Recent advances and concepts in substrate specificity determination of proteases using tailored libraries of fluorogenic substrates with unnatural amino acids

Rut Wioletta; Kasperkiewicz Paulina; Byzia Anna; Poreba Marcin; Groborz Katarzyna; Drag Marcin

首页> 外文期刊>Biological chemistry >Recent advances and concepts in substrate specificity determination of proteases using tailored libraries of fluorogenic substrates with unnatural amino acids

【24h】

Recent advances and concepts in substrate specificity determination of proteases using tailored libraries of fluorogenic substrates with unnatural amino acids

机译：使用具有非天然氨基酸的荧光底物的量身定制的库，在蛋白酶的底物特异性测定中的最新进展和概念

获取原文

获取原文并翻译 | 示例

掌桥外文数据库（机构版） >>

开具论文收录证明 >>

文献代查 >>

页面导航

摘要
著录项
相似文献
相关主题

摘要

Substrate specificity of proteases can be determined using several methods among which the most frequently used are positional scanning library, proteomics and phage display. Classic approaches can deliver information about preferences for natural amino acids in binding pockets of virtually all proteases. However, recent studies demonstrate the ability to obtain much more information by application of unnatural amino acids to positional scanning library approaches. This knowledge can be used for the design of more active and specific substrates, inhibitors and activity based probes. In this minireview we describe recent strategies and concepts for the design and application of fluorogenic substrates library tailored for exopeptidases and endopeptidases.

机译：蛋白酶的底物特异性可以使用几种方法确定，其中最常用的是位置扫描文库，蛋白质组学和噬菌体展示。经典方法可以在几乎所有蛋白酶的结合口袋中提供有关天然氨基酸偏好的信息。但是，最近的研究表明，通过将非天然氨基酸应用于位置扫描库方法，可以获得更多信息的能力。该知识可用于设计更具活性和特异性的底物，抑制剂和基于活性的探针。在本小型审查中，我们描述了针对外肽酶和内肽酶量身定制的荧光底物文库的设计和应用的最新策略和概念。

著录项

来源
《Biological chemistry》 |2015年第4期|共9页
作者
Rut Wioletta; Kasperkiewicz Paulina; Byzia Anna; Poreba Marcin; Groborz Katarzyna; Drag Marcin;
展开▼
作者单位

展开▼
收录信息
原文格式 PDF
正文语种 eng
中图分类生物化学;
关键词
combinatorial library; endopeptidase; exopeptidase; fluorogenic substrates; unnatural amino acids;

机译：组合文库;内肽酶;外肽酶;荧光底物;非天然氨基酸;

相似文献

外文文献
中文文献
专利

1. Recent advances and concepts in substrate specificity determination of proteases using tailored libraries of fluorogenic substrates with unnatural amino acids [J] . Rut Wioletta, Kasperkiewicz Paulina, Byzia Anna, Biological chemistry . 2015,第4期

机译：使用具有非天然氨基酸的荧光底物的量身定制的库，在蛋白酶的底物特异性测定中的最新进展和概念
2. Fluorescein-based amino acids for solid phase synthesis of fluorogenic protease substrates [J] . Olga N. Burchak, Laurent Mugherli, Francois Chatelain, Bioorganic and medicinal chemistry . 2006,第8期

机译：基于荧光素的氨基酸，用于固相合成荧光蛋白酶底物
3. Fluorescein-based amino acids for solid phase synthesis of fluorogenic protease substrates [J] . Olga N. Burchak, Laurent Mugherli, Francois Chatelain, Bioorganic and Medicinal Chemistry . 2006,第8期

机译：基于荧光素的氨基酸，用于固相合成荧光蛋白酶底物
4. Construction of the mutant D-amino acid aminotransferases with broad substrate specificity and their application to the D-amino acid production [C] . Tohru Yoshimura, Aldo Gutierrrez, Nobuyoshi Esaki The Fifth China-Japn joint symposium on enzyme engineering . 1998

机译：具有广泛底物特异性的突变D-氨基酸氨基转移酶的构建及其在D-氨基酸生产中的应用
5. Bead based peptidyl libraries for the selective recognition of glycoproteins, differentiation of carcinogenic cell types, and determination of enzyme substrate specificity. [D] . Bicker, Kevin Lee. 2010

机译：基于珠的肽基文库，用于糖蛋白的选择性识别，致癌细胞类型的分化以及酶底物特异性的确定。
6. The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases. [O] . J. J. Onuffer, B. T. Ton, I. Klement, 1995

机译：使用天然和非天然氨基酸底物来定义大肠杆菌天冬氨酸和酪氨酸氨基转移酶的底物特异性差异。
7. The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases. [O] . Onuffer, J. J., Ton, B. T., Klement, I., 1995

机译：使用天然和非天然氨基酸底物来定义大肠杆菌天冬氨酸和酪氨酸氨基转移酶的底物特异性差异。

Recent advances and concepts in substrate specificity determination of proteases using tailored libraries of fluorogenic substrates with unnatural amino acids

摘要

著录项

相似文献

相关主题

期刊订阅