Plant growth regulator daminozide is a selective inhibitor of human KDM2/7 histone demethylases. Rose, N., R., Woon, E., C., Y., Tumber, A., Walport, L., J., Chowdhury, R., Li, X., S., King, O., N., F., Lejeune, C., Ng, S., S., Krojer, T., Chan, M., C., Rydzik, A., M., Hopkinson, R., J., Che, K., H., Daniel, M., Strain-Damerell, C., Gileadi, C., Kochan, G., Leung, I., K., H., Dunford, J., Yeoh, K., K., Ratcliffe, P., J., Burgess-Brown, N., Von Delft, F., Muller, S., Marsden, B., Brennan, P., E., McDonough, M., A., Oppermann, U., Klose, R., J., Schofield, C., J., & Kawamura, A. Journal of Medicinal Chemistry, 55(14):6639-6643, American Chemical Society, 2012.
Plant growth regulator daminozide is a selective inhibitor of human KDM2/7 histone demethylases [pdf]Paper  Plant growth regulator daminozide is a selective inhibitor of human KDM2/7 histone demethylases [link]Website  doi  abstract   bibtex   
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.

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