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. 2021 Feb 10;4:181. doi: 10.1038/s42003-021-01684-3

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a–c Elution profiles of Pnp1, with its known substrate inosine (a,b) and putative ligand xanthine (c) (Supplementary Data S6 and S7). The intensity was calculated relative to the maximum intensity of the molecule measured across size exclusion chromatography fractions. The theoretical molecular weight (MW) was calculated using reference proteins. d Xanthine inhibits Pnp1 activity. Total activity of recombinant Pnp1 in the presence of 100 µM xanthine was measured using an liquid chromatography-mass spectrometry-based assay (Supplementary Data S18). Inhibition was calculated in relation to Pnp1 activity in the absence of xanthine. Data represent the means ± SD, n = 6 independent samples. Asterisks denote significant difference (non-paired, two-tailed t test P value < 0.05). e Scheme of purine degradation pathway with predicted regulatory interaction between Pnp1 and xanthine. Molecules discussed in this study are depicted in bold. Enzymes are additionally marked in blue.