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Chem Commun (Camb). 2017 Dec 12;53(99):13264-13267. doi: 10.1039/c7cc08028j.

Investigating d-lysine stereochemistry for epigenetic methylation, demethylation and recognition.

Author information

1
Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands. j.mecinovic@science.ru.nl.

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.

PMID:
29186216
PMCID:
PMC6345366
DOI:
10.1039/c7cc08028j
[Indexed for MEDLINE]
Free PMC Article

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