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Issue 99, 2017
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Investigating D-lysine stereochemistry for epigenetic methylation, demethylation and recognition

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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.

Graphical abstract: Investigating d-lysine stereochemistry for epigenetic methylation, demethylation and recognition

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Publication details

The article was received on 17 Oct 2017, accepted on 23 Nov 2017 and first published on 23 Nov 2017


Article type: Communication
DOI: 10.1039/C7CC08028J
Citation: Chem. Commun., 2017,53, 13264-13267
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    Investigating D-lysine stereochemistry for epigenetic methylation, demethylation and recognition

    R. Belle, A. H. K. Al Temimi, K. Kumar, B. J. G. E. Pieters, A. Tumber, J. E. Dunford, C. Johansson, U. Oppermann, T. Brown, C. J. Schofield, R. J. Hopkinson, R. S. Paton, A. Kawamura and J. Mecinović, Chem. Commun., 2017, 53, 13264
    DOI: 10.1039/C7CC08028J

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