|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:
|Escherichia coli K-12 substr. MG1655:||NADPH-dependent aldehyde reductase: yqhD|
|Rattus norvegicus:||2-oxoaldehyde dehydrogenase|
|Saccharomyces cerevisiae:||potassium-activated aldehyde dehydrogenase, mitochondrial: ALD4|
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 direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3. 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 220.127.116.11 2-oxoaldehyde dehydrogenase (NAD+).
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
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493