The Enzyme Database

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EC 1.2.1.28     
Accepted name: benzaldehyde dehydrogenase (NAD+)
Reaction: benzaldehyde + NAD+ + H2O = benzoate + NADH + 2 H+
Other name(s): benzaldehyde (NAD) dehydrogenase; benzaldehyde dehydrogenase (NAD)
Systematic name: benzaldehyde:NAD+ oxidoreductase
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-93-4
References:
1.  Gunsalus, C.F., Stanier, R.Y. and Gunsalus, I.C. The enzymatic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the soluble enzymes. J. Bacteriol. 66 (1953) 548–553. [PMID: 13108854]
[EC 1.2.1.28 created 1972]
 
 
EC 1.2.1.29     
Accepted name: aryl-aldehyde dehydrogenase
Reaction: an aromatic aldehyde + NAD+ + H2O = an aromatic acid + NADH + H+
Systematic name: aryl-aldehyde:NAD+ oxidoreductase
Comments: Oxidizes a number of aromatic aldehydes, but not aliphatic aldehydes.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-94-5
References:
1.  Raison, J.K., Henson, G. and Rienits, K.G. The oxidation of gentisaldehyde by nicotinamide-adenine dinucleotide-specific, aromatic aldehyde dehydrogenase from rabbit liver. Biochim. Biophys. Acta 118 (1966) 285–298. [PMID: 4289834]
[EC 1.2.1.29 created 1972]
 
 
EC 1.2.1.30     
Accepted name: carboxylate reductase (NADP+)
Reaction: an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Other name(s): aromatic acid reductase; aryl-aldehyde dehydrogenase (NADP+)
Systematic name: aryl-aldehyde:NADP+ oxidoreductase (ATP-forming)
Comments: The enzyme contains an adenylation domain, a phosphopantetheinyl binding 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 phosphopantetheinyl binding domain. The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to an aldehyde and released.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9074-94-6
References:
1.  Gross, G.G. and Zenk, M.H. Reduktion aromatischer Säuer zu Aldehyden und Alkoholen im zellfreien System. 1. Reinigung und Eigenschaften von Aryl-Aldehyd:NADP-Oxidoreduktase aus Neurospora crassa. Eur. J. Biochem. 8 (1969) 413–419. [DOI] [PMID: 4389863]
2.  Gross, G.G. Formation and reduction of intermediate acyladenylate by aryl-aldehyde. NADP oxidoreductase from Neurospora crassa. Eur. J. Biochem. 31 (1972) 585–592. [DOI] [PMID: 4405494]
3.  Venkitasubramanian, P., Daniels, L. and Rosazza, J.P. Reduction of carboxylic acids by Nocardia aldehyde oxidoreductase requires a phosphopantetheinylated enzyme. J. Biol. Chem. 282 (2007) 478–485. [PMID: 17102130]
4.  Stolterfoht, H., Schwendenwein, D., Sensen, C.W., Rudroff, F. and Winkler, M. Four distinct types of E.C. 1.2.1.30 enzymes can catalyze the reduction of carboxylic acids to aldehydes. J. Biotechnol. 257 (2017) 222–232. [PMID: 28223183]
[EC 1.2.1.30 created 1972, modified 2019]
 
