Unknown

Dataset Information

0

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

ABSTRACT: 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.

SUBMITTER: Hur S 

PROVIDER: S-EPMC122163 | biostudies-literature | 2002 Feb

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

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

Hur Sun S   Bruice Thomas C TC  

Proceedings of the National Academy of Sciences of the United States of America 20020129 3

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  ...[more]