Acyl-CoA dehydrogenases and acyl-CoA oxidases. Structural basis for mechanistic similarities and differences.
Acyl-CoA dehydrogenases and acyl-CoA oxidases are two closely related FAD-containing enzyme families that are present in mitochondria and peroxisomes, respectively. They catalyze the dehydrogenation of acyl-CoA thioesters to the corresponding trans-2-enoyl-CoA. This review examines the structure of medium chain acyl-CoA dehydrogenase, as a representative of the dehydrogenase family, with respect to the catalytic mechanism and its broad chain length specificity. Comparing the structures of four other acyl-CoA dehydrogenases provides further insights into the structural basis for the substrate specificity of each of these enzymes. In addition, the structure of peroxisomal acyl-CoA oxidase II from rat liver is compared to that of medium chain acyl-CoA dehydrogenase, and the structural basis for their different oxidative half reactions is discussed.
Kim
Jung-Ja P
JJ
Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI 53226, USA. jjkim@mcw.edu
Miura
Retsu
R
D044944:Acyl-CoA Dehydrogenases / Q000737:chemistry / Q000378:metabolism*; D042962:Acyl-CoA Oxidase / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D044944:Acyl-CoA Dehydrogenases; D042962:Acyl-CoA Oxidase