Inhibitors of both the <i>N</i>-methyl lysyl- and arginyl-demethylase activities of the JmjC oxygenases.

ABSTRACT: The Jumonji C (JmjC) family of 2-oxoglutarate (2OG)-dependent oxygenases have established roles in the regulation of transcription via the catalysis of demethylation of Nε-methylated lysine residues in histone tails, especially the N-terminal tail of histone H3. Most human JmjC N^ɛ -methyl lysine demethylases (KDMs) are complex enzymes, with 'reader domains' in addition to their catalytic domains. Recent biochemical evidence has shown that some, but not all, JmjC KDMs also have Nω-methyl arginyl demethylase (RDM) activity. JmjC KDM activity has been linked to multiple cancers and some JmjC proteins are therapeutic targets. It is, therefore, important to test not only whether compounds in development inhibit the KDM activity of targ

SUBMITTER: Bonnici J 

PROVIDER: S-EPMC5915715 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature