Enzyme Nomenclature

Continued from EC 1.1.4 to EC 1.1.99

EC 1.2

ACTING ON THE ALDEHYDE OR OXO GROUP OF DONORS

Sections

EC 1.2.1 With NAD+ or NADP+ as acceptor
EC 1.2.2 With a cytochrome as acceptor
EC 1.2.3 With oxygen as acceptor
EC 1.2.4 With a disulfide as acceptor
EC 1.2.7 With an iron-sulfur protein as acceptor
EC 1.2.98 With other, known, physiological acceptors
EC 1.2.99 With unknown physiological acceptors


EC 1.2.1 With NAD+ or NADP+ as acceptor

See separate file for EC 1.2.1.51 to EC 1.2.1.99

Contents

EC 1.2.1.1 replaced by EC 1.1.1.284 and EC 4.4.1.22
EC 1.2.1.2 formate dehydrogenase
EC 1.2.1.3 aldehyde dehydrogenase (NAD+)
EC 1.2.1.4 aldehyde dehydrogenase (NADP+)
EC 1.2.1.5 aldehyde dehydrogenase [NAD(P)+]
EC 1.2.1.6 deleted
EC 1.2.1.7 benzaldehyde dehydrogenase (NADP+)
EC 1.2.1.8 betaine-aldehyde dehydrogenase
EC 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+)
EC 1.2.1.10 acetaldehyde dehydrogenase (acetylating)
EC 1.2.1.11 aspartate-semialdehyde dehydrogenase
EC 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
EC 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)
EC 1.2.1.14 now EC 1.1.1.205
EC 1.2.1.15 malonate-semialdehyde dehydrogenase
EC 1.2.1.16 succinate-semialdehyde dehydrogenase [NAD(P)+]
EC 1.2.1.17 glyoxylate dehydrogenase (acylating)
EC 1.2.1.18 malonate-semialdehyde dehydrogenase (acetylating)
EC 1.2.1.19 aminobutyraldehyde dehydrogenase
EC 1.2.1.20 glutarate-semialdehyde dehydrogenase
EC 1.2.1.21 glycolaldehyde dehydrogenase
EC 1.2.1.22 lactaldehyde dehydrogenase
EC 1.2.1.23 2-oxoaldehyde dehydrogenase (NAD+)
EC 1.2.1.24 succinate-semialdehyde dehydrogenase (NAD+)
EC 1.2.1.25 2-oxoisovalerate dehydrogenase (acylating)
EC 1.2.1.26 2,5-dioxovalerate dehydrogenase
EC 1.2.1.27 methylmalonate-semialdehyde dehydrogenase (CoA-acylating)
EC 1.2.1.28 benzaldehyde dehydrogenase (NAD+)
EC 1.2.1.29 aryl-aldehyde dehydrogenase
EC 1.2.1.30 aryl-aldehyde dehydrogenase (NADP+)
EC 1.2.1.31 L-aminoadipate-semialdehyde dehydrogenase
EC 1.2.1.32 aminomuconate-semialdehyde dehydrogenase
EC 1.2.1.33 (R)-dehydropantoate dehydrogenase
EC 1.2.1.34 deleted, included in EC 1.1.1.131
EC 1.2.1.35 now EC 1.1.1.203
EC 1.2.1.36 retinal dehydrogenase
EC 1.2.1.37 now EC 1.1.1.204
EC 1.2.1.38 N-acetyl-γ-glutamyl-phosphate reductase
EC 1.2.1.39 phenylacetaldehyde dehydrogenase
EC 1.2.1.40 now EC 1.14.13.15
EC 1.2.1.41 glutamate-5-semialdehyde dehydrogenase
EC 1.2.1.42 hexadecanal dehydrogenase (acylating)
EC 1.2.1.43 formate dehydrogenase (NADP+)
EC 1.2.1.44 cinnamoyl-CoA reductase
EC 1.2.1.45 transferred now EC 1.1.1.312
EC 1.2.1.46 formaldehyde dehydrogenase
EC 1.2.1.47 4-trimethylammoniobutyraldehyde dehydrogenase
EC 1.2.1.48 long-chain-aldehyde dehydrogenase
EC 1.2.1.49 2-oxoaldehyde dehydrogenase (NADP+)
EC 1.2.1.50 long-chain acyl-protein thioester reductase
See the following files for:
EC 1.2.1.51 to EC 1.2.1.99

[EC 1.2.1.1 Deleted entry: glutathione-dependent formaldehyde dehydrogenase. This enzyme was classified on the basis of an incorrect reaction. It has been replaced by two enzymes, EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase and EC 4.4.1.22, S-(hydroxymethyl)glutathione synthase (EC 1.2.1.1 created 1961, modified 1982, modified 2002, deleted 2005)]

