Ontology highlight
ABSTRACT:
SUBMITTER: Hopkinson RJ
PROVIDER: S-EPMC3798130 | biostudies-literature | 2013 Jul
REPOSITORIES: biostudies-literature
Hopkinson Richard J RJ Walport Louise J LJ Münzel Martin M Rose Nathan R NR Smart Tristan J TJ Kawamura Akane A Claridge Timothy D W TD Schofield Christopher J CJ
Angewandte Chemie (International ed. in English) 20130620 30
Jobs on the side: Substrate selectivity studies indicate that members of the biomedically important JmjC demethylase family of histone N(ε)-methyllysine demethylases are capable of catalyzing the de-N-alkylation of groups other than N-methyl and can catalyze reactions that form stable hydroxylated products. The differences in binding preferences in this set of enzymes may be helpful in the design of selective inhibitors. ...[more]