Urea hydrolase involved in nitrogen recycling from ureide, purine, and arginine catabolism (PubMed:26690979). Is known to be highly toxic and lethal when given by intravenous route, producing convulsions and other signs of central nervous system intoxication associated with the high levels of ammonia formed in the blood of mice and rabbits (PubMed:26690979). Is neurotoxic in mammals, when directly injected into hippocampus (PubMed:33631299). It may induce seizures by acting at a neuronal network level, thereby disturbing electroencephalographic rhythms and causing metabolic alterations in key areas related to epileptogenesis and to neurogenic pulmonary edema (PubMed:33631299). It increases calcium influx and neuronal firing rate in the hippocampus (PubMed:33631299). Is able to insert itself into lipid bilayers, altering physicochemical properties of artificial membranes, and forming cation-selective ion channels (PubMed:24583269). In vitro, has the ability to induce platelet aggregation, platelet granules secretion and release of ATP (PubMed:11696010). In contrast to canatoxin, another urease from C.ensiformis, is not lethal to mice when intraperitoneally injected (PubMed:11696010). 2 H(+) + H2O + urea = CO2 + 2 NH4(+) Binds 2 nickel ions per subunit. P-hydroxymercuribenzoate irreversibly abolishes ureolytic activity, but does not inhibit the ability to activate platelets (PubMed:11696010). Also inhibited by acetohydroxamic acid (AHA), a chelator of Ni2+ and Zn2+ ions (PubMed:11696010). Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. Homohexamer (Probable). Other oligomeric forms may exist depending on pH and presence of salts (Probable). Carboxylation allows a single lysine to coordinate two nickel ions. Was isolated in 1926 by James B. Sumner. It was the first enzyme ever obtained in a crystalline form, demonstrating that enzymes could be proteins. In the C-terminal section; belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.