磷酸三酯酶的同源模建及分子对接理论

J4 ›› 2013, Vol. 51 ›› Issue (03): 514-517.

磷酸三酯酶的同源模建及分子对接理论

郑文琦¹, 赵丽², 宋亚伟², 韩葳葳²

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

收稿日期:2012-07-29 出版日期:2013-05-26 发布日期:2013-05-17
通讯作者: 韩葳葳 E-mail:weiweihan@jlu.edu.cn

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

ZHENG Wen qi¹, ZHAO Li², SONG Ya wei², HAN Wei wei²

1. Department of Basic Science, Jilin Architectural and Civil Engineering Institute, Changchun 130118, China;2. Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education,Jilin University, Changchun 130012, China

Received:2012-07-29 Online:2013-05-26 Published:2013-05-17
Contact: HAN Wei wei E-mail:weiweihan@jlu.edu.cn

摘要/Abstract

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.

关键词: 磷酸三酯酶；同源模建；分子对接

Abstract:

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.

Key words: phosphotriesterase-like lactonases, homology modeling, molecular docking

中图分类号:

O623

郑文琦, 赵丽, 宋亚伟, 韩葳葳. 磷酸三酯酶的同源模建及分子对接理论[J]. J4, 2013, 51(03): 514-517.

ZHENG Wen-Qi, DIAO Li, SONG E-Wei, HAN Wei-Wei. Homology Modeling and Docking of Phosphotriesterase-LikeLactonases from Thermaerobacter marianensis[J]. J4, 2013, 51(03): 514-517.