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Acyl-CoA dehydrogenase

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== Structural highlights ==
== Structural highlights ==
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SCAD is a homodimer with a single FAD binding site. <scene name='49/491924/Cv/7'>MCAD is a homotetramer</scene> with 4 FAD binding sites in the subunits interface and 4 binding sites for acyl-CoA substrate within each monomer.
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SCAD is a homodimer with a single FAD binding site. <scene name='49/491924/Cv/12'>MCAD is a homotetramer</scene> with 4 FAD binding sites in the subunits interface and 4 binding sites for acyl-CoA substrate within each monomer.
*One of the <scene name='49/491924/Cv/9'>FAD binding sites</scene> in homotetramer of rat ACDH. Water molecules are shown as red spheres.
*One of the <scene name='49/491924/Cv/9'>FAD binding sites</scene> in homotetramer of rat ACDH. Water molecules are shown as red spheres.
*One of the <scene name='49/491924/Cv/11'>CoA binding sites</scene> in homotetramer of rat ACDH.<ref>PMID:11812788</ref>
*One of the <scene name='49/491924/Cv/11'>CoA binding sites</scene> in homotetramer of rat ACDH.<ref>PMID:11812788</ref>

Revision as of 10:50, 20 December 2018

Rat short chain acyl-CoA hydrogenase complex with cofactor FAD and CoA (PDB code 1jqi)

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3D structures of acyl-CoA dehydrogenase

Updated on 20-December-2018

References

  1. Thorpe C, Kim JJ. Structure and mechanism of action of the acyl-CoA dehydrogenases. FASEB J. 1995 Jun;9(9):718-25. PMID:7601336
  2. Battaile KP, Molin-Case J, Paschke R, Wang M, Bennett D, Vockley J, Kim JJ. Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases. J Biol Chem. 2002 Apr 5;277(14):12200-7. Epub 2002 Jan 25. PMID:11812788 doi:10.1074/jbc.M111296200

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