|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 1.2.5.c
Supersedes EC number: 220.127.116.11
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: aldehyde dehydrogenase (quinone)
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): 5.5617523 [Latendresse13]
Enzyme Commission Summary:
Wide specificity; acts on straight-chain aldehydes up to C10, aromatic aldehydes, glyoxylate and glyceraldehyde. The enzymes contains a pyrroloquinoline quinone cofactor and multiple hemes that deliver the electrons to the membrane quinone pool.
Unification Links: KEGG:R00544
Ameyama81: Ameyama, M., Osada, K., Shinagawa, E., Matsushita, K., Adachi, O. (1981). "Purification and characterization of aldehyde dehydrogenase of Acetobacter aceti." Agric. Biol. Chem. 45:1189-1890.
GomezManzo10: Gomez-Manzo S, Chavez-Pacheco JL, Contreras-Zentella M, Sosa-Torres ME, Arreguin-Espinosa R, Perez de la Mora M, Membrillo-Hernandez J, Escamilla JE (2010). "Molecular and catalytic properties of the aldehyde dehydrogenase of Gluconacetobacter diazotrophicus, a quinoheme protein containing pyrroloquinoline quinone, cytochrome b, and cytochrome c." J Bacteriol 192(21);5718-24. PMID: 20802042
Patel80a: Patel RN, Hou CT, Derelanko P, Felix A (1980). "Purification and properties of a heme-containing aldehyde dehydrogenase from Methylosinus trichosporium." Arch Biochem Biophys 203(2);654-62. PMID: 6779711
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