Klebsiella aerogenes urease (KAU) (KAU)

Klebsiella aerogenes urease is a nickel-dependent metalloenzyme that plays a critical role in bacterial pathogenesis by catalyzing the hydrolysis of urea into ammonia and carbon dioxide (Hausinger, R. P., 1993, "The biological aspects of nickel"). This enzymatic activity leads to a rapid increase in local pH, which serves as a key virulence factor by neutralizing acidic environments and promoting the formation of magnesium ammonium phosphate (struvite) stones (Griffith, D. P., et al., 1976, "Urease-producing bacteria, urea, and staghorn calculi"). The enzyme is structured as a heterotrimer composed of alpha (UreC), beta (UreB), and gamma (UreA) subunits, with a binuclear nickel center essential for its catalytic function (UniProt P18314, P18315, P18316). Clinically, this enzyme is a significant therapeutic target in the management of chronic urinary tract infections and the prevention of infection-induced urolithiasis (NCBI, "Klebsiella aerogenes"). Pharmacological intervention typically involves the use of urease inhibitors like acetohydroxamic acid, which competitively bind to the nickel active site to prevent urea breakdown (PubChem CID 1974). While effective in reducing stone recurrence and urinary ammonia levels, the clinical utility of these inhibitors is often constrained by safety concerns, including potential teratogenicity and hematological toxicity.

Other names

Urea amidohydrolaseEnterobacter aerogenes ureaseUrease

Competitive inhibition of the urease enzyme by binding to the nickel-containing active site, thereby preventing urea hydrolysis and subsequent ammonia production.