Glutaryl-CoA dehydrogenase
FunctionGlutaryl-CoA dehydrogenase (GCD) converts glutaryl-CoA to crotonyl-CoA. GCD is part of the metabolism of lysine and tryptophan[1]. See also Acyl-CoA dehydrogenase and Beta oxidation.
DiseaseDefective GCD causes the often fatal glutaric acidemia[2]. The active GCD is a tetramer. Mutations which result in GCD dimers or monomers are associated with glutaric acidemia. Structural highlightsThe bilogical assembly of GCD from Desulfococcus multivorans is . GCD active site is in a cleft formed by its α,β,α domains[3]. . Water molecules are shown as red spheres. |
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3D structures of glutaryl-CoA dehydrogenase3D structures of glutaryl-CoA dehydrogenase
Updated on 15-February-2023
3d6b, 3eom, 3ii9 – BpGCD – Burkholderia pseudomallei
3eon – BpGCD + difluorophenyl methanol
3gqt – BpGCD + quinoxaline derivative
3gnc – BpGCD + piperazine derivative
3mpi – DmGCD + FAD + glutaryl-CoA – Desulfococcus multivorans
3mpj – DmGCD + FAD + peptide
1siq, 1sir – hGCD + FAD - human
2r0m – hGCD (mutant) + FAD + dienolate intermediate
2r0n – hGCD (mutant) + FAD + thiaglutarate-CoA
3sf6, 3swo – GCD + FDA – Mycobacterium smegmatis
ReferencesReferences
- ↑ Rao KS, Albro M, Dwyer TM, Frerman FE. Kinetic mechanism of glutaryl-CoA dehydrogenase. Biochemistry. 2006 Dec 26;45(51):15853-61. Epub 2006 Dec 2. PMID:17176108 doi:http://dx.doi.org/10.1021/bi0609016
- ↑ . PMID:249723495
- ↑ Wischgoll S, Demmer U, Warkentin E, Gunther R, Boll M, Ermler U. Structural basis for promoting and preventing decarboxylation in glutaryl-coenzyme a dehydrogenases. Biochemistry. 2010 Jun 29;49(25):5350-7. PMID:20486657 doi:10.1021/bi100317m