MISC

2006年1月

All electron quantum chemical calculation of the entire enzyme system confirms a collective catalytic device in the chorismate mutase reaction

JOURNAL OF PHYSICAL CHEMISTRY B
  • T Ishida
  • ,
  • DG Fedorov
  • ,
  • K Kitaura

110
3
開始ページ
1457
終了ページ
1463
記述言語
英語
掲載種別
DOI
10.1021/jp0557159
出版者・発行元
AMER CHEMICAL SOC

To elucidate the catalytic power of enzymes, we analyzed the reaction profile of Claisen rearrangement of Bacillus subtilis chorismate mutase (BsCM) by all electron quantum chemical calculations using the fragment molecular orbital (FMO) method. To the best of our knowledge, this is the first report of ab initio-based quantum chemical calculations of the entire enzyme system, where we provide a detailed analysis of the catalytic factors that accomplish transition-state stabilization (TSS). FMO calculations deliver an ab initio-level estimate of the intermolecular interaction between the substrate and the amino acid residues of the enzyme. To clarify the catalytic role of Arg90, we calculated the reaction profile of the wild-type BsCM as well as Lys90 and Cit90 mutant BsCMs. Structural refinement and the reaction path determination were performed at the ab initio QM/MM level, and FMO calculations were applied to the QM/MM refined structures. Comparison between three types of reactions established two collective catalytic factors in the BsCM reaction: (1) the hydrogen bonds connecting, the Glu78-Arcr90- substrate cooperatively control the stability of TS relative to the ES complex and (2) the positive charge on Ar-90 polarizes the substrate in the TS region to gain more electrostatic stabilization.

Web of Science ® 被引用回数 : 50

リンク情報
DOI
https://doi.org/10.1021/jp0557159
CiNii Articles
http://ci.nii.ac.jp/naid/30010843107
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/16471697
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000235046300052&DestApp=WOS_CPL
ID情報
  • DOI : 10.1021/jp0557159
  • ISSN : 1520-6106
  • CiNii Articles ID : 30010843107
  • PubMed ID : 16471697
  • Web of Science ID : WOS:000235046300052

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