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Butyrate—CoA ligase

ATP + a carboxylic acid + CoA ${\displaystyle \rightleftharpoons }$ AMP + diphosphate + an acyl-CoA

The 3 substrates of this enzyme are ATP, carboxylic 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 the glycine conjugation of xenobiotics^[1] and butanoate metabolism.

Nomenclature[edit]

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.

Human proteins containing this domain[edit]

• ACSM1
• ACSM2A
• ACSM2B
• ACSM3
• ACSM4
• ACSM5
• ACSM6

References[edit]

• 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.