2024/04/29 by Sarah Westarp, Felix Brandt, Lena Neumair +7 · 1 voice
Biochemistry, Genetics and Molecular Biology · Medicine · #Biochemical and Molecular Research #HIV/AIDS drug development and treatment #Peptidase Inhibition and Analysis
paper · pdf · doi:10.1038/s41467-024-47287-4
openalex publication_date 2024/04/29 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
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.