Journal article
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
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(Version of record, pdf, 2.2MB)
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- Publisher copy:
- 10.1039/c8cc04057e
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Authors
Funding
+ Systems Approaches to Biomedical Science
Industrial Doctoral Centre
More from this funder
Funding agency for:
Langley, G
Grant:
EP/G037280/1
+ St. Edmund Hall, Oxford
More from this funder
Funding agency for:
Hopkinson, R
Grant:
William R. Miller
Junior Research Fellowship
+ European Union
More from this funder
Funding agency for:
Walport, L
Grant:
Marie Skłodowska-Curie grant agreement no.
657292
+ Royal Society
More from this funder
Funding agency for:
Kawamura, A
Grant:
Dorothy
Hodgkin Fellowship
Expand funders...
Bibliographic Details
- 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
- Pmid:
-
29961803
- Source identifiers:
-
864214
Item Description
- Language:
- English
- Pubs id:
-
pubs:864214
- UUID:
-
uuid:9cea0a11-383d-4a34-9b2f-9638240ee449
- Local pid:
- pubs:864214
- Deposit date:
- 2018-09-03
Terms of use
- Copyright holder:
- Hopkinson et al
- Copyright date:
- 2018
- Notes:
- This article is licensed under a Creative Commons Attribution 3.0 Unported Licence.
- Licence:
- CC Attribution (CC BY)
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