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Originally published In Press as doi:10.1074/jbc.R500023200 on November 2, 2005

J. Biol. Chem., Vol. 281, Issue 3, 1305-1308, January 20, 2006
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A Structural Perspective on Enzymes Activated by Monovalent Cations*

Enrico Di Cera1

From the Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110

Enzymes activated by monovalent cations are abundantly represented in plants and the animal world. They have evolved to exploit Na+ and K+, readily available in biological environments, as major driving forces for substrate binding and catalysis. Recent progress in the structural biology of such enzymes has answered long standing questions about the molecular mechanism of activation and the origin of monovalent cation selectivity. That enables a simple classification of these functionally diverse enzymes and reveals unanticipated connections with ion transporters.

* This minireview will be reprinted in the 2006 Minireview Compendium, which will be available in January, 2007. This work was supported in part by National Institutes of Health Research Grants HL49413, HL58141, and HL73813.

1 To whom correspondence should be addressed. Tel.: 314-362-4185; Fax: 314-747-5354;E-mail: enrico{at}wustl.edu.


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