E1-Catalyzed Ubiquitin C-Terminal Amidation for the Facile Synthesis of Deubiquitinase Substrates

被引：12

作者：

Wang, Xiaoyan Aria ^{[1
]}

Kurra, Yadagiri ^{[1
]}

Huang, Ying ^{[1
]}

Lee, Yan-Jiun ^{[1
]}

Liu, Wenshe R. ^{[1
]}

机构：

[1] Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA

来源：

CHEMBIOCHEM | 2014年 / 15卷 / 01期

关键词：

deubiquitinases; diubiquitin; protein engineering; synthetic biology; ubiquitin functionalization; AZIDE-ALKYNE CYCLOADDITION; NATIVE CHEMICAL LIGATION; NONCANONICAL AMINO-ACIDS; POLYUBIQUITIN CHAINS; GENETIC INCORPORATION; CONJUGATING ENZYMES; PROTEIN-ACTIVATION; ESCHERICHIA-COLI; DIUBIQUITIN; CHEMISTRY;

D O I：

10.1002/cbic.201300608

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Will Ub my partner? The ubiquitin (Ub)-activating enzyme (E1) was used to catalyze an amidation reaction to functionalize the C terminus of Ub with unique functional groups, such as thiol, azide, alkyne, and alkene groups, with high efficiency and yield (>90 %). These groups were then applied for the facile synthesis of fluorophore-conjugated ubiquitin and specifically conjugated diubiquitin substrates for deubiquitinases. Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：37 / 41

页数：5

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