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Lysine-241 has a role in coupling 2OG turnover with substrate oxidation during KDM4-catalysed histone demethylation

Abstract:

The JmjC histone demethylases (KDMs) play important roles in modulating histone methylation states and have the potential to be regulated by oxygen availability. Lys-241 of the KDM4 subfamily is proposed to be important in oxygen binding by KDM4A. We report evidence that, although K241 is unlikely to be directly involved in oxygen binding, it has an important role in coupling 2-oxoglutarate cosubstrate oxidation with lysine demethylase activity. The results suggest that compounds promoting un...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1002/cbic.201800002

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
ORCID:
0000-0003-2141-5988
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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
Role:
Author
More from this funder
Name:
British Heart Foundation Centre for Research Excellence
Funding agency for:
Flashman, E
Kawamura, A
Grant:
RE/13/130181
RE/13/130181
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Name:
Kellogg College, Oxford
Funding agency for:
Abboud, M
Grant:
Junior Research Fellowship
More from this funder
Name:
Engineering and Physical Sciences Research Council
Grant:
EP/L003376/1
More from this funder
Name:
Biotechnology and Biological Sciences Research Council
Grant:
BB/E527620/1
More from this funder
Name:
Wellcome Trust
Grant:
091857/7/10/7
Publisher:
Wiley‐VCH Verlag
Journal:
Chembiochem More from this journal
Volume:
19
Issue:
9
Pages:
917-921
Publication date:
2018-04-06
Acceptance date:
2018-02-13
DOI:
EISSN:
1439-7633
ISSN:
1439-4227
Pmid:
29443450
Language:
English
Keywords:
Pubs id:
pubs:826200
UUID:
uuid:e72718d3-2267-4420-91e0-977e57bc12c6
Local pid:
pubs:826200
Deposit date:
2018-02-26

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