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Nucleoside Phosphorylases make N7-xanthosine

Author

Listed:
  • Sarah Westarp

    (Technische Universität Berlin
    BioNukleo GmbH)

  • Felix Brandt

    (Technische Universität Braunschweig)

  • Lena Neumair

    (Technische Universität Berlin)

  • Christina Betz

    (Technische Universität Berlin)

  • Amin Dagane

    (Technische Universität Berlin)

  • Sebastian Kemper

    (Technische Universität Berlin)

  • Christoph R. Jacob

    (Technische Universität Braunschweig)

  • Peter Neubauer

    (Technische Universität Berlin)

  • Anke Kurreck

    (Technische Universität Berlin
    BioNukleo GmbH)

  • Felix Kaspar

    (Technische Universität Braunschweig)

Abstract

Modern, highly evolved nucleoside-processing enzymes are known to exhibit perfect regioselectivity over the glycosylation of purine nucleobases at N9. We herein report an exception to this paradigm. Wild-type nucleoside phosphorylases also furnish N7-xanthosine, a “non-native” ribosylation regioisomer of xanthosine. This unusual nucleoside possesses several atypical physicochemical properties such as redshifted absorption spectra, a high equilibrium constant of phosphorolysis and low acidity. Ultimately, the biosynthesis of this previously unknown natural product illustrates how even highly evolved, essential enzymes from primary metabolism are imperfect catalysts.

Suggested Citation

  • Sarah Westarp & Felix Brandt & Lena Neumair & Christina Betz & Amin Dagane & Sebastian Kemper & Christoph R. Jacob & Peter Neubauer & Anke Kurreck & Felix Kaspar, 2024. "Nucleoside Phosphorylases make N7-xanthosine," Nature Communications, Nature, vol. 15(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-47287-4
    DOI: 10.1038/s41467-024-47287-4
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