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首页> 外文会议>the European Peptide Symposium >SITE-SPECIFIC N-TERMINAL MODIFICATION OF PROTEINS USING A RATIONALLY DESIGNED TRYPSIN VARIANT
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SITE-SPECIFIC N-TERMINAL MODIFICATION OF PROTEINS USING A RATIONALLY DESIGNED TRYPSIN VARIANT

机译：使用合理设计的胰蛋白酶变体的特异性N末端改性蛋白质

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摘要

Site-specific covalent modification of proteins is a fundamental tool in medicine, biology and biochemistry. Despite the extraordinary interest in selectively modified proteins, there is however a lack of generally usable and flexible methods, which restore full biological function of the modified proteins in all cases. In the present contribution, we describe the suitability of the genetically optimized trypsin variant K60E/N143H/E151H/D189K for N-terminal modifications of proteins with synthetic functionalities under native state conditions. The trypsin variant possesses a strongly reduced proteolytic activity combined with an artificial metal binding site within the S'-subsite region of the biocatalyst. The latter was shown to mediate highly specific histidine complexations via zinc ions leading to an increased specificity of the enzyme towards histidine-containing peptide sequences.
机译：特异性的蛋白质的共价修饰是医学，生物学和生物化学的基本工具。尽管对选择性修饰的蛋白质具有非凡的兴趣，但是缺乏通常可用和灵活的方法，其在所有情况下恢复改性蛋白质的全生物功能。在本贡献中，我们描述了基因优化的胰蛋白酶变异K60E / N143 / E151H / D189K在天然状态条件下具有合成官能团的蛋白质的N-末端改性的适用性。胰蛋白酶变体具有强烈降低的蛋白水解活性，与生物催化剂的S'-底座区域内的人造金属结合位点联合。显示后者通过锌离子介导高特异性的组氨酸络合，导致酶对含组氨酸的肽序列的增加。

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