Computational Biology and Chemistry, Volume (83), No (3), Year (2019-12) , Pages (107121-107129)

Title : ( Modeling, stability and the activity assessment of glutathione reductase from Streptococcus Thermophilus; Insights from the in-silico simulation study )

Authors: Nazanin Gholampour-Faroji , Razieh Farazmand , Jafar Hemmat , Aliakbar Haddad-Mashadrizeh ,

Citation: BibTeX | EndNote

Abstract

Antioxidant enzymes (AEs) are the main parts of the natural barriers of the body which deactivate the oxidant factors. To discover and understand their structures and function will deserve a deeper investigation. Accordingly, as an AE of probiotic strains, glutathione reductase of Streptococcus thermophilus (GRst), is characterized and modeled by in-silico methods. The investigation indicated the physicochemical properties of the enzyme and estimated its half-life of being more than 10 h. The analysis revealed that the enzyme is composed of 86 strands, 123 helices, and 241 random coils. Homology modeling of the GRst led to the construction of the enzyme’s 3D model that 62% of which is analogous to the glutathione reductase of Escherichia Coli (GRec), and which is qualitatively high in terms of Molpdf, ERRAT, Verify-3D and Ramachandran scores. Moreover, the structural stability of the model was substantiated within 10 and 20 ns at 400 and 300 K, respectively. Interestingly, these data showed that the enzyme is more stable than GRec at 400 K. In other words, the active cavity of the constructed model is characteristic of 38 amino acid residues within 4 Å around the NADPH and GSSG as corresponding ligands of GRst. Noteworthy, herein is the fact that, CYS40 and CYS45 are specified as the active site residues of this enzyme. Furthermore, the interaction assays of the model support its antioxidant capability which is even more than that of GRec. In general, these data provide a new model of AEs being inclusive of high antioxidant capacity and thermostability.

Keywords

Antioxidant; Glutathione reductase; Thermostability; Streptococcus thermophilus; Homology modeling; Simulation
برای دانلود از شناسه و رمز عبور پرتال پویا استفاده کنید.

@article{paperid:1075919,
author = {Nazanin Gholampour-Faroji and راضیه فرازمند and جعفر همت and Haddad-Mashadrizeh, Aliakbar},
title = {Modeling, stability and the activity assessment of glutathione reductase from Streptococcus Thermophilus; Insights from the in-silico simulation study},
journal = {Computational Biology and Chemistry},
year = {2019},
volume = {83},
number = {3},
month = {December},
issn = {1476-9271},
pages = {107121--107129},
numpages = {8},
keywords = {Antioxidant; Glutathione reductase; Thermostability; Streptococcus thermophilus; Homology modeling; Simulation},
}

[Download]

%0 Journal Article
%T Modeling, stability and the activity assessment of glutathione reductase from Streptococcus Thermophilus; Insights from the in-silico simulation study
%A Nazanin Gholampour-Faroji
%A راضیه فرازمند
%A جعفر همت
%A Haddad-Mashadrizeh, Aliakbar
%J Computational Biology and Chemistry
%@ 1476-9271
%D 2019

[Download]