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J. Biol. Chem., Vol. 282, Issue 49, 35425-35429, December 7, 2007

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Minireview

Structure and Mechanism of Lysine-specific Demethylase Enzymes^*

Ruchi Anand and Ronen Marmorstein¹

From the Program in Gene Expression and Regulation, The Wistar Institute, and the Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104

The discovery of histone-demethylating enzymes has revealed yet another reversible histone modification mark. In this review, we describe the structural and chemical insights that we have now derived underlying the activity of these enzymes. The recent co-crystal structures of LSD1 bound to a proparylamine-derivatized histone H3 peptide and JHDM structures bound to two different methylated histone H3 peptides illustrate the steric requirements and structural basis for substrate specificity.

Note Added in Proof—The following additional studies providing important information on structural and biochemical aspects of demethylation were published after the submission of this Minireview (Forneris, F., Binda, C., Adamo, A., Battaglioli, E., and Mattevi, A. (2007) J. Biol. Chem. 282, 20070–20074; Chen, Z., Zang, J., Kappler, J., Hong, X., Crawford, F., Wang, Q., Lan, F., Jiang, C., Whetstine, J., Dai, S., Hansen, K., Shi, Y., and Zhang, G. (2007) Proc. Natl. Acad. Sci. U. S. A. 104, 10818–10823; Couture, J. F., Collazo, E., Ortiz-Tello, P. A., Brunzelle, J. S., and Trievel, R. C. (2007) Nat. Struct. Mol. Biol. 14, 689–695).

^* This minireview will be reprinted in the 2007 Minireview Compendium, which will be available in January, 2008.

¹ To whom correspondence should be addressed. E-mail: marmor{at}wistar.org.

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