Molecular Basis for Stereospecific Hydrolysis of Ethyl Mandelate by Thermophilic Esterase  

作　　者：ZHANG Guo-yan TAO Jin ZHENG Liang-yu CAO Shu-gui 

机构地区：[1]Key Laboratory for Molecular Enzymology and Engineering, Ministry of Education [2]College of Chemistry, Jilin University, Changchun 130012, P. R. China

出　　处：《Chemical Research in Chinese Universities》2011年第5期841-844,共4页高等学校化学研究（英文版）

基　　金：Supported by the National Natural Science Foundation of China(Nos.30870539, 21072075);the 38th Postdoctoral Foundation of China(No.801050321413)

摘　　要：The stereospecific hydrolysis of mandelate can be effectively catalyzed by hyperthermophilic acylpeptide esterase APE 1547（Aeropyrum pernix esterase 1547）. APE 1547 used in this reaction showed a remarkable stereodi-scrimination in favour of R-mandelic acid（99% e.e.） with an enantiomeric ratio E〉200. The results of computer simulation are consistent with the experimental results. It can be inferred that the R-substrate adopted a binding mode productive of the reaction due to the formation of the hydrogen bond at the active site of APE 1547.The stereospecific hydrolysis of mandelate can be effectively catalyzed by hyperthermophilic acylpeptide esterase APE 1547（Aeropyrum pernix esterase 1547）. APE 1547 used in this reaction showed a remarkable stereodi-scrimination in favour of R-mandelic acid（99% e.e.） with an enantiomeric ratio E〉200. The results of computer simulation are consistent with the experimental results. It can be inferred that the R-substrate adopted a binding mode productive of the reaction due to the formation of the hydrogen bond at the active site of APE 1547.

关 键 词：Hyperthermophilic acylpeptide esterase BIOCATALYST Stereospecific hydrolysis Mandelic acid Computer simulation 

分 类 号：TQ245.4[化学工程—有机化工] TQ936.1