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

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.
Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted Manuscript

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Publisher copy:
10.1039/c7cc08028j

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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
Al Temimi, AHK More by this author
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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
Pieters, BJGE More by this author
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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
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Grant:
Starting Grant to J. M. (ChemEpigen-715691)
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Grant:
Dorothy Hodgkin Fellowship (A. K.)
Wellcome Trust More from this funder
Cancer Research UK More from this funder
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Publisher:
Royal Society of Chemistry Publisher's website
Journal:
Chemical Communications Journal website
Volume:
53
Issue:
99
Pages:
13264-13267
Publication date:
2017-11-23
Acceptance date:
2017-11-23
DOI:
EISSN:
1364-548X
ISSN:
1359-7345
Pubs id:
pubs:809659
URN:
uri:2c17b09b-ec29-44cd-91a6-ea1241e7b638
UUID:
uuid:2c17b09b-ec29-44cd-91a6-ea1241e7b638
Local pid:
pubs:809659
Language:
English

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