Acyl-CoA dehydrogenase
From Proteopedia
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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. | 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> |
==3D structures of acyl-CoA dehydrogenase== | ==3D structures of acyl-CoA dehydrogenase== | ||
Revision as of 12:09, 22 March 2021
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References
- ↑ Thorpe C, Kim JJ. Structure and mechanism of action of the acyl-CoA dehydrogenases. FASEB J. 1995 Jun;9(9):718-25. PMID:7601336
- ↑ 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
