常州大学学报（自然科学版）2026，Vol.38Issue(4)：73-80,8.DOI:10.3969/j.issn.2095-0411.2026.04.008
构效关系分析环氧水解酶对映体选择性机制
Structure-activity relationship analysis of enantioselectivity mechanism of epoxide hydrolases
摘要
Abstract
To investigate the effect mechanism of substrates substituent groups on the enantioselectivi-ty of epoxide hydrolases,the Three-Dimensional Quantitative Structure-Activity Relationship(3D-QSAR)model was constructed between epoxides and AuEH2 mutant enantioselectivity.Comparative Molecular Field Analysis(CoMFA)and Comparative Molecular Similarity Indices Analysis(CoM-SIA)models were constructed using the Partial Least Squares(PLS)method with the enantiomer ra-tios E as the dependent variables.The relevant statistical indicators of CoMFA and CoMSIA models met the standards.The CoMSIA model showed the hydrophobic and electrostatic field contribution factors were 45.5%and 30.0%.The E values of 17 training sets and 3 test sets predicted by CoMSIA model are highly consistent with the experimental values.Based on the above 3D-QSAR model,two high value-added epoxides 2-(2-fluorophenyl)oxirane(21a)and 2-[(3-methoxyphenoxy)methyl]ox-irane(22a)with high E values of 85 and 54,respectively,were predicted and verified by experiments.The constructed 3D-QSAR model was robust and effective for prediction.The hydrophobic and elec-trostatic fields of epoxides play the most important roles in determining the enantioselectivity of AuEH2 mutants.The 3D-QSAR model provides a theoretical basis for enantioselectivity recognition mechanism of epoxide hydrolases.关键词
环氧水解酶/三维定量构效关系/对映选择性预测/等势图/底物谱Key words
epoxide hydrolases/three-dimensional quantitative structure-activity relationship/enanti-oselectivity prediction/equipotential map/substrate spectrum分类
生物科学引用本文复制引用
胡蝶,鲁志毅,白凝,李佳琳,任庆功,何玉财..构效关系分析环氧水解酶对映体选择性机制[J].常州大学学报（自然科学版）,2026,38(4):73-80,8.基金项目
国家自然科学基金青年基金资助项目(2230081863) （2230081863）
常州市"龙城英才计划"第四批市领军型创新人才引进培育资助项目(CQ20230097) （CQ20230097）
常州市应用基础研究计划资助项目(CJ20252015). （CJ20252015）
