In enzymology, a glutaconyl-CoA decarboxylase (EC 7.2.4.5) is an enzyme that catalyzes the chemical reaction[1]
| glutaconyl-CoA decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 7.2.4.5 | ||||||||
| 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 | ||||||||
| |||||||||
- (2E)-glutaconyl-CoA + H+ + Na+(in) (2E)-butenoyl-CoA + CO
2 + Na+(out)
Hence, this enzyme has one substrate, (2E)-glutaconyl-CoA, and two products, (2E)-butenoyl-CoA and CO2. During the process, an sodium ion is transported across the membrane. Previously, this enzyme was classified as EC 4.1.1.70.[1][2]
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.
As a decarboxylase, the enzyme requires biotin for its function.[1][2]
Structural studies
editAs of mid-2024, five structures have been solved for this class of enzymes, with the PDB accession codes 1PIX, 3GF3, 3GF7, 3GLM and 3GMA.
References
edit- ^ a b c "ENZYME - 7.2.4.5 glutaconyl-CoA decarboxylase". enzyme.expasy.org. Retrieved 2024-07-16.
- ^ a b Kress, Daniel; Brügel, Daniela; Schall, Iris; Linder, Dietmar; Buckel, Wolfgang; Essen, Lars-Oliver (October 2009). "An Asymmetric Model for Na+-translocating Glutaconyl-CoA Decarboxylases". Journal of Biological Chemistry. 284 (41): 28401–28409. doi:10.1074/jbc.m109.037762. ISSN 0021-9258. PMC 2788889. PMID 19654317.
- 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.
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