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Discovery of the cryptic function of terpene cyclases as aromatic prenyltransferases

Author

Listed:
  • Haibing He

    (University of Tokyo)

  • Guangkai Bian

    (Key Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education and School of Pharmaceutical Sciences, Wuhan University)

  • Corey J. Herbst-Gervasoni

    (Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania)

  • Takahiro Mori

    (University of Tokyo)

  • Stephen A. Shinsky

    (Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania)

  • Anwei Hou

    (Key Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education and School of Pharmaceutical Sciences, Wuhan University)

  • Xin Mu

    (Key Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education and School of Pharmaceutical Sciences, Wuhan University)

  • Minjian Huang

    (Key Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education and School of Pharmaceutical Sciences, Wuhan University)

  • Shu Cheng

    (Key Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education and School of Pharmaceutical Sciences, Wuhan University)

  • Zixin Deng

    (Key Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education and School of Pharmaceutical Sciences, Wuhan University)

  • David W. Christianson

    (Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania)

  • Ikuro Abe

    (University of Tokyo)

  • Tiangang Liu

    (Key Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education and School of Pharmaceutical Sciences, Wuhan University
    Hubei Engineering Laboratory for Synthetic Microbiology, Wuhan Institute of Biotechnology)

Abstract

Catalytic versatility is an inherent property of many enzymes. In nature, terpene cyclases comprise the foundation of molecular biodiversity as they generate diverse hydrocarbon scaffolds found in thousands of terpenoid natural products. Here, we report that the catalytic activity of the terpene cyclases AaTPS and FgGS can be switched from cyclase to aromatic prenyltransferase at basic pH to generate prenylindoles. The crystal structures of AaTPS and FgGS provide insights into the catalytic mechanism of this cryptic function. Moreover, aromatic prenyltransferase activity discovered in other terpene cyclases indicates that this cryptic function is broadly conserved among the greater family of terpene cyclases. We suggest that this cryptic function is chemoprotective for the cell by regulating isoprenoid diphosphate concentrations so that they are maintained below toxic thresholds.

Suggested Citation

  • Haibing He & Guangkai Bian & Corey J. Herbst-Gervasoni & Takahiro Mori & Stephen A. Shinsky & Anwei Hou & Xin Mu & Minjian Huang & Shu Cheng & Zixin Deng & David W. Christianson & Ikuro Abe & Tiangang, 2020. "Discovery of the cryptic function of terpene cyclases as aromatic prenyltransferases," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17642-2
    DOI: 10.1038/s41467-020-17642-2
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    Cited by:

    1. Zhong Li & Lilan Zhang & Kangwei Xu & Yuanyuan Jiang & Jieke Du & Xingwang Zhang & Ling-Hong Meng & Qile Wu & Lei Du & Xiaoju Li & Yuechan Hu & Zhenzhen Xie & Xukai Jiang & Ya-Jie Tang & Ruibo Wu & Re, 2023. "Molecular insights into the catalytic promiscuity of a bacterial diterpene synthase," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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