Molecular Mechanism of Mg-ATPase Activity

Molecular Mechanism of Mg-ATPase Activity 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. The Journal of Membrane Biology Springer Journals

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Springer US
Copyright © 2015 by Springer Science+Business Media New York
Life Sciences; Biochemistry, general; Human Physiology
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