Study on the relationship between structure and enantioselectivity of a hyperthermophilic esterase from archaeon Aeropyrum pernix K1，成果详细信息-中国科技论文在线

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期刊论文

Study on the relationship between structure and enantioselectivity of a hyperthermophilic esterase from archaeon Aeropyrum pernix K1

冯雁， Guirong Zhang a ， b ， Renjun Gaoa ， Liangyu Zheng a ， Aijun Zhang a ， Yuanhong Wang a ， c ， Qiuyan Wang a ， Yan Feng a ， Shugui Caoa ， ∗

Journal of Molecular Catalysis B: Enzymatic 38(2006)148-153，-0001，（）：

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摘要/描述

To enhance the enantioselectivity of a hyperthermophilic esterase from archaeon Aeropyrum pernix K1 (APE1547), a directed evolution approach is employed to generate mutant library from the native enzyme. A mutation (TBC26) is identified after one round of epPCR. The enantioselectivity of TBC26 is increased up to 2.6-fold compared to that of wild type enzyme. TBC26 contains five amino acid substitutions (R11G, L36P, V223A, I551L, A564T). The five mutation sites are spatially distant to the catalytic center. According to the published crystal structure ofWTand considering the changes of secondary and tertiary structure, here we try to explain the change of enantioselectivity of the TBC26. The results suggest that the change of enantioselectivity of enzyme has a close relationship to the configuration of the enzyme.

关键词: Directed evolution ， Enantioselectivity ， Screening ， 2-Octanol acetate ， Configuration ， Mutant

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