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Elucidation of divergent desaturation pathways in the formation of vinyl isonitrile and isocyanoacrylate

Author

Listed:
  • Wantae Kim

    (University of Texas)

  • Tzu-Yu Chen

    (NC State University)

  • Lide Cha

    (NC State University)

  • Grace Zhou

    (University of Texas)

  • Kristi Xing

    (University of Texas)

  • Nicholas Koenig Canty

    (NC State University)

  • Yan Zhang

    (University of Texas
    University of Texas)

  • Wei-chen Chang

    (NC State University)

Abstract

Two different types of desaturations are employed by iron- and 2-oxoglutarate-dependent (Fe/2OG) enzymes to construct vinyl isonitrile and isocyanoacrylate moieties found in isonitrile-containing natural products. A substrate-bound protein structure reveals a plausible strategy to affect desaturation and hints at substrate promiscuity of these enzymes. Analogs are synthesized and used as mechanistic probes to validate structural observations. Instead of proceeding through hydroxylated intermediate as previously proposed, a plausible carbocation species is utilized to trigger C=C bond installation. These Fe/2OG enzymes can also accommodate analogs with opposite chirality and different functional groups including isonitrile-(D)-tyrosine, N-formyl tyrosine, and phloretic acid, while maintaining the reaction selectivity.

Suggested Citation

  • Wantae Kim & Tzu-Yu Chen & Lide Cha & Grace Zhou & Kristi Xing & Nicholas Koenig Canty & Yan Zhang & Wei-chen Chang, 2022. "Elucidation of divergent desaturation pathways in the formation of vinyl isonitrile and isocyanoacrylate," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32870-4
    DOI: 10.1038/s41467-022-32870-4
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    References listed on IDEAS

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    1. Sophie L. Mader & Alois Bräuer & Michael Groll & Ville R. I. Kaila, 2018. "Catalytic mechanism and molecular engineering of quinolone biosynthesis in dioxygenase AsqJ," Nature Communications, Nature, vol. 9(1), pages 1-8, December.
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