title: Molecular mechanism of Mg-ATPase activity.
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 Mg(2+) 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 Mg(2+) transport through the 1Mg(2+):1ATP stochiometry. Based on the results of these analyses, the kinetic scheme for Mg-ATPase has been developed.
authors.affiliation: Departament of Membranology, Iv. Beritashvili Center of Experimental Biomedicine, 14 Gotua Street, 0160, Tbilisi, Georgia, noki2601@mail.ru.
authors.forename: Eka
authors.initials: E
authors.lastname: Nozadze
authors.forename: Nana
authors.initials: N
authors.lastname: Arutinova
authors.forename: Leila
authors.initials: L
authors.lastname: Tsakadze
authors.forename: Lia
authors.initials: L
authors.lastname: Shioshvili
authors.forename: Marina
authors.initials: M
authors.lastname: Leladze
authors.forename: Sopio
authors.initials: S
authors.lastname: Dzneladze
authors.forename: Gvantsa
authors.initials: G
authors.lastname: Chkadua
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism*; D004789:Enzyme Activation; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D051381:Rats
chemical_list: D000255:Adenosine Triphosphate; D017301:Ca(2+) Mg(2+)-ATPase; D008274:Magnesium