In enzymology, a glutaconyl-CoA decarboxylase (EC 7.2.4.5) is an enzyme that catalyzes the chemical reaction
(2E)-glutaconyl-CoA + H+ + Na+(in) ⇌ {\displaystyle \rightleftharpoons } (2E)-butenoyl-CoA + CO2 + Na+(out) Hence, this enzyme has one substrate, (2E)-glutaconyl-CoA, and two products, (2E)-butenoyl-CoA and CO2. During the process, a sodium ion is transported across the membrane. Previously, this enzyme was classified as EC 4.1.1.70. 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.
Structural studies As of mid-2024, five structures have been solved for this class of enzymes, with the PDB accession codes PDB: 1PIX, PDB: 3GF3, PDB: 3GF7, PDB: 3GLM and PDB: 3GMA.
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.
