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ID: ALA1130593

Journal: Bioorg Med Chem Lett

Title: The importance of GLU361 position in the reaction catalyzed by cholesterol oxidase.

Authors: Kass IJ, Sampson NS.

Abstract: Cholesterol oxidase stereospecifically isomerizes cholest-5-en-3-one to cholest-4-en-3-one. When the base catalyst for isomerization, Glu361, is mutated to Asp, the rate of deprotonation of cholest-5-en-3-one is not affected, but protonation of the dienolic intermediate becomes rate-limiting. This may be a consequence of the large distance between the catalytic base and carbon-6 of the intermediate in the mutant enzyme.

CiteXplore: 9873599

DOI: 10.1016/s0960-894x(98)00478-8