Glutaryl-CoA dehydrogenase
From Proteopedia
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| - | <StructureSection load='3mpi' size=' | + | <StructureSection load='3mpi' size='350' side='right' caption='Structure of glutaryl-CoA dehydrogenase complex with FAD and glutaryl-CoA (PDB code [[3mpi]]).' scene='59/593951/Cv/1'> |
== Function == | == Function == | ||
| - | '''Glutaryl-CoA dehydrogenase''' (GCD) converts glutaryl-CoA to crotonyl-CoA. | + | '''Glutaryl-CoA dehydrogenase''' (GCD) converts glutaryl-CoA to crotonyl-CoA. GCD is part of the metabolism of lysine and tryptophan<ref>PMID:17176108</ref>. See also [[Acyl-CoA dehydrogenase]] and [[Beta oxidation]]. |
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== Disease == | == Disease == | ||
| - | Defective GCD causes the often fatal glutaric acidemia<ref>PMID:249723495</ref>. | + | Defective GCD causes the often fatal glutaric acidemia<ref>PMID:249723495</ref>. The active GCD is a tetramer. Mutations which result in GCD dimers or monomers are associated with glutaric acidemia. |
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== Structural highlights == | == Structural highlights == | ||
| - | GCD active site is in a cleft formed by its α,β,α domains<ref>PMID:20486657</ref>. | + | The bilogical assembly of GCD from ''Desulfococcus multivorans'' is <scene name='59/593951/Cv/8'>homotetramer</scene>. GCD active site is in a cleft formed by its α,β,α domains<ref>PMID:20486657</ref>. |
| + | <scene name='59/593951/Cv/7'>Glutaryl-CoA binding site</scene>. Water molecules are shown as red spheres. | ||
| + | </StructureSection> | ||
==3D structures of glutaryl-CoA dehydrogenase== | ==3D structures of glutaryl-CoA dehydrogenase== | ||
Current revision
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3D 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
References
- ↑ 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
