The JmjC oxygenases catalyze the N-demethylationof Nε-methyl lysine residues inhistones and are current therapeutic targets. A set of human 2-oxoglutarateanalogues were screened usinga unified assay platform for JmjC demethylases and related oxygenases.Results led to the finding that daminozide (N-(dimethylamino)succinamicacid, 160 Da), a plant growth regulator, selectively inhibits theKDM2/7 JmjC subfamily. Kinetic and crystallographic studies revealthat daminozide chelates the active site metal via its hydrazide carbonyland dimethylamino groups. [ABSTRACT FROM AUTHOR]