Nucleoside Phosphorylases make N7-xanthosine

Sarah Westarp, Felix Brandt, Lena Neumair, Christina Betz, Amin Dagane, Sebastian Kemper, Christoph R. Jacob, Peter Neubauer, Anke Kurreck () and Felix Kaspar ()
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Sarah Westarp: Technische Universität Berlin
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
Felix Kaspar: Technische Universität Braunschweig

Nature Communications, 2024, vol. 15, issue 1, 1-7

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-47287-4

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