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. 2018 Feb 15;8:3102. doi: 10.1038/s41598-018-21476-w

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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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Inhibition of human USP2 deubiquitinating activity by 6MP or 6TG. (A) The activity of USP2 in the presence of various concentrations of 6MP was measured. (B) The activity of USP2 (left panel) or its C276S mutant (right panel) in the presence of various concentrations of 6TG was measured. In panel A and B, 1 μM Ub-AFC and 0.2 μM USP2 was used as the substrate and the enzyme, respectively. (C) Noncompetitive inhibition of USP2 by 6TG. Enzyme activity was measured under various concentrations of Ub-AFC (0.5–5 μM) and 6TG (0–100 μM), while protein concentration was held at 0.2 μM. The assays were performed in 20 mM phosphate (pH 7.6) at 30 °C and repeated to ensure reproducibility. The symbols and bars represent the mean and standard error, respectively. The solid lines represent the best global fit to the noncompetitive inhibition equation. R_sqr is 0.981 and the kinetic parameters from the best fit are shown in Table 1.