LSD1 and the chemistry of histone demethylation.

Philip A Cole, Jeffrey C Culhane

Journal: Current opinion in chemical biology 2007;11(5):561-8

PMID: 17851108

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Abstract

The recent discovery that histone demethylation can be catalyzed by the flavin-dependent amine oxidase LSD1 has ushered in a new chapter in the chromatin-remodeling community. Herein, we discuss the rapid progress of the histone demethylase field including the recent identification of the non-heme iron-dependent histone demethylases (JmjC family), the basis for LSD1 substrate site specificity and the newly emerging potential for inhibition of these enzymes in structural and functional analysis.

Address: Department of Pharmacology and Molecular Sciences, The Johns Hopkins School of Medicine, Baltimore, MD 21205, United States.

DOI: 10.1016/j.cbpa.2007.07.014

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MeSH Terms: Catalysis, Chromatin Assembly and Disassembly, Enzyme Inhibitors, F-Box Proteins, Histone Demethylases, Histones, Humans, Jumonji Domain-Containing Histone Demethylases, Methylation, Oxidoreductases, N-Demethylating, Protein Processing, Post-Translational, Substrate Specificity