|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 126.96.36.199
Enzymes and Genes:
|Escherichia coli K-12 substr. MG1655 :||NADPH-dependent aldehyde reductase
|Rattus norvegicus :||2-oxoaldehyde dehydrogenase
|Saccharomyces cerevisiae :||potassium-activated aldehyde dehydrogenase, mitochondrial
aldehyde dehydrogenase, mitochondrial : ALD5
magnesium-activated aldehyde dehydrogenase, cytosolic : ALD6
In Pathway: methylglyoxal degradation VIII
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 (NADP+)
Enzyme Commission Synonyms: α-ketoaldehyde dehydrogenase, methylglyoxal dehydrogenase, NADP+-linked α-ketoaldehyde dehydrogenase, 2-ketoaldehyde dehydrogenase, NADP+-dependent α-ketoaldehyde dehydrogenase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -14.563599 [Latendresse13]
Enzyme Commission Summary:
Not identical with EC 188.8.131.52 2-oxoaldehyde dehydrogenase (NAD+).
Instance reaction of [an aldehyde + NADP+ + H2O → a carboxylate + NADPH + 2 H+] (184.108.40.206):
i1: methylglyoxal + NADP+ + H2O → pyruvate + NADPH + 2 H+ (220.127.116.11)
Unification Links: KEGG:R00205
Ray82a: 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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