Molecular Mechanisms of Enzyme Activation by Monovalent Cations

J Biol Chem. 2016 Sep 30;291(40):20840-20848. doi: 10.1074/jbc.R116.737833. Epub 2016 Jul 26.

Abstract

Regulation of enzymes through metal ion complexation is widespread in biology and underscores a physiological need for stability and high catalytic activity that likely predated proteins in the RNA world. In addition to divalent metals such as Ca2+, Mg2+, and Zn2+, monovalent cations often function as efficient and selective promoters of catalysis. Advances in structural biology unravel a rich repertoire of molecular mechanisms for enzyme activation by Na+ and K+ Strategies range from short-range effects mediated by direct participation in substrate binding, to more distributed effects that propagate long-range to catalytic residues. This review addresses general considerations and examples.

Keywords: enzyme kinetics; evolution; potassium; pyruvate kinase; sodium; structure-function; thrombin.

Publication types

  • Review

MeSH terms

  • Catalysis
  • Cations, Monovalent / chemistry
  • Cations, Monovalent / metabolism
  • Enzymes* / chemistry
  • Enzymes* / genetics
  • Enzymes* / metabolism
  • Potassium* / chemistry
  • Potassium* / metabolism
  • Sodium* / chemistry
  • Sodium* / metabolism

Substances

  • Cations, Monovalent
  • Enzymes
  • Sodium
  • Potassium

Associated data

  • PDB/1DIO
  • PDB/1GJV
  • PDB/1KP8
  • PDB/1GQT
  • PDB/1DKA
  • PDB/1BKS
  • PDB/1SG8