PMID: 8454629Mar 25, 1993Paper

Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in the amino-terminal domain of the multifunctional fatty acid oxidation protein from Escherichia coli.

The Journal of Biological Chemistry
S Y Yang, M Elzinga

Abstract

An Escherichia coli mutant multienzyme complex of fatty acid oxidation, composed of two 41-kDa beta-subunits and two 79-kDa mutant alpha-subunits with the alpha/Gly116-->Phe substitution, has been overproduced and purified. The catalytic properties of 3-ketoacyl-coenzyme A (CoA) thiolase and L-3-hydroxyacyl-CoA dehydrogenase were found to be virtually identical with those of the wild type, whereas both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities were eliminated by the alpha/Gly116-->Phe mutation. delta 3-cis-delta 2-trans-Enoyl-CoA isomerase was only slightly affected by the mutation. The results of this study, together with the sequence analysis of the large alpha-subunit of the E. coli complex (Yang, X.-Y. H., Schulz, H., Elzinga, M., and Yang, S.-Y. (1991) Biochemistry 30, 6788-6795) and a demonstration of the epimerization of D-3-hydroxyacyl-CoAs in E. coli via a dehydration/hydration mechanism (Smeland, T. E., Cuebas, D., and Schulz, H. (1991) J. Biol. Chem. 266, 23904-23908), lead to the conclusion that enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase are associated with a common active site in the amino-terminal domain of the multifunctional fatty acid oxidation protein. Thus the E. coli hydratase a...Continue Reading

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