Journal
CHEMICAL SCIENCE
Volume 8, Issue 12, Pages 7947-7953Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c7sc03631k
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Funding
- DFG [RE2796/2-1]
- Fonds der Chemischen Industrie (Dozentenpreis)
- Fonds der Chemischen Industrie
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Site-specific alkylation of complex biomolecules is critical for late-stage product diversification as well as post-synthetic labeling and manipulation of proteins and nucleic acids. Promiscuous methyltransferases in combination with analogs of S-adenosyl-L-methionine (AdoMet) can functionalize all major classes of biomolecules. We show that benzylic moieties are transferred by Ecm1 with higher catalytic efficiency than the natural AdoMet. A relative specificity of up to 80% is achieved when a norbornene moiety is placed in para-position, enabling for the first time enzymatic norbornene transfer to specific positions in DNA and RNA-even in cell lysate. Subsequent tetrazine ligation of the stable norbornene moiety is fast, efficient, biocompatible and - in combination with an appropriate tetrazine - fluorogenic.
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