The enzyme citryl-CoA lyase (EC 4.1.3.34) catalyzes the chemical reaction
| citryl-CoA lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.3.34 | ||||||||
| CAS no. | 131095-35-7 | ||||||||
| 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 | ||||||||
| |||||||||
- (3S)-citryl-CoA acetyl-CoA + oxaloacetate
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon–carbon bonds. The systematic name of this enzyme class is (3S)-citryl-CoA oxaloacetate-lyase (acetyl-CoA-forming). This enzyme is also called (3S)-citryl-CoA oxaloacetate-lyase. This enzyme participates in citrate cycle (tca cycle).
References
edit- Dimroth P, Loyal R, Eggerer H (1977). "Characterization of the isolated transferase subunit of citrate lyase as a CoA-Transferase. Evidence against a covalent enzyme-substrate intermediate". Eur. J. Biochem. 80 (2): 479–88. doi:10.1111/j.1432-1033.1977.tb11903.x. PMID 336371.
- 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.
