the findings of a k+-uncoupled basal activity , inhibition by high k+ concentrations , lower atp saturation values for the phosphorylation than for the overall atpase reaction , and presumed reversibility of the phosphoprotein formation by excess adp indicated similarities in fundamental principles of the reaction cycle between the kdp-atpase and eukaryotic e1e2-atpases .
C0031715
phosphorylation
C1538110
kdp