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  • Title: Cl anion-dependent Mg-ATPase.
    Author: Dzneladze S, Tsakadze L, Leladze M, Kometiani Z.
    Journal: J Membr Biol; 2012 Mar; 245(3):151-6. PubMed ID: 22399260.
    Abstract:
    We studied, in the rat brain, the synaptosomal and microsomal membrane fractions of Cl⁻ ion-activated, Mg²⁺-dependent ATPase, satisfying the necessary kinetic peculiarities of transport ATPases, by a novel method of kinetic analysis of the multisite enzyme systems: (1) the [Mg-ATP] complex constitutes the substrate of the enzymic reaction; (2) the V = f(Cl⁻) dependence-reflecting curve is bell-shaped; (3) substrate dependence, V = f(S), curves at a constant concentration of free ligands (Mg(f), ATP(f), Cl⁻); (4) as known from the literature, in the process of reaction a phosphorylated intermediate is formed (Gerencser, Crit Rev Biochem Mol Biol 31:303-337, 1996). We report on the Cl-ATPase molecular mechanism and its place in the "P-type ATPase" classification.
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