 
EC 1.2.1.31     
Accepted name: L-aminoadipate-semialdehyde dehydrogenase
Reaction: (S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+ (overall reaction)
(1a) (S)-2-amino-6-oxohexanoate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O (spontaneous)
(1b) (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD(P)+ + 2 H2O = L-2-aminoadipate + NAD(P)H + H+
For diagram of lysine catabolism, click here and for diagram of L-Lysine synthesis, click here
Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate
Other name(s): aminoadipate semialdehyde dehydrogenase; 2-aminoadipate semialdehyde dehydrogenase; α-aminoadipate-semialdehyde dehydrogenase; α-aminoadipate reductase; 2-aminoadipic semialdehyde dehydrogenase; L-α-aminoadipate δ-semialdehyde oxidoreductase; L-α-aminoadipate δ-semialdehyde:NAD+ oxidoreductase; L-α-aminoadipate δ-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase; L-2-aminoadipate 6-semialdehyde:NAD(P)+ 6-oxidoreductase
Systematic name: (S)-2-amino-6-oxohexanoate:NAD(P)+ 6-oxidoreductase
Comments: (S)-2-amino-6-oxohexanoate undergoes a spontaneous dehydration forming the cyclic (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which serves as a substrate for the hydrogenation reaction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9067-87-2
References:
1.  Calvert, A.F. and Rodwell, V.W. Metabolism of pipecolic acid in a Pseudomonas species. 3. L-α-Aminoadipate δ-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase. J. Biol. Chem. 241 (1966) 409–414. [PMID: 4285660]
2.  Rodwell, V.W. Δ1-piperideine-6-carboxylic acid and α-aminoadipic acid δ-semialdehyde. Method Enzymol 17B (1971) 188–199.
3.  de La Fuente, J.L., Rumbero, A., Martin, J.F. and Liras, P. Δ-1-piperideine-6-carboxylate dehydrogenase, a new enzyme that forms α-aminoadipate in Streptomyces clavuligerus and other cephamycin C-producing actinomycetes. Biochem. J. 327 (1997) 59–64. [PMID: 9355735]
4.  Fujii, T., Narita, T., Agematu, H., Agata, N. and Isshiki, K. Cloning and characterization of pcd encoding Δ’-piperideine-6-carboxylate dehydrogenase from Flavobacterium lutescens IFO3084. J. Biochem. 128 (2000) 975–982. [PMID: 11098140]
[EC 1.2.1.31 created 1972, modified 2011]
 
 
EC 1.2.1.32     
Accepted name: aminomuconate-semialdehyde dehydrogenase
Reaction: 2-aminomuconate 6-semialdehyde + NAD+ + H2O = 2-aminomuconate + NADH + 2 H+
For diagram of the later stages of tryptophan catabolism, click here
Other name(s): 2-aminomuconate semialdehyde dehydrogenase; 2-hydroxymuconic acid semialdehyde dehydrogenase; 2-hydroxymuconate semialdehyde dehydrogenase; α-aminomuconic ε-semialdehyde dehydrogenase; α-hydroxymuconic ε-semialdehyde dehydrogenase; 2-hydroxymuconic semialdehyde dehydrogenase
Systematic name: 2-aminomuconate-6-semialdehyde:NAD+ 6-oxidoreductase
Comments: Also acts on 2-hydroxymuconate semialdehyde.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-95-6
References:
1.  Ichiyama, A., Nakamura, S., Kawai, H., Honjo, T., Nishizuka, Y., Hayaishi, O. and Senoh, S. Studies on the metabolism of the benzene ring of tryptophan in mammalian tissues. II. Enzymic formation of α-aminomuconic acid from 3-hydroxyanthranilic acid. J. Biol. Chem. 240 (1965) 740–749. [PMID: 14275130]
[EC 1.2.1.32 created 1972]
 
 
EC 1.2.1.38     
Accepted name: N-acetyl-γ-glutamyl-phosphate reductase
Reaction: N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-L-glutamyl 5-phosphate + NADPH + H+
For diagram of ornithine biosynthesis, click here
Other name(s): reductase, acetyl-γ-glutamyl phosphate; N-acetylglutamate 5-semialdehyde dehydrogenase; N-acetylglutamic γ-semialdehyde dehydrogenase; N-acetyl-L-glutamate γ-semialdehyde:NADP+ oxidoreductase (phosphorylating)
Systematic name: N-acetyl-L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37251-00-6
References:
1.  Baich, A. and Vogel, H.J. N-Acetyl-γ-glutamokinase and N-acetylglutamic γ-semialdehyde dehydrogenase: repressible enzymes of arginine synthesis in Escherichia coli. Biochem. Biophys. Res. Commun. 7 (1962) 491–496. [PMID: 13863980]
2.  Glansdorff, N. and Sand, G. Coordination of enzyme synthesis in the arginine pathway of Escherichia coli K-12. Biochim. Biophys. Acta 108 (1965) 308–311. [PMID: 5325238]
[EC 1.2.1.38 created 1972]
 
