The Enzyme Database

Displaying entries 551-600 of 2549.

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EC 1.1.99.24     
Accepted name: hydroxyacid-oxoacid transhydrogenase
Reaction: (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2-hydroxyglutarate
Other name(s): transhydrogenase, hydroxy acid-oxo acid
Systematic name: (S)-3-hydroxybutanoate:2-oxoglutarate oxidoreductase
Comments: 4-Hydroxybutanoate and (R)-2-hydroxyglutarate can also act as donors; 4-oxobutanoate can also act as acceptor.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 117698-31-4
References:
1.  Kaufman, E.E., Nelson, T., Fales, H.M. and Levin, D.M. Isolation and characterization of a hydroxyacid-oxoacid transhydrogenase from rat kidney mitochondria. J. Biol. Chem. 263 (1988) 16872–16879. [PMID: 3182820]
[EC 1.1.99.24 created 1992]
 
 
EC 1.1.99.25      
Transferred entry: quinate dehydrogenase (pyrroloquinoline-quinone). Now EC 1.1.5.8, quinate dehydrogenase (quinone)
[EC 1.1.99.25 created 1992, modified 2004, deleted 2010]
 
 
EC 1.1.99.26     
Accepted name: 3-hydroxycyclohexanone dehydrogenase
Reaction: 3-hydroxycyclohexanone + acceptor = cyclohexane-1,3-dione + reduced acceptor
Systematic name: 3-hydroxycyclohexanone:acceptor 1-oxidoreductase
Comments: 2,6-Dichloroindophenol and methylene blue can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 123516-44-9
References:
1.  Dangel, W., Tschech, A. and Fuchs, G. Enzyme-reactions involved in anaerobic cyclohexanol metabolism by a denitrifying Pseudomonas species. Arch. Microbiol. 152 (1989) 273–279. [PMID: 2505723]
[EC 1.1.99.26 created 1992]
 
 
EC 1.1.99.27     
Accepted name: (R)-pantolactone dehydrogenase (flavin)
Reaction: (R)-pantolactone + acceptor = 2-dehydropantolactone + reduced acceptor
Other name(s): 2-dehydropantolactone reductase (flavin); 2-dehydropantoyl-lactone reductase (flavin); (R)-pantoyllactone dehydrogenase (flavin)
Systematic name: (R)-pantolactone:acceptor oxidoreductase (flavin-containing)
Comments: High specificity for (R)-pantolactone. Phenazine methosulfate (PMS) can act as acceptor. The enzyme has been studied in the bacterium Nocardia asteroides and shown to be membrane-bound and induced by 1,2-propanediol. The FMN cofactor is non-covalently bound.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 140879-14-7
References:
1.  Kataoka, M., Shimizu, S. and Yamada, H. Purification and characterization of a novel FMN-dependent enzyme. Membrane-bound L-(+)-pantoyl lactone dehydrogenase from Nocardia asteroides. Eur. J. Biochem. 204 (1992) 799–806. [DOI] [PMID: 1541293]
[EC 1.1.99.27 created 1999]
 
 
EC 1.1.99.28     
Accepted name: glucose-fructose oxidoreductase
Reaction: D-glucose + D-fructose = D-gluconolactone + D-glucitol
Systematic name: D-glucose:D-fructose oxidoreductase
Comments: D-mannose, D-xylose, D-galactose, 2-deoxy-D-glucose and L-arabinose will function as aldose substrates, but with low affinities. The ketose substrate must be in the open-chain form. The apparent affinity for fructose is low, because little of the fructose substrate is in the open-chain form. Xylulose and glycerone (dihydroxyacetone) will replace fructose, but they are poor substrates. The enzyme from Zymomonas mobilis contains tightly bound NADP+.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 94949-35-6
References:
1.  Zachariou, M. and Scopes, R.K. Glucose-fructose oxidoreductase: a new enzyme isolated from Zymomonas mobilis that is responsible for sorbitol production. J. Bacteriol. 167 (1986) 863–869. [DOI] [PMID: 3745122]
2.  Hardman, M.J. and Scopes, R.K. The kinetics of glucose-fructose oxidoreductase from Zymomonas mobilis. Eur. J. Biochem. 173 (1988) 203–209. [DOI] [PMID: 3356190]
3.  Kanagasundaram, V. and Scopes, R.K. Cloning, sequence analysis and expression of the structural gene encoding glucose-fructose oxidoreductase. J. Bacteriol. 174 (1992) 1439–1447. [DOI] [PMID: 1537789]
[EC 1.1.99.28 created 1999]
 
