Importance of the main chain of lysine for histone lysine methyltransferase catalysis. Issue 23 (28th May 2019)

• Record Type: Journal Article
• Authors: Al Temimi, Abbas H. K.; Teeuwen, Ruben S.; Tran, Vu; Altunc, Arthur J.; Lenstra, Danny C.; Ren, Wansheng; Qian, Ping; Guo, Hong; Mecinović, Jasmin
• Is Part Of: Organic & biomolecular chemistry. Volume 17:Issue 23(2019)
• Page Start: 5693
• Page End: 5697
• Publication Date: 2019-05-28
• Subjects: Chemistry, Organic -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1039/c9ob01038f
• Languages: English
• ISSNs: 1477-0520

Abstract

Abstract : Enzymatic and computational studies on the simplest lysine analogues that possess a modified main chain demonstrate that the lysine's backbone contributes significantly to functional KMT binding and catalysis. Abstract : Histone lysine methyltransferases (KMTs) are biomedicinally important class of epigenetic enzymes that catalyse methylation of lysine residues in histones and other proteins. Enzymatic and computational studies on the simplest lysine analogues that possess a modified main chain demonstrate that the lysine's backbone contributes significantly to functional KMT binding and catalysis.