Branched-chain-fatty-acid kinase
From Wikipedia, the free encyclopedia
In enzymology, a branched-chain-fatty-acid kinase (EC 2.7.2.14) is an enzyme that catalyzes the chemical reaction
- ATP + 2-methylpropanoate
ADP + 2-methylpropanoyl phosphate
Thus, the two substrates of this enzyme are ATP and 2-methylpropanoate, whereas its two products are ADP and 2-methylpropanoyl phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:branched-chain-fatty-acid 1-phosphotransferase. This enzyme is also called isobutyrate kinase.
[edit] References
- IUBMB entry for 2.7.2.14
- BRENDA references for 2.7.2.14 (Recommended.)
- PubMed references for 2.7.2.14
- PubMed Central references for 2.7.2.14
- Google Scholar references for 2.7.2.14
- Harwood CS, Canale-Parola E (1982). "Properties of acetate kinase isozymes and a branched-chain fatty acid kinase from a spirochete". J. Bacteriol. 152: 246–54. PMID 6288660.
[edit] External links
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- The CAS registry number for this enzyme class is 84177-54-8.

