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    Uncommon P450 Reactions Expand Natural Products Chemical Space
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    Update time: 2017-09-15
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    P450 enzymes (P450s), a super family of proteins widely distributed in animals, plants and microorganisms, represent the most versatile biocatalysts in nature. P450s play important roles in the biosynthesis of natural products due to their substrate diversity and catalytic reactions diversity.

    In last few years, Professor LI Shengying’s group from Qingdao Institute of Bioenergy and Bioprocess Technology (QIBEBT), Chinese Academy of Sciences (CAS), had been focusing on the biochemical function, catalytic mechanism and protein structure of P450s, and the research results had been published on a series of journals. Recently, Professor LI’s group was invited to write a review to summarize the uncommon P450 reactions. The review was published in issue 9 (2017) of Natural Product Reports as a cover article.

    Figure: The front cover of Natural Product Reports (issue 9, 2017). The central portrait of the Monkey King (a powerful and influential demon in Chinese fairy) represents the substrate of a biosynthetic P450 enzyme, while the surrounding postures illustrate the common and uncommon P450 reactions discussed in this review (clockwise from bottom left: common hydroxylation/epoxidation, uncommon twisting, coupling, cylization, and cleavage). (Image by Wang Yilin and DU Lei)

    The review starts with general introduction of natural product biosynthesis, the classical P450 catalytic cycle, and the common roles of P450 enzymes in natural product biosynthesis. After that, the authors focus on the “uncommon” P450 catalyzed reactions related to “new chemistry”, “skeleton construction”, and “structural re-shaping” via their own unique catalytic power or intriguing protein-protein interactions between P450s and other proteins. These uncommon P450 reactions lead to a higher level of chemical space expansion for natural products, through which a broader spectrum of bioactivities would be gained by the host organisms.

    This work and related findings were supported by National Natural Science Foundation of China under the Grant number NSFC 31422002, Shandong Provincial Natural Science Foundation Grant JQ201407, and the Key Frontier Project of Chinese Academy of Sciences, Grant No. QYZDB-SSW-SMC042.

    (Text by ZHANG Xingwang and LI Shengying)

    Contacts:

    Prof. LI Shengying, Ph.D., Principal Investigator
    Qingdao Institute of Bioenergy and Bioprocess Technology,
    Chinese Academy of Sciences (http://english.qibebt.cas.cn/)
    Qingdao, Shandong, 266101, China
    Tel: +86-0532-80662676     
    E-mail:
    lishengying@qibebt.ac.cn

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