Structure and mechanism of action of the Acyl‐CoA dehydrogenases 1

作者：Colin Thorpe, Jujng‐Ja P. Kim · 发表于：The FASEB Journal · 年份：1995 · DOI：10.1096/fasebj.9.9.7601336 · 被引用次数：221 · 研究领域：Metabolism and Genetic Disorders、Peroxisome Proliferator-Activated Receptors、Biochemical and Molecular Research

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.