Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase

被引：97

作者：

Pollack, RM ^{[1
]}

机构：

[1] Univ Maryland Baltimore Cty, Dept Chem & Biochem, Baltimore, MD 21250 USA

来源：

BIOORGANIC CHEMISTRY | 2004年 / 32卷 / 05期

基金：

美国国家卫生研究院;

关键词：

ketosteroid isomerase; mechanism; enolization; Marcus; energetics; structure; transition states;

D O I：

10.1016/j.bioorg.2004.06.005

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Breaking a carbon-hydrogen bond adjacent to a carbonyl is a slow step in a large number of chemical reactions. However, many enzymes are capable of catalyzing this reaction with great efficiency. One of the most proficient of these enzymes is 3-oxo-Delta(5)-steroid isomerase (KSI), which catalyzes the isomerization of a wide variety of 3-oxo-Delta(5)-steroids to their Delta(4)-conjugated isomers. In this review, the mechanism of KSI is discussed, with particular emphasis on energetic considerations. Both experimental and theoretical approaches are considered to explain the mechanistic details of the reaction. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：341 / 353

页数：13

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