IntEnz

EC 1.3.8.6 - Glutaryl-CoA dehydrogenase (ETF)

IntEnz Enzyme Nomenclature
EC 1.3.8.6

Names

Reaction

• 13389 [IUBMB]
  glutaryl-CoA

  glutaryl-CoA

  Name origin: UniProt - CHECKED (C)

  CHEBI:57378

  Formula: C26H37N7O19P3S
  Charge: -5

  ChEBI compound status: CHECKED (C)

  

  +

  2

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  oxidized [electron-transfer flavoprotein]

  oxidized [electron-transfer flavoprotein]

  GENERIC:10685

  Is ROOT: no
  ROOT compound: GENERIC:10684

  Number of residues: 1

  FAD FAD Name origin: UniProt - CHECKED (C) CHEBI:57692 Formula: C27H30N9O15P2 Charge: -3 Position: undefined ChEBI compound status: CHECKED (C)

  =

  (2E)-butenoyl-CoA

  (2E)-butenoyl-CoA

  Name origin: UniProt - CHECKED (C)

  CHEBI:57332

  Formula: C25H36N7O17P3S
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

  +

  CO₂

  CO2

  Name origin: UniProt - CHECKED (C)

  CHEBI:16526

  Formula: CO2
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  reduced [electron-transfer flavoprotein]

  reduced [electron-transfer flavoprotein]

  GENERIC:10686

  Is ROOT: no
  ROOT compound: GENERIC:10684

  Number of residues: 1

  FADH2 FADH2 Name origin: UniProt - CHECKED (C) CHEBI:58307 Formula: C27H33N9O15P2 Charge: -2 Position: undefined ChEBI compound status: CHECKED (C)

Cofactor

• FAD

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 4.1.1.70, 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

1. Besrat, A., Polan, C.E. and Henderson, L.M.
   Mammalian metabolism of glutaric acid.
   J. Biol. Chem. 244: 1461-1467 (1969). [PMID: 4304226]
2. Hartel, U., Eckel, E., Koch, J., Fuchs, G., Linder, D., Buckel, W.
   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]
3. Dwyer, T. M., Zhang, L., Muller, M., Marrugo, F., Frerman, F.
   The functions of the flavin contact residues, alphaArg249 and betaTyr16, in human electron transfer flavoprotein.
   Biochim. Biophys. Acta 1433: 139-152 (1999). [PMID: 10446367]
4. Rao, K. S., Albro, M., Dwyer, T. M., Frerman, F. E.
   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]