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Issue 57, 2018
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Human histone demethylase KDM6B can catalyse sequential oxidations

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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.

Graphical abstract: Human histone demethylase KDM6B can catalyse sequential oxidations

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Supplementary files

Article information


Submitted
21 May 2018
Accepted
06 Jun 2018
First published
02 Jul 2018

This article is Open Access

Chem. Commun., 2018,54, 7975-7978
Article type
Communication

Human histone demethylase KDM6B can catalyse sequential oxidations

R. J. Hopkinson, G. W. Langley, R. Belle, L. J. Walport, K. Dunne, M. Münzel, E. Salah, A. Kawamura, T. D. W. Claridge and C. J. Schofield, Chem. Commun., 2018, 54, 7975
DOI: 10.1039/C8CC04057E

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