Glutaconyl-CoA decarboxylase
| glutaconyl-CoA decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.1.70 | ||||||||
| CAS no. | 84399-93-9 | ||||||||
| 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 glutaconyl-CoA decarboxylase (EC 4.1.1.70) is an enzyme that catalyzes the chemical reaction
- 4-carboxybut-2-enoyl-CoA but-2-enoyl-CoA + CO2
Hence, this enzyme has one substrate, 4-carboxybut-2-enoyl-CoA, and two products, but-2-enoyl-CoA and CO2.
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 4-carboxybut-2-enoyl-CoA carboxy-lyase (but-2-enoyl-CoA-forming). Other names in common use include glutaconyl coenzyme A decarboxylase, pent-2-enoyl-CoA carboxy-lyase, and 4-carboxybut-2-enoyl-CoA carboxy-lyase. This enzyme participates in benzoate degradation via coa ligation and butanoate metabolism.
Structural studies[edit]
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1PIX.
References[edit]
- Buckel W, Semmler R (1983). "Purification, characterisation and reconstitution of glutaconyl-CoA decarboxylase, a biotin-dependent sodium pump from anaerobic bacteria". Eur. J. Biochem. 136 (2): 427–34. doi:10.1111/j.1432-1033.1983.tb07760.x. PMID 6628393.
- Buckel W (2001). "Sodium ion-translocating decarboxylases". Biochim. Biophys. Acta. 1505 (1): 15–27. doi:10.1016/s0005-2728(00)00273-5. PMID 11248185.
