Urease (Helicobacter pylori) (HPU)

Helicobacter pylori urease is a large, nickