| Glutarate—CoA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.2.1.6 | ||||||||
| CAS no. | 9023-68-1 | ||||||||
| 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 glutarate—CoA ligase (EC 6.2.1.6) is an enzyme that catalyzes the chemical reaction
- ATP + glutarate + CoA ADP + phosphate + glutaryl-CoA
The 3 substrates of this enzyme are ATP, glutarate, and CoA, whereas its 3 products are ADP, phosphate, and glutaryl-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 glutarate:CoA ligase (ADP-forming). Other names in common use include glutaryl-CoA synthetase, and glutaryl coenzyme A synthetase. This enzyme participates in fatty acid metabolism and lysine degradation.
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Transcription
References
- Menon GK, Friedman DL, Stern JR (1960). "Enzymic synthesis of glutaryl-coenzyme A". Biochim. Biophys. Acta. 44: 375–377. doi:10.1016/0006-3002(60)91583-3. PMID 13769477.
This page was last edited on 26 August 2023, at 14:18