期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2003
卷号：100
期号：21
页码：12015-12020
DOI：10.1073/pnas.1534873100
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Standard free energies ({Delta}GN{degrees}) for formation of near attack conformers, those ground state conformers that can convert directly to the transition state, were calculated for the Claisen rearrangement of chorismate to prephenate in six different environments: water, wild-type enzymes from Bacillus subtilis and Escherichia coli, their Arg90Cit and Glu52Ala mutants, and the 1F7 catalytic antibody. Values of the calculated {Delta}GN{degrees}s and the experimentally determined activation energies ({Delta}G{ddagger}) are linearly related with the slope of {approx}1. This demonstrates that the relative rate of the chorismate [->] prephenate reaction is overwhelmingly dependent on the efficiency of formation of near attack conformers in the ground state.
