Non-enzymatic properties of Proteus mirabilis urease subunits

Ureases are moonlighting proteins displaying non-catalytic properties, including platelet activation, antifungal and entomotoxic effects. The structure-activity mapping of these properties is poorly developed. Proteus mirabilis urease (PMU) consists three subunits, PmUre?, PmUre? PmUre?, in an (???)3 organization. In order to study the relationships PMU we obtained recombinant subunits this evaluated their biological activities. holo-urease promoted aggregation, toxicity fungal insect models. Similar Jaburetox, a plant urease-derived polypeptide, showed highest against yeasts insects, activated human platelets. PmUre? PmUre? presented insecticidal action upon injection. addition, only promote hemocytes aggregation. Bioinformatics analyses revealed gene/segment duplication evolutionary divergence among ureases. Our findings show that (and probably its counterparts other ureases) carries most non-enzymatic activities proteins.