Bacterial urease (Ure)

Bacterial urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea into ammonia and carbon dioxide (Konieczna et al., 2012, Journal of Applied Genetics). This enzymatic activity is a primary virulence factor for several pathogenic bacteria, most notably Helicobacter pylori, which uses the produced ammonia to neutralize gastric acid and survive in the human stomach (Mobley et al., 1995, Microbiology and Molecular Biology Reviews). In the urinary tract, urease-producing organisms like Proteus mirabilis cause an increase in urine pH, leading to the formation of infection-induced kidney stones, known as struvite stones (Griffith et al., 1976, Investigative Urology). Because the urease enzyme is not expressed by humans, it serves as a highly specific target for antimicrobial and adjuvant therapies (Upadhyay, 2012, Indian Journal of Biotechnology). Pharmacological inhibition, primarily through hydroxamic acid derivatives like acetohydroxamic acid, works by binding to the nickel ions in the active site, thereby blocking urea access and preventing the downstream pathological effects of ammonia production (Modolo et al., 2015, Journal of Advanced Research).

Other names

Urea amidohydrolaseNickel-dependent urease

Inhibition of the urease enzyme active site, typically through coordination with nickel ions, which prevents the hydrolysis of urea and the subsequent rise in local pH (Modolo et al., 2015).