 
EC 1.2.1.39     
Accepted name: phenylacetaldehyde dehydrogenase
Reaction: phenylacetaldehyde + NAD+ + H2O = phenylacetate + NADH + 2 H+
Systematic name: phenylacetaldehyde:NAD+ oxidoreductase
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 58943-37-6
References:
1.  Fujioka, M., Morino, Y. and Wada, H. Metabolism of phenylalanine (Achromobacter eurydice). III. Phenylacetaldehyde dehydrogenase. Methods Enzymol. 17A (1970) 593–596.
[EC 1.2.1.39 created 1976]
 
 
EC 1.2.1.41     
Accepted name: glutamate-5-semialdehyde dehydrogenase
Reaction: L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH + H+
For diagram of proline biosynthesis, click here
Other name(s): β-glutamylphosphate reductase; γ-glutamyl phosphate reductase; β-glutamylphosphate reductase; glutamate semialdehyde dehydrogenase; glutamate-γ-semialdehyde dehydrogenase
Systematic name: L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 54596-29-1
References:
1.  Baich, A. The biosynthesis of proline in Escherichia coli: phosphate-dependent glutamate-semialdehyde dehydrogenase (NADP), the second enzyme in the pathway. Biochim. Biophys. Acta 244 (1971) 129–134. [DOI] [PMID: 4399189]
[EC 1.2.1.41 created 1976]
 
 
EC 1.2.1.44     
Accepted name: cinnamoyl-CoA reductase
Reaction: cinnamaldehyde + CoA + NADP+ = cinnamoyl-CoA + NADPH + H+
Other name(s): feruloyl-CoA reductase; cinnamoyl-coenzyme A reductase; ferulyl-CoA reductase; feruloyl coenzyme A reductase; p-hydroxycinnamoyl coenzyme A reductase; cinnamoyl-CoA:NADPH reductase
Systematic name: cinnamaldehyde:NADP+ oxidoreductase (CoA-cinnamoylating)
Comments: Acts also on a number of substituted cinnamoyl esters of coenzyme A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 59929-39-4
References:
1.  Gross, G.G. and Kreiten, W. Reduction of coenzyme A thioesters of cinnamic acids with an enzyme preparation from lignifying tissue of Forsythia. FEBS Lett. 54 (1975) 259–262. [DOI] [PMID: 236926]
2.  Sarni, F., Grand, C. and Baudet, A.M. Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase from poplar stems (Populus X euramericana). Eur. J. Biochem. 139 (1984) 259–265. [DOI] [PMID: 6365550]
3.  Wengenmayer, H., Ebel, J. and Grisebach, H. Enzymic synthesis of lignin precursors. Purification and properties of a cinnamoyl-CoA: NADPH reductase from cell suspension cultures of soybean (Glycinemax). Eur. J. Biochem. 65 (1976) 529–536. [DOI] [PMID: 7454]
[EC 1.2.1.44 created 1978]
 
 
EC 1.2.1.45      
Transferred entry: 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase. Now EC 1.1.1.312, 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase.
[EC 1.2.1.45 created 1978, deleted 2011]
 
 
EC 1.2.1.46     
Accepted name: formaldehyde dehydrogenase
Reaction: formaldehyde + NAD+ + H2O = formate + NADH + 2 H+
Other name(s): NAD-linked formaldehyde dehydrogenase; NAD-dependent formaldehyde dehydrogenase
Systematic name: formaldehyde:NAD+ oxidoreductase
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-84-6
References:
1.  Hohnloser, W., Osswald, B. and Lingens, F. Enzymological aspects of caffeine demethylation and formaldehyde oxidation by Pseudomonas putida C1. Hoppe-Seyler's Z. Physiol. Chem. 361 (1980) 1763–1766. [PMID: 7461603]
[EC 1.2.1.46 created 1982]
 
 
EC 1.2.1.47     
Accepted name: 4-trimethylammoniobutyraldehyde dehydrogenase
Reaction: 4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate + NADH + 2 H+
Other name(s): 4-trimethylaminobutyraldehyde dehydrogenase; 4-N-trimethylaminobutyraldehyde dehydrogenase
Systematic name: 4-trimethylammoniobutanal:NAD+ 1-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 73361-01-0
References:
1.  Rebouche, C.J. and Engel, A.G. Tissue distribution of carnitine biosynthetic enzymes in man. Biochim. Biophys. Acta 630 (1980) 22–29. [DOI] [PMID: 6770910]
[EC 1.2.1.47 created 1983]
 
