Human histone demethylase KDM6B can catalyse sequential oxidations
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Published version
Author(s)
Type
Journal Article
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.
Date Issued
2018-07-21
Date Acceptance
2018-06-06
Citation
Chemical Communications, 2018, 54 (57), pp.7975-7978
ISSN
1359-7345
Publisher
Royal Society of Chemistry
Start Page
7975
End Page
7978
Journal / Book Title
Chemical Communications
Volume
54
Issue
57
Copyright Statement
© 2018 Royal Society of Chemistry. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (https://creativecommons.org/licenses/by/3.0/). Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.
Identifier
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000438548100023&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
Subjects
Science & Technology
Physical Sciences
Chemistry, Multidisciplinary
Chemistry
GENE-EXPRESSION
5-METHYLCYTOSINE
MACROPHAGES
PROTEINS
JMJD3
DNA
Publication Status
Published
Date Publish Online
2018-07-02