Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate.
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ABSTRACT:
SUBMITTER: Zhou Y
PROVIDER: S-EPMC3213857 | biostudies-literature | 2011 Feb
REPOSITORIES: biostudies-literature
Publications
Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate.
Chemical communications (Cambridge, England) 20101129 5
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. ...[more]
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