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Histone demethylation catalysed by LSD1 is a flavin‐dependent oxidative process
Author(s) -
Forneris Federico,
Binda Claudia,
Vai Maria Antonietta,
Mattevi Andrea,
Battaglioli Elena
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.015
Subject(s) - flavin group , demethylase , chemistry , demethylation , histone , biochemistry , flavoprotein , lysine , enzyme , gene expression , dna , amino acid , dna methylation , gene
Lysine‐specific histone demethylase 1 (LSD1) is a very recently discovered enzyme which specifically removes methyl groups from Lys4 of histone 3. We have addressed the functional properties of the protein demonstrating that histone demethylation involves the flavin‐catalysed oxidation of the methylated lysine. The nature of the substrate that acts as the electron acceptor required to complete the catalytic cycle was investigated. LSD1 converts oxygen to hydrogen peroxide although this reactivity is not as pronounced as that of other flavin‐dependent oxidases. Our findings raise the possibility that in vivo LSD1 might not necessarily function as an oxidase, but it might use alternative electron acceptors.