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. 2023 Mar 27;14:1705. doi: 10.1038/s41467-023-37215-3

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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. 3 — a Structure of the EndoS (gray) complex with Fc (pink) in which the regions with alanine mutants are color coded based on the relative rates of removal of the N-glycans from Fc alanine mutants by EndoS and vice versa. The rates were measured via LC-MS kinetic analyses. Red indicates the largest increase in hydrolytic activity while blue indicates no hydrolytic activity. b Rates of removal of the first glycan of Fc and Fc alanine mutants by EndoS alanine mutants and EndoS respectively, normalized to EndoS vs. Fc. The kinetic rates were derived using three independent experiments. Data is presented as mean values + /- SD. All rates were statistically significant (multiple comparison test, one-way ANOVA, Tukey method, p < 0.0001 with 95% CI).