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Acyl-CoA dehydrogenases and acyl-CoA oxidases - Structural basis for mechanistic similarities and differences

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EUROPEAN JOURNAL OF BIOCHEMISTRY
卷 271, 期 3, 页码 483-493

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BLACKWELL PUBLISHING LTD
DOI: 10.1046/j.1432-1033.2003.03948.x

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  1. NIGMS NIH HHS [GM29076] Funding Source: Medline

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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.

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