Citrate lyase deacetylase
| [citrate-(pro-3S)-lyase] thiolesterase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.2.16 | ||||||||
| CAS no. | 58319-93-0 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme citrate lyase deacetylase (EC 3.1.2.16) catalyzes the reaction
- acetyl-[citrate (pro-3S)-lyase] + H2O = holo-[citrate (pro-3S)-lyase] + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is acetyl-[citrate-(pro-3S)-lyase] hydrolase. This enzyme is also called [citrate-(pro-3S)-lyase] thiolesterase.
References
- Giffhorn F, Rode H, Kuhn A, Gottschalk G (1980). "Citrate lyase deacetylase of Rhodopseudomonas gelatinosa. Isolation of the enzyme and studies on the inhibition by L-glutamate". Eur. J. Biochem. 111 (2): 461–71. doi:10.1111/j.1432-1033.1980.tb04961.x. PMID 7460909.