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Enzymatic one-step ring contraction for quinolone biosynthesis

Author

Listed:
  • Shinji Kishimoto

    (University of Shizuoka)

  • Kodai Hara

    (University of Shizuoka)

  • Hiroshi Hashimoto

    (University of Shizuoka)

  • Yuichiro Hirayama

    (University of Shizuoka)

  • Pier Alexandre Champagne

    (University of California)

  • Kendall N. Houk

    (University of California
    University of California)

  • Yi Tang

    (University of California
    University of California)

  • Kenji Watanabe

    (University of Shizuoka)

Abstract

The 6,6-quinolone scaffolds on which viridicatin-type fungal alkaloids are built are frequently found in metabolites that display useful biological activities. Here we report in vitro and computational analyses leading to the discovery of a hemocyanin-like protein AsqI from the Aspergillus nidulans aspoquinolone biosynthetic pathway that forms viridicatins via a conversion of the cyclopenin-type 6,7-bicyclic system into the viridicatin-type 6,6-bicyclic core through elimination of carbon dioxide and methylamine through methyl isocyanate.

Suggested Citation

  • Shinji Kishimoto & Kodai Hara & Hiroshi Hashimoto & Yuichiro Hirayama & Pier Alexandre Champagne & Kendall N. Houk & Yi Tang & Kenji Watanabe, 2018. "Enzymatic one-step ring contraction for quinolone biosynthesis," Nature Communications, Nature, vol. 9(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05221-5
    DOI: 10.1038/s41467-018-05221-5
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    Cited by:

    1. Manuel Einsiedler & Tobias A. M. Gulder, 2023. "Discovery of extended product structural space of the fungal dioxygenase AsqJ," Nature Communications, Nature, vol. 14(1), pages 1-9, December.

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