EC 1.2.1.2

Accepted name: formate dehydrogenase

Reaction: formate + NAD+ = CO2 + NADH

Other name(s): formate-NAD oxidoreductase; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase

Systematic name: formate:NAD+ oxidoreductase

Comments: The enzyme from most aerobic organisms is devoid of redox-active centres but that from the proteobacterium Methylosinus trichosporium contains iron-sulfur centres, flavin and a molybdenum centre [3]. Together with EC 1.12.1.2 hydrogen dehydrogenase, forms a system previously known as formate hydrogenlyase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9028-85-7

References:

1. Davison, D.C. Studies on plant formic dehydrogenase. Biochem. J. 49 (1951) 520-526. [PMID: 14886318]

2. Quayle, J.R. Formate dehydrogenase. Methods Enzymol. 9 (1966) 360-364.

3. Jollie, D.R. and Lipscomb, J.D. Formate dehydrogenase from Methylosinus trichosporium OB3b. Purification and spectroscopic characterization of the cofactors. J. Biol. Chem. 266 (1991) 21853-21863. [PMID: 1657982]

[EC 1.2.1.2 created 1961]

EC 1.2.1.3

Accepted name: aldehyde dehydrogenase (NAD+)

Reaction: an aldehyde + NAD+ + H2O = a carboxylate + NADH + H+

Other name(s): CoA-independent aldehyde dehydrogenase; m-methylbenzaldehyde dehydrogenase; NAD-aldehyde dehydrogenase; NAD-dependent 4-hydroxynonenal dehydrogenase; NAD-dependent aldehyde dehydrogenase; NAD-linked aldehyde dehydrogenase; propionaldehyde dehydrogenase; aldehyde dehydrogenase (NAD)

Systematic name: aldehyde:NAD+ oxidoreductase

Comments: Wide specificity, including oxidation of D-glucuronolactone to D-glucarate. Formerly EC 1.1.1.70.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9028-86-8

References:

1. Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.

2. Racker, E. Aldehyde dehydrogenase, a diphosphopyridine nucleotide-linked enzyme. J. Biol. Chem. 177 (1949) 883-892.

[EC 1.2.1.3 created 1961 (EC 1.1.1.70 created 1965, incorporated 1978)]

EC 1.2.1.4

Accepted name: aldehyde dehydrogenase (NADP+)

Reaction: an aldehyde + NADP+ + H2O = a carboxylate + NADPH + H+

Other name(s): NADP-acetaldehyde dehydrogenase; NADP-dependent aldehyde dehydrogenase; aldehyde dehydrogenase (NADP)

Systematic name: aldehyde:NADP+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9028-87-9

References:

1. Adachi, O., Matsushita, K., Shinagawa, E. and Ameyama, M. Crystallization and properties of NADP-dependent aldehyde dehydrogenase from Gluconobacter melanogenus. Agric. Biol. Chem. 44 (1980) 155-164.

2. Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.

3. Nakayama, T. Acetic acid bacteria. II. Intracellular distribution of enzymes related to acetic acid fermentation, and some properties of a highly purified triphosphopyridine nucleotide (TPN)-dependent aldehyde dehydrogenase. J. Biochem. (Tokyo) 48 (1960) 812-830.

4. Seegmiller, J.E. Triphosphopyridine nucleotide-linked aldehyde dehydrogenase from yeast. J. Biol. Chem. 201 (1953) 629-637.

[EC 1.2.1.4 created 1961]

EC 1.2.1.5

Accepted name: aldehyde dehydrogenase [NAD(P)+]

Reaction: an aldehyde + NAD(P)+ + H2O = a carboxylate + NAD(P)H + H+

Other name(s): aldehyde dehydrogenase [NAD(P)]; ALDH

Systematic name: aldehyde:NAD(P)+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9028-88-0

References:

1. Black, S. Yeast aldehyde dehydrogenase. Arch. Biochem. Biophys. 34 (1951) 86-97.

2. Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.

3. King, T.E. and Cheldelin, V.H. Oxidation of acetaldehyde by Aerobacter suboxydans. J. Biol. Chem. 220 (1956) 177-191.

4. Steinman, C.R. and Jakoby, W.B. Yeast aldehyde dehydrogenase. I. Purification and crystallization. J. Biol. Chem. 242 (1967) 5019-5023. [PMID: 4293780]

5. Tanenbaum, S.W. The metabolism of Acetobacter peroxidans. I. Oxidative enzymes. Biochim. Biophys. Acta 21 (1956) 335-342.

