Differential susceptibility of Plasmodium falciparum versus yeast and mammalian enolases to dissociation into active monomers

摘要: In the past, several unsuccessful attempts have been made to dissociate homodimeric enolases into their active monomeric forms. The main objective of these studies had understand whether intersubunit interactions are essential for catalytic and structural stability enolases. Further motivation investigate properties enolase has arisen from recent reports on involvement in diverse nonglycolytic (moonlighting) functions, where it may occur form. Here, we report successful dissociation dimeric Plasmodium falciparum, yeast rabbit muscle isolatable monomers. Dimeric could be dissociated monomers by high concentrations (∼ 250 mm) imidazole and/or hydrogen ions. Two forms were separated using Superdex-75 gel filtration chromatography. A detailed comparison kinetic recombinant P. falciparum showed differences specific activity, salt-induced inhibition inactivation, thermal stability, etc. Furthermore, found that three species differ dimer profiles. Specifically, challenge with imidazole, Mg(II) protected but not dissociation. observed differential interface respect mammalian exploited selectively parasite enzyme its catalytically inefficient, thermally unstable Thus a novel therapeutic target malaria.