Inclusion of thiamine diphosphate and S-adenosylmethionine at their chemically active sites.
[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.
Schrader
Thomas
T
Department of Chemistry, University of Marburg, Hans-Meerwein-Strasse, 35032 Marburg, Germany. schradet@staff.uni-marburg.de
Fokkens
Michael
M
Klärner
Frank-Gerrit
FG
Polkowska
Jolanta
J
Bastkowski
Frank
F
D001665:Binding Sites; D046911:Macromolecular Substances / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D012436:S-Adenosylmethionine / Q000737:chemistry*; D012995:Solubility; D013835:Thiamine Pyrophosphate / Q000737:chemistry*; D014867:Water
D046911:Macromolecular Substances; D014867:Water; D012436:S-Adenosylmethionine; D013835:Thiamine Pyrophosphate