The importance of GLU361 position in the reaction catalyzed by cholesterol oxidase |
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Authors: | IJ Kass NS Sampson |
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Affiliation: | Department of Chemistry, State University of New York, Stony Brook, NY 11794-3400, USA. |
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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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