Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate

Yanzi Zhou; Yingkai Zhang

doi:10.1039/c0cc04112b

Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate

Yanzi Zhou, Yingkai Zhang

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

The acylation mechanism of a prototypical serine protease trypsin and its complete free energy reaction profile have been determined by Born–Oppenheimer ab initio QM/MM molecular dynamics simulations with umbrella sampling.

Original language	English (US)
Pages (from-to)	1577-1579
Number of pages	3
Journal	Chemical Communications
Volume	47
Issue number	5
DOIs	https://doi.org/10.1039/c0cc04112b
State	Published - Feb 7 2011

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/c0cc04112b

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title = "Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate",

abstract = "The acylation mechanism of a prototypical serine protease trypsin and its complete free energy reaction profile have been determined by Born–Oppenheimer ab initio QM/MM molecular dynamics simulations with umbrella sampling.",

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Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate

Abstract

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