[EC 1.2.1.5 created 1961]

[EC 1.2.1.6 Deleted entry: benzaldehyde dehydrogenase (EC 1.2.1.6 created 1961, deleted 1965)]

EC 1.2.1.7

Accepted name: benzaldehyde dehydrogenase (NADP+)

Reaction: benzaldehyde + NADP+ + H2O = benzoate + NADPH + 2 H+

Other name(s): NADP-linked benzaldehyde dehydrogenase; benzaldehyde dehydrogenase (NADP)

Systematic name: benzaldehyde:NADP+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 9028-89-1

References:

1. Gunsalus, C.F., Stanier, R.Y., 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.

2. Stachow, C.S., Stevenson, I.L. and Day, D. Purification and properties of nicotinamide adenine dinucleotide phosphate-specific benzaldehyde dehydrogenase from Pseudomonas. J. Biol. Chem. 242 (1967) 5294-5300. [PMID: 4383635]

[EC 1.2.1.7 created 1961]

EC 1.2.1.8

Accepted name: betaine-aldehyde dehydrogenase

Reaction: betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+

Glossary: betaine = glycine betaine = N,N,N-trimethylglycine = N,N,N-trimethylammonioacetate
betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium

Other name(s): betaine aldehyde oxidase; BADH; betaine aldehyde dehydrogenase; BetB

Systematic name: betaine-aldehyde:NAD+ oxidoreductase

Comments: In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) [5]. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9028-90-4

References:

1. Rothschild, H.A. and Barron, E.S.G. The oxidation of betaine aldehyde by betaine aldehyde dehydrogenase. J. Biol. Chem. 209 (1954) 511-523. [PMID: 13192104]

2. Livingstone, J.R., Maruo, T., Yoshida, I., Tarui, Y., Hirooka, K., Yamamoto, Y., Tsutui, N. and Hirasawa, E. Purification and properties of betaine aldehyde dehydrogenase from Avena sativa. J. Plant Res. 116 (2003) 133-140. [PMID: 12736784]

3. Muñoz-Clares, R.A., González-Segura, L., Mújica-Jiménez, C. and Contreras-Diaz, L. Ligand-induced conformational changes of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves affecting the reactivity of the catalytic thiol. Chem. Biol. Interact. (2003) 129-137. [PMID: 12604197]

4. Johansson, K., El-Ahmad, M., Ramaswamy, S., Hjelmqvist, L., Jornvall, H. and Eklund, H. Structure of betaine aldehyde dehydrogenase at 2.1 Å resolution. Protein Sci. 7 (1998) 2106-2117. [PMID: 9792097]

5. Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932-4942. [PMID: 12466265]

[EC 1.2.1.8 created 1961, modified 2005, modified 2011]

EC 1.2.1.9

Accepted name: glyceraldehyde-3-phosphate dehydrogenase (NADP+)

Reaction: D-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-D-glycerate + NADPH + 2 H+

For diagram of reaction click here.

Other name(s): triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate); glyceraldehyde phosphate dehydrogenase (NADP); glyceraldehyde 3-phosphate dehydrogenase (NADP); NADP-glyceraldehyde phosphate dehydrogenase; NADP-glyceraldehyde-3-phosphate dehydrogenase; glyceraldehyde-3-phosphate:NADP reductase; nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase; glyceraldehyde-3-phosphate dehydrogenase (NADP)

Systematic name: D-glyceraldehyde-3-phosphate:NADP+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9028-92-6

References:

1. Rosenberg, L.L. and Arnon, D.I. The preparation and properties of a new glyceraldehyde-3-phosphate dehydrogenase from photosynthetic tissues. J. Biol. Chem. 217 (1955) 361-371.

[EC 1.2.1.9 created 1961]

EC 1.2.1.10

Accepted name: acetaldehyde dehydrogenase (acetylating)

Reaction: acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+

For diagram of reaction click here and another click here and another.

Other name(s): aldehyde dehydrogenase (acylating); ADA; acylating acetaldehyde dehyrogenase; DmpF

Systematic name: acetaldehyde:NAD+ oxidoreductase (CoA-acetylating)

Comments: Also acts, more slowly, on glycolaldehyde, propanal and butanal. In several bacterial species this 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 1.2.1.87, propanal dehydrogenase (propanoylating). Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols. NADP+ can replace NAD+ but the rate of reaction is much slower [3].

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9028-91-5

References:

1. Burton, R.M. and Stadtman, E.R. The oxidation of acetaldehyde to acetyl coenzyme A. J. Biol. Chem. 202 (1953) 873-890. [PMID: 13061511]

2. Smith, L.T. and Kaplan, N.O. Purification, properties, and kinetic mechanism of coenzyme A-linked aldehyde dehydrogenase from Clostridium kluyveri. Arch. Biochem. Biophys. 203 (1980) 663-675. [PMID: 7458347]

3. Powlowski, J., Sahlman, L. and Shingler, V. Purification and properties of the physically associated meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600. J. Bacteriol. 175 (1993) 377-385. [PMID: 8419288]

4. 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]

5. 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 1.2.1.10 created 1961, modified 2006, modified 2011]

EC 1.2.1.11

Accepted name: aspartate-semialdehyde dehydrogenase

Reaction: L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+

For diagram click here.

