Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process.

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Citation

Forneris F, Binda C, Vanoni MA, Mattevi A, Battaglioli E

Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process.

FEBS Lett. 2005 Apr 11;579(10):2203-7.

PubMed ID
15811342 [ View in PubMed
]
Abstract

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.

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Polypeptides
NameUniProt ID
Lysine-specific histone demethylase 1AO60341Details