Neue Veröffentlichung in "Chemistry Select"
We investigate in this paper the substrate competitive inhibition of the H3K36 specific NSD1, NSD2 and SETD2 protein lysine methyltransferases by the H3K36M oncohistone found in pediatric chondroblastomas at very high frequencies. Using steady-state kinetic analyses with a H3 peptide substrate and a corresponding K36M inhibitor peptide, we show a similar ratio of K I/K M with all three enzymes, suggesting a common mechanism of inhibition. The pH dependence of the inhibition is discussed.
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