磷酸三酯酶的同源模建及分子对接理论  

Homology Modeling and Docking of Phosphotriesterase-Like Lactonases from Thermaerobacter marianensis

作　　者：郑文琦[1] 赵丽[2] 宋亚伟[2] 韩葳葳[2] 

机构地区：[1]吉林建筑工程学院基础科学部,长春130118 [2]吉林大学分子酶学工程教育部重点实验室,长春130012

出　　处：《吉林大学学报（理学版）》2013年第3期514-517,共4页Journal of Jilin University:Science Edition

基　　金：国家自然科学基金(批准号:31070638);吉林省自然科学基金(批准号:201015109);吉林大学教育部平台项目(批准号:450060445311)

摘　　要：利用同源模建和分子动力学模拟方法模建了来源于Thermaerobacter marianensis的磷酸三酯酶样内酯酶(PLLs)三维结构.通过与不同底物的对接可知,Arg44与两种底物(磷酸三酯和内酯)均形成氢键,从而Arg44是两种底物与酶结合时重要的氨基酸残基.Three dimensional structures of phosphotriesterase-like lactonases（PLLs ） from Thermaerobacter marianensis were modeled by means of homology and molecular dynamics methods. On the basis of the modeling,the components and the structures of active sites TmPLLs were analyzed and compared.The docking was also performed.Arg44 was key residue for the combination of two substrates（γ-nonanoic lactone and ethyl paraoxon） with the enzyme.

关 键 词：磷酸三酯酶 同源模建 分子对接 

分 类 号：O623[理学—有机化学]