Other name(s): aspartate semialdehyde dehydrogenase; aspartic semialdehyde dehydrogenase; L-aspartate-β-semialdehyde:NADP oxidoreductase (phosporylating); aspartic β-semialdehyde dehydrogenase; ASA dehydrogenase

Systematic name: L-aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating)

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9000-98-0

References:

1. Black, S. and Wright, N.G. Aspartic β-semialdehyde dehydrogenase and aspartic β-semialdehyde. J. Biol. Chem. 213 (1955) 39-50.

2. Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.

[EC 1.2.1.11 created 1961]

EC 1.2.1.12

Accepted name: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

Reaction: D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+

For reaction pathway click here.

Other name(s): triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD); glyceraldehyde-3-phosphate dehydrogenase (NAD); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase

Systematic name: D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating)

Comments: Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-50-7

References:

1. Caputto, R. and Dixon, M. Crystallization and identity of the triose and triosephosphate dehydrogenase of muscle. Nature (Lond.) 156 (1945) 630-631.

2. Cori, G.T., Slein, M.W. and Cori, C.F. Crystalline D-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle. J. Biol. Chem. 173 (1948) 605-618.

3. Hageman, R.H. and Arnon, D.I. The isolation of triosephosphate dehydrogenase from pea seeds. Arch. Biochem. Biophys. 55 (1955) 162-168.

4. Velick, S.F. and Furfine, C. Glyceraldehyde 3-phosphate dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 243-273.

5. Warburg, O. and Christian, W. Isolierung und Krystallisation des Proteins des oxydierenden Gärungsferments. Biochem. Z. 303 (1939) 40-68.

[EC 1.2.1.12 created 1961]

EC 1.2.1.13

Accepted name: glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)

Reaction: D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+

For diagram of reaction click here, another presentation click here.

Other name(s): triosephosphate dehydrogenase (NADP); dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate) (phosphorylating); glyceraldehyde phosphate dehydrogenase (nicotinamide adenine dinucleotide phosphate) (phosphorylating); NADP-glyceraldehyde-3-phosphate dehydrogenase; NADP-glyceraldehyde phosphate dehydrogenase; NADP-dependent glyceraldehyde phosphate dehydrogenase; NADP-triose phosphate dehydrogenase; glyceraldehyde-3-phosphate dehydrogenase (NADP) (phosphorylating); GAPDH

Systematic name: D-glyceraldehyde-3-phosphate:NADP+ oxidoreductase (phosphorylating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-87-6

References:

1. Brenneman, F.N. and Volk, W.A. Glyceraldehyde phosphate dehydrogenase activity with triphosphopyridine nucleotide and with diphosphopyridine nucleotide. J. Biol. Chem. 234 (1959) 2443-2447.

2. Gibbs, M. TPN triosephosphate dehydrogenase from plant tissue. Methods Enzymol. 1 (1955) 411-415.

3. Rosenberg, L.L. and Arnon, D.I. The preparation and properties of a new glyceraldehyde-3-phosphate dehydrogenase from photosynthetic tissues. J. Biol. Chem. 217 (1955) 361-371.

[EC 1.2.1.13 created 1961]

[EC 1.2.1.14 Transferred entry: now EC 1.1.1.205 IMP dehydrogenase (EC 1.2.1.14 created 1961, deleted 1984)]

EC 1.2.1.15

Accepted name: malonate-semialdehyde dehydrogenase

Reaction: 3-oxopropanoate + NAD(P)+ + H2O = malonate + NAD(P)H + 2 H+

Systematic name: 3-oxopropanoate:NAD(P)+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9028-94-8

References:

1. Nakamura, K. and Bernheim, F. Studies on malonic semialdehyde dehydrogenase from Pseudomonas aeruginosa. Biochim. Biophys. Acta 50 (1961) 147-152.

[EC 1.2.1.15 created 1965]

EC 1.2.1.16

Accepted name: succinate-semialdehyde dehydrogenase [NAD(P)+]

Reaction: succinate semialdehyde + NAD(P)+ + H2O = succinate + NAD(P)H + 2 H+

For diagram of reaction click here.

