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Human histone demethylase KDM6B can catalyse sequential oxidations

Lookup NU author(s): Professor Akane KawamuraORCiD

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).

Abstract

© 2018 The Royal Society of Chemistry. 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 metadata

Author(s): Hopkinson RJ, Langley GW, Belle R, Walport LJ, Dunne K, Munzel M, Salah E, Kawamura A, Claridge TDW, Schofield CJ

Publication type: Article

Publication status: Published

Journal: Chemical Communications

Year: 2018

Volume: 54

Issue: 57

Pages: 7975-7978

Print publication date: 21/07/2018

Online publication date: 02/07/2018

Acceptance date: 06/09/2018

Date deposited: 14/10/2019

ISSN (print): 1359-7345

ISSN (electronic): 1364-548X

Publisher: Royal Society of Chemistry

URL: https://doi.org/10.1039/c8cc04057e

DOI: 10.1039/c8cc04057e

PubMed id: 29961803

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