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.
MeSH terms
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Amino Acid Sequence
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Biocatalysis
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Humans
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Jumonji Domain-Containing Histone Demethylases / chemistry
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Jumonji Domain-Containing Histone Demethylases / metabolism*
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Lysine / metabolism
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Oxidation-Reduction
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Peptides / chemical synthesis
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Peptides / metabolism
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Substances
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Peptides
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Jumonji Domain-Containing Histone Demethylases
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KDM6B protein, human
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Lysine