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
收藏
页码：37 / 41
页数：5
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