4-coumarate-CoA ligase

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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, specifically 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.

[edit] References

IUBMB entry for 6.2.1.12
BRENDA references for 6.2.1.12 (Recommended.)
PubMed references for 6.2.1.12
PubMed Central references for 6.2.1.12
Google Scholar references for 6.2.1.12
Gross GG, Zenk MH (1974). "Isolation and properties of hydroxycinnamate: CoA ligase from lignifying tissue of Forsythia". Eur. J. Biochem. 42: 453–9. 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: 457–64. PMID 4699252.