A designed phenylalanyl-tRNA synthetase variant allows efficient in vivo incorporation of aryl ketone functionality into proteins

被引：108

作者：

Datta, D ^{[1
]}

Wang, P ^{[1
]}

Carrico, IS ^{[1
]}

Mayo, SL ^{[1
]}

Tirrell, DA ^{[1
]}

机构：

[1] CALTECH, Howard Hughes Med Inst, Div Biol, Div Chem & Chem Engn, Pasadena, CA 91125 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2002年 / 124卷 / 20期

关键词：

D O I：

10.1021/ja0177096

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Incorporation of non-natural amino acids into proteins in vivo expands the scope of protein synthesis and design. p-Acetylphenylalanine was incorporated into recombinant dihydrofolate reductase (DHFR) in Escherichia coli via a computationally designed mutant form of the phenylalanyl-tRNA synthetase of the host. DHFR outfitted with ketone functionality can be chemoselectively ligated with hydrazide reagents under mild conditions. Copyright © 2002 American Chemical Society.

引用

页码：5652 / 5653

页数：2

共 22 条

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