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 ofβ-glucosidase J384W locus mutation

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。

In order to improve the conversion efficiency of ginsenoside Rb1 byβ-glucosidase,the key regions and sites involved in substrate recognition and binding in the conversion of ginsenoside Rb1 byβ-glucosidase were obtained by molecular docking,the J384 site was fixed-point mutated to W384,and the physicochemical properties,hydrophilic/hydrophobicity,transmembrane region,and secondary/tertiary structure of the wild enzyme and the mutant enzyme were compared by bioinformatics.The results showed that altering the internal structure of the enzyme resulted 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.