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. 2017 Nov 22;7:16027. doi: 10.1038/s41598-017-16266-9

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© The Author(s) 2017

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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Optimization of hydrophobic CORE packing by Val-to-Ile substitutions in AKNc. (a,b) V28I (a) and V118I/V173I (b) substitutions improve CORE packing with other hydrophobic residues in the crystal structure of the V28I/V118I/V173I mutant of AKNc (pink). The three mutated Ile residues are highlighted in green. The structure of WT AKNc (yellow) is aligned with that of the mutant. (c) Temperature dependence of activity of WT AKNc and the V28I/V118I/V173I mutant. The activities in the direction of ATP formation were measured at various temperatures. The Val-to-Ile mutations reduced the catalytic activity at low temperatures (5–35 °C). At each temperature, three independent measurements were made. Data are represented as mean ± standard error of mean.