title: LSD1 and the chemistry of histone demethylation.
abstract: 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.
authors.affiliation: Department of Pharmacology and Molecular Sciences, The Johns Hopkins School of Medicine, Baltimore, MD 21205, United States.
authors.forename: Jeffrey C
authors.initials: JC
authors.lastname: Culhane
authors.forename: Philip A
authors.initials: PA
authors.lastname: Cole
mesh_terms: D002384:Catalysis; D042002:Chromatin Assembly and Disassembly; D004791:Enzyme Inhibitors; D044783:F-Box Proteins; D056466:Histone Demethylases; D006657:Histones / Q000378:metabolism*; D006801:Humans; D056484:Jumonji Domain-Containing Histone Demethylases; D008745:Methylation; D010089:Oxidoreductases, N-Demethylating / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D013379:Substrate Specificity
chemical_list: D004791:Enzyme Inhibitors; D044783:F-Box Proteins; D006657:Histones; D056466:Histone Demethylases; D056484:Jumonji Domain-Containing Histone Demethylases; C534524:KDM2A protein, human; C495195:KDM1A protein, human; D010089:Oxidoreductases, N-Demethylating