Molecular Dynamics Simulation of E412 Catalytic Residue Mutation of GOx-IPBCC

Authors : Asrul FANANİ, Popi Asri KURNİATİN, Setyanto Tri WAHYUDİ, Waras NURCHOLİS, Laksmi AMBARSARİ

Pages : 1091-1106

Doi:10.18596/jotcsa.1088587

View : 10 | Download : 5

Publication Date : 2022-11-30

Article Type : Research Paper

Abstract :The enzyme glucose oxidase from Aspergillus niger has a homodimeric structure, consisting of two identical subunits with a molecular weight of 150,000 Daltons. In this study, we used the structure of the enzyme glucose oxidase from Aspergillus niger IPBCC.08.610 insert ignore into journalissuearticles values(GOx-IPBCC);, this enzyme had a total activity of 92.87 U insert ignore into journalissuearticles values(μmol/min); and a Michaelis-Menten constant insert ignore into journalissuearticles values(Km); of 2.9 mM insert ignore into journalissuearticles values(millimolar);. This study was conducted to predict the molecular dynamics of E412 insert ignore into journalissuearticles values(Glu412); residue catalytic mutation belonging to the GOx-IPBCC enzyme was determine the effect of changes in the catalytic residue on substrate binding insert ignore into journalissuearticles values(β-D-glucose);. The results of molecular docking of 19 mutant structures, six E412 mutant homologous structures were selected insert ignore into journalissuearticles values(E412C, E412K, E412Q, E412T, E412, E412V, and E412W);, which were evaluated using molecular dynamics simulation for 50 ns. The results showed a decrease in ∆G values in two mutant structures is E412C and E412T, and there is one mutant structure that increased ∆G values, namely E412W, these three mutant structures showed the best stability, bond interaction, and salt bridge profile according to molecular dynamics simulation.
Keywords : GOx IPBCC enzyme, molecular docking, molecular dynamics simulation