Lysine-specific histone demethylase

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Lysine-specific histone demethylase 1 (LSD1) is a flavin-dependent oxidase that catalyzes the removal of methyl groups from mono- and dimethylated lysine 4 of histone H3. LSD1 is a nuclear homolog of amine oxidase. It functions as histone demethylase and transcriptional corepressor. LSD1 demethylation occurs via a reaction which produces formaldehyde. LSD1 is a component of transcriptional corepressor complex which also contains CoREST (corepressor of element-1-silencing transcription factor)[1].

3D structures of lysine-specific histone demethylase 1

Updated on 13-April-2016

References

  1. ↑ Chen Y, Jie W, Yan W, Zhou K, Xiao Y. Lysine-specific histone demethylase 1 (LSD1): A potential molecular target for tumor therapy. Crit Rev Eukaryot Gene Expr. 2012;22(1):53-9. PMID:22339659

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Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky

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