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Conformational Variability of Organophosphorous Hydrolase upon Soman and Paraoxon Binding

The bacterial enzyme organophosphorous hydrolase (OPH) exhibits both catalytic and substrate promiscuity. It hydrolyzes bonds in a variety of phosphotriester (P-O), phosphonothioate (P-S), phosphofluoridate (P-F) and phosphonocyanate (F-CN) compounds. However, its catalytic efficiency varies markedl...

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Detalhes bibliográficos
Main Authors: Gomes, Diego E.B., Lins, Roberto D., Pascutti, Pedro G., Lei, Chenghong, Soares, Thereza A.
Formato: Artigo
Idioma:Inglês
Publicado em: 2011
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3549322/
https://ncbi.nlm.nih.gov/pubmed/22098575
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/jp208787g
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