LSD1 and the chemistry of histone demethylation

Curr Opin Chem Biol. 2007 Oct;11(5):561-8. doi: 10.1016/j.cbpa.2007.07.014. Epub 2007 Sep 11.


The recent discovery that histone demethylation can be catalyzed by the flavin-dependent amine oxidase LSD1 has ushered in a new chapter in the chromatin-remodeling community. Herein, we discuss the rapid progress of the histone demethylase field including the recent identification of the non-heme iron-dependent histone demethylases (JmjC family), the basis for LSD1 substrate site specificity and the newly emerging potential for inhibition of these enzymes in structural and functional analysis.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Catalysis
  • Chromatin Assembly and Disassembly*
  • Enzyme Inhibitors
  • F-Box Proteins
  • Histone Demethylases
  • Histones / metabolism*
  • Humans
  • Jumonji Domain-Containing Histone Demethylases
  • Methylation
  • Oxidoreductases, N-Demethylating / metabolism*
  • Protein Processing, Post-Translational*
  • Substrate Specificity


  • Enzyme Inhibitors
  • F-Box Proteins
  • Histones
  • Histone Demethylases
  • Jumonji Domain-Containing Histone Demethylases
  • KDM2A protein, human
  • KDM1A protein, human
  • Oxidoreductases, N-Demethylating