Glutaryl-CoA dehydrogenase

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<StructureSection load='3mpi' size='450' side='right' caption='Structure of glutaryl-CoA dehydrogenase complex with FAD and glutaryl-CoA (PDB code [[3mpi]]).' scene='59/593951/Cv/1'>
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<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 ==
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'''Glutaryl-CoA dehydrogenase''' (GCD) converts glutaryl-CoA to crotonyl-CoA. GCD is part of the metabolism of lysine and tryptophan<ref>PMID:17176108</ref>.
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'''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 ==
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== Structural highlights ==
== Structural highlights ==
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The bilogical assembly of GCD from ''Desulfococcus multivorans'' is <scene name='59/593951/Cv/2'>homotetramer</scene>. GCD active site is in a cleft formed by its α,β,α domains<ref>PMID:20486657</ref>.
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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>.
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<scene name='59/593951/Cv/7'>Glutaryl-CoA binding site</scene>. Water molecules are shown as red spheres.
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</StructureSection>
==3D structures of glutaryl-CoA dehydrogenase==
==3D structures of glutaryl-CoA dehydrogenase==

Current revision

Structure of glutaryl-CoA dehydrogenase complex with FAD and glutaryl-CoA (PDB code 3mpi).

Drag the structure with the mouse to rotate

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

  1. ↑ 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
  2. ↑ . PMID:249723495
  3. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel

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