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MetaCyc Reaction: 1.2.1.23

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 1.2.1.23

Enzymes and Genes:

Corynebacterium glutamicum ATCC 13032 : acetaldehyde dehydrogenase : ald
Homo sapiens :
Pseudomonas oleovorans : aldehyde dehydrogenase : alkH
Pseudomonas putida : methylglyoxal oxidase Inferred from experiment
Pseudomonas sp. NCIB 8858 : methylglyoxal oxidase Inferred from experiment
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 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Not identical with EC 1.2.1.49 2-oxoaldehyde dehydrogenase (NADP+).

Citations: [Monder67, Ray82a, Ray82b]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reaction of [an aldehyde + NAD+ + H2O → a carboxylate + NADH + 2 H+] (1.2.1.3):
i1: methylglyoxal + NAD+ + H2O → pyruvate + NADH + 2 H+ (1.2.1.23)

Unification Links: KEGG:R00203

Relationship Links: BRENDA:EC:1.2.1.23 , ENZYME:EC:1.2.1.23 , IUBMB-ExplorEnz:EC:1.2.1.23


References

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Monder67: Monder C (1967). "Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate." J Biol Chem 242(20);4603-9. PMID: 4383524

Ray82a: Ray M, Ray S (1982). "On the interaction of nucleotides and glycolytic intermediates with NAD-linked alpha-ketoaldehyde dehydrogenase." J Biol Chem 257(18);10571-4. PMID: 7107626

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Mon May 25, 2015, biocyc11.