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A Highly Active DNA Polymerase with a Fluorous Core

2010; Wiley; Volume: 49; Issue: 7 Linguagem: Inglês

10.1002/anie.200905978

1521-3773

Bastian Holzberger, Marina Rubini, Heiko M. Möller, Andreas Marx,

RNA modifications and cancer

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. Detailed facts of importance to specialist readers are published as "Supporting Information". Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.