Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process
Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process
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DOI：
10.1016/j.febslet.2005.03.015
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发表时间：
2005-04-11
期刊：
影响因子：
3.5
通讯作者：
Battaglioli, E
中科院分区：
文献类型：
--
作者：
Forneris, F;Binda, C;Battaglioli, E
Lysine-specific historical demethylase 1（LSD1）是最近发现的一种酶，它能特异性地去除Lys4的甲基。我们已经解决了蛋白质的功能特性，证明组蛋白去甲基化涉及黄素催化氧化甲基化赖氨酸。研究了作为完成催化循环所需的电子受体的底物的性质。LSD1将氧转化为过氧化氢，尽管这种反应性不像其他依赖黄素的氧化酶那样明显。我们的发现提出了一种可能性，即在体内LSD1可能不一定作为氧化酶起作用，但它可能使用替代的电子受体。(c) 2005年欧洲生化学会联合会。Elsevier B.V.版权所有。
Lysine-specific historic demethylase 1(LSD1) is a very recently discovered enzyme which specifically removes methyl groups from Lys4 of historic 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. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.