|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 184.108.40.206
Enzymes and Genes:
|Corynebacterium glutamicum ATCC 13032 :||acetaldehyde dehydrogenase
|Homo sapiens :|
|Pseudomonas oleovorans :||aldehyde dehydrogenase
|Pseudomonas putida :||methylglyoxal oxidase
|Pseudomonas sp. NCIB 8858 :||methylglyoxal oxidase
|Saccharomyces cerevisiae :|
In Pathway: methylglyoxal degradation VII
Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: 2-oxoaldehyde dehydrogenase (NAD+)
Enzyme Commission Synonyms: α-ketoaldehyde dehydrogenase, methylglyoxal dehydrogenase, NAD+-linked α-ketoaldehyde dehydrogenase, 2-ketoaldehyde dehydrogenase, NAD+-dependent α-ketoaldehyde dehydrogenase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -13.315338 [Latendresse13]
Enzyme Commission Summary:
Not identical with EC 220.127.116.11 2-oxoaldehyde dehydrogenase (NADP+).
Instance reaction of [an aldehyde + NAD+ + H2O → a carboxylate + NADH + 2 H+] (18.104.22.168):
i1: methylglyoxal + NAD+ + H2O → pyruvate + NADH + 2 H+ (22.214.171.124)
Unification Links: KEGG:R00203
Ray82b: Ray S, Ray M (1982). "Purification and characterization of NAD and NADP-linked alpha-ketoaldehyde dehydrogenases involved in catalyzing the oxidation of methylglyoxal to pyruvate." J Biol Chem 257(18);10566-70. PMID: 7107625
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