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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >The importance of the non-active site and non-periodical structure located histidine residue respect to the structure and function of exo-inulinase
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The importance of the non-active site and non-periodical structure located histidine residue respect to the structure and function of exo-inulinase

机译：非活性位点和非周期性结构的重要性定位组氨酸残基对外氨基硫脲的结构和功能

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摘要

Here, we have studied the role of a histidine residue with the lowest solvent accessibility among other histidine residues at the end of a short connecting structure ((189)AELH(192)) of the catalytic domain of the exo-inulinase through creation of H192A mutant. Site-directed mutagenesis method was applied to create the mutant enzyme. Molecular dynamics (MD) simulations, spectroscopic, calorimetric and kinetics analysis were used to study the structural and functional consequences of His192 substitution. Accordingly, the thermo-stabilities and catalytic performance were decreased upon H192A mutation. In silico and experimental approaches evidently confirm that His192 residue of exo-inulinase possesses structural and functional importance regardless of the lack of direct interaction with the substrate or involvement in the catalytic activity of exo-inulinase. (C) 2017 Elsevier B.V. All rights reserved.
机译：在这里，我们研究了组氨酸残基的作用，其在外氨基蛋白酶的催化结构域的短的连接结构（（189）AelH（192））通过产生H192a的催化结构域的末端的最低溶剂可偏转性。 突变体。 施用突变诱变方法以产生突变酶。 分子动力学（MD）模拟，光谱，量热量和动力学分析用于研究他的192年替代的结构和功能后果。 因此，H192A突变对热稳定性和催化性能降低。 在硅藻和实验方法明显证实，无论缺乏与基材的直接相互作用，还具有结构和功能性的exo-胆素酶的残留物，或者涉及外氨基蛋白酶的催化活性。 （c）2017年Elsevier B.V.保留所有权利。

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