Literature DB >> 16267046

A structural perspective on enzymes activated by monovalent cations.

Enrico Di Cera1.   

Abstract

Enzymes activated by monovalent cations are abundantly represented in plants and the animal world. They have evolved to exploit Na+ and K+, readily available in biological environments, as major driving forces for substrate binding and catalysis. Recent progress in the structural biology of such enzymes has answered long standing questions about the molecular mechanism of activation and the origin of monovalent cation selectivity. That enables a simple classification of these functionally diverse enzymes and reveals unanticipated connections with ion transporters.

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Year:  2005        PMID: 16267046     DOI: 10.1074/jbc.R500023200

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  37 in total

1.  Structural identification of cation binding pockets in the plasma membrane proton pump.

Authors:  Kira Ekberg; Bjørn P Pedersen; Danny M Sørensen; Ann K Nielsen; Bjarke Veierskov; Poul Nissen; Michael G Palmgren; Morten J Buch-Pedersen
Journal:  Proc Natl Acad Sci U S A       Date:  2010-11-22       Impact factor: 11.205

2.  Mechanism of Na(+) binding to thrombin resolved by ultra-rapid kinetics.

Authors:  Stefano Gianni; Ylva Ivarsson; Alaji Bah; Leslie A Bush-Pelc; Enrico Di Cera
Journal:  Biophys Chem       Date:  2007-09-29       Impact factor: 2.352

3.  Structural identification of the pathway of long-range communication in an allosteric enzyme.

Authors:  Prafull S Gandhi; Zhiwei Chen; F Scott Mathews; Enrico Di Cera
Journal:  Proc Natl Acad Sci U S A       Date:  2008-02-04       Impact factor: 11.205

4.  Ions and inhibitors in the binding site of HIV protease: comparison of Monte Carlo simulations and the linearized Poisson-Boltzmann theory.

Authors:  Dezso Boda; Mónika Valiskó; Douglas Henderson; Dirk Gillespie; Bob Eisenberg; Michael K Gilson
Journal:  Biophys J       Date:  2009-02-18       Impact factor: 4.033

5.  Intracellular potassium stabilizes human ether-à-go-go-related gene channels for export from endoplasmic reticulum.

Authors:  Lu Wang; Adrienne T Dennis; Phan Trieu; Francois Charron; Natalie Ethier; Terence E Hebert; Xiaoping Wan; Eckhard Ficker
Journal:  Mol Pharmacol       Date:  2009-01-12       Impact factor: 4.436

6.  Evolution of the genetic code by incorporation of amino acids that improved or changed protein function.

Authors:  Brian R Francis
Journal:  J Mol Evol       Date:  2013-06-07       Impact factor: 2.395

7.  Analyses of cobalt-ligand and potassium-ligand bond lengths in metalloproteins: trends and patterns.

Authors:  Natércia F Brás; António J M Ribeiro; Marina Oliveira; Nathália M Paixão; Juan A Tamames; Pedro A Fernandes; Maria J Ramos
Journal:  J Mol Model       Date:  2014-05-22       Impact factor: 1.810

8.  Crystal Structure of human pyridoxal kinase: structural basis of M(+) and M(2+) activation.

Authors:  Faik N Musayev; Martino L di Salvo; Tzu-Ping Ko; Amit K Gandhi; Ashwini Goswami; Verne Schirch; Martin K Safo
Journal:  Protein Sci       Date:  2007-08-31       Impact factor: 6.725

9.  Na+ binding to meizothrombin desF1.

Authors:  M E Papaconstantinou; P S Gandhi; Z Chen; A Bah; E Di Cera
Journal:  Cell Mol Life Sci       Date:  2008-11       Impact factor: 9.261

Review 10.  Serine proteases.

Authors:  Enrico Di Cera
Journal:  IUBMB Life       Date:  2009-05       Impact factor: 3.885

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