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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.

References

  • Harwood CS, Canale-Parola E (1982). "Properties of acetate kinase isozymes and a branched-chain fatty acid kinase from a spirochete". J. Bacteriol. 152 (1): 246–54. PMC 221398. PMID 6288660.


This page was last edited on 26 August 2023, at 13:23
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