Enzyme Nomenclature

EC 1.2.1 (continued)

with NAD or NADP as acceptor

Continued from EC 1.2.1.1 to EC 1.2.1.50

Contents

EC 1.2.1.51 pyruvate dehydrogenase (NADP+)
EC 1.2.1.52 oxoglutarate dehydrogenase (NADP+)
EC 1.2.1.53 4-hydroxyphenylacetaldehyde dehydrogenase
EC 1.2.1.54 γ-guanidinobutyraldehyde dehydrogenase
EC 1.2.1.55 now EC 1.1.1.279
EC 1.2.1.56 now EC 1.1.1.280
EC 1.2.1.57 butanal dehydrogenase
EC 1.2.1.58 phenylglyoxylate dehydrogenase (acylating)
EC 1.2.1.59 glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)
EC 1.2.1.60 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase
EC 1.2.1.61 4-hydroxymuconic semialdehyde dehydrogenase
EC 1.2.1.62 4-formylbenzenesulfonate dehydrogenase
EC 1.2.1.63 6-oxohexanoate dehydrogenase
EC 1.2.1.64 4-hydroxybenzaldehyde dehydrogenase (NAD+)
EC 1.2.1.65 salicylaldehyde dehydrogenase
EC 1.2.1.66 transferred now EC 1.1.1.306
EC 1.2.1.67 vanillin dehydrogenase
EC 1.2.1.68 coniferyl-aldehyde dehydrogenase
EC 1.2.1.69 fluoroacetaldehyde dehydrogenase
EC 1.2.1.70 glutamyl-tRNA reductase
EC 1.2.1.71 succinylglutamate-semialdehyde dehydrogenase
EC 1.2.1.72 erythrose-4-phosphate dehydrogenase
EC 1.2.1.73 sulfoacetaldehyde dehydrogenase
EC 1.2.1.74 abieta-7,13-dien-18-al dehydrogenase
EC 1.2.1.75 malonyl CoA reductase (malonate semialdehyde-forming)
EC 1.2.1.76 succinate-semialdehyde dehydrogenase (acetylating)
EC 1.2.1.77 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)
EC 1.2.1.78 2-formylbenzoate dehydrogenase
EC 1.2.1.79 succinate-semialdehyde dehydrogenase (NADP+)
EC 1.2.1.80 long-chain acyl-[acyl-carrier-protein] reductase
EC 1.2.1.81 sulfoacetaldehyde dehydrogenase (acylating)
EC 1.2.1.82 β-apo-4'-carotenal oxygenase
EC 1.2.1.83 3-succinoylsemialdehyde-pyridine dehydrogenase
EC 1.2.1.84 alcohol-forming fatty acyl-CoA reductase
EC 1.2.1.85 2-hydroxymuconate-6-semialdehyde dehydrogenase
EC 1.2.1.86 geranial dehydrogenase
EC 1.2.1.87 propanal dehydrogenase (CoA-propanoylating)
EC 1.2.1.88 L-glutamate γ-semialdehyde dehydrogenase
EC 1.2.1.89 D-glyceraldehyde dehydrogenase (NADP+)
EC 1.2.1.90 glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+]
EC 1.2.1.91 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase
EC 1.2.1.92 3,6-anhydro-α-L-galactose dehydrogenase
EC 1.2.1.93 transferred now EC 1.17.1.11
EC 1.2.1.94 farnesal dehydrogenase
EC 1.2.1.95 L-2-aminoadipate reductase
EC 1.2.1.96 4-hydroxybenzaldehyde dehydrogenase (NADP+)
EC 1.2.1.97 3-sulfolactaldehyde dehydrogenase
EC 1.2.1.98 2-hydroxy-2-methylpropanal dehydrogenase
EC 1.2.1.99 4-(γ-glutamylamino)butanal dehydrogenase


EC 1.2.1.51

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]

[EC 1.2.1.51 created 1989]

EC 1.2.1.52

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]

[EC 1.2.1.52 created 1989]

EC 1.2.1.53

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]

[EC 1.2.1.53 created 1989]

EC 1.2.1.54

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 1.2.1.54 created 1989]

[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)]

EC 1.2.1.57

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.

