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. 2018 May 3;8:7002. doi: 10.1038/s41598-018-25476-8

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© The Author(s) 2018

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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Aminolysis of E2-25K thioester by lysine. For the general reaction (a), the kinetics of thioester aminolysis by 30 mM lysine are shown in (b), where apparent rates are derived from exponential fits of the data (lines). Second order rate constants (k_cat2) derived from the concentration dependence of aminolysis kinetics by neutral lysine are shown in (c), and plotted as a function of side chain accessible surface area for position 126 of wildtype E2-25K wildtype (Q), and Q126L, Q126I, Q126V, and Q126A mutants.