Other name(s): succinate semialdehyde dehydrogenase (nicotinamide adenine dinucleotide (phosphate)); succinate-semialdehyde dehydrogenase [NAD(P)]

Systematic name: succinate-semialdehyde:NAD(P)+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 37250-88-7

References:

1. Jakoby, W.B. Aldehyde dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.

2. Jakoby, W.B. and Scott, E.M. Aldehyde oxidation. III. Succinic semialdehyde dehydrogenase. J. Biol. Chem. 234 (1959) 937-940.

3. Nirenberg, M.W. and Jakoby, W.B. Enzymatic utilization of γ-hydroxybutyric acid. J. Biol. Chem. 235 (1960) 954-960.

[EC 1.2.1.16 created 1965]

EC 1.2.1.17

Accepted name: glyoxylate dehydrogenase (acylating)

Reaction: glyoxylate + CoA + NADP+ = oxalyl-CoA + NADPH + H+

Systematic name: glyoxylate:NADP+ oxidoreductase (CoA-oxalylating)

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9028-96-0

References:

1. Quayle, J.R. and Taylor, G.A. Carbon assimilation by Pseudomonas oxalaticus (OX1). 5. Purification and properties of glyoxylic dehydrogenase. Biochem. J. 78 (1961) 611-615.

[EC 1.2.1.17 created 1965]

EC 1.2.1.18

Accepted name: malonate-semialdehyde dehydrogenase (acetylating)

Reaction: 3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H

Other name(s): malonic semialdehyde oxidative decarboxylase

Systematic name: 3-oxopropanoate:NAD(P)+ oxidoreductase (decarboxylating, CoA-acetylating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9028-97-1

References:

1. Hayaishi, O., Nishizuka, Y., Tatibana, M., Takeshita, M. and Kuno, S. Enzymatic studies on the metabolism of β-alanine. J. Biol. Chem. 236 (1961) 781-790.

2. Jakoby, W.B. Aldehyde dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.

3. Yamada, E.W. and Jakoby, W.B. Aldehyde oxidation. V. Direct conversion of malonic semialdehyde to acetyl-coenzyme A. J. Biol. Chem. 235 (1960) 589-594.

[EC 1.2.1.18 created 1965]

EC 1.2.1.19

Accepted name: aminobutyraldehyde dehydrogenase

Reaction: 4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH + 2 H+

For diagram click here.

Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA

Other name(s): ABAL dehydrogenase; 4-aminobutyraldehyde dehydrogenase; 4-aminobutanal dehydrogenase; γ-aminobutyraldehyde dehydroganase; 1-pyrroline dehydrogenase; ABALDH; YdcW; γ-guanidinobutyraldehyde dehydrogenase (ambiguous)

Systematic name: 4-aminobutanal:NAD+ 1-oxidoreductase

Comments: The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates [9]. The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54 γ-guanidinobutyraldehyde dehydrogenase). As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate. The enzyme forms part of the arginine-catabolism pathway [8] and belongs in the aldehyde dehydrogenase superfamily [9].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9028-98-2

References:

1. Callewaert, D.M., Rosemblatt, M.S. and Tchen, T.T. Purification and properties of 4-aminobutanal dehydrogenase from a Pseudomonas species. J. Biol. Chem. 249 (1974) 1737-1741. [PMID: 4817964]

2. Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 203-221.

3. Jakoby, W.B. and Fredericks, J. Pyrrolidine and putrescine metabolism: γ-aminobutyraldehyde dehydrogenase. J. Biol. Chem. 234 (1959) 2145-2150. [PMID: 13673029]

4. Matsuda, H. and Suzuki, Y. γ-Guanidinobutyraldehyde dehydrogenase of Vicia faba leaves. Plant Physiol. 76 (1984) 654-657. [PMID: 16663901]

5. 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.

6. Prieto-Santos, M.I., Martin-Checa, J., Balaña-Fouce, R. and Garrido-Pertierra, A. A pathway for putrescine catabolism in Escherichia coli. Biochim. Biophys. Acta 880 (1986) 242-244. [PMID: 3510672]

7. Prieto, M.I., Martin, J., Balaña-Fouce, R. and Garrido-Pertierra, A. Properties of γ-aminobutyraldehyde dehydrogenase from Escherichia coli. Biochimie 69 (1987) 1161-1168. [PMID: 3129020]

8. Samsonova, N.N., Smirnov, S.V., Novikova, A.E. and Ptitsyn, L.R. Identification of Escherichia coli K12 YdcW protein as a γ-aminobutyraldehyde dehydrogenase. FEBS Lett. 579 (2005) 4107-4112. [PMID: 16023116]

9. Gruez, A., Roig-Zamboni, V., Grisel, S., Salomoni, A., Valencia, C., Campanacci, V., Tegoni, M. and Cambillau, C. Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase. J. Mol. Biol. 343 (2004) 29-41. [PMID: 15381418]

