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Lysine-241 Has a Role in Coupling 2OG Turnover with Substrate Oxidation During KDM4-Catalysed Histone Demethylation

Lookup NU author(s): Professor Akane KawamuraORCiD

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Abstract

© 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.

Publication metadata

Author(s): Hancock RL, Abboud MI, Smart TJ, Flashman E, Kawamura A, Schofield CJ, Hopkinson RJ

Publication type: Article

Publication status: Published

Journal: ChemBioChem

Year: 2018

Volume: 19

Issue: 9

Pages: 917-921

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

URL: https://doi.org/10.1002/cbic.201800002

DOI: 10.1002/cbic.201800002

PubMed id: 29443450

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