| 4-Coumarate—CoA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.2.1.12 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
4-coumarate—CoA ligase (EC 6.2.1.12) is an enzyme that catalyzes the chemical reaction
The enzyme produces the thioester of p-coumaric acid with coenzyme A. The reaction is driven to completion by the energy produced by the hydrolysis of adenosine triphosphate (ATP) to its monophosphate AMP, releasing diphosphate.[1][2] This reaction is an important step in the biosynthesis of phenylpropanoids.[3]
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, caffeoyl 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.[4]
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. doi:10.1016/0005-2744(73)90174-5. PMID 4699252.
- Ververidis Filippos, F.; Trantas Emmanouil; Douglas Carl; Vollmer Guenter; Kretzschmar Georg; Panopoulos Nickolas (October 2007). "Biotechnology of flavonoids and other phenylpropanoid-derived natural products. Part I: Chemical diversity, impacts on plant biology and human health". Biotechnology Journal. 2 (10): 1214–34. doi:10.1002/biot.200700084. PMID 17935117.
- Enzyme 6.2.1.12 at KEGG Pathway Database.