THEORY OF ENZYMATIC REVERSE-PROTONATION CATALYSIS

被引:12
作者
MOCK, WL
机构
[1] Department of Chemistry, University of Illinois at Chicago, Chicago
基金
美国国家卫生研究院;
关键词
D O I
10.1016/0045-2068(92)90047-7
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
Consideration of the requirements for realization of concurrent acid-base catalysis, together with the consequences of differential binding energy for enzyme-substrate complexes within kinetically equivalent protonation states, provides an indication of a general mechanism for promotion of substrate conversion at enzyme active sites. © 1992.
引用
收藏
页码:377 / 381
页数:5
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