Description
Lysine-
specific demethylase 1 (LSD1) belongs to the family of flavin adenine dinucleotide (FAD)-
dependent amine oxidases that include monoamine oxidases (MAOs) and polyamine oxidase (PAO).
1 LSD1 specifically demethylates mono- and dimethylated histone H3 lysine 4, resulting in transcriptional repression.
2 It also controls the tumor suppressor activity of p53 by demethylating a specific p53 lysine residue (LYS
370).
3 GSK-LSD1 is an irreversible, mechanism-based inhibitor of LSD1 (IC
50 = 16 nM) that is >1,000-fold selective over the closely related FAD-utilizing enzymes LSD2, MAO-A, and MAO-B.
4 GSK-LSD1 induces gene expression changes in various cancer cell lines, inhibiting their proliferation (EC
50s <5 nM).
4 See the
Structural Genomics Consortium (SGC) website for more information.
References
1. Shi, Y., Lan, F., Matson, C., et al.
Histone demethylation mediated by the nuclear amine oxidase homolog LSD1 Cell 119(7),941-953(2004).
2. Forneris, F., Binda, C., Vanoni, M.A., et al.
Human histone demethylase LSD1 reads the histone code J. Biol. Chem. 280(50),41360-41365(2005).
3. Huang, J., Sengupta, R., Espejo, A.B., et al.
p53 is regulated by the lysine demethylase LSD1 Nature 449,105-108(2007).
4.
Epigenetics probes collection ,(2014).
