ATP−ADP Exchange Reaction Catalyzed by Na+,K+-ATPase: Dephosphorylation by ADP of the E1P Enzyme Form
Author:
Affiliation:
1. División de Biofísica, Instituto de Investigación Médica “Mercedes y Martín Ferreyra”, Casilla de Correo 389, 5000 Córdoba, Argentina
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi971087c
Reference39 articles.
1. Annual review prize lecture. ‘All hands to the sodium pump’.
2. Sodium ions, acting at high-affinity extracellular sites, inhibit sodium-ATPase activity of the sodium pump by slowing dephosphorylation.
3. Synthesis of adenosine triphosphate and exchange between inorganic phosphate and adenosine triphosphate in sodium and potassium ion transport adenosine triphosphatase.
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1. Charge Translocation by the Na+/K+ Pump under Na+/Na+ Exchange Conditions: Intracellular Na+ Dependence;Biophysical Journal;2006-03
2. Sodium/Calcium Exchanger: Influence of Metabolic Regulation on Ion Carrier Interactions;Physiological Reviews;2006-01
3. Effect of ADP on Na+-Na+ Exchange Reaction Kinetics of Na,K-ATPase;Biophysical Journal;2004-08
4. Breakdown of Na+/K+-exchanging ATPase phosphoenzymes formed from ATP and from inorganic phosphate during Na+-ATPase activity.;European Journal of Biochemistry;2001-11
5. Lipids, Membranes, and Cell Coats;Biochemistry;2001
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