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Structure and mechanism of action of the Acyl‐CoA dehydrogenases 1
Author(s) -
Thorpe Colin,
Kim JujngJa P.
Publication year - 1995
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.9.9.7601336
Subject(s) - acyl coa dehydrogenase , biochemistry , dehydrogenase , flavoprotein , acyl coa , enzyme , chemistry , residue (chemistry) , beta oxidation , stereochemistry , mechanism of action , fatty acid , in vitro
Mitochondrial β‐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 catalyti‐cally essential amino acid residue that nevertheless is not conserved in the acyl‐CoA dehydrogenase family is discussed.—Thorpe, C., Kim, J‐J. P. Structure and mechanism of action of the acyl‐CoA dehydrogenases. FASEB J. 9, 718‐725 (1995)