Investigating d-lysine stereochemistry for epigenetic methylation, demethylation and recognition. Issue 99 (29th November 2017)

• Record Type: Journal Article
• Authors: Belle, Roman; Al Temimi, Abbas H. K.; Kumar, Kiran; Pieters, Bas J. G. E.; Tumber, Anthony; Dunford, James E.; Johansson, Catrine; Oppermann, Udo; Brown, Tom; Schofield, Christopher J.; Hopkinson, Richard J.; Paton, Robert S.; Kawamura, Akane; Mecinović, Jasmin
• Is Part Of: Chemical communications. Volume 53:Issue 99(2017)
• Page Start: 13264
• Page End: 13267
• Publication Date: 2017-11-29
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c7cc08028j
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Writers, erasers and readers show the selectivity for the acceptance of (methyl)d -lysine. Abstract : Histone lysine methylation is regulated by N ε -methyltransferases, demethylases, and N ε -methyl lysine binding proteins. Thermodynamic, catalytic and computational studies were carried out to investigate the interaction of three epigenetic protein classes with synthetic histone substrates containingl - andd -lysine residues. The results reveal that out of the three classes, N ε -methyl lysine binding proteins are superior in accepting lysines with thed -configuration.