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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প্রধান লেখক: Hopkinson, R, Langley, G, Belle, R, Walport, L, Dunne, K, Münzel, M, Salah, E, Kawamura, A, Claridge, T, Schofield, C
বিন্যাস: Journal article
ভাষা:English
প্রকাশিত: Royal Society of Chemistry 2018
বিবরন
সংক্ষিপ্ত: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.