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Lysine-241 has a role in coupling 2OG turnover with substrate oxidation during KDM4-catalysed histone demethylation

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posted on 2018-03-27, 08:33 authored by Richard Hopkinson, R Hancock, M Abboud, T Smart, E Flashman, A Kawamura, C Schofield
The JmjC histone demethylases (KDMs) play important roles in modulating histone methylation states and have the potential to be regulated by oxygen availability. Lys‐241 of the KDM4 subfamily is proposed to be important in oxygen binding by KDM4A. We report evidence that, although K241 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 uncoupling of substrate oxidation are of interest as JmjC‐KDM inhibitors.

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Citation

ChemBioChem, 2018

Author affiliation

/Organisation/COLLEGE OF SCIENCE AND ENGINEERING/Department of Chemistry

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  • AM (Accepted Manuscript)

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ChemBioChem

Publisher

Wiley

issn

1439-4227

eissn

1439-7633

Acceptance date

2018-02-14

Copyright date

2018

Available date

2019-02-14

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https://onlinelibrary.wiley.com/doi/abs/10.1002/cbic.201800002

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The file associated with this record is under embargo until 12 months after publication, in accordance with the publisher's self-archiving policy. The full text may be available through the publisher links provided above.

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en

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