| Title : A general acid-base mechanism for the stabilization of a tetrahedral adduct in a serine-carboxyl peptidase: a computational study - Guo_2005_J.Am.Chem.Soc_127_15662 |
| Author(s) : Guo H , Wlodawer A |
| Ref : Journal of the American Chemical Society , 127 :15662 , 2005 |
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Abstract :
The QM/MM MD and free energy simulations show that serine-carboxyl peptidases (sedolisins) may stabilize the tetrahedral intermediates and tetrahedral adducts primarily through a general acid-base mechanism involving Asp (Asp164 for kumamolisin-As) rather than the oxyanion-hole interactions as in the cases of serine proteases. |
| PubMedSearch : Guo_2005_J.Am.Chem.Soc_127_15662 |
| PubMedID: 16277482 |
Guo H, Wlodawer A (2005)
A general acid-base mechanism for the stabilization of a tetrahedral adduct in a serine-carboxyl peptidase: a computational study
Journal of the American Chemical Society
127 :15662
Guo H, Wlodawer A (2005)
Journal of the American Chemical Society
127 :15662