 
EC 1.2.1.48     
Accepted name: long-chain-aldehyde dehydrogenase
Reaction: a long-chain aldehyde + NAD+ + H2O = a long-chain carboxylate + NADH + 2 H+
Other name(s): long-chain aliphatic aldehyde dehydrogenase; long-chain fatty aldehyde dehydrogenase; fatty aldehyde:NAD+ oxidoreductase
Systematic name: long-chain-aldehyde:NAD+ oxidoreductase
Comments: The best substrate is dodecylaldehyde.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 59298-89-4
References:
1.  Le Beault, J.M., Roche, B., Duvnjak, Z. and Azoulay, E. Alcool- et aldéhyde-déshydrogénases particulaires de Candida tropicalis cultivé sur hydrocarbures. Biochim. Biophys. Acta 220 (1970) 373–385. [DOI] [PMID: 5499619]
2.  Moreau, R.A. and Huang, A.H.C. Oxidation of fatty alcohol in the cotyledons of jojoba seedlings. Arch. Biochem. Biophys. 194 (1979) 422–430. [DOI] [PMID: 36040]
3.  Moreau, R.A. and Huang, A.H.C. Enzymes of wax ester catabolism in jojoba. Methods Enzymol. 71 (1981) 804–813.
[EC 1.2.1.48 created 1984]
 
 
EC 1.2.1.49     
Accepted name: 2-oxoaldehyde dehydrogenase (NADP+)
Reaction: a 2-oxoaldehyde + NADP+ + H2O = a 2-oxo carboxylate + NADPH + H+
Other name(s): α-ketoaldehyde dehydrogenase; methylglyoxal dehydrogenase; NADP+-linked α-ketoaldehyde dehydrogenase; 2-ketoaldehyde dehydrogenase; NADP+-dependent α-ketoaldehyde dehydrogenase
Systematic name: 2-oxoaldehyde:NADP+ 2-oxidoreductase
Comments: Not identical with EC 1.2.1.23 2-oxoaldehyde dehydrogenase (NAD+).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83588-97-0, 97162-76-0
References:
1.  Ray, M. and Ray, S. On the interaction of nucleotides and glycolytic intermediates with NAD-linked α-ketoaldehyde dehydrogenase. J. Biol. Chem. 257 (1982) 10571–10574. [PMID: 7107626]
2.  Ray, S. and Ray, M. Purification and characterization of NAD and NADP-linked α-ketoaldehyde dehydrogenases involved in catalyzing the oxidation of methylglyoxal to pyruvate. J. Biol. Chem. 257 (1982) 10566–10570. [PMID: 7107625]
[EC 1.2.1.49 created 1986]
 
 
EC 1.2.1.50     
Accepted name: long-chain acyl-protein thioester reductase
Reaction: a long-chain aldehyde + [protein]-L-cysteine + NADP+ = a [protein]-S-(long-chain fatty acyl)-L-cysteine + NADPH + H+
Other name(s): luxC (gene name); acyl-CoA reductase; acyl coenzyme A reductase; long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming); long-chain-fatty-acyl-CoA reductase
Systematic name: long-chain-aldehyde:NADP+ oxidoreductase (protein thioester-forming)
Comments: Together with a hydrolase component (EC 3.1.2.2 and EC 3.1.2.14) and a synthetase component (EC 6.2.1.19), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3). The enzyme is acylated by receiving an acyl group from EC 6.2.1.19, and catalyses the reduction of the acyl group, releasing the aldehyde product. The enzyme is also able to accept the acyl group from a long-chain acyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 50936-56-6
References:
1.  Riendeau, D., Rodrigues, A. and Meighen, E. Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex. J. Biol. Chem. 257 (1982) 6908–6915. [PMID: 7085612]
2.  Wall, L. and Meighen, E.A. Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum. Biochemistry 25 (1986) 4315–4321.
3.  Lin, J.W., Chao, Y.F. and Weng, S.F. Nucleotide sequence of the luxC gene encoding fatty acid reductase of the lux operon from Photobacterium leiognathi. Biochem. Biophys. Res. Commun. 191 (1993) 314–318. [DOI] [PMID: 8447834]
[EC 1.2.1.50 created 1986, modified 2016]
 
