Branched-chain-fatty-acid kinase
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
branched-chain fatty acid kinase | |||||||||
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Identifiers | |||||||||
EC number | 2.7.2.14 | ||||||||
CAS number | 84177-54-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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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.
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