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. 2023 Oct 20;14:6658. doi: 10.1038/s41467-023-42393-1

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© The Author(s) 2023

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. 5 — a The glycosylation conversion rates of the wild type (WT) and mutants, using 2 as sugar acceptor, and UDP-Api, UDP-Xyl, or UDP-Glc as sugar donor. b HPLC chromatograms of enzyme catalytic products. c Substrate promiscuity of GuApiGT mutants L369/H373Q and I136T/G370/H373Q. For substrate structures, see Fig. 3. d Deuterium uptake differences of L369/H373Q-WT and I136T/L369/H373Q-WT for all peptides in the HDX-MS experiments, calculated as the sum of all time points. The enzyme secondary structure and the PSPG box is shown on the top. e Deuterium uptake plots of peptides 135-156 and 363-372 at different time points. f Protein thermal shift assay measuring the changes in melting temperature (ΔT_m) of WT and mutants. Top, co-incubated with UDP-Xyl; bottom, co-incubated with UDP-Glc. Data are presented as mean values ± SD (n = 3 biologically independent samples) (5a, c and f). The source data underlying Fig. (5a, c–f) are provided in a Source Data file.