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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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Publication details

The article was received on 21 May 2018, accepted on 06 Jun 2018 and first published on 02 Jul 2018


Article type: Communication
DOI: 10.1039/C8CC04057E
Citation: Chem. Commun., 2018,54, 7975-7978
  • Open access: Creative Commons BY license
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    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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