Human histone demethylase KDM6B can catalyse sequential oxidations.

ABSTRACT: 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.

SUBMITTER: Hopkinson RJ 

PROVIDER: S-EPMC6044289 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature