β-葡萄糖苷酶J384W位点突变的生物信息学及分子对接
Bioinformatics and molecular docking study of β-glucosidase J384W locus mutation
潘虹 1姚向钰 1洪一楠 1王晓军 1樊雨柔1
作者信息
- 1. 西安工程大学 环境与化学工程学院,陕西 西安 710048
- 折叠
摘要
为提高β-葡萄糖苷酶对人参皂苷Rb1的转化效率,通过分子对接得到β-葡萄糖苷酶转化人参皂苷Rb1中参与底物识别及结合的关键区域和位点.将J384位点进行定点突变为 W384,并通过生物信息学比较野生酶和突变酶的理化性质、亲/疏水性、跨膜区、二/三级结构.结果表明:改变酶的内部结构可使结合位点数增加,整体的稳定性更强;突变酶比野生酶与人参皂苷Rb1更容易自发进行结合,最低结合能为-9.02 kJ/mol.
Abstract
In order to improve the conversion efficiency of ginsenoside Rb1 by β-glucosidase,the key regions and sites involved in substrate recognition and binding in the conversion of ginsen-oside Rb1 by β-glucosidase were obtained by molecular docking,the J384 site was fixed-point mu-tated to W384,and the physicochemical properties,hydrophilic/hydrophobicity,transmembrane region,and secondary/tertiary structure of the wild enzyme and the mutant enzyme were com-pared by bioinformatics.The results showed that altering the internal structure of the enzyme re-sulted in an increase in the number of binding sites and greater overall stability;and the mutant enzyme was more likely to spontaneously bind to ginsenoside Rb1 than the wild enzyme,with a minimum binding energy of-9.02 KJ/mol.
关键词
β-葡萄糖苷酶/定点突变/生物信息学/分子对接Key words
β-glucosidase/sentinel mutation/bioinformatics/molecular docking引用本文复制引用
基金项目
陕西省自然科学基础研究计划(2021JQ-672)
陕西省教育厅专项科研项目(22JK0399)
出版年
2024
国家科技期刊平台
NSTL
万方数据