 
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. [DOI] [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+
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 1.2.1.54 created 1989]
 
 
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. [DOI] [PMID: 3384801]
[EC 1.2.1.57 created 1992]
 
 
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: P. Mathis (Ed.), Photosynthesis: From Light to Biosphere, vol. 1, Kluwer Academic Publishers, 1995, pp. 959–962.
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. [DOI] [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, 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. [DOI] [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. [DOI] [PMID: 7026235]
[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 4-nitrophenol metabolism, 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
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. [PMID: 16348446]
[EC 1.2.1.61 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, 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. [DOI] [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. [DOI] [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, 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. [DOI] [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: 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]
[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 diagram of reaction, 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. [DOI] [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. [DOI] [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 of the early stages of porphyrin biosynthesis, 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. [DOI] [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. [DOI] [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. [DOI] [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 of arginine catabolism, 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
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. [DOI] [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. [DOI] [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]
7.  Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V. Erratum report: Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev. 51 (1987) 178. [PMID: 16350242]
[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 of pyridoxal biosynthesis, 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 cofactor 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. [DOI] [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. [DOI] [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
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. [DOI] [PMID: 18506422]
[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 abietadiene, abietate, isopimaradiene, labdadienol and sclareol biosynthesis, 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
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. [DOI] [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 the 3-hydroxypropanoate cycle, click here and for diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
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
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 11948153]
[EC 1.2.1.75 created 2009]
 
 
EC 1.2.1.76     
Accepted name: succinate-semialdehyde dehydrogenase (acylating)
Reaction: succinate semialdehyde + CoA + NADP+ = succinyl-CoA + NADPH + H+
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): succinyl-coA reductase; coenzyme-A-dependent succinate-semialdehyde dehydrogenase
Systematic name: succinate semialdehyde:NADP+ oxidoreductase (CoA-acylating)
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-hydroxypropanonate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [2,3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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. [DOI] [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. [DOI] [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. [DOI] [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 Benzoyl-CoA catabolism, 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
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. [DOI] [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. [DOI] [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
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. [DOI] [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+
For diagram of the citric acid cycle, click here
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
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. [DOI] [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. [DOI] [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 = an aldehyde derived from a fatty acid with an aliphatic chain of 13-22 carbons.
an [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 and C18 activated fatty acids. Requires Mg2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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. [DOI] [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
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. [DOI] [PMID: 20693281]
[EC 1.2.1.81 created 2011]
 
 
EC 1.2.1.82     
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
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. [DOI] [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. [DOI] [PMID: 21749649]
[EC 1.2.1.82 created 2011, modified 2023]
 
 
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
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. [DOI] [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); long-chain acyl-CoA:NADPH reductase
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
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 catechol catabolism (meta ring cleavage), 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
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. [DOI] [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. [DOI] [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. [DOI] [PMID: 19717587]
[EC 1.2.1.85 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, PDB
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. [DOI] [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. [DOI] [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. [DOI] [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, PDB, 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. [DOI] [PMID: 17554163]
[EC 1.2.1.88 created 1972 as EC 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, PDB
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. [DOI] [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. [DOI] [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 (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
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. [DOI] [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. [DOI] [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. [DOI] [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 aerobic phenylacetate catabolism, 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
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. [DOI] [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. [DOI] [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. [DOI] [PMID: 20660314]
[EC 1.2.1.91 created 2011 as EC 1.17.1.7, transferred 2014 to EC 1.2.1.91]
 
 
EC 1.2.1.94     
Accepted name: farnesal dehydrogenase
Reaction: (2E,6E)-farnesal + NAD+ + H2O = (2E,6E)-farnesoate + NADH + 2 H+
For diagram of juvenile hormone biosynthesis, 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
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. [DOI] [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. [DOI] [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
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. [DOI] [PMID: 10320345]
[EC 1.2.1.95 created 2015]
 
 


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