Division of Bioorganic Chemistry, Faculty of Chemistry, Wroclaw University of Technology, 50-370 Wroclaw, Poland.
Biol Chem. 2012 Sep;393(9):843-51. doi: 10.1515/hsz-2012-0167.
Proteases recognize their endogenous substrates based largely on a sequence of proteinogenic amino acids that surrounds the cleavage site. Currently, several methods are available to determine protease substrate specificity based on approaches employing proteinogenic amino acids. The knowledge about the specificity of proteases can be significantly extended by application of structurally diverse families of non-proteinogenic amino acids. From a chemical point of view, this information may be used to design specific substrates, inhibitors, or activity-based probes, while biological functions of proteases, such as posttranslational modifications can also be investigated. In this review, we discuss current and prospective technologies for application of non-proteinogenic amino acids in protease substrate specificity profiling.
蛋白酶主要根据位于切割位点周围的蛋白质氨基酸序列来识别其内源性底物。目前，有几种方法可用于根据使用蛋白质氨基酸的方法来确定蛋白酶的底物特异性。通过应用结构多样的非蛋白质氨基酸家族，可大大扩展蛋白酶特异性的知识。从化学角度来看，该信息可用于设计特定的底物、抑制剂或基于活性的探针，同时还可以研究蛋白酶的生物学功能，如翻译后修饰。在这篇综述中，我们讨论了在蛋白酶底物特异性分析中应用非蛋白质氨基酸的当前和有前景的技术。