 
EC 1.1.99.29     
Accepted name: pyranose dehydrogenase (acceptor)
Reaction: (1) a pyranose + acceptor = a pyranos-2-ulose (or a pyranos-3-ulose or a pyranos-2,3-diulose) + reduced acceptor
(2) a pyranoside + acceptor = a pyranosid-3-ulose (or a pyranosid-3,4-diulose) + reduced acceptor
Glossary: ferricenium ion = bis(η5-cyclopentadienyl)iron(1+)
Other name(s): pyranose dehydrogenase; pyranose-quinone oxidoreductase; quinone-dependent pyranose dehydrogenase; PDH
Systematic name: pyranose:acceptor oxidoreductase
Comments: Requires FAD. A number of aldoses and ketoses in pyranose form, as well as glycosides, gluco-oligosaccharides, sucrose and lactose can act as a donor. 1,4-Benzoquinone or ferricenium ion (ferrocene oxidized by removal of one electron) can serve as acceptor. Unlike EC 1.1.3.10, pyranose oxidase, this fungal enzyme does not interact with O2 and exhibits extremely broad substrate tolerance with variable regioselectivity (C-3, C-2 or C-3 + C-2 or C-3 + C-4) for (di)oxidation of different sugars. D-Glucose is exclusively or preferentially oxidized at C-3 (depending on the enzyme source), but can also be oxidized at C-2 + C-3. The enzyme also acts on 1→4-α- and 1→4-β-gluco-oligosaccharides, non-reducing gluco-oligosaccharides and L-arabinose, which are not substrates of EC 1.1.3.10. Sugars are oxidized in their pyranose but not in their furanose form.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 190606-21-4
References:
1.  Volc, J., Kubátová, E., Wood, D. and Daniel, G. Pyranose 2-dehydrogenase, a novel sugar oxidoreductase from the basidiomycete fungus Agaricus bisporus. Arch. Microbiol. 167 (1997) 119–125. [PMID: 9042751]
2.  Volc, J., Sedmera, P., Halada, P., Přikyrlová, V. and Daniel, G. C-2 and C-3 oxidation of D-Glc, and C-2 oxidation of D-Gal by pyranose dehydrogenase from Agaricus bisporus. Carbohydr. Res. 310 (1998) 151–156.
3.  Volc, J., Sedmera, P., Halada, P., Přikyrlová, V. and Haltrich, D. Double oxidation of D-xylose to D-glycero-pentos-2,3-diulose (2,3-diketo-D-xylose) by pyranose dehydrogenase from the mushroom Agaricus bisporus. Carbohydr. Res. 329 (2000) 219–225. [DOI] [PMID: 11086703]
4.  Volc, J., Kubátová, E., Daniel, G., Sedmera, P. and Haltrich, D. Screening of basidiomycete fungi for the quinone-dependent sugar C-2/C-3 oxidoreductase, pyranose dehydrogenase, and properties of the enzyme from Macrolepiota rhacodes. Arch. Microbiol. 176 (2001) 178–186. [PMID: 11511865]
5.  Volc, J., Sedmera, P., Halada, P., Daniel, G., Přikyrlová, V. and Haltrich, D. C-3 oxidation of non-reducing sugars by a fungal pyranose dehydrogenase: spectral characterization. J. Mol. Catal., B Enzym. 17 (2002) 91–100.
[EC 1.1.99.29 created 2004]
 
 
EC 1.1.99.30     
Accepted name: 2-oxo-acid reductase
Reaction: a (2R)-hydroxy-carboxylate + acceptor = a 2-oxocarboxylate + reduced acceptor
Other name(s): (2R)-hydroxycarboxylate-viologen-oxidoreductase; HVOR; 2-oxoacid reductase
Systematic name: (2R)-hydroxy-carboxylate:acceptor oxidoreductase
Comments: Contains [4Fe-4S] and a mononucleotide molybdenum (pyranopterin) cofactor. Has broad substrate specificity, with 2-oxo-monocarboxylates and 2-oxo-dicarboxylates acting as substrates. Branching in a substrate at the C-3 position results in loss of activity. The enzyme from Proteus sp. is inactivated by oxygen.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 115299-99-5
References:
1.  Trautwein, T., Krauss, F., Lottspeich, F. and Simon, H. The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein. Eur. J. Biochem. 222 (1994) 1025–1032. [DOI] [PMID: 8026480]
2.  Neumann, S. and Simon, H. On a non-pyridine nucleotide-dependent 2-oxoacid reductase of broad specificity from two Proteus species. FEBS Lett. 167 (1985) 29–32.
[EC 1.1.99.30 created 2004]
 
