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Updated: Aug 14, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
Published on: November 22, 2014
Inclusion of thiamine diphosphate and S-adenosylmethionine at their chemically active sites
Thomas Schrader1, Michael Fokkens, Frank-Gerrit Klärner
1Department of Chemistry, University of Marburg, Hans-Meerwein-Strasse, 35032 Marburg, Germany. schradet@staff.uni-marburg.de
Abstract:
[structure: see text] Molecular clips functionalized by phosphonate or phosphate groups bind thiamine diphosphate (TPP) and S-adenosylmethionine (SAM) with high affinity in water; both sulfur-based cofactors transfer organic groups to biomolecules. For TPP, various analytical tools point toward a simultaneous insertion of both heterocyclic rings into the electron-rich clip cavity. Similarly, SAM is also embedded with its sulfonium moiety inside the receptor cavity. This paves the way for enzyme models and direct interference with enzymatic processes.
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