The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme

被引：60

作者：

Hur, S ^{[1
]}

Bruice, TC ^{[1
]}

机构：

[1] Univ Calif Santa Barbara, Dept Chem & Biochem, Santa Barbara, CA 93106 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2002年 / 99卷 / 03期

关键词：

D O I：

10.1073/pnas.022628599

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Molecular dynamics studies of the Escherichia coli chorismate mutase (EcCM), containing at the active site chorismate and in turn the transition state (TS), have been performed. The simulations show that TS is not bound any tighter than chorismate. Comparison of average polar interactions show they are virtually identical for interactions of EcCM with chorismate and the TS, whereas hydrophobic interactions with TS are much weaker than with chorismate. Interactions and the mechanism of catalysis of chorismate --> prephenate by the EcCM enzyme are discussed.

引用

页码：1176 / 1181

页数：6

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