| Autor: |
Al Temimi AHK; Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands., Teeuwen RS, Tran V, Altunc AJ, Lenstra DC, Ren W, Qian P, Guo H, Mecinović J |
| Jazyk: |
angličtina |
| Zdroj: |
Organic & biomolecular chemistry [Org Biomol Chem] 2019 Jun 12; Vol. 17 (23), pp. 5693-5697. |
| DOI: |
10.1039/c9ob01038f |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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