|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 18.104.22.168
Enzymes and Genes:
|Saccharomyces cerevisiae:||2-keto-methylvalerate decarboxylase: THI3|
2-oxo acid decarboxylase: ARO10
pyruvate decarboxylase 3: PDC6
pyruvate decarboxylase 2: PDC5
pyruvate decarboxylase 1: PDC1
In Pathway: L-isoleucine degradation II
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: 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] (22.214.171.124):
i1: pyruvate + H+ → acetaldehyde + CO2 (126.96.36.199)
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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