Structure and mechanism of action of the acyl-CoA dehydrogenases.
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.
Thorpe
C
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Department of Chemistry and Biochemistry, University of Delaware, Newark 19716, USA.
Kim
J J
JJ
D000214:Acyl Coenzyme A / Q000378:metabolism*; D042964:Acyl-CoA Dehydrogenase; D044944:Acyl-CoA Dehydrogenases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D005420:Flavoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008052:Lipid Metabolism, Inborn Errors; D008928:Mitochondria / Q000201:enzymology*; D013379:Substrate Specificity
D000214:Acyl Coenzyme A; D005420:Flavoproteins; D044944:Acyl-CoA Dehydrogenases; D042964:Acyl-CoA Dehydrogenase