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Chemical Research in Chinese Universities ›› 2011, Vol. 27 ›› Issue (5): 841-844.

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Molecular Basis for Stereospecific Hydrolysis of Ethyl Mandelate by Thermophilic Esterase

ZHANG Guo-yan1,2, TAO Jin1, ZHENG Liang-yu1 and CAO Shu-gui1*   

  1. 1. Key Laboratory for Molecular Enzymology and Engineering, Ministry of Education,
    2. College of Chemistry, Jilin University, Changchun 130012, P. R. China
  • Received:2010-11-26 Revised:2011-04-11 Online:2011-09-25 Published:2011-09-06
  • Contact: CAO Shu-gui E-mail:sgcao@jlu.edu.cn
  • Supported by:

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

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Abstract: 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 stereodiscrimination 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.

Key words: Hyperthermophilic acylpeptide esterase, Biocatalyst, Stereospecific hydrolysis, Mandelic acid, Computer simulation