Citrate—CoA ligase
| citrate-CoA ligase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 6.2.1.18 | ||||||
| CAS number | 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 / EGO | ||||||
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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.