Selective, Small-Molecule Co-Factor Binding Site Inhibition of a Su(var)3–9, Enhancer of Zeste, Trithorax Domain Containing Lysine Methyltransferase
Abstract
The first chemical probe to primarily occupy the co-factor binding site of a Su(var)3−9, enhancer of a zeste, trithorax (SET) domain containing protein lysine methyltransferase (PKMT) is reported. Protein methyltransferases require S-adenosylmethionine (SAM) as a co-factor (methyl donor) for enzymatic activity. However, SAM itself represents a poor medicinal chemistry starting point for a selective, cell-active inhibitor given its extreme...
Paper Details
Title
Selective, Small-Molecule Co-Factor Binding Site Inhibition of a Su(var)3–9, Enhancer of Zeste, Trithorax Domain Containing Lysine Methyltransferase
Published Date
Aug 15, 2019
Volume
62
Issue
17
Pages
7669 - 7683
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