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Histone N(ϵ)-methyl lysine demethylases are important in epigenetic regulation. KDM4E (histone lysine demethylase 4E) is a representative member of the large Fe(II)/2-oxoglutarate- dependent family of human histone demethylases. In the present study we report kinetic studies on the reaction of KDM4E with O2. Steady-state assays showed that KDM4E has a graded response to O2 over a physiologically relevant range of O2 concentrations. Pre-steady state assays implied that KDM4E reacts slowly with O2 and that there are variations in the reaction kinetics which are dependent on the methylation status of the substrate. The results demonstrate the potential for histone demethylase activity to be regulated by oxygen availability.

Original publication

DOI

10.1042/BJ20121155

Type

Journal article

Journal

Biochem J

Publication Date

15/01/2013

Volume

449

Pages

491 - 496

Keywords

Biocatalysis, Dose-Response Relationship, Drug, Histones, Humans, Iron, Jumonji Domain-Containing Histone Demethylases, Ketoglutaric Acids, Kinetics, Lysine, Molecular Structure, Oxygen, Peptides, Spectrophotometry, Substrate Specificity, Succinates