[EC 1.2.1.19 created 1965, modified 1989 (EC 1.5.1.35 created 2006, incorporated 2007)]

EC 1.2.1.20

Accepted name: glutarate-semialdehyde dehydrogenase

Reaction: glutarate semialdehyde + NAD+ + H2O = glutarate + NADH + 2 H+

Other name(s): glutarate semialdehyde dehydrogenase

Systematic name: glutarate-semialdehyde:NAD+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9028-99-3

References:

1. Ichihara, A. and Ichihara, E.A. Metabolism of L-lysine by bacterial enzymes. V. Glutaric semialdehyde dehydrogenase. J. Biochem. (Tokyo) 49 (1961) 154-157.

[EC 1.2.1.20 created 1965]

EC 1.2.1.21

Accepted name: glycolaldehyde dehydrogenase

Reaction: glycolaldehyde + NAD+ + H2O = glycolate + NADH + 2 H+

Other name(s): glycol aldehyde dehydrogenase

Systematic name: glycolaldehyde:NAD+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-89-8

References:

1. Davies, D.D. The purification and properties of glycolaldehyde dehydrogenase. J. Exp. Bot. 11 (1960) 289-295.

[EC 1.2.1.21 created 1972]

EC 1.2.1.22

Accepted name: lactaldehyde dehydrogenase

Reaction: (S)-lactaldehyde + NAD+ + H2O = (S)-lactate + NADH + 2 H+

Other name(s): L-lactaldehyde:NAD oxidoreductase; nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase

Systematic name: (S)-lactaldehyde:NAD+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-90-1

References:

1. Rembold, H. and Simmersbach, F. Catabolism of pteridine cofactors. II. A specific pterin deaminase in rat liver. Biochim. Biophys. Acta 184 (1969) 589-596. [PMID: 5821022]

2. Sridhara, S. and Wu, T.T. Purification and properties of lactaldehyde dehydrogenase from Escherichia coli. J. Biol. Chem. 244 (1969) 5233-5238. [PMID: 4310089]

[EC 1.2.1.22 created 1972]

EC 1.2.1.23

Accepted name: 2-oxoaldehyde dehydrogenase (NAD+)

Reaction: a 2-oxoaldehyde + NAD+ + H2O = a 2-oxo carboxylate + NADH + H+

Other name(s): α-ketoaldehyde dehydrogenase; methylglyoxal dehydrogenase; NAD-linked α-ketoaldehyde dehydrogenase; 2-ketoaldehyde dehydrogenase; NAD-dependent α-ketoaldehyde dehydrogenase; 2-oxoaldehyde dehydrogenase (NAD)

Systematic name: 2-oxoaldehyde:NAD+ 2-oxidoreductase

Comments: Not identical with EC 1.2.1.49 2-oxoaldehyde dehydrogenase (NADP+).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-91-2

References:

1. Monder, C. α-Keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate. J. Biol. Chem. 242 (1967) 4603-4609. [PMID: 4383524]

2. 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]

3. 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 1.2.1.23 created 1972, modified 1986]

EC 1.2.1.24

Accepted name: succinate-semialdehyde dehydrogenase (NAD+)

Reaction: succinate semialdehyde + NAD+ + H2O = succinate + NADH + 2 H+

For diagram of reaction click here.

Other name(s): succinate semialdehyde dehydrogenase (NAD+); succinic semialdehyde dehydrogenase (NAD+); succinyl semialdehyde dehydrogenase (NAD+); succinate semialdehyde:NAD+ oxidoreductase

Systematic name: succinate-semialdehyde:NAD+ oxidoreductase

Comments: This enzyme participates in the degradation of glutamate and 4-aminobutyrate. It is similar to EC 1.2.1.79 [succinate-semialdehyde dehydrogenase (NADP+)], and EC 1.2.1.16 [succinate-semialdehyde dehydrogenase (NAD(P)+)], but is specific for NAD+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9028-95-9

References:

1. Albers, R.W. and Koval, G.J. Succinic semialdehyde dehydrogenase : purification and properties of the enzyme from monkey brain. Biochim. Biophys. Acta 52 (1961) 29-35. [PMID: 13860092]

2. Ryzlak, M.T. and Pietruszko, R. Human brain "high Km" aldehyde dehydrogenase: purification, characterization, and identification as NAD+-dependent succinic semialdehyde dehydrogenase. Arch. Biochem. Biophys. 266 (1988) 386-396. [PMID: 3190233]

3. Busch, K.B. and Fromm, H. Plant succinic semialdehyde dehydrogenase. Cloning, purification, localization in mitochondria, and regulation by adenine nucleotides. Plant Physiol. 121 (1999) 589-597. [PMID: 10517851]

