1 results match your criteria: "The Netherlands. Floris.Rutjes@ru.nl and University of Southern Denmark[Affiliation]"
Methylation of geometrically constrained lysine analogues by histone lysine methyltransferases.
Chem Commun (Camb)
March 2020
Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands. and University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark.
Article Synopsis
- The study investigates how human histone lysine methyltransferases catalyze the methylation of histones with lysine and its structurally modified analogues (E)-alkene, (Z)-alkene, and alkyne.
- Both G9a and GLP methyltransferases exhibit a higher efficiency for regular lysine, with a decreasing ability for the rigid analogues in the order of K > KE > KZ ∼ Kyne.
- In contrast, the monomethyltransferase SETD8 only supports the methylation of lysine and its (E)-alkene analogue, showing limited activity with the others.