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Molecular Mechanism of Mg-ATPase Activity

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Abstract

Mg-ATPase is very important in living organisms. To better understand the molecular mechanism of Mg-ATPase activity, we applied the method of kinetic analysis of multi-sited enzyme systems; this is a suitable approach used for kinetic investigation of multi-sited enzyme systems. The study of Mg-ATPase has demonstrated: (1) It is a multi-sited enzyme system whose functional unit is minimum a dimmer; (2) Its substrate is MgATP, while free ATP and Mg2+ appear to be the enzyme modifiers with a dual effect; (3) The enzyme system for MgATP has at least three sites: i.e., the essential activator, full inhibitor, and partial effect modifiers sites; (4) Mg-ATPase carries out Mg2+ transport through the 1Mg2+:1ATP stochiometry. Based on the results of these analyses, the kinetic scheme for Mg-ATPase has been developed.

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Authors and Affiliations

  1. Departament of Membranology, Iv. Beritashvili Center of Experimental Biomedicine, 14 Gotua Street, 0160, Tbilisi, Georgia

    Eka Nozadze, Nana Arutinova, Leila Tsakadze, Lia Shioshvili, Marina Leladze, Sopio Dzneladze & Gvantsa Chkadua

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  1. Eka Nozadze
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  2. Nana Arutinova
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  3. Leila Tsakadze
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  4. Lia Shioshvili
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  5. Marina Leladze
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  6. Sopio Dzneladze
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  7. Gvantsa Chkadua
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Correspondence to Eka Nozadze.

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Nozadze, E., Arutinova, N., Tsakadze, L. et al. Molecular Mechanism of Mg-ATPase Activity. J Membrane Biol 248, 295–300 (2015). https://doi.org/10.1007/s00232-014-9769-2

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  • DOI: https://doi.org/10.1007/s00232-014-9769-2

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