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. 2020 Dec 3;10:21043. doi: 10.1038/s41598-020-77992-1

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© The Author(s) 2020

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Inhibition by GKRP of wild type and mutant GK activity. (A) Surface accessibility of the Thr60 and Ala201 residues on the 3D structure of GK in super-open (left) and closed (right) conformation. (B) Enzyme kinetic constants of wild type and mutant GK are shown as mean ± SD for n independent measurements. (C) GKRP inhibition assays of wild type and mutant GK. Enzymatic activity was measured with 61 nM of the GST-GK fusion and the indicated concentration of Flag-GKRP.