Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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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:
methylglyoxal oxidase Inferred from experiment ( Pseudomonas putida )
methylglyoxal oxidase Inferred from experiment ( Pseudomonas sp. NCIB 8858 )
aldehyde dehydrogenase : alkH ( Pseudomonas oleovorans )
mitochondrial aldehyde dehydrogenase : ALDH2 ( Homo sapiens )
aldehyde dehydrogenase, mitochondrial : ALD5 ( Saccharomyces cerevisiae )
potassium-activated aldehyde dehydrogenase, mitochondrial : ALD4 ( Saccharomyces cerevisiae )
aldehyde dehydrogenase : ALD2 ( Saccharomyces cerevisiae )
aldehyde dehydrogenase : ALD3 ( Saccharomyces cerevisiae )
fatty aldehyde dehydrogenase : ALDH3A2 ( Homo sapiens )
4-trimethylaminobutyraldehyde dehydrogenase : ALDH9A1 ( Homo sapiens )

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, Ray82, Ray82a]

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

Ray82: 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

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


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 18.5 on Mon Nov 24, 2014, biocyc13.