Butyrate—CoA ligase

Butyrate—CoA ligase, also known as xenobiotic/medium-chain fatty acid-ligase (XM-ligase), is an enzyme (EC 6.2.1.2) that catalyzes the chemical reaction:

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

Butyrate—CoA ligase
Identifiers
EC no.	6.2.1.2
CAS no.	9080-51-7
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
Search PMC articles PubMed articles NCBI proteins

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

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

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