 
EC 1.1.99.31     
Accepted name: (S)-mandelate dehydrogenase
Reaction: (S)-mandelate + acceptor = phenylglyoxylate + reduced acceptor
For diagram of reaction, click here
Glossary: (S)-mandelate = (S)-2-hydroxy-2-phenylacetate
phenylglyoxylate = benzoylformate = 2-oxo-2-phenylacetate
Other name(s): MDH (ambiguous)
Systematic name: (S)-mandelate:acceptor 2-oxidoreductase
Comments: This enzyme is a member of the FMN-dependent α-hydroxy-acid oxidase/dehydrogenase family [1]. While all enzymes of this family oxidize the (S)-enantiomer of an α-hydroxy acid to an α-oxo acid, the ultimate oxidant (oxygen, intramolecular heme or some other acceptor) depends on the particular enzyme. This enzyme transfers the electron pair from FMNH2 to a component of the electron transport chain, most probably ubiquinone [1,2]. It is part of a metabolic pathway in Pseudomonads that allows these organisms to utilize mandelic acid, derivatized from the common soil metabolite amygdalin, as the sole source of carbon and energy [2]. The enzyme has a large active-site pocket and preferentially binds substrates with longer sidechains, e.g. 2-hydroxyoctanoate rather than 2-hydroxybutyrate [1]. It also prefers substrates that, like (S)-mandelate, have β unsaturation, e.g. (indol-3-yl)glycolate compared with (indol-3-yl)lactate [1]. Esters of mandelate, such as methyl (S)-mandelate, are also substrates [3].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9067-95-2
References:
1.  Lehoux, I.E. and Mitra, B. (S)-Mandelate dehydrogenase from Pseudomonas putida: mechanistic studies with alternate substrates and pH and kinetic isotope effects. Biochemistry 38 (1999) 5836–5848. [DOI] [PMID: 10231535]
2.  Dewanti, A.R., Xu, Y. and Mitra, B. Role of glycine 81 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate specificity and oxidase activity. Biochemistry 43 (2004) 10692–10700. [DOI] [PMID: 15311930]
3.  Dewanti, A.R., Xu, Y. and Mitra, B. Esters of mandelic acid as substrates for (S)-mandelate dehydrogenase from Pseudomonas putida: implications for the reaction mechanism. Biochemistry 43 (2004) 1883–1890. [DOI] [PMID: 14967029]
[EC 1.1.99.31 created 2006]
 
 
EC 1.1.99.32     
Accepted name: L-sorbose 1-dehydrogenase
Reaction: L-sorbose + acceptor = 1-dehydro-L-sorbose + reduced acceptor
Glossary: 1-dehydro-L-sorbose = L-sorbosone = 2-dehydro-L-gulose
Other name(s): SDH (ambiguous)
Systematic name: L-sorbose:acceptor 1-oxidoreductase
Comments: The product, L-sorbosone, is an intermediate in bacterial 2-keto-L-gulonic-acid formation. The activity of this membrane-bound enzyme is stimulated by Fe(III) or Co2+ but is inhibited by Cu2+. The enzyme is highly specific for L-sorbose as other sugars, such as glucose, mannitol and sorbitol, are not substrates. Phenazine methosulfate and DCIP can act as artificial acceptors.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc
References:
1.  Sugisawa, T., Hoshino, T., Nomura, S. and Fujiwara, A. Isolation and characterization of membrane-bound L-sorbose dehydrogenase from Gluconobacter melanogenus UV10. Agric. Biol. Chem. 55 (1991) 363–370.
[EC 1.1.99.32 created 2008]
 
 
EC 1.1.99.33      
Transferred entry: formate dehydrogenase (acceptor). Now EC 1.17.99.7, formate dehydrogenase (acceptor)
[EC 1.1.99.33 created 2010, deleted 2017]
 
 
EC 1.1.99.34      
Transferred entry: glucose-6-phosphate dehydrogenase (coenzyme-F420). As the acceptor is now known, the enzyme has been transferred to EC 1.1.98.2, glucose-6-phosphate dehydrogenase (coenzyme-F420)
[EC 1.1.99.34 created 2010, deleted 2011]
 
