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.
Paper
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.
@article{
title = {Plant growth regulator daminozide is a selective inhibitor of human KDM2/7 histone demethylases},
type = {article},
year = {2012},
pages = {6639-6643},
volume = {55},
websites = {http://dx.doi.org/10.1021/jm300677j},
publisher = {American Chemical Society},
id = {d4e1d094-2211-397b-91c5-34fc48ac9855},
created = {2015-10-01T17:18:01.000Z},
file_attached = {true},
profile_id = {64f7fb50-d000-335d-a02d-06c5f340a97a},
last_modified = {2018-09-03T10:20:45.878Z},
read = {false},
starred = {false},
authored = {true},
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hidden = {false},
citation_key = {Rose2012},
source_type = {Journal Article},
private_publication = {false},
abstract = {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.},
bibtype = {article},
author = {Rose, Nathan R. and Woon, Esther C Y and Tumber, Anthony and Walport, Louise J. and Chowdhury, Rasheduzzaman and Li, Xuan Shirley and King, Oliver N F and Lejeune, Clarisse and Ng, Stanley S. and Krojer, Tobias and Chan, Mun Chiang and Rydzik, Anna M. and Hopkinson, Richard J. and Che, Ka Hing and Daniel, Michelle and Strain-Damerell, Claire and Gileadi, Carina and Kochan, Grazyna and Leung, Ivanhoe K H and Dunford, James and Yeoh, Kar Kheng and Ratcliffe, Peter J. and Burgess-Brown, Nicola and Von Delft, Frank and Muller, Susanne and Marsden, Brian and Brennan, Paul E. and McDonough, Michael A. and Oppermann, Udo and Klose, Robert J. and Schofield, Christopher J. and Kawamura, Akane},
doi = {10.1021/jm300677j},
journal = {Journal of Medicinal Chemistry},
number = {14}
}
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