|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:
pyruvate decarboxylase 1 : PDC1 ( Saccharomyces cerevisiae )
pyruvate decarboxylase 2 : PDC5 ( Saccharomyces cerevisiae )
pyruvate decarboxylase 3 : PDC6 ( Saccharomyces cerevisiae )
2-oxo acid decarboxylase : ARO10 ( Saccharomyces cerevisiae )
2-keto-methylvalerate decarboxylase : THI3 ( Saccharomyces cerevisiae )
In Pathway: L-isoleucine degradation II
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: branched-chain-2-oxoacid decarboxylase
Enzyme Commission Synonyms: branched-chain oxo acid decarboxylase, branched-chain α-keto acid decarboxylase, branched-chain keto acid decarboxylase, BCKA, (3S)-3-methyl-2-oxopentanoate carboxy-lyase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -3.465889 [Latendresse13]
Enzyme Commission Summary:
Acts on a number of 2-oxo acids, with a high affinity towards branched-chain substrates. The aldehyde formed may be enzyme-bound, and may be an intermediate in the bacterial system for the biosynthesis of branched-chain fatty acids.
Instance reaction of [a 2-oxo carboxylate + H+ = an aldehyde + CO2] (188.8.131.52):
i1: pyruvate + H+ → acetaldehyde + CO2 (184.108.40.206)
Oku88: Oku H, Kaneda T (1988). "Biosynthesis of branched-chain fatty acids in Bacillus subtilis. A decarboxylase is essential for branched-chain fatty acid synthetase." J Biol Chem 263(34);18386-96. PMID: 3142877
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