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Molecular Basis for Stereospecific Hydrolysis of Ethyl Mandelate by Thermophilic Esterase

Molecular Basis for Stereospecific Hydrolysis of Ethyl Mandelate by Thermophilic Esterase
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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.
出处 《Chemical Research in Chinese Universities》 SCIE CAS CSCD 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)
关键词 Hyperthermophilic acylpeptide esterase BIOCATALYST Stereospecific hydrolysis Mandelic acid Computer simulation Hyperthermophilic acylpeptide esterase Biocatalyst Stereospecific hydrolysis Mandelic acid Computer simulation
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