| 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
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1PIX.
References
- 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.
| 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
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1PIX.
References
- 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.