Home Bratislava Medical Journal 2019 Bratislava Medical Journal Vol.120, No.2, p.139–143, 2019

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Published Monthly, in English
Founded: 1919
ISSN 0006-9248
(E)ISSN 1336-0345

Impact factor 1.564


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Bratislava Medical Journal Vol.120, No.2, p.139–143, 2019

Title: Evaluation of the substitutions in 212, 342 and 215 amino acid positions in binding site of organophosphorus acid anhydrolase using the molecular docking and laboratory analysis
Author: M. F. Heidari, S. S. Arab, A. Noroozi-aghideh, H. Tebyanian, A. M. Latifi

Abstract: OBJECTIVE: Organophosphorus Acid Anhydrolase (OPAA) is used as one of the most important enzymes in the decontamination process of organophosphate compounds. In this study, we aimed to evaluate the effects of amino acid substitution in OPAA’s substrate-binding site on its catalytic activity using the rational engineering strategy.
METHODS: The native and three mutant forms of OPAA enzyme including 4ZWP, 4ZWU and Mut6 were studied using the docking technique toward parathion, paraoxon and R-VX compounds. Furthermore, enzyme assay was performed on the native OPAA and Mut6 toward parathion.
RESULTS: Docking results showed a decreased catalytic activity of the mutant forms toward parathion and paraoxon. Furthermore, enzyme assay showed in accordance with docking results a decreased activity of Mut6 compared to the native form. The results of docking prediction for R-VX showed an increased catalytic activity of 4ZWP and 4ZWU. 4ZWU had the highest activity, while the activity of Mut6 was lower than the native form.
CONCLUSION: Amino acid positions of 212 and 342 seem to be important sites in the small pocket of OPAA affecting the enzyme catalytic activity. Therefore, substitution of these sites with appropriate amino acids depending on the substrate structure, can affect the enzyme catalytic efficiency (Tab. 2, Fig. 3, Ref. 30).

Keywords: organophosphorus acid anhydrolase (OPAA), enzyme activity, molecular docking
Published online: 17-Feb-2019
Year: 2019, Volume: 120, Issue: 2 Page From: 139, Page To: 143

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