Forneris Federico, Binda Claudia, Vanoni Maria Antonietta, Mattevi Andrea, Battaglioli Elena
Dipartimento di Genetica e Microbiologia, Università di Pavia, Via Ferrata 1, 27100 Pavia, Italy.
FEBS Lett. 2005 Apr 11;579(10):2203-7. doi: 10.1016/j.febslet.2005.03.015.
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.
赖氨酸特异性组蛋白去甲基化酶1（LSD1）是一种最近才发现的酶，它能特异性地从组蛋白3的赖氨酸4上去除甲基基团。我们已经研究了该蛋白的功能特性，证明组蛋白去甲基化涉及黄素催化的甲基化赖氨酸氧化反应。我们还研究了作为完成催化循环所需电子受体的底物的性质。LSD1可将氧气转化为过氧化氢，尽管这种反应活性不如其他黄素依赖性氧化酶那么显著。我们的研究结果表明，在体内LSD1不一定作为氧化酶发挥作用，它可能使用其他电子受体。
