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  • Title: The importance of GLU361 position in the reaction catalyzed by cholesterol oxidase.
    Author: Kass IJ, Sampson NS.
    Journal: Bioorg Med Chem Lett; 1998 Oct 06; 8(19):2663-8. PubMed ID: 9873599.
    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.
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