trans-2-Phenylcyclopropylamine is a mechanism-based inactivator of the histone demethylase LSD1.

@article{Schmidt2007trans2PhenylcyclopropylamineIA,
  title={trans-2-Phenylcyclopropylamine is a mechanism-based inactivator of the histone demethylase LSD1.},
  author={Dawn M Z Schmidt and Dewey Granville McCafferty},
  journal={Biochemistry},
  year={2007},
  volume={46 14},
  pages={4408-16}
}
The catalytic domain of the flavin-dependent human histone demethylase lysine-specific demethylase 1 (LSD1) belongs to the family of amine oxidases including polyamine oxidase and monoamine oxidase (MAO). We previously assessed monoamine oxidase inhibitors (MAOIs) for their ability to inhibit the reaction catalyzed by LSD1 [Lee, M. G., et al. (2006) Chem. Biol. 13, 563-567], demonstrating that trans-2-phenylcyclopropylamine (2-PCPA, tranylcypromine, Parnate) was the most potent with respect to… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 88 extracted citations

Targeting FBPase is an emerging novel approach for cancer therapy

Cancer Cell International • 2018
View 11 Excerpts
Highly Influenced

Flavin-Dependent Enzymes in Cancer Prevention

International journal of molecular sciences • 2012
View 6 Excerpts
Highly Influenced

Kinetics, mechanism, and inhibition of monoamine oxidase

Journal of Neural Transmission • 2018
View 1 Excerpt

Similar Papers

Loading similar papers…