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.
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CITATION STYLE
Gohara, D. W., & Di Cera, E. (2016, September 30). Molecular mechanisms of enzyme activation by monovalent cations. Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology Inc. https://doi.org/10.1074/jbc.R116.737833
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