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The effect of N1-substituted analogs of ATP on the hydrolysis of umbelliferone phosphate by Na,K-ATPase has demonstrated: analogs having a negatively charged substituent (N1-oxy- or N1-carbo-methoxy-ATP) and capable of accepting H+ induce an activation similar to that of ATP; N1-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.
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A A Boldyrev, and
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A A Boldyrev, and
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A A Boldyrev, and
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