368 (2007) 639-651. [PMID: 17367808]
6. Bunik, V.I. and Degtyarev, D. Structure-function relationships in the 2-oxo acid dehydrogenase family: substrate-specific signatures and functional predictions for the 2-oxoglutarate dehydrogenase-like proteins. Proteins 71 (2008) 874-890. [PMID: 18004749]
7. Shim da, J., Nemeria, N.S., Balakrishnan, A., Patel, H., Song, J., Wang, J., Jordan, F. and Farinas, E.T. Assignment of function to histidines 260 and 298 by engineering the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase complex; substitutions that lead to acceptance of substrates lacking the 5-carboxyl group. Biochemistry 50 (2011) 7705-7709. [PMID: 21809826]
Accepted name: [amino-group carrier protein]-5-phospho-L-glutamate reductase
Reaction: an [amino-group carrier protein]-C-terminal-γ-(L-glutamate 5-semialdehyde-2-yl)-L-glutamate + phosphate + NADP+ = an [amino-group carrier protein]-C-terminal-γ-(5-phospho-L-glutamyl)-L-glutamate + NADPH + H+
Other name(s): lysY (gene name)
Systematic name: [amino-group carrier protein]-C-terminal-γ-(L-glutamate 5-semialdehyde-2-yl)-L-glutamate:NADP+ 5-oxidoreductase (phosphorylating)
Comments: The enzyme participates in an L-arginine biosynthesis pathway in certain species of archaea and bacteria. In some organisms the enzyme is bifunctional and also catalyses the activity of EC 1.2.1.103, [amino-group carrier protein]-6-phospho-L-2-aminoadipate reductase.
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EXPASY,
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References:
1. Ouchi, T., Tomita, T., Horie, A., Yoshida, A., Takahashi, K., Nishida, H., Lassak, K., Taka, H., Mineki, R., Fujimura, T., Kosono, S., Nishiyama, C., Masui, R., Kuramitsu, S., Albers, S.V., Kuzuyama, T. and Nishiyama, M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat. Chem. Biol. 9 (2013) 277-283. [PMID: 23434852]
2. Yoshida, A., Tomita, T., Atomi, H., Kuzuyama, T. and Nishiyama, M. Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system. J. Biol. Chem. 291 (2016) 21630-21643. [PMID: 27566549]
Accepted name: glyceraldehyde-3-phosphate dehydrogenase (arsenate-transferring)
Reaction: D-glyceraldehyde 3-phosphate + arsenate + NAD+ = 1-arsono-3-phospho-D-glycerate + NADH + H+
Glossary: 1-arsono-3-phosphoglycerate = [(2R)-2-hydroxy-3-phosphopropanoyl]oxyarsonate
Systematic name: D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (arsenate-transferring)
Comments: The enzyme, discovered in bacteria, is very similar to EC 1.2.1.12, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating). However, the gene encoding it is located in arsenic resistance islands in the chromosome, next to a gene (arsJ) that encodes a transporter that removes the product, 1-arseno-3-phosphoglycerate, from the cell. Together the two proteins form an arsenic detoxification system.
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References:
1. Chen, J., Yoshinaga, M., Garbinski, L.D. and Rosen, B.P. Synergistic interaction of glyceraldehydes-3-phosphate dehydrogenase and ArsJ, a novel organoarsenical efflux permease, confers arsenate resistance. Mol. Microbiol. 100 (2016) 945-953. [PMID: 26991003]
2. Wu, S., Wang, L., Gan, R., Tong, T., Bian, H., Li, Z., Du, S., Deng, Z. and Chen, S. Signature arsenic detoxification pathways in Halomonas sp. strain GFAJ-1. mBio 9 (2018) . [PMID: 29717010]
5-pyridoxate = 3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate
Continued with EC 1.2.2 to EC 1.2.99
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