A model for the reaction pathways of the K+-dependent phosphatase activity of the ()-dependent ATPase
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Cited by (32)
Synergistic stimulation by potassium and ammonium of K<sup>+</sup>- phosphatase activity in gill microsomes from the crab Callinectes ornatus acclimated to low salinity: Novel property of a primordial pump
2013, Archives of Biochemistry and BiophysicsCitation Excerpt :In addition to furnishing energy for ion pumping, ATP accelerates K+ deocclusion and the conversion of the E2 K to E1 K form without undergoing hydrolysis, both rate limiting steps of the (Na+, K+)-ATPase cycle (for review see [12,13]. Besides ATP, the (Na+, K+)-ATPase also hydrolyzes other phosphate-donating substrates like p-nitrophenylphosphate [7,10,14–16], O-methylfluorescein phosphate [17], acetyl phosphate [18], 2,4-dinitrophenyl phosphate and β-(2-furyl)acryloyl phosphate [19]. Such hydrolytic activity is related to the K+-phosphatase activity of the enzyme.
Na,K-ATPase activity and epithelial interfaces in gills of the freshwater shrimp Macrobrachium amazonicum (Decapoda, Palaemonidae)
2009, Comparative Biochemistry and Physiology - A Molecular and Integrative PhysiologyDissecting the hydrolytic activities of sarcoplasmic reticulum ATPase in the presence of acetyl phosphate
2002, Journal of Biological ChemistryCitation Excerpt :The Ca2+-independent activity in this study is mechanistically similar to the Na+,K+-ATPase activity when AcP or pNPP is hydrolyzed in the presence of K+ and absence of Na+. The so-called phosphatase activity does not support cation transport and has been attributed to E2 conformations (35, 36). The present results highlight the interdependence of Ca2+-dependent and Ca2+-independent hydrolytic activities catalyzed by SR Ca2+-ATPase, and therefore, the versatility of the enzyme reaction cycle.
Testing the Versatility of the Sarcoplasmic Reticulum Ca <sup>2+</sup>-ATPase Reaction Cycle When p-Nitrophenyl Phosphate Is the Substrate
2001, Journal of Biological ChemistryDeterminants of the pH of the Golgi complex
2000, Journal of Biological ChemistryCitation Excerpt :The high intra-Golgi [K+], together with the presence of K+ permeation pathways, suggest that efflux of this cation could serve to neutralize the inward pumping of H+ by the V-ATPase. The physiological significance of the high intra-Golgi K+ is otherwise not clear, but it is conceivable that, as described for some cytosolic pathways (50), some of the enzymes within the Golgi perform optimally at high concentrations of this cation. In vitro determinations using isolated Golgi fractions had shown earlier that increasing counter-ion conductance by means of ionophores enhanced luminal acidification (51).
Probing energy coupling in the yeast plasma membrane H<sup>+</sup>-ATPase with acetyl phosphate
1997, Archives of Biochemistry and Biophysics