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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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| Main Authors: | , , , , |
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| Format: | Artigo |
| Jezik: | Inglês |
| Izdano: |
2011
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| Teme: | |
| Online dostop: | 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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