Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate.
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.
Department of Chemistry, New York University, New York, NY 10003, USA.
Yanzi
Y
Zhou
Yingkai
Y
Zhang
D000215:Acylation; D006639:Histidine / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D011789:Quantum Theory; D013816:Thermodynamics; D014357:Trypsin / Q000737:chemistry*
D006639:Histidine; D014357:Trypsin