Histone demethylation catalysed by LSD1 is a flavin‐dependent oxidative process

作者：Federico Forneris, Claudia Binda, Maria Antonietta Vanoni, Andrea Mattevi, Elena Battaglioli · 发表于：FEBS Letters · 年份：2005 · DOI：10.1016/j.febslet.2005.03.015 · 被引用次数：281 · 研究领域：Epigenetics and DNA Methylation、Amino Acid Enzymes and Metabolism、Genetic Syndromes and Imprinting

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.