| Literature DB >> 27462078 |
David W Gohara1, Enrico Di Cera2.
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.Entities:
Keywords: enzyme kinetics; evolution; potassium; pyruvate kinase; sodium; structure-function; thrombin
Mesh:
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Year: 2016 PMID: 27462078 PMCID: PMC5076497 DOI: 10.1074/jbc.R116.737833
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157