4-Coumarate-CoA ligase

4-Coumarate-CoA ligase
Identifiers
EC number	6.2.1.12
CAS number	37332-51-7
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 / EGO
Search PMC articles PubMed articles

In enzymology, a 4-coumarate-CoA ligase (EC 6.2.1.12) is an enzyme that catalyzes the chemical reaction

ATP + 4-coumarate + CoA $\rightleftharpoons$ AMP + diphosphate + 4-coumaroyl-CoA

The 3 substrates of this enzyme are ATP, 4-coumarate, and CoA, whereas its 3 products are AMP, diphosphate, and 4-coumaroyl-CoA.

This enzyme belongs to the family of ligases, to be specific those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is 4-coumarate:CoA ligase (AMP-forming). Other names in common use include 4-coumaroyl-CoA synthetase, p-coumaroyl CoA ligase, p-coumaryl coenzyme A synthetase, p-coumaryl-CoA synthetase, p-coumaryl-CoA ligase, feruloyl CoA ligase, hydroxycinnamoyl CoA synthetase, 4-coumarate:coenzyme A ligase, caffeolyl coenzyme A synthetase, p-hydroxycinnamoyl coenzyme A synthetase, feruloyl coenzyme A synthetase, sinapoyl coenzyme A synthetase, 4-coumaryl-CoA synthetase, hydroxycinnamate:CoA ligase, p-coumaryl-CoA ligase, p-hydroxycinnamic acid:CoA ligase, and 4CL. This enzyme participates in phenylpropanoid biosynthesis.

References

• Gross GG, Zenk MH (1974). "Isolation and properties of hydroxycinnamate: CoA ligase from lignifying tissue of Forsythia". Eur. J. Biochem. 42 (2): 453–9. doi:10.1111/j.1432-1033.1974.tb03359.x. PMID 4364250. 
• Lindl T, Kreuzaler F, Hahlbrock K (1973). "Synthesis of p-coumaroyl coenzyme a with a partially purified p-coumarate:CoA ligase from cell suspension cultures of soybean (Glycine max)". Biochim. Biophys. Acta. 302 (2): 457–64. PMID 4699252.