Activation by Adenosine Triphosphate in the Phosphorylation Kinetics of Sodium and Potassium Ion Transport Adenosine Triphosphatase
TLDR
It was concluded that adenosine triphosphate was activating the enzyme in a fashion functionally distinct from its action as a phosphate donor, since the concentration of adenosines triph phosphate required for activation was much higher than that required for phosphorylation.About:
This article is published in Journal of Biological Chemistry.The article was published on 1972-10-25 and is currently open access. It has received 809 citations till now. The article focuses on the topics: Potassium ion transport & Magnesium ion.read more
Citations
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Journal ArticleDOI
Biochemistry of Na,K-ATPase
TL;DR: The Na,K-ATPase or sodium pump carries out the coupled extrusion and uptake of Na and K ions across the plasma membranes of cells of most higher eukaryotes, and areas where there is still considerable uncertainty are highlighted.
Journal ArticleDOI
Energy limitation as a selective pressure on the evolution of sensory systems
TL;DR: Assessing evidence from a wide range of vertebrate and invertebrate examples, it is shown that reducing energy expenditure can account for many of the morphological features of sensory systems and has played a key role in their evolution.
Journal ArticleDOI
Crystal structure of the sodium–potassium pump
J. Preben Morth,J. Preben Morth,Bjørn Panyella Pedersen,Bjørn Panyella Pedersen,Mads S. Toustrup-Jensen,Mads S. Toustrup-Jensen,Thomas Sorensen,Janne Petersen,Janne Petersen,Jens Peter Andersen,Jens Peter Andersen,Bente Vilsen,Bente Vilsen,Poul Nissen,Poul Nissen +14 more
TL;DR: The X-ray crystal structure of the pig renal Na+,K+-ATPase with two rubidium ions bound (as potassium congeners) in an occluded state in the transmembrane part of the α-subunit is presented.
Journal ArticleDOI
Structural changes in the calcium pump accompanying the dissociation of calcium
Chikashi Toyoshima,Hiromi Nomura +1 more
TL;DR: The structure of the enzyme stabilized by thapsigargin, a potent inhibitor, shows large conformation differences from that in E1Ca2+.
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PLANT PLASMA MEMBRANE H+-ATPases: Powerhouses for Nutrient Uptake.
TL;DR: The elucidation of the three-dimensional structure of a related Ca2+ pump has implications for understanding of structure-function relationships for the plant plasma membrane H+-ATPase.
References
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Further investigations on a Mg++ + Na+-activated adenosintriphosphatase, possibly related to the active, linked transport of Na+ and K+ across the nerve membrane
TL;DR: The observations lend further support to the suggestion made previously that this enzyme is involved in the active, linked transport of Na+ and K+ across the nerve membrane.
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The effect of arsenate on aerobic phosphorylation.
Robert K. Crane,Fritz Lipmann +1 more
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Flexibility of an active center in sodium-plus-potassium adenosine triphosphatase.
TL;DR: There is a conformational change in the active center for phosphorylation during the normal reaction sequence and this change may be linked to one required theoretically for active translocation of ions across the cell membrane.
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A phosphorylated intermediate in adenosine triphosphate-dependent sodium and potassium transport across kidney membranes.
TL;DR: On the basis of tracer exchange experiments with (Na+ + K+)-ATPase in crab nerve, Skou proposed an enzyme-high energy phosphate inter- mediate, E - P, consistent with reciprocal competitive inhibitory effects.
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Binding of Adenosine Triphosphate to Sodium and Potassium Ion-stimulated Adenosine Triphosphatase
C. Hegyvary,Robert L. Post +1 more
TL;DR: Binding was stable between pH 5.6 and 7.6, but declined sharply above pH 8.0, and in the presence of potassium ion alone, there appeared to be one or more binding sites on this enzyme with a much lower affinity for adenosine triphosphate.