N-terminal protein modification through a biomimetic transamination reaction

被引：306

作者：

Gilmore, Joshua M.

Scheck, Rebecca A.

Esser-Kahn, Aaron P.

Joshi, Neel S.

Francis, Matthew B. ^{[1
]}

机构：

[1] Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Lawrence Berkeley Lab, Div Sci Mat, Berkeley, CA 94720 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2006年 / 45卷 / 32期

关键词：

bioconjugation; bioorganic chemistry; oximes; protein modifications;

D O I：

10.1002/anie.200600368

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Chemical Equation Presented) One hit wonder: A biomimetic transamination reaction has been developed that employs pyridoxal-5-phosphate to modify the N terminus of proteins and peptides under mild conditions. This technique introduces a uniquely reactive carbonyl group in a single location (see scheme), thus allowing further elaboration through oxime or hydrazone formation. This modification strategy is also compatible with proteins containing a free cysteine residue. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：5307 / 5311

页数：5

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[11] Pyridoxal phosphate enzymes: Mechanistic, structural, and evolutionary considerations [J].