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Lookup NU author(s): Professor Akane Kawamura
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. The JmjC histone lysyl demethylases (KDMs) play important roles in modulating histone methylation states and have the potential to be regulated by oxygen availability. Lys241 of the KDM4 subfamily is proposed to be important in oxygen binding by KDM4A. We report evidence that, although Lys241 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 the uncoupling of substrate oxidation are of interest as JmjC-KDM inhibitors.
Author(s): Hancock RL, Abboud MI, Smart TJ, Flashman E, Kawamura A, Schofield CJ, Hopkinson RJ
Publication type: Article
Publication status: Published
Print publication date: 04/05/2018
Online publication date: 14/02/2018
Acceptance date: 03/01/2018
Date deposited: 14/10/2019
ISSN (print): 1439-4227
ISSN (electronic): 1439-7633
Publisher: Wiley - VCH Verlag GmbH & Co. KGaA
PubMed id: 29443450
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