EC 1 - Oxidoreductases
EC 1.3 - Acting on the CH-CH group of donors
EC 1.3.8 - With a flavin as acceptor
EC 1.3.8.6 - Glutaryl-CoA dehydrogenase (ETF)
IntEnz Enzyme Nomenclature
EC 1.3.8.6
Names
glutaryl-CoA:(acceptor) 2,3-oxidoreductase (decarboxylating)
glutaryl-CoA dehydrogenase
Reactions
- (1) glutaryl-CoA + electron-transfer flavoprotein = crotonyl-CoA + CO2 + reduced electron-transfer flavoprotein
- (1a) glutaryl-CoA + electron-transfer flavoprotein = (E)-glutaconyl-CoA + reduced electron-transfer flavoprotein
- (1b) (E)-glutaconyl-CoA = crotonyl-CoA + CO2
Cofactor
Comments:
Contains FAD. The enzyme catalyses the oxidation of glutaryl-CoA to glutaconyl-CoA (which remains bound to the enzyme), and the decarboxylation of the latter to crotonyl-CoA (cf. EC 7.2.4.5, glutaconyl-CoA decarboxylase). FAD is the electron acceptor in the oxidation of the substrate, and its reoxidation by electron-transfer flavoprotein completes the catalytic cycle. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (this entry), and a non-decarboxylating enzyme that only catalyses the oxidation to glutaconyl-CoA (EC 1.3.99.32).
Links to other databases
References
-
Mammalian metabolism of glutaric acid.J. Biol. Chem. 244 : 1461-1467 (1969). [PMID: 4304226]
-
Purification of glutaryl-CoA dehydrogenase from Pseudomonas sp., an enzyme involved in the anaerobic degradation of benzoate.Arch. Microbiol. 159 : 174-181 (1993). [PMID: 8439237]
-
The functions of the flavin contact residues, alphaArg249 and betaTyr16, in human electron transfer flavoprotein.Biochim. Biophys. Acta 1433 : 139-152 (1999). [PMID: 10446367]
-
Kinetic mechanism of glutaryl-CoA dehydrogenase.Biochemistry 45 : 15853-15861 (2006). [PMID: 17176108]
[EC 1.3.8.6 created 1972 as EC 1.3.99.7, transferred 2012 to EC 1.3.8.6, modified 2013]