Chin. J. Org. Chem. ›› 2019, Vol. 39 ›› Issue (4): 903-915.DOI: 10.6023/cjoc201810023 Previous Articles     Next Articles



郑禾a,b, 周玉珂a, 林贤福a, 吴起a   

  1. a 浙江大学化学系 杭州 310027;
    b 中国科学院上海生命科学研究院 上海 200031
  • 收稿日期:2018-10-19 修回日期:2018-12-13 发布日期:2018-12-28
  • 通讯作者: 吴起
  • 基金资助:


Recent Developments in Protein Engineering and Catalytic Oxidations of Baeyer-Villiger Monooxygenase

Zheng Hea,b, Zhou Yukea, Lin Xianfua, Wu Qia   

  1. a Department of Chemistry, Zhejiang University, Hangzhou 310027;
    b Shanghai Institute for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031
  • Received:2018-10-19 Revised:2018-12-13 Published:2018-12-28
  • Contact: 10.6023/cjoc201810023
  • Supported by:

    Project supported by the National Natural Science Foundation of China (Nos.21472169,21574113).

Baeyer-Villiger monooxygenase (BVMO) is an important biocatalyst for Baeyer-Villiger oxidation of various organic ketone/aldehyde compounds, and sulfur, selenium, or boron-containing heteroatoms compounds. As an indispensable tool, BVMO-catalyzed oxidation displays some advantages, such as high selectivity, mild reaction conditions and high efficiency, leading to wide applications into the synthesis of chiral compounds. In recent years, bioinformatics analysis and genome mining have been used to find more novel BVMOs from microorganisms. Besides natural substrates, these BVMOs can accept various organic compounds showing wide substrate scope. Meanwhile, protein engineering has been widely used to improve the catalytic performance of BVMOs, such as the expanded substrate scope, high thermostability and activity, high stereo-, regio-and chemo-selectivities. Based on the Baeyer-Villiger oxidation reaction with different substrate structures, the recent advancements in the research on the catalytic oxidation of wild type and protein-engineered BVMOs in the past five years are summarized.

Key words: Baeyer-Villiger monooxygenase, Baeyer-Villiger oxidation, biocatalysis, asymmetric synthesis, protein engineering