Ontology highlight
ABSTRACT:
SUBMITTER: Hopkinson RJ
PROVIDER: S-EPMC6044289 | biostudies-literature | 2018 Jul
REPOSITORIES: biostudies-literature
Hopkinson Richard J RJ Langley Gareth W GW Belle Roman R Walport Louise J LJ Dunne Kate K Münzel Martin M Salah Eidarus E Kawamura Akane A Claridge Timothy D W TDW Schofield Christopher J CJ
Chemical communications (Cambridge, England) 20180701 57
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. ...[more]