A Highly Active DNA Polymerase with a Fluorous Core

被引：35
|
作者：
Holzberger, Bastian
Rubini, Marina
Moeller, Heiko M.
Marx, Andreas [1 ]
机构：
[1] Univ Konstanz, Dept Chem, D-78457 Constance, Germany
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2010年 / 49卷 / 07期
关键词：
DNA polymerases; NMR spectroscopy; non-natural amino acids; protein engineering; trifluoromethionine; FINGERS SUBDOMAIN; AMINO-ACIDS; PROTEINS; EVOLUTION; FIDELITY;
D O I：
10.1002/anie.200905978
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
(Chemical Equation Presented) A multifluorinated DNA polymerase with all 14 methionine residues (Met; red in the structure) globally replaced by the non-natural amino acid trifluoromethionine (TFM) exhibits enzymatic activity and selectivity similar to the wild type. The fluorinated enzyme serves as a 19F NMR probe, and despite its size of 63 kDa, individual 19F resonances allow the study of enzyme dynamics during DNA synthesis by NMR spectroscopy. © 2010 Wiley-VCH Verlag GmbH &. Co. KGaA.
引用
收藏
页码：1324 / 1327
页数：4
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