[EC 1.2.1.24 created 1972, modified 2010]

EC 1.2.1.25

Accepted name: 2-oxoisovalerate dehydrogenase (acylating)

Reaction: 3-methyl-2-oxobutanoate + CoA + NAD+ = 2-methylpropanoyl-CoA + CO2 + NADH

Other name(s): 2-oxoisovalerate dehydrogenase; α-ketoisovalerate dehydrogenase

Systematic name: 3-methyl-2-oxobutanoate:NAD+ 2-oxidoreductase (CoA-methyl-propanoylating)

Comments: Also acts on (S)-3-methyl-2-oxopentanoate and 4-methyl-2-oxopentanoate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37211-61-3

References:

1. Namba, Y., Yoshizawa, K., Ejima, A., Hayashi, T. and Kaneda, T. Coenzyme A- and nicotinamide adenine dinucleotide-dependent branched chain α-keto acid dehydrogenase. I. Purification and properties of the enzyme from Bacillus subtilis. J. Biol. Chem. 244 (1969) 4437-4447. [PMID: 4308861]

[EC 1.2.1.25 created 1972]

EC 1.2.1.26

Accepted name: 2,5-dioxovalerate dehydrogenase

Reaction: 2,5-dioxopentanoate + NADP+ + H2O = 2-oxoglutarate + NADPH + 2 H+

Other name(s): 2-oxoglutarate semialdehyde dehydrogenase; α-ketoglutaric semialdehyde dehydrogenase

Systematic name: 2,5-dioxopentanoate:NADP+ 5-oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-92-3

References:

1. Adams, E. and Rosso, G. α-Ketoglutaric semialdehyde dehydrogenase of Pseudomonas. Properties of the purified enzyme induced by hydroxyproline and of the glucarate-induced and constitutive enzymes. J. Biol. Chem. 242 (1967) 1803-1814.

[EC 1.2.1.26 created 1972]

EC 1.2.1.27

Accepted name: methylmalonate-semialdehyde dehydrogenase (CoA-acylating)

Reaction: 2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH

For diagram of reaction click here.

Glossary: methylmalonate semialdehyde = 2-methyl-3-oxopropanoate

Other name(s): MSDH; MMSA dehydrogenase; iolA (gene name); methylmalonate-semialdehyde dehydrogenase (acylating)

Systematic name: 2-methyl-3-oxopropanoate:NAD+ 3-oxidoreductase (CoA-propanoylating)

Comments: Also converts 3-oxopropanoate into acetyl-CoA [3]. The reaction occurs in two steps with the decarboxylation process preceding CoA-binding [3]. Bicarbonate rather than CO2 is released as a final product [3].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37205-49-5

References:

1. Sokatch, J.R., Sanders, L.E. and Marshall, V.P. Oxidation of methylmalonate semialdehyde to propionyl coenzyme A in Pseudomonas aeruginosa grown on valine. J. Biol. Chem. 243 (1968) 2500-2506. [PMID: 4297649]

2. Dubourg, H., Stines-Chaumeil, C., Didierjean, C., Talfournier, F., Rahuel-Clermont, S., Branlant, G. and Aubry, A. Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 1435-1437. [PMID: 15272169]

3. Stines-Chaumeil, C., Talfournier, F. and Branlant, G. Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis. Biochem. J. 395 (2006) 107-115. [PMID: 16332250]

[EC 1.2.1.27 created 1972, modified 2014]

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, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 37250-93-4

References:

1. Gunsalus, C.F., Stanier, R.Y. and Gunsalus, I.C. The enzymic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the soluble enzymes. J. Bacteriol. 66 (1953) 548-553.

[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, EXPASY, KEGG, Metacyc, UM-BBD, 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: aryl-aldehyde dehydrogenase (NADP+)

Reaction: an aromatic aldehyde + NADP+ + AMP + diphosphate + H2O = an aromatic acid + NADPH + H+ + ATP

Other name(s): aromatic acid reductase; aryl-aldehyde dehydrogenase (NADP)

Systematic name: aryl-aldehyde:NADP+ oxidoreductase (ATP-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9074-94-6

References:

1. Gross, G.G. Formation and reduction of intermediate acyladenylate by aryl-aldehyde. NADP oxidoreductase from Neurospora crassa. Eur. J. Biochem. 31 (1972) 585-592. [PMID: 4405494]

2. 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. [PMID: 4389863]

[EC 1.2.1.30 created 1972]

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 click here, another example.

Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine

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

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]

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 reaction 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, EXPASY, KEGG, Metacyc, UM-BBD, 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.

