期刊
BIOLOGICAL CHEMISTRY
卷 393, 期 9, 页码 843-851出版社
WALTER DE GRUYTER GMBH
DOI: 10.1515/hsz-2012-0167
关键词
combinatorial library; endopeptidase; exopeptidase
资金
- Foundation for Polish Science
- State for Scientific Research in Poland [N N401 042838]
- European Union Human Capital National Cohesion Strategy
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.
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