Urease subunit beta (UreB)

Urease subunit beta (UreB) is a primary structural and functional component of the urease enzyme complex, most notably studied in the human pathogen Helicobacter pylori. This nickel-dependent enzyme catalyzes the hydrolysis of urea into ammonia and carbon dioxide, a process essential for the survival of the bacteria in the highly acidic environment of the human stomach. By producing ammonia, UreB facilitates the neutralization of gastric acid, creating a localized alkaline microenvironment that supports bacterial colonization and persistence. In addition to its enzymatic activity, UreB is highly immunogenic, making it a major candidate for vaccine development and a key target for diagnostic assays like the rapid urease test. Clinically, UreB is targeted by inhibitors such as acetohydroxamic acid to treat chronic urea-splitting urinary tract infections and to augment the eradication of H. pylori. Research into UreB continues to focus on its role as a virulence factor and its potential as a target for novel antimicrobial agents designed to disrupt bacterial acid resistance. (Sources: UniProt P14916; PubMed PMID: 30251700; StatPearls: Helicobacter Pylori).

Other names

Urease subunit BUrease beta subunitUrease large subunitUrea amidohydrolase subunit beta

Inhibition of the nickel-dependent active site of the urease enzyme complex, preventing the hydrolysis of urea into ammonia and carbon dioxide, which disrupts the pathogen's ability to survive in acidic environments.