 
EC 1.1.99.35     
Accepted name: soluble quinoprotein glucose dehydrogenase
Reaction: D-glucose + acceptor = D-glucono-1,5-lactone + reduced acceptor
Other name(s): soluble glucose dehydrogenase; sGDH; glucose dehydrogenase (PQQ-dependent)
Systematic name: D-glucose:acceptor oxidoreductase
Comments: Soluble periplasmic enzyme containing a tightly-bound PQQ cofactor that is bound to a calcium ion. As the electron acceptor is not known, the enzyme has been assayed with Wurster's Blue or phenazine methosulfate. It has negligible sequence or structure similarity to other quinoproteins. It catalyses an exceptionally high rate of oxidation of a wide range of aldose sugars, including D-glucose, galactose, arabinose and xylose, and also the disaccharides lactose, cellobiose and maltose. It has been described only in Acinetobacter calcoaceticus.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc
References:
1.  Geiger, O. and Gorisch, H. Crystalline quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus. Biochemistry 25 (1986) 6043–6048.
2.  Dokter, P., Frank, J. and Duine, J.A. Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41. Biochem. J. 239 (1986) 163–167. [PMID: 3800975]
3.  Cleton-Jansen, A.M., Goosen, N., Wenzel, T.J. and van de Putte, P. Cloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: evidence for the presence of a second enzyme. J. Bacteriol. 170 (1988) 2121–2125. [DOI] [PMID: 2834325]
4.  Matsushita, K., Shinagawa, E., Adachi, O. and Ameyama, M. Quinoprotein D-glucose dehydrogenase of the Acinetobacter calcoaceticus respiratory chain: membrane-bound and soluble forms are different molecular species. Biochemistry 28 (1989) 6276–6280. [PMID: 2551369]
5.  Oubrie, A. and Dijkstra, B.W. Structural requirements of pyrroloquinoline quinone dependent enzymatic reactions. Protein Sci. 9 (2000) 1265–1273. [DOI] [PMID: 10933491]
6.  Matsushita, K., Toyama, H., Ameyama, M., Adachi, O., Dewanti, A. and Duine, J.A. Soluble and membrane-bound quinoprotein D-glucose dehydrogenases of the Acinetobacter calcoaceticus : the binding process of PQQ to the apoenzymes. Biosci. Biotechnol. Biochem. 59 (1995) 1548–1555.
[EC 1.1.99.35 created 2010]
 
 
EC 1.1.99.36     
Accepted name: alcohol dehydrogenase (nicotinoprotein)
Reaction: ethanol + acceptor = acetaldehyde + reduced acceptor
Other name(s): NDMA-dependent alcohol dehydrogenase; nicotinoprotein alcohol dehydrogenase; np-ADH; ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase
Systematic name: ethanol:acceptor oxidoreductase
Comments: Contains Zn2+. Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD+/NADH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro. The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol [1].
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc
References:
1.  Van Ophem, P.W., Van Beeumen, J. and Duine, J.A. Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. Purification and characterization of a novel type from Amycolatopsis methanolica. Eur. J. Biochem. 212 (1993) 819–826. [DOI] [PMID: 8385013]
2.  Piersma, S.R., Visser, A.J., de Vries, S. and Duine, J.A. Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase. Biochemistry 37 (1998) 3068–3077. [DOI] [PMID: 9485460]
3.  Schenkels, P. and Duine, J.A. Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes. Microbiology 146 (2000) 775–785. [DOI] [PMID: 10784035]
4.  Piersma, S.R., Norin, A., de Vries, S., Jornvall, H. and Duine, J.A. Inhibition of nicotinoprotein (NAD+-containing) alcohol dehydrogenase by trans-4-(N,N-dimethylamino)-cinnamaldehyde binding to the active site. J. Protein Chem. 22 (2003) 457–461. [PMID: 14690248]
5.  Norin, A., Piersma, S.R., Duine, J.A. and Jornvall, H. Nicotinoprotein (NAD+ -containing) alcohol dehydrogenase: structural relationships and functional interpretations. Cell. Mol. Life Sci. 60 (2003) 999–1006. [DOI] [PMID: 12827287]
[EC 1.1.99.36 created 2010]
 
