Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/44402
Title: Investigating d-lysine stereochemistry for epigenetic methylation, demethylation and recognition.
Authors: Belle, R
Al Temimi, AHK
Kumar, K
Pieters, BJGE
Tumber, A
Dunford, JE
Johansson, C
Oppermann, U
Brown, T
Schofield, CJ
Hopkinson, RJ
Paton, RS
Kawamura, A
Mecinović, J
First Published: 23-Nov-2017
Publisher: Royal Society of Chemistry
Citation: Chemical Communications, 2017, 53 (99), pp. 13264-13267
Abstract: Histone lysine methylation is regulated by Nε-methyltransferases, demethylases, and Nε-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 containing l- and d-lysine residues. The results reveal that out of the three classes, Nε-methyl lysine binding proteins are superior in accepting lysines with the d-configuration.
DOI Link: 10.1039/c7cc08028j
eISSN: 1364-548X
Links: https://pubs.rsc.org/en/content/articlelanding/2017/CC/C7CC08028J#!divAbstract
http://hdl.handle.net/2381/44402
Version: Post-print
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © 2017, Royal Society of Chemistry. Deposited with reference to the publisher’s open access archiving policy. (http://www.rioxx.net/licenses/all-rights-reserved)
Description: Electronic supplementary information (ESI) available: Supporting figures, enzyme assays, peptide synthesis, protein production, synthesis, NMR data. See DOI: 10.1039/c7cc08028j
Appears in Collections:Published Articles, Dept. of Chemistry

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