Na,K‐dependent adenosine triphosphate phosphohydrolase: activation of the phosphatase reaction by ATP analogs

1 October 1984

journal article
Published by Wiley in FEBS Letters

Vol. 175 (2) , 303-306
https://doi.org/10.1016/0014-5793(84)80756-5

Abstract

The effect of N₁‐substituted analogs of ATP on the hydrolysis of umbelliferone phosphate by Na,K‐ATPase has demonstrated: (i) analogs having a negatively charged substituent (N ₁‐oxy‐ or N ₁‐carbo‐methoxy‐ATP) and capable of accepting H⁺ induce an activation similar to that of ATP; ii) N ₁‐methoxy‐ATP, containing an uncharged substituent, does not affect the phosphatase reaction at low concentration and inhibits it at higher concentration. It has been assumed that ATP binding to Na,K‐ATPase induces formation of a hydrogen bond between the nitrogen atom at the first position of the purine base and appropriate amino acid of active centre, with a subsequent attachment of H⁺ to ATP, thus facilitating the transition of Na,K‐ATPase from the K⁺‐ to the Na⁺‐form.

Keywords

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