[EC 1.2.1.57 created 1992]

EC 1.2.1.58

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]

[EC 1.2.1.58 created 1999]

EC 1.2.1.59

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]

[EC 1.2.1.59 created 1999]

EC 1.2.1.60

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.

[EC 1.2.1.60 created 2000]

EC 1.2.1.61

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.

[EC 1.2.1.61 created 2000]

EC 1.2.1.62

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]

[EC 1.2.1.62 created 2000]

EC 1.2.1.63

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]

[EC 1.2.1.63 created 2000]

EC 1.2.1.64

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, 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. 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]

[EC 1.2.1.64 created 2000, modified 2015]

EC 1.2.1.65

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 1.2.1.65 created 2000, modified 2011]

[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)]

EC 1.2.1.67

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]

[EC 1.2.1.67 created 2000]

EC 1.2.1.68

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]

[EC 1.2.1.68 created 2000]

EC 1.2.1.69

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]

[EC 1.2.1.69 created 2003]

EC 1.2.1.70

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]

[EC 1.2.1.70 created 2004]

EC 1.2.1.71

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]

[EC 1.2.1.71 created 2006]

EC 1.2.1.72

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]

[EC 1.2.1.72 created 2006]

EC 1.2.1.73

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.

[EC 1.2.1.73 created 2008]

EC 1.2.1.74

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]

[EC 1.2.1.74 created 2009, modified 2012]

EC 1.2.1.75

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, 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]

[EC 1.2.1.75 created 2009]

EC 1.2.1.76

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, 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]

[EC 1.2.1.76 created 2009]

EC 1.2.1.77

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, 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]

[EC 1.2.1.77 created 2010]

EC 1.2.1.78

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.

[EC 1.2.1.78 created 2010]

EC 1.2.1.79

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]

[EC 1.2.1.79 created 2010]

EC 1.2.1.80

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)H–dependent 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]

[EC 1.2.1.80 created 2011]

EC 1.2.1.81

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]

[EC 1.2.1.81 created 2011]

EC 1.2.1.82

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]

[EC 1.2.1.82 created 2011]

EC 1.2.1.83

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]

[EC 1.2.1.83 created 2012]

EC 1.2.1.84

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, 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]

[EC 1.2.1.84 created 2012]

EC 1.2.1.85

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]

[EC 1.2.1.85 created 2012]

EC 1.2.1.86

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]

[EC 1.2.1.86 created 2012]

EC 1.2.1.87

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, 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]

[EC 1.2.1.87 created 2013]

EC 1.2.1.88

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]

[EC 1.2.1.88 created 1972 as 1.5.1.12, modified 2008, transferred 2013 to EC 1.2.1.88]

EC 1.2.1.89

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, 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]

[EC 1.2.1.89 created 2014]

EC 1.2.1.90

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; 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, 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]

[EC 1.2.1.90 created 2014]

EC 1.2.1.91

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, 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]

[EC 1.2.1.91 created 2011 as EC 1.17.1.7, transferred 2014 to EC 1.2.1.91]

EC 1.2.1.92

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 1.2.1.92 created 2014]

[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)]

EC 1.2.1.94

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, 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]

[EC 1.2.1.94 created 2015]

EC 1.2.1.95

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.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

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]

[EC 1.2.1.95 created 2015]

EC 1.2.1.96

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+).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

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]

[EC 1.2.1.96 created 2015]

EC 1.2.1.97

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)-2-hydroxy-3-oxopropane-1-sulfonate

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.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

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]

[EC 1.2.1.97 created 2015]

EC 1.2.1.98

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.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

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]

[EC 1.2.1.98 created 2016]

EC 1.2.1.99

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+).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

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]

[EC 1.2.1.99 created 2017]


Continued with EC 1.2.2 to EC 1.2.99
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