Abstract
The ATP hydrolysis reactions responsible for the Na +/K +-ATPase phosphorylation, according to recent experimental evidences, also occur for the PTX–Na +/K + pump complex. Moreover, it has been demonstrated that PTX interferes with the enzymes phosphorylation status. However, the reactions involved in the PTX–Na +/K + pump complex phosphorylation are not very well established yet. This work aims at proposing a reaction model for PTX–Na +/K + pump complex, with similar structure to the Albers–Post model, to contribute to elucidate the PTX effect over Na +/K +-ATPase phosphorylation and dephosphorylation. Computational simulations with the proposed model support several hypotheses and also suggest: (i) phosphorylation promotes an increase of the open probability of induced channels; (ii) PTX reduces the Na +/K + pump phosphorylation rate; (iii) PTX may cause conformational changes to substates where the Na +/K +-ATPase may not be phosphorylated; (iv) PTX can bind to substates of the two principal states E1 and E2, with highest affinity to phosphorylated enzymes and with ATP bound to its low-affinity sites. The proposed model also allows previewing the behavior of the PTX–pump complex substates for different levels of intracellular ATP concentrations.
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