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Lookup NU author(s): Dr Joanna BonniciORCiD, Professor Akane KawamuraORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
Jumonji C histone lysine demethylases (JmjC-KDMs) are key chromatin regulators best known for catalysing histone lysine demethylation. There is growing evidence that JmjC-KDMs have a broader catalytic scope. This review summarises recent advances on JmjC-KDM activities beyond histone lysine demethylation, including arginine demethylation and arginine hydroxylation. We discuss how emerging insights into sequence-reactivity and inter-domain relationships, combinatorial post-translational modifications (PTMs), and cellular context shape substrate selectivity and enzymatic outcomes. These findings highlight substantial mechanistic flexibility within the JmjC-KDM family and may help prompt reconsideration of how their biochemistry is connected to physiological roles. We discuss implications for JmjC-KDM inhibitor development and outline outstanding questions, guiding future research concerning their roles in epigenetic regulation. Funding data Cancer Research UK Grant numbers C8717/A18245;C8717/A28285
Author(s): Bonnici J, Schofield CJ, Kawamura A
Publication type: Review
Publication status: Published
Journal: CHIMIA
Year: 2026
Volume: 80
Issue: 3
Print publication date: 25/03/2026
Online publication date: 25/03/2026
Acceptance date: 02/02/2026
ISSN (print): 0009-4293
ISSN (electronic): 2673-2424
URL: https://doi.org/10.2533/chimia.2026.138
DOI: 10.2533/chimia.2026.138
PubMed id: 41902679
