title: Structure and mechanism of lysine-specific demethylase enzymes.
abstract: The discovery of histone-demethylating enzymes has revealed yet another reversible histone modification mark. In this review, we describe the structural and chemical insights that we have now derived underlying the activity of these enzymes. The recent co-crystal structures of LSD1 bound to a proparylamine-derivatized histone H3 peptide and JHDM structures bound to two different methylated histone H3 peptides illustrate the steric requirements and structural basis for substrate specificity.
authors: Program in Gene Expression and Regulation, The Wistar Institute, Philadelphia, Pennsylvania, USA.
authors: Ruchi
authors: R
authors: Anand
authors: Ronen
authors: R
authors: Marmorstein
mesh_terms: D000818:Animals; D006657:Histones / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D010089:Oxidoreductases, N-Demethylating / Q000737:chemistry* / Q000378:metabolism; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D020836:Protein Structure, Quaternary; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
chemical_list: D006657:Histones; D010455:Peptides; D010089:Oxidoreductases, N-Demethylating