Acyl-CoA dehydrogenase

spinqualitylabelsall models Rat short chain acyl-CoA hydrogenase complex with cofactor FAD and CoA (PDB code 1jqi) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Acyl-CoA dehydrogenase (ACDH) catalyzes the introduction of a double bond between C2 and C3 of the thio-ester CoA substrate. This is the first reaction in fatty acid metabolism which produces acetyl-CoA. FAD is the cofactor of ACDH activity. ACDH is classified according to the length of its substrates as short- (SCAD), medium- (MCAD), very- and very long-chain (VLCAD) ACDH. MCAD can bind a broad range of chain length acyl-CoA substrates. See also Beta oxidation and Glutaryl-CoA dehydrogenase. Glutaryl-CoA dehydrogenase is required for the metabolism of Lys, Trp and hydroxyLys. Isovaleryl-CoA dehydrogenase catalyzes the conversion of isovaleryl-CoA to 3-methylcrotonyl-CoA. 3-hydroxyacyl-CoA dehydrogenase oxidates straight chain 3-hydroxyacyl-CoA. Disease Impairment of the activity of ACDH causes a variety of diseases associated with lack of fatty acid metabolism. MCAD mutations are associated with Sudden Infant Death and with Medium-chain Acyl-CoA Dehydrogenase Deficiency (MCADD). For details see Investigating the Mechanisms of Active Site Mutations to the 1T9G WT MCAD Protein to Better Understand Medium Chain Acyl-CoA Dehydrogenase Deficiency (MCADD). SCAD deficiency is a recessive disorder of fatty acid β-oxidation. Structural highlights SCAD is a homodimer with a single FAD binding site. MCAD is a homotetramer with 4 FAD binding sites in the subunits interface and 4 binding sites for acyl-CoA substrate within each monomer. One of the FAD binding sites in homotetramer of rat ACDH. Water molecules are shown as red spheres. One of the CoA binding sites in homotetramer of rat ACDH. 3D structures of acyl-CoA dehydrogenase Acyl-CoA dehydrogenase 3D structures

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