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The FASEB Journal, Vol 9, 718-725, Copyright © 1995 by The Federation of American Societies for Experimental Biology

REVIEWS

Structure and mechanism of action of the acyl-CoA dehydrogenases

C Thorpe and JJ Kim
Department of Chemistry and Biochemistry, University of Delaware, Newark 19716, USA.

Mitochondrial beta-oxidation involves a family of flavoproteins that introduce a C-C double bond into their fatty acyl-CoA substrates. Deficiencies of these acyl-CoA dehydrogenases lead to fatty acid oxidation disorders involving life-threatening episodes of metabolic derangement. This review focuses on the medium chain acyl-CoA dehydrogenase as the best-understood member of its class. The crystal structure of the enzyme and salient features of its substrate specificity and mechanism of action are summarized. The surprising observation of a catalytically essential amino acid residue that nevertheless is not conserved in the acyl-CoA dehydrogenase family is discussed.


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Copyright © 1995 by The Federation of American Societies for Experimental Biology.