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Medientyp:
E-Artikel
Titel:
Role of Na+and K+in Enzyme Function
Beteiligte:
Page, Michael J.;
Di Cera, Enrico
Erschienen:
American Physiological Society, 2006
Erschienen in:Physiological Reviews
Sprache:
Englisch
DOI:
10.1152/physrev.00008.2006
ISSN:
0031-9333;
1522-1210
Entstehung:
Anmerkungen:
Beschreibung:
<jats:p>Metal complexation is a key mediator or modifier of enzyme structure and function. In addition to divalent and polyvalent metals, group IA metals Na<jats:sup>+</jats:sup>and K<jats:sup>+</jats:sup>play important and specific roles that assist function of biological macromolecules. We examine the diversity of monovalent cation (M<jats:sup>+</jats:sup>)-activated enzymes by first comparing coordination in small molecules followed by a discussion of theoretical and practical aspects. Select examples of enzymes that utilize M<jats:sup>+</jats:sup>as a cofactor (type I) or allosteric effector (type II) illustrate the structural basis of activation by Na<jats:sup>+</jats:sup>and K<jats:sup>+</jats:sup>, along with unexpected connections with ion transporters. Kinetic expressions are derived for the analysis of type I and type II activation. In conclusion, we address evolutionary implications of Na<jats:sup>+</jats:sup>binding in the trypsin-like proteases of vertebrate blood coagulation. From this analysis, M<jats:sup>+</jats:sup>complexation has the potential to be an efficient regulator of enzyme catalysis and stability and offers novel strategies for protein engineering to improve enzyme function.</jats:p>