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Papers In Press, published online ahead of print January 25, 2002
Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI 53226
Corresponding Author: jjkim{at}mcw.edu
The acyl CoA-dehydrogenases are a family of flavin adenine dinucleotide-containing enzymes that catalyze the first step in the
J. Biol. Chem, 10.1074/jbc.M111296200
Submitted on November 27, 2001
Revised on January 22, 2002
Accepted on January 25, 2002
Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA; comparison with other acyl-CoA dehydrogenases
-oxidation of fatty acids and catabolism of some amino acids. They exhibit high sequence identity, yet are quite specific in their substrate binding. Short chain acyl-CoA dehydrogenase has maximal activity towards butyryl-CoA and negligible activity towards substrates longer than octanoyl-CoA. The crystal structure of rat short chain acyl-CoA dehydrogenase complexed with the inhibitor acetoacetyl-CoA has been determined at 2.25 Å resolution. Short chain acyl-CoA dehydrogenase is a homotetramer with a subunit mass of 43 kDa and crystallizes in the space group P321 with a=143.61 Å and c=77.46 Å. There are 2 monomers in the asymmetric unit. The overall structure of short chain acyl-CoA dehydrogenase is very similar to those of medium chain acyl-CoA dehydogenase, isovaleryl-CoA dehydrogenase and bacterial short chain acyl-CoA dehydrogenase with a three-domain structure composed of N- and C-terminal 
-helical domains separated by a -sheet domain. Comparison to other acyl-CoA dehydrogenases has provided additional insight to the basis of substrate specificity and the nature of the oxidase activity in this enzyme family. Ten reported pathogenic human mutations and two polymorphisms have been mapped onto the structure of short chain acyl-CoA dehydrogenase. None of the mutations directly affect the binding cavity or inter-subunit interactions.
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