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The JmjC oxygenases catalyze the N-demethylation of N(ε)-methyl lysine residues in histones and are current therapeutic targets. A set of human 2-oxoglutarate analogues were screened using a unified assay platform for JmjC demethylases and related oxygenases. Results led to the finding that daminozide (N-(dimethylamino)succinamic acid, 160 Da), a plant growth regulator, selectively inhibits the KDM2/7 JmjC subfamily. Kinetic and crystallographic studies reveal that daminozide chelates the active site metal via its hydrazide carbonyl and dimethylamino groups.

Original publication

DOI

10.1021/jm300677j

Type

Journal article

Journal

J Med Chem

Publication Date

26/07/2012

Volume

55

Pages

6639 - 6643

Keywords

Enzyme Inhibitors, Humans, Inhibitory Concentration 50, Jumonji Domain-Containing Histone Demethylases, Models, Molecular, Plant Growth Regulators, Protein Conformation, Substrate Specificity, Succinates