Continued from EC 1.1.4 to EC 1.1.99
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
See separate file for EC 1.2.1.51 to EC 1.2.1.107
EC 1.2.1.51 to EC 1.2.1.107
[EC 1.2.1.2 Transferred entry: formate dehydrogenase. Now EC 1.17.1.9, formate dehydrogenase (EC 1.2.1.2 created 1961, deleted 2017)]
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, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, 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.
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.
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 1.2.1.6 Deleted entry: benzaldehyde dehydrogenase (EC 1.2.1.6 created 1961, deleted 1965)]
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, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, 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]
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]
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 (ambiguous); 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.
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]
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.
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 (ambiguous); 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.
6. Ryzlak, M.T. and Pietruszko, R. Heterogeneity of glyceraldehyde-3-phosphate dehydrogenase from human brain. Biochim. Biophys. Acta 954 (1988) 309Ð324. [PMID: 3370218]
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 1.2.1.14 Transferred entry: now EC 1.1.1.205 IMP dehydrogenase (EC 1.2.1.14 created 1961, deleted 1984)]
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.
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, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, 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.
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.
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.
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]
Accepted name: glutarate-semialdehyde dehydrogenase
Reaction: 5-oxopentanoate + NADP+ + H2O = glutarate + NADPH + H+
Glossary: 5-oxopentanoate = glutarate semialdehyde
Other name(s): glutarate semialdehyde dehydrogenase; davD (gene name)
Systematic name: glutarate-semialdehyde:NADP+ oxidoreductase
Comments: The enzyme, characterized from multiple Pseudomonas strains, participates in L-lysine degradation. Unlike earlier claims, it prefers NADP+ to NAD+.
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. [PMID: 13717359]
2. Chang, Y. F. and Adams, E. Glutaric semialdehyde dehydrogenase (Pseudomonas putida). Methods Enzymol. 17B (1971) 166-171.
3. Fothergill, J.C. and Guest, J.R. Catabolism of L-lysine by Pseudomonas aeruginosa. J. Gen. Microbiol. 99 (1977) 139-155. [PMID: 405455]
4. Chang, Y.F. and Adams, E. Glutarate semialdehyde dehydrogenase of Pseudomonas. Purification, properties, and relation to L-lysine catabolism. J. Biol. Chem. 252 (1977) 7979-7986. [PMID: 914857]
5. Yamanishi, Y., Mihara, H., Osaki, M., Muramatsu, H., Esaki, N., Sato, T., Hizukuri, Y., Goto, S. and Kanehisa, M. Prediction of missing enzyme genes in a bacterial metabolic network. Reconstruction of the lysine-degradation pathway of Pseudomonas aeruginosa. FEBS J. 274 (2007) 2262-2273. [PMID: 17388807]
Accepted name: glycolaldehyde dehydrogenase
Reaction: glycolaldehyde + NAD+ + H2O = glycolate + NADH + 2 H+
For diagram of reaction click here.
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.
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]
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]
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]
Accepted name: branched-chain α-keto acid dehydrogenase system
Reaction: 3-methyl-2-oxobutanoate + CoA + NAD+ = 2-methylpropanoyl-CoA + CO2 + NADH
Other name(s): branched-chain α-keto acid dehydrogenase complex; 2-oxoisovalerate dehydrogenase; α-ketoisovalerate dehydrogenase; 2-oxoisovalerate dehydrogenase (acylating)
Systematic name: 3-methyl-2-oxobutanoate:NAD+ 2-oxidoreductase (CoA-methylpropanoylating)
Comments: This enzyme system catalyses the oxidative decarboxylation of branched-chain α-keto acids derived from L-leucine, L-isoleucine, and L-valine to branched-chain acyl-CoAs. It belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.104, pyruvate dehydrogenase system, EC 1.2.1.105, 2-oxoglutarate dehydrogenase system, EC 1.4.1.27, glycine cleavage system, and EC 2.3.1.190, acetoin dehydrogenase system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). The reaction catalysed by this system is the sum of three activities: EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring), EC 2.3.1.168, dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The system 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]
2. Pettit, F.H., Yeaman, S.J. and Reed, L.J. Purification and characterization of branched chain α-keto acid dehydrogenase complex of bovine kidney. Proc. Natl. Acad. Sci. USA 75 (1978) 4881-4885. [PMID: 283398]
3. Harris, R.A., Hawes, J.W., Popov, K.M., Zhao, Y., Shimomura, Y., Sato, J., Jaskiewicz, J. and Hurley, T.D. Studies on the regulation of the mitochondrial α-ketoacid dehydrogenase complexes and their kinases. Adv. Enzyme Regul. 37 (1997) 271-293. [PMID: 9381974]
4. Evarsson, A., Chuang, J.L., Wynn, R.M., Turley, S., Chuang, D.T. and Hol, W.G. Crystal structure of human branched-chain α-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease. Structure 8 (2000) 277-291. [PMID: 10745006]
5. Reed, L.J. A trail of research from lipoic acid to α-keto acid dehydrogenase complexes. J. Biol. Chem. 276 (2001) 38329-38336. [PMID: 11477096]
Accepted name: 2,5-dioxovalerate dehydrogenase
Reaction: 2,5-dioxopentanoate + NADP+ + H2O = 2-oxoglutarate + NADPH + 2 H+
For diagram of reaction click here or click here.
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, PDB, 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.
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]
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 enzymic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the soluble enzymes. J. Bacteriol. 66 (1953) 548-553.
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]
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. [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. [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]
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]
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, 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.
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 1.2.1.34 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)]
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 1.2.1.37 Transferred entry: now EC 1.1.1.204 xanthine dehydrogenase (EC 1.2.1.37 created 1972, deleted 1984)]
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.
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 1.2.1.40 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)]
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]
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, EAWAG-BBD, EXPASY, KEGG, Metacyc, 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 1.2.1.43 Transferred entry: formate dehydrogenase (NADP+). Now EC 1.17.1.10, formate dehydrogenase (NADP+) (EC 1.2.1.43 created 1978, deleted 2017)]
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. [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 1.2.1.45 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)]
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]
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. [PMID: 6770910]
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. [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.
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]
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, 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. [PMID: 8447834]