Helicobacter pylori urease (HPU)

Helicobacter pylori urease is a nickel-dependent metalloenzyme that plays a fundamental role in the pathogenesis and survival of the bacterium within the human stomach (UniProt P14916). By catalyzing the hydrolysis of urea into ammonia and carbon dioxide, the enzyme neutralizes gastric acidity, allowing H. pylori to colonize the gastric mucosa (PubMed 11274153). This process not only facilitates bacterial persistence but also generates toxic byproducts like ammonia that cause inflammation and tissue damage, leading to chronic gastritis and peptic ulcers (StatPearls NBK534233). Due to its high expression and essentiality, urease is the primary target for non-invasive diagnostic procedures, including the Urea Breath Test (Mayo Clinic). While antibiotics remain the standard of care, urease inhibitors such as acetohydroxamic acid and various bismuth-containing compounds are utilized to interfere with bacterial metabolism and enhance eradication rates (PubChem CID 1990). Furthermore, the enzyme's critical role in H. pylori-associated gastric cancer makes it a significant focus for vaccine development and novel antimicrobial strategies (PubMed 27602000).

Other names

Urea amidohydrolaseH. pylori ureaseNickel-dependent urease

Competitive or non-competitive inhibition of the nickel-containing active site, preventing the hydrolysis of urea into ammonia and carbon dioxide, which eliminates the bacterium's acid-neutralizing capability and disrupts its survival in the gastric environment.