Serien protease; acylation process mechanism; ab initio calculations
Abstract :
[en] This work proposes a very detailed ab initio study of the hypothesis for a one-step serine protease acylation process with one water molecule acting as the main catalyst reactant. For the 11 increasing complexity models considered, the minimum and transition state conformations for the reaction are determined by full geometry optimizations at the ab initio self-consistent field (scF) levels within several basis sets, from MINI-1 to 6-31G, and, for the smallest complexes, at the post-SCF MP2 level within the 6-31G** basis set. The related thermodynamical quantities are calculated for all the conformations. The influence of the oxyanion hole stabilizer and of the dyad His57-Asp102 is quantified and a very good agreement is obtained with point mutagenesis. The activation barrier is found in the range 15-18 kcal/mol. (C) 1996 John Wiley & Sons, Inc.
Disciplines :
Mathematics
Author, co-author :
Dive, Georges ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Dehareng, Dominique ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Peeters, Daniel
Language :
English
Title :
Proposition for the acylation mechanism of serine proteases: A one-step process?
Publication date :
1996
Journal title :
International Journal of Quantum Chemistry
ISSN :
0020-7608
eISSN :
1097-461X
Publisher :
John Wiley & Sons, Inc, Hoboken, United States - New Jersey
Volume :
58
Issue :
1
Pages :
85-107
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
F.R.S.-FNRS - Fonds de la Recherche Scientifique BELSPO - SPP Politique scientifique - Service Public Fédéral de Programmation Politique scientifique
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Results available on request.
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