In enzymology, a butyrate-CoA ligase, also known as XM-ligase, (EC 18.104.22.168) is an enzyme that catalyzes the chemical reaction
- ATP + an acid + CoA AMP + diphosphate + an acyl-CoA
The 3 substrates of this enzyme are ATP, acid, and CoA, whereas its 3 products are AMP, diphosphate, and acyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. This enzyme participates in butanoate metabolism.
The systematic name of this enzyme class is butanoate:CoA ligase (AMP-forming). Other names in common use include:
- butyryl-CoA synthetase, fatty acid thiokinase (medium chain),
- acyl-activating enzyme, fatty acid elongate,
- fatty acid activating enzyme,
- fatty acyl coenzyme A synthetase,
- medium chain acyl-CoA synthetase,
- butyryl-coenzyme A synthetase,
- L-(+)-3-hydroxybutyryl CoA ligase,
- xenobiotic/medium-chain fatty acid ligase, and
- short-chain acyl-CoA synthetase.
- Mahler HR, Wakil SJ, Bock RM (1953). "Studies on fatty acid oxidation. I. Enzymatic activation of fatty acids". J. Biol. Chem. 204 (1): 453–68. PMID 13084616.
- Massaro EJ; Lennarz WJ (1965). "The partial purification and characterization of a bacterial fatty acyl coenzyme A synthetase". Biochemistry. 4: 85–90. doi:10.1021/bi00877a015. PMID 14285249.
- Websterlt JR, Gerowin LD, Rakita L (1965). "Purification and characteristics of a butyryl coenzyme A synthetase from bovine heart mitochondria". J. Biol. Chem. 240: 29–33. PMID 14253428.