Asymmetric biocatalysis of the nerve agent VX by human serum paraoxonase 1: Molecular Docking and Reaction Mechanism calculations

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18450%2F16%3A50005093" target="_blank" >RIV/62690094:18450/16:50005093 - isvavai.cz</a>

Result on the web

<a href="https://link.springer.com/article/10.1007/s00044-016-1704-x" target="_blank" >https://link.springer.com/article/10.1007/s00044-016-1704-x</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00044-016-1704-x" target="_blank" >10.1007/s00044-016-1704-x</a>

Result language

angličtina

Original language name

Asymmetric biocatalysis of the nerve agent VX by human serum paraoxonase 1: Molecular Docking and Reaction Mechanism calculations

Original language description

Organophosphorus compounds have been employed in agricultural activity for a long time, causing serious public health problems. Due to their toxic properties, these compounds have also been used as chemical weapons. In view of this scenario, the catalytic degradation and the development of bioremediation processes of organophosphorus compounds have been of wide interest. Among several enzymes capable of degrading organophosphorus compounds, the human serum paraoxonase 1 has shown good potential for this purpose. To evaluate the interaction mode between the human serum paraoxonase 1 (wild-type and mutants) enzymes and the VX compound, one of the most toxic organophosphorus compounds known, molecular docking calculations were conducted. In addition, seeking to analyze the reaction pathway and the stereochemistry preference by human serum paraoxonase 1 and the Rp and Sp enantiomers of VX, quantum mechanical/molecular mechanics calculations were performed. Our theoretical findings put in evidence that the wild-type and mutant human serum paraoxonase 1 enzymes strongly interact with VX. Moreover, with the quantum mechanical/molecular mechanics study, we observed that the human serum paraoxonase 1 preferentially degrades one enantiomer in relation to the other. The current results indicate key points for designing new, more efficient mutant human serum paraoxonase 1 enzymes for VX degradation.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10401 - Organic chemistry

Project

—

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2016

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Medicinal chemistry research

ISSN

1054-2523

e-ISSN

—

Volume of the periodical

25

Issue of the periodical within the volume

11

Country of publishing house

US - UNITED STATES

Number of pages

13

Pages from-to

2521-2533

UT code for WoS article

000386763500009

EID of the result in the Scopus database

2-s2.0-84981205697