Comparative study of the nucleophilic attack step in the proteases catalytic activity: A theoretical study |
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| Authors: | Sebastián A. Cuesta Cesar H. Zambrano F. Javier Torres Luis Rincón |
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| Affiliation: | 1. Instituto de Simulación Computacional (ISM), Universidad San Francisco de Quito (USFQ), Quito, Ecuador;2. Departamento de Ingeniería Química – Grupo de Química Computacional y Teórica (QCT), Universidad San Francisco de Quito (USFQ), Quito, Ecuador |
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| Abstract: | ABSTRACT The nucleophilic attack step of the hydrolysis reaction mechanism of the glycine-glycine peptide bond mediated by the enzymatic action of various proteases was elucidated by means of DFT calculations. Five different protease models were considered; namely: cysteine (Cys), threonine (Thr), serine (Ser), aspartyl (Asp) proteases, and a metalloprotease containing zinc (Zn). The model was simplified in order to gain information about the nucleophilic attack in this type of reaction. As a comparative study, this work is focused on the trend in the reactivity of the models. According to the computed activation energies, the reactivity order was determined as follows Cys?
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| Keywords: | Proteolysis transition state mechanism metalloproteases enzymatic catalysis |
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