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Sodium and Potassium Ions in Proteins and Enzyme Catalysis

  • Chapter
The Alkali Metal Ions: Their Role for Life

Part of the book series: Metal Ions in Life Sciences ((MILS,volume 16))

Abstract

The group I alkali metal ions Na+ and K+ are ubiquitous components of biological fluids that surround biological macromolecules. They play important roles other than being nonspecific ionic buffering agents or mediators of solute exchange and transport. Molecular evolution and regulated high intracellular and extracellular M+ concentrations led to incorporation of selective Na+ and K+ binding sites into enzymes to stabilize catalytic intermediates or to provide optimal positioning of substrates. The mechanism of M+ activation, as derived from kinetic studies along with structural analysis, has led to the classification of cofactor-like (type I) or allosteric effector (type II) activated enzymes. In the type I mechanism substrate anchoring to the enzyme active site is mediated by M+, often acting in tandem with a divalent cation like Mg2+, Mn2+ or Zn2+. In the allosteric type II mechanism, M+ binding enhances enzyme activity through conformational transitions triggered upon binding to a distant site. In this chapter, following the discussion of the coordination chemistry of Na+ and K+ ions and the structural features responsible for the metal binding site selectivity in M+-activated enzymes, well-defined examples of M+-activated enzymes are used to illustrate the structural basis for type I and type II activation by Na+ and K+.

Please cite as: Met. Ions Life Sci. 16 (2016) 259–290

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Acknowledgment

Financial support from the University of Zurich (J.S.) is gratefully acknowledged. M.V. would like to thank my friend and colleague Professor Roland K.O. Sigel for his hospitality and the office space at the Department of Chemistry, University of Zurich.

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  1. Department of Chemistry B, University of Zürich, Winterthurerstrasse 190, CH-8057, Zürich, Switzerland

    Milan Vašák & Joachim Schnabl

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  2. Joachim Schnabl
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Correspondence to Milan Vašák .

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Editors and Affiliations

  1. Department of Chemistry Inorganic Chemistry, University of Basel, Basel, Basel Stadt, Switzerland

    Astrid Sigel

  2. Department of Chemistry Inorganic Chemistry, University of Basel, Basel, Switzerland

    Helmut Sigel

  3. Department of Chemistry, University of Zürich, Zürich, Switzerland

    Roland K. O. Sigel

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Vašák, M., Schnabl, J. (2016). Sodium and Potassium Ions in Proteins and Enzyme Catalysis. In: Sigel, A., Sigel, H., Sigel, R. (eds) The Alkali Metal Ions: Their Role for Life. Metal Ions in Life Sciences, vol 16. Springer, Cham. https://doi.org/10.1007/978-3-319-21756-7_8

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