Improving Sensitivity of Enzyme to Organophosphorous Compounds by Combining Experiment and Theory Methods  

作　　者：WANG Yue-xi WANG Ye HAN Wei-wei FENG Yan 

机构地区：[1]Key Laboratory for Molecular Enzymology and Engineering,Ministry of Education,Jilin University,Changchun 130012,P.R.China [2]State Key Laboratory of Microbial Metabolism,College of Life Science and Biotechnology,Shanghai Jiaotong University,Shanghai 200240,P.R.China

出　　处：《Chemical Research in Chinese Universities》2012年第4期707-711,共5页高等学校化学研究（英文版）

基　　金：Supported by the National Program on Key Basic Research Project of China(No.2012CB721003);the National Natural Science Foundation of China(No.31070638);the Natural Science Foundation of Jilin Province,China(No.201015109)

摘　　要：In this paper,we compared the sensitivities of AFEST（a thermophilic esterase from the archaea Archaeoglobus fulgidus） and acetylcholinesterase（AChE） towards five organophosphorus compounds（OPs） by means of molecular docking,and found that only the docking energy between AFEST and dichlorvos is lower than that between AChE and dichlorvos.Via the docking model of AFEST and dichlorvos,Arg43 was found to play an important role in the interaction between AFEST and dichlorvos by means of stabilizing the complex.Then mutant R43S was constructed,the IC 50（the concentration required to reduce virus-induced cytopathicity by 50% is estimated as 50% inhibitory concentration） of which to dichlorvos was lower than that of the wild type AFEST by a factor of 1.56,indicating the enhanced sensitivity of mutant R43S to dichlorvos.Combining of theory with experiment,we have obtained important structure-function information of AFEST,which will be helpful to the further studies of esterase.In this paper,we compared the sensitivities of AFEST（a thermophilic esterase from the archaea Archaeoglobus fulgidus） and acetylcholinesterase（AChE） towards five organophosphorus compounds（OPs） by means of molecular docking,and found that only the docking energy between AFEST and dichlorvos is lower than that between AChE and dichlorvos.Via the docking model of AFEST and dichlorvos,Arg43 was found to play an important role in the interaction between AFEST and dichlorvos by means of stabilizing the complex.Then mutant R43S was constructed,the IC 50（the concentration required to reduce virus-induced cytopathicity by 50% is estimated as 50% inhibitory concentration） of which to dichlorvos was lower than that of the wild type AFEST by a factor of 1.56,indicating the enhanced sensitivity of mutant R43S to dichlorvos.Combining of theory with experiment,we have obtained important structure-function information of AFEST,which will be helpful to the further studies of esterase.

关 键 词：Organophosphorus compound Thermophilic esterase DOCKING MUTAGENESIS INHIBITION 

分 类 号：S379.5[农业科学—农产品加工] Q556[农业科学—农艺学]