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

Ignatius J. Kass; Nicole S. Sampson

doi:10.1016/S0960-894X(98)00478-8

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

Ignatius J. Kass
, Nicole S. Sampson

Chemistry

Stony Brook University

Research output: Contribution to journal › Article › peer-review

34 Scopus citations

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.

Original language	English
Pages (from-to)	2663-2668
Number of pages	6
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	8
Issue number	19
DOIs	https://doi.org/10.1016/S0960-894X(98)00478-8
State	Published - Oct 6 1998

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title = "The importance of GLU361 position in the reaction catalyzed by cholesterol oxidase",

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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AU - Sampson, Nicole S.

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N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0032491078

U2 - 10.1016/S0960-894X(98)00478-8

DO - 10.1016/S0960-894X(98)00478-8

M3 - Article

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AN - SCOPUS:0032491078

SN - 0960-894X

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EP - 2668

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 19

ER -

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

Abstract

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