Human histone demethylase KDM6B can catalyse sequential oxidations

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 t...

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Veröffentlicht in:	Chemical communications (Cambridge, England) England), 2018, Vol.54 (57), p.7975-7978
Hauptverfasser:	Hopkinson, Richard J, Langley, Gareth W, Belle, Roman, Walport, Louise J, Dunne, Kate, Münzel, Martin, Salah, Eidarus, Kawamura, Akane, Claridge, Timothy D W, Schofield, Christopher J
Format:	Artikel
Sprache:	eng
Schlagworte:	Alkylation Amino Acid Sequence Biocatalysis Gene expression Histones Humans Jumonji Domain-Containing Histone Demethylases - chemistry Jumonji Domain-Containing Histone Demethylases - metabolism Lysine Lysine - metabolism Oxidation-Reduction Peptides - chemical synthesis Peptides - metabolism Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Zusammenfassung:	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.
ISSN:	1359-7345 1364-548X
DOI:	10.1039/c8cc04057e