[EC 1.2.1.32 created 1972]

EC 1.2.1.33

Accepted name: (R)-dehydropantoate dehydrogenase

Reaction: (R)-4-dehydropantoate + NAD+ + H2O = (R)-3,3-dimethylmalate + NADH + 2 H+

For diagram of reaction click here.

Other name(s): D-aldopantoate dehydrogenase; D-2-hydroxy-3,3-dimethyl-3-formylpropionate:diphosphopyridine nucleotide (DPN+) oxidoreductase

Systematic name: (R)-4-dehydropantoate:NAD+ 4-oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-96-7

References:

1. Magee, P.T. and Snell, E.E. The bacterial degradation of pantothenic acid. IV. Enzymatic conversion of aldopantoate to α-ketoisovalerate. Biochemistry 5 (1966) 409-416. [PMID: 4287371]

[EC 1.2.1.33 created 1972]

[EC 1.2.1.34 Transferred entry: now included with EC 1.1.1.131 mannuronate reductase (EC 1.2.1.34 created 1972, deleted 1983 [transferred to EC 1.1.1.180, deleted 1984])]

[EC 1.2.1.35 Transferred entry: now EC 1.1.1.203 uronate dehydrogenase (EC 1.2.1.35 created 1972, deleted 1984)]

EC 1.2.1.36

Accepted name: retinal dehydrogenase

Reaction: retinal + NAD+ + H2O = retinoate + NADH + 2 H+

For diagram of reaction click here.

Other name(s): cytosolic retinal dehydrogenase

Systematic name: retinal:NAD+ oxidoreductase

Comments: A metalloflavoprotein (FAD). Acts on both the 11-trans- and 13-cis-forms of retinal.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-99-0

References:

1. Moffa, D.J., Lotspeich, F.J. and Krause, R.F. Preparation and properties of retinal-oxidizing enzyme from rat intestinal mucosa. J. Biol. Chem. 245 (1970) 439-447. [PMID: 4312676]

[EC 1.2.1.36 created 1972]

[EC 1.2.1.37 Transferred entry: now EC 1.1.1.204 xanthine dehydrogenase (EC 1.2.1.37 created 1972, deleted 1984)]

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 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.

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.

[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, EXPASY, KEGG, Metacyc, UM-BBD, 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 1.2.1.40 Deleted entry: 3α,7α,12α-trihydroxycholestan-26-al 26-oxidoreductase. The activity is part of EC 1.14.13.15, cholestanetriol 26-monooxygenase (EC 1.2.1.40 created 1976, deleted 2012)]

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 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. [PMID: 4399189]

[EC 1.2.1.41 created 1976]

EC 1.2.1.42

Accepted name: hexadecanal dehydrogenase (acylating)

Reaction: hexadecanal + CoA + NAD+ = hexadecanoyl-CoA + NADH + H+

Other name(s): fatty acyl-CoA reductase

Systematic name: hexadecanal:NAD+ oxidoreductase (CoA-acylating)

Comments: Also acts, more slowly, on octadecanoyl-CoA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 72561-01-4

References:

1. Johnson, R.C. and Gilbertson, J.R. Isolation, characterization, and partial purification of a fatty acyl coenzyme A reductase from bovine cardiac muscle. J. Biol. Chem. 247 (1972) 6991-6998. [PMID: 4343165]

[EC 1.2.1.42 created 1978]

EC 1.2.1.43

Accepted name: formate dehydrogenase (NADP+)

Reaction: formate + NADP+ = CO2 + NADPH

Other name(s): NADP-dependent formate dehydrogenase; formate dehydrogenase (NADP)

Systematic name: formate:NADP+ oxidoreductase

Comments: A tungsten-selenium-iron protein.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 51377-43-6

References:

1. Andreesen, J.R. and Ljungdahl, L.G. Nicotinamide adenine dinucleotide phosphate-dependent formate dehydrogenase from Clostridium thermoaceticum: purification and properties. J. Bacteriol. 120 (1974) 6-14. [PMID: 4154039]

2. Yamamoto, I., Saiki, T., Liu, S.-M. and Ljungdahl, L.G. Purification and properties of NADP-dependent formate dehydrogenase from Clostridium thermoaceticum, a tungsten-selenium-iron protein. J. Biol. Chem. 258 (1983) 1826-1832. [PMID: 6822536]

[EC 1.2.1.43 created 1978]

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, 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. [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. [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. [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, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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, 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. [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, EXPASY, KEGG, Metacyc, UM-BBD, 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. [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. [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; 2-oxoaldehyde dehydrogenase (NADP)

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 and 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 thioesther-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, 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. [PMID: 8447834]

[EC 1.2.1.50 created 1986, modified 2016]


Continued with EC 1.2.1.51 to EC 1.2.1.99
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