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Human histone demethylase KDM6B can catalyse sequential oxidations.

ABSTRACT: Jumonji domain-containing demethylases (JmjC-KDMs) catalyse demethylation of N?-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 N?-alkylated lysine analogues, forming alcohol, aldehyde and carboxylic acid products.

SUBMITTER: Hopkinson RJ 

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

REPOSITORIES: biostudies-literature

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Human histone demethylase KDM6B can catalyse sequential oxidations.

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]

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