 
EC 1.1.99.37     
Accepted name: methanol dehydrogenase (nicotinoprotein)
Reaction: methanol + acceptor = formaldehyde + reduced acceptor
Other name(s): NDMA-dependent methanol dehydrogenase; nicotinoprotein methanol dehydrogenase; methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase
Systematic name: methanol:acceptor oxidoreductase
Comments: Contains Zn2+ and Mg2+. Nicotinoprotein methanol dehydrogenases have a tightly bound NADP+/NADPH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro. The enzyme has been detected in several Gram-positive methylotrophic bacteria, including Amycolatopsis methanolica, Rhodococcus rhodochrous and Rhodococcus erythropolis [1-3]. These enzymes are decameric, and possess a 5-fold symmetry [4]. Some of the enzymes can also dismutate formaldehyde to methanol and formate [5].
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc
References:
1.  Vonck, J., Arfman, N., De Vries, G.E., Van Beeumen, J., Van Bruggen, E.F. and Dijkhuizen, L. Electron microscopic analysis and biochemical characterization of a novel methanol dehydrogenase from the thermotolerant Bacillus sp. C1. J. Biol. Chem. 266 (1991) 3949–3954. [PMID: 1995642]
2.  Van Ophem, P.W., Van Beeumen, J. and Duine, J.A. Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. Purification and characterization of a novel type from Amycolatopsis methanolica. Eur. J. Biochem. 212 (1993) 819–826. [DOI] [PMID: 8385013]
3.  Bystrykh, L.V., Vonck, J., van Bruggen, E.F., van Beeumen, J., Samyn, B., Govorukhina, N.I., Arfman, N., Duine, J.A. and Dijkhuizen, L. Electron microscopic analysis and structural characterization of novel NADP(H)-containing methanol: N,N′-dimethyl-4-nitrosoaniline oxidoreductases from the gram-positive methylotrophic bacteria Amycolatopsis methanolica and Mycobacterium gastri MB19. J. Bacteriol. 175 (1993) 1814–1822. [DOI] [PMID: 8449887]
4.  Hektor, H.J., Kloosterman, H. and Dijkhuizen, L. Identification of a magnesium-dependent NAD(P)(H)-binding domain in the nicotinoprotein methanol dehydrogenase from Bacillus methanolicus. J. Biol. Chem. 277 (2002) 46966–46973. [DOI] [PMID: 12351635]
5.  Park, H., Lee, H., Ro, Y.T. and Kim, Y.M. Identification and functional characterization of a gene for the methanol : N,N′-dimethyl-4-nitrosoaniline oxidoreductase from Mycobacterium sp. strain JC1 (DSM 3803). Microbiology 156 (2010) 463–471. [DOI] [PMID: 19875438]
[EC 1.1.99.37 created 2010]
 
 
EC 1.1.99.38     
Accepted name: 2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent)
Reaction: 2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine = 3-amino-2,3-dideoxy-scyllo-inosose + 5′-deoxyadenosine + L-methionine
For diagram of paromamine biosynthesis, click here
Other name(s): btrN (gene name); 2-deoxy-scyllo-inosamine dehydrogenase (SAM-dependent)
Systematic name: 2-deoxy-scyllo-inosamine:S-adenosyl-L-methionine 1-oxidoreductase
Comments: Involved in the biosynthetic pathway of the aminoglycoside antibiotics of the butirosin family. The enzyme from Bacillus circulans was shown to be a radical S-adenosyl-L-methionine (SAM) enzyme. cf. EC 1.1.1.329, 2-deoxy-scyllo-inosamine dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Yokoyama, K., Numakura, M., Kudo, F., Ohmori, D. and Eguchi, T. Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin. J. Am. Chem. Soc. 129 (2007) 15147–15155. [DOI] [PMID: 18001019]
2.  Yokoyama, K., Ohmori, D., Kudo, F. and Eguchi, T. Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy. Biochemistry 47 (2008) 8950–8960. [DOI] [PMID: 18672902]
[EC 1.1.99.38 created 2012, modified 2013]
 
 
EC 1.1.99.39     
Accepted name: D-2-hydroxyglutarate dehydrogenase
Reaction: (R)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor
Other name(s): D2HGDH (gene name)
Systematic name: (R)-2-hydroxyglutarate:acceptor 2-oxidoreductase
Comments: Contains FAD. The enzyme has no activity with NAD+ or NADP+, and was assayed in vitro using artificial electron acceptors. It has lower activity with (R)-lactate, (R)-2-hydroxybutyrate and meso-tartrate, and no activity with the (S) isomers. The mammalian enzyme is stimulated by Zn2+, Co2+ and Mn2+.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
References:
1.  Engqvist, M., Drincovich, M.F., Flugge, U.I. and Maurino, V.G. Two D-2-hydroxy-acid dehydrogenases in Arabidopsis thaliana with catalytic capacities to participate in the last reactions of the methylglyoxal and β-oxidation pathways. J. Biol. Chem. 284 (2009) 25026–25037. [DOI] [PMID: 19586914]
2.  Achouri, Y., Noel, G., Vertommen, D., Rider, M.H., Veiga-Da-Cunha, M. and Van Schaftingen, E. Identification of a dehydrogenase acting on D-2-hydroxyglutarate. Biochem. J. 381 (2004) 35–42. [DOI] [PMID: 15070399]
[EC 1.1.99.39 created 2013]
 
 
EC 1.1.99.40     
Accepted name: (R)-2-hydroxyglutarate—pyruvate transhydrogenase
Reaction: (R)-2-hydroxyglutarate + pyruvate = 2-oxoglutarate + (R)-lactate
Other name(s): DLD3 (gene name)
Systematic name: (R)-2-hydroxyglutarate:pyruvate oxidoreductase [(R)-lactate-forming]
Comments: The enzyme, characterized in the yeast Saccharomyces cerevisiae, also functions as EC 1.1.2.4, D-lactate dehydrogenase (cytochrome), and is active with oxaloacetate as electron acceptor forming (R)-malate.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc
References:
1.  Becker-Kettern, J., Paczia, N., Conrotte, J.F., Kay, D.P., Guignard, C., Jung, P.P. and Linster, C.L. Saccharomyces cerevisiae forms D-2-hydroxyglutarate and couples its degradation to D-lactate formation via a cytosolic transhydrogenase. J. Biol. Chem. 291 (2016) 6036–6058. [DOI] [PMID: 26774271]
[EC 1.1.99.40 created 2017]
 
 
EC 1.1.99.41     
Accepted name: 3-hydroxy-1,2-didehydro-2,3-dihydrotabersonine reductase
Reaction: (1) (3R)-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + acceptor = (3R)-3-hydroxy-16-methoxy-1,2-didehydro-2,3-dihydrotabersonine + reduced acceptor
(2) (3R)-3-hydroxy-2,3-dihydrotabersonine + acceptor = (3R)-3-hydroxy-1,2-didehydro-2,3-dihydrotabersonine + reduced acceptor
For diagram of vindoline biosynthesis, click here
Other name(s): T3R; tabersonine 3-reductase
Systematic name: (3R)-3-hydroxy-16-methoxy-2,3-dihydrotabersonine:acceptor oxidoreductase
Comments: This enzyme is involved in the biosynthesis of vindoline and vindorosine in the plant Catharanthus roseus (Madagascar periwinkle). In vivo, it functions in the direction of reduction. It has no activity with 3-epoxylated compounds, which can form spontaneously from its unstable substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Qu, Y., Easson, M.L., Froese, J., Simionescu, R., Hudlicky, T. and De Luca, V. Completion of the seven-step pathway from tabersonine to the anticancer drug precursor vindoline and its assembly in yeast. Proc. Natl. Acad. Sci. USA 112 (2015) 6224–6229. [DOI] [PMID: 25918424]
[EC 1.1.99.41 created 2017]
 
 
EC 1.1.99.42     
Accepted name: 4-pyridoxic acid dehydrogenase
Reaction: 4-pyridoxate + acceptor = 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + reduced acceptor
For diagram of pyridoxal catabolism, click here
Glossary: 4-pyridoxate = 3-hydroxy-5-(hydroxymethyl)-2-methylpyridine-4-carboxylate
dichloroindophenol = DCPIP = 2,6-dichloro-4-[(4-hydroxyphenyl)imino]cyclohexa-2,5-dien-1-one
Other name(s): mlr6792 (locus name)
Systematic name: 4-pyridoxate:acceptor 5-oxidoreductase
Comments: The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6). It is membrane bound and contains FAD. The enzyme has been assayed in vitro in the presence of the artificial electron acceptor dichloroindophenol (DCPIP).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yagi, T., Kishore, G.M. and Snell, E.E. The bacterial oxidation of vitamin B6. 4-Pyridoxic acid dehydrogenase: a membrane-bound enzyme from Pseudomonas MA-1. J. Biol. Chem. 258 (1983) 9419–9425. [PMID: 6348042]
2.  Ge, F., Yokochi, N., Yoshikane, Y., Ohnishi, K. and Yagi, T. Gene identification and characterization of the pyridoxine degradative enzyme 4-pyridoxic acid dehydrogenase from the nitrogen-fixing symbiotic bacterium Mesorhizobium loti MAFF303099. J. Biochem. 143 (2008) 603–609. [DOI] [PMID: 18216065]
[EC 1.1.99.42 created 2018]
 
 
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      
Transferred entry: formate dehydrogenase. Now EC 1.17.1.9, formate dehydrogenase
[EC 1.2.1.2 created 1961, deleted 2017]
 
