| EC |
4.1.1.72 |
| Accepted name: |
branched-chain-2-oxoacid decarboxylase |
| Reaction: |
(3S)-3-methyl-2-oxopentanoate = 2-methylbutanal + CO2 |
| Other name(s): |
branched-chain oxo acid decarboxylase; branched-chain α-keto acid decarboxylase; branched-chain keto acid decarboxylase; BCKA; (3S)-3-methyl-2-oxopentanoate carboxy-lyase |
| Systematic name: |
(3S)-3-methyl-2-oxopentanoate carboxy-lyase (2-methylbutanal-forming) |
| Comments: |
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. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 63653-19-0 |
| References: |
| 1. |
Oku, H. and Kaneda, T. Biosynthesis of branched-chain fatty acids in Bacillus subtilis. A decarboxylase is essential for branched-chain fatty acid synthetase. J. Biol. Chem. 263 (1988) 18386–18396. [PMID: 3142877] |
| 2. |
de la Plaza, M., Fernandez de Palencia, P., Pelaez, C. and Requena, T. Biochemical and molecular characterization of α-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactis. FEMS Microbiol. Lett. 238 (2004) 367–374. [PMID: 15358422] |
| 3. |
Smit, B.A., van Hylckama Vlieg, J.E., Engels, W.J., Meijer, L., Wouters, J.T. and Smit, G. Identification, cloning, and characterization of a Lactococcus lactis branched-chain α-keto acid decarboxylase involved in flavor formation. Appl. Environ. Microbiol. 71 (2005) 303–311. [PMID: 15640202] |
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| [EC 4.1.1.72 created 1990] |
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