Structure and Mechanism of Action of the acyl-CoA Dehydrogenases

FASEB J. 1995 Jun;9(9):718-25. doi: 10.1096/fasebj.9.9.7601336.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Acyl Coenzyme A / metabolism*
  • Acyl-CoA Dehydrogenase
  • Acyl-CoA Dehydrogenases / chemistry
  • Acyl-CoA Dehydrogenases / genetics
  • Acyl-CoA Dehydrogenases / metabolism*
  • Animals
  • Binding Sites
  • Flavoproteins / chemistry
  • Flavoproteins / genetics
  • Flavoproteins / metabolism*
  • Humans
  • Lipid Metabolism, Inborn Errors
  • Mitochondria / enzymology*
  • Substrate Specificity

Substances

  • Acyl Coenzyme A
  • Flavoproteins
  • Acyl-CoA Dehydrogenases
  • Acyl-CoA Dehydrogenase