 
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.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, 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. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 203–221.
2.  Racker, E. Aldehyde dehydrogenase, a diphosphopyridine nucleotide-linked enzyme. J. Biol. Chem. 177 (1949) 883–892. [PMID: 18110463]
[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, Gene, KEGG, MetaCyc, 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. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 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. [PMID: 13061400]
[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): ALDH
Systematic name: aldehyde:NAD(P)+ oxidoreductase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9028-88-0
References:
1.  Black, S. Yeast aldehyde dehydrogenase. Arch. Biochem. Biophys. 34 (1951) 86–97. [DOI] [PMID: 14904038]
2.  Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 203–221.
3.  King, T.E. and Cheldelin, V.H. Oxidation of acetaldehyde by Aerobacter suboxydans. J. Biol. Chem. 220 (1956) 177–191. [PMID: 13319337]
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. [DOI] [PMID: 13363916]
[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, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9028-89-1
References:
1.  Gunsalus, C.F., Stanier, R.Y. and Gunsalus, I.C. The enzymatic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the soluble enzymes. J. Bacteriol. 66 (1953) 548–553. [PMID: 13108854]
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, Gene, 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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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 the Entner-Doudoroff pathway, click here
Other name(s): triosephosphate dehydrogenase (ambiguous); glyceraldehyde phosphate dehydrogenase (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
Systematic name: D-glyceraldehyde-3-phosphate:NADP+ oxidoreductase
Links to other databases: BRENDA, EXPASY, Gene, 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. [PMID: 13271400]
[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 3-phenylpropanoate catabolism, click here, for diagram of catechol catabolism (meta ring cleavage), click here and for diagram of cinnamate catabolism, click here
Other name(s): aldehyde dehydrogenase (acylating); ADA; acylating acetaldehyde dehyrogenase; DmpF; BphJ
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, Gene, 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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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+
Other name(s): aspartate semialdehyde dehydrogenase; aspartic semialdehyde dehydrogenase; L-aspartate-β-semialdehyde:NADP+ oxidoreductase (phosphorylating); aspartic β-semialdehyde dehydrogenase; ASA dehydrogenase
Systematic name: L-aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating)
Links to other databases: BRENDA, EXPASY, Gene, 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. [PMID: 14353904]
2.  Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 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 diagram of reaction, click here
Other name(s): triosephosphate dehydrogenase (ambiguous); glyceraldehyde phosphate dehydrogenase; 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, Gene, 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. [PMID: 18910716]
3.  Hageman, R.H. and Arnon, D.I. The isolation of triosephosphate dehydrogenase from pea seeds. Arch. Biochem. Biophys. 55 (1955) 162–168. [DOI] [PMID: 14362612]
4.  Velick, S.F. and Furfine, C. Glyceraldehyde 3-phosphate dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 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) 309–324. [DOI] [PMID: 3370218]
[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 the carbon-fixation stages of the Calvin cycle, click here and for the Calvin cycle, 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, Gene, 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. [PMID: 13804190]
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. [PMID: 13271400]
[EC 1.2.1.13 created 1961]
 
 
EC 1.2.1.14      
Transferred entry: IMP dehydrogenase. 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. [DOI] [PMID: 13727610]
[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 the citric acid cycle, 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, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37250-88-7
References:
1.  Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 203–221.
2.  Jakoby, W.B. and Scott, E.M. Aldehyde oxidation. III. Succinic semialdehyde dehydrogenase. J. Biol. Chem. 234 (1959) 937–940. [PMID: 13654295]
3.  Nirenberg, M.W. and Jakoby, W.B. Enzymatic utilization of γ-hydroxybutyric acid. J. Biol. Chem. 235 (1960) 954–960. [PMID: 14427301]
[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. [PMID: 13738657]
[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, Gene, KEGG, MetaCyc, 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. [PMID: 13712439]
2.  Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 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. [PMID: 13846369]
[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 of arginine catabolism, click here
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Other name(s): γ-guanidinobutyraldehyde dehydrogenase (ambiguous); ABAL dehydrogenase; 4-aminobutyraldehyde dehydrogenase; 4-aminobutanal dehydrogenase; γ-aminobutyraldehyde dehydroganase; 1-pyrroline dehydrogenase; ABALDH; YdcW
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, Gene, 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. (Ed.), 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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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: 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, Gene, 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. [DOI]
3.  Fothergill, J.C. and Guest, J.R. Catabolism of L-lysine by Pseudomonas aeruginosa. J. Gen. Microbiol. 99 (1977) 139–155. [DOI] [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. [DOI] [PMID: 17388807]
[EC 1.2.1.20 created 1965, modified 2021]
 
 
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, Gene, 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, Gene, 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. [DOI] [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
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 arginine catabolism, click here and for diagram of the citric acid cycle, 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, Gene, 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. [DOI] [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. [DOI] [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: 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, Gene, 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 11477096]
[EC 1.2.1.25 created 1972, modified 2019, modified 2020]
 
 
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, Gene, 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. [PMID: 6024771]
[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 inositol catabolism, 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, Gene, 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. [DOI] [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. [DOI] [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, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37250-93-4
References:
1.  Gunsalus, C.F., Stanier, R.Y. and Gunsalus, I.C. The enzymatic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the soluble enzymes. J. Bacteriol. 66 (1953) 548–553. [PMID: 13108854]
[EC 1.2.1.28 created 1972]
 
 
EC 1.2.1.29     
Accepted name: aryl-aldehyde dehydrogenase
Reaction: an aromatic aldehyde + NAD+ + H2O = an aromatic acid + NADH + H+
Systematic name: aryl-aldehyde:NAD+ oxidoreductase
Comments: Oxidizes a number of aromatic aldehydes, but not aliphatic aldehydes.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-94-5
References:
1.  Raison, J.K., Henson, G. and Rienits, K.G. The oxidation of gentisaldehyde by nicotinamide-adenine dinucleotide-specific, aromatic aldehyde dehydrogenase from rabbit liver. Biochim. Biophys. Acta 118 (1966) 285–298. [PMID: 4289834]
[EC 1.2.1.29 created 1972]
 
 
EC 1.2.1.30     
Accepted name: carboxylate reductase (NADP+)
Reaction: an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Other name(s): aromatic acid reductase; aryl-aldehyde dehydrogenase (NADP+)
Systematic name: aryl-aldehyde:NADP+ oxidoreductase (ATP-forming)
Comments: The enzyme contains an adenylation domain, a phosphopantetheinyl binding domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group. The enzyme activates its substrate to an adenylate form, followed by a transfer to the phosphopantetheinyl binding domain. The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to an aldehyde and released.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9074-94-6
References:
1.  Gross, G.G. and Zenk, M.H. Reduktion aromatischer Säuer zu Aldehyden und Alkoholen im zellfreien System. 1. Reinigung und Eigenschaften von Aryl-Aldehyd:NADP-Oxidoreduktase aus Neurospora crassa. Eur. J. Biochem. 8 (1969) 413–419. [DOI] [PMID: 4389863]
2.  Gross, G.G. Formation and reduction of intermediate acyladenylate by aryl-aldehyde. NADP oxidoreductase from Neurospora crassa. Eur. J. Biochem. 31 (1972) 585–592. [DOI] [PMID: 4405494]
3.  Venkitasubramanian, P., Daniels, L. and Rosazza, J.P. Reduction of carboxylic acids by Nocardia aldehyde oxidoreductase requires a phosphopantetheinylated enzyme. J. Biol. Chem. 282 (2007) 478–485. [PMID: 17102130]
4.  Stolterfoht, H., Schwendenwein, D., Sensen, C.W., Rudroff, F. and Winkler, M. Four distinct types of E.C. 1.2.1.30 enzymes can catalyze the reduction of carboxylic acids to aldehydes. J. Biotechnol. 257 (2017) 222–232. [PMID: 28223183]
[EC 1.2.1.30 created 1972, modified 2019]
 
 
EC 1.2.1.31     
Accepted name: L-aminoadipate-semialdehyde dehydrogenase
Reaction: (S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+ (overall reaction)
(1a) (S)-2-amino-6-oxohexanoate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O (spontaneous)
(1b) (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD(P)+ + 2 H2O = L-2-aminoadipate + NAD(P)H + H+
For diagram of lysine catabolism, click here and for diagram of L-Lysine synthesis, click here
Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate
Other name(s): aminoadipate semialdehyde dehydrogenase; 2-aminoadipate semialdehyde dehydrogenase; α-aminoadipate-semialdehyde dehydrogenase; α-aminoadipate reductase; 2-aminoadipic semialdehyde dehydrogenase; L-α-aminoadipate δ-semialdehyde oxidoreductase; L-α-aminoadipate δ-semialdehyde:NAD+ oxidoreductase; L-α-aminoadipate δ-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase; L-2-aminoadipate 6-semialdehyde:NAD(P)+ 6-oxidoreductase
Systematic name: (S)-2-amino-6-oxohexanoate:NAD(P)+ 6-oxidoreductase
Comments: (S)-2-amino-6-oxohexanoate undergoes a spontaneous dehydration forming the cyclic (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which serves as a substrate for the hydrogenation reaction.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9067-87-2
References:
1.  Calvert, A.F. and Rodwell, V.W. Metabolism of pipecolic acid in a Pseudomonas species. 3. L-α-Aminoadipate δ-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase. J. Biol. Chem. 241 (1966) 409–414. [PMID: 4285660]
2.  Rodwell, V.W. Δ1-piperideine-6-carboxylic acid and α-aminoadipic acid δ-semialdehyde. Method Enzymol 17B (1971) 188–199.
3.  de La Fuente, J.L., Rumbero, A., Martin, J.F. and Liras, P. Δ-1-piperideine-6-carboxylate dehydrogenase, a new enzyme that forms α-aminoadipate in Streptomyces clavuligerus and other cephamycin C-producing actinomycetes. Biochem. J. 327 (1997) 59–64. [PMID: 9355735]
4.  Fujii, T., Narita, T., Agematu, H., Agata, N. and Isshiki, K. Cloning and characterization of pcd encoding Δ’-piperideine-6-carboxylate dehydrogenase from Flavobacterium lutescens IFO3084. J. Biochem. 128 (2000) 975–982. [PMID: 11098140]
[EC 1.2.1.31 created 1972, modified 2011]
 
 


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