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Human histone demethylase KDM6B can catalyse sequential oxidations

Abstract:
Jumonji domain-containing demethylases (JmjC-KDMs) catalyse demethylation of Nε-methylated lysines on histones and play important roles in gene regulation. We report selectivity studies on KDM6B (JMJD3), a disease-relevant JmjC-KDM, using synthetic lysine analogues. The results unexpectedly reveal that KDM6B accepts multiple Nε-alkylated lysine analogues, forming alcohol, aldehyde and carboxylic acid products.
Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1039/c8cc04057e

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Institution:
University of Oxford
Oxford college:
St Edmund Hall
ORCID:
0000-0001-7610-8163
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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Subgroup:
Organic Chemistry
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Subgroup:
Organic Chemistry
Oxford college:
St Edmund Hall
ORCID:
0000-0002-3795-8365
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Funding agency for:
Hopkinson, RJ
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Funding agency for:
Walport, LJ
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Funding agency for:
Kawamura, A
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Publisher:
Royal Society of Chemistry Publisher's website
Journal:
Chemical Communications Journal website
Volume:
54
Issue:
57
Pages:
7975-7978
Publication date:
2018-07-02
Acceptance date:
2018-06-06
DOI:
EISSN:
1364-548X
ISSN:
1359-7345
Pubs id:
pubs:864214
URN:
uri:9cea0a11-383d-4a34-9b2f-9638240ee449
UUID:
uuid:9cea0a11-383d-4a34-9b2f-9638240ee449
Local pid:
pubs:864214
Language:
English

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