沈阳大学学报（自然科学版）2019，Vol.31Issue(1)：11-17,7.
Cel48F产物排出过程中酶-底物相互作用及关键残基的分子动力学模拟
Molecular Dynamics Simulation in Studying Enzyme-Substrate Interactions and Role of Key Residues in Product Excluding Process of Cel48F
摘要
Abstract
Using molecular dynamics simulation method, through the conformation comparison of the products in different binding positions and the statistical analysis of their interaction, the changes of the interaction between enzymes before and after the hydrolysis of Cel48 Fand the product discharge were studied, and some key residues and their effects were revealed.As the conclusion, the product moves a little via the interactions from Glu 44 and Trp 611 toward the exit of product cleft.The movement can lead the product far away from the residual substrate and some key catalytic residues to prevent the reverse reaction.When the product moves toward the exit sequentially, the Trp 411 will drag the inner sugar unit on the product to move toward it and form hydrogen bond with its neighbored Thr 410.However, the outer sugar unit has a small movement due to the restrictions of Asp 494.The two interactions rotate the product synergistically to favor the solvent water molecules to surround the product and bring it out of the enzyme.关键词
Cel48F/产物排出/分子动力学模拟/酶-底物间相互作用Key words
Cel48F/product excluding/molecular dynamics simulation/enzyme-substrate Interactions interaction分类
化学化工引用本文复制引用
刘天志,董莹,鄂镜雯,韩菲,李卓,张浩..Cel48F产物排出过程中酶-底物相互作用及关键残基的分子动力学模拟[J].沈阳大学学报（自然科学版）,2019,31(1):11-17,7.基金项目
国家自然科学基金资助项目(21443008) （21443008）
吉林省教育厅十三五规划项目(2016408). （2016408）
