| Citrate—CoA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.2.1.18 | ||||||||
| CAS no. | 856428-87-0 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a citrate—CoA ligase (EC 6.2.1.18) is an enzyme that catalyzes the chemical reaction
- ATP + citrate + CoA ADP + phosphate + (3S)-citryl-CoA
The 3 substrates of this enzyme are ATP, citrate, and CoA, whereas its 3 products are ADP, phosphate, and (3S)-citryl-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 citrate:CoA ligase (ADP-forming). Other names in common use include citryl-CoA synthetase, citrate:CoA ligase, and citrate thiokinase. This enzyme participates in citric acid cycle.
References
- Lill U, Schreil A, Eggerer H (1982). "Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase". Eur. J. Biochem. 125 (3): 645–50. doi:10.1111/j.1432-1033.1982.tb06731.x. PMID 6749502.
- Aoshima M, Ishii M, Igarashi Y (2004). "A novel enzyme, citryl-CoA synthetase, catalysing the first step of the citrate cleavage reaction in Hydrogenobacter thermophilus TK-6". Mol. Microbiol. 52 (3): 751–61. doi:10.1111/j.1365-2958.2004.04009.x. PMID 15101981.
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