Inclusion of thiamine diphosphate and S-adenosylmethionine at their chemically active sites
In: J Org Chem (J.Org.Chem.), Jg. 70 (2005) ; Nr. 25, S. 10227-10237
Zeitschriftenaufsatz / Fach: Chemie
[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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