Helicobacter pylori urease (HPU) (HPU)

Helicobacter pylori urease is a complex, nickel-dependent metalloenzyme that plays a fundamental role in the pathogenesis of H. pylori by catalyzing the hydrolysis of urea into ammonia and carbon dioxide (UniProt: P14916). This reaction is vital for the bacterium's survival in the acidic gastric environment, as the produced ammonia neutralizes stomach acid to create a habitable neutral microenvironment (PubMed: 11283408). In addition to urease, related surface and membrane components such as adhesins (e.g., BabA, SabA) and toxins (e.g., VacA, CagA) facilitate bacterial attachment and host tissue damage (StatPearls: NBK544281). Urease is a primary target for diagnostic procedures like the Urea Breath Test and is a focal point for therapeutic strategies, including the use of urease inhibitors like acetohydroxamic acid and bismuth-based compounds (PubChem: CID 1990). Targeting these components is a key approach in treating chronic gastritis and peptic ulcers while reducing the risk of gastric adenocarcinoma (PubMed: 28955100). However, therapeutic challenges include the need for high specificity to avoid affecting host enzymes and the management of side effects associated with current inhibitors (PubMed: 25503454).

Other names

UreaseUrea amidohydrolaseH. pylori urease complexUreA/UreB complex

Inhibition of the urease enzyme prevents the conversion of urea to ammonia, thereby preventing the neutralization of gastric acid and hindering the survival and colonization of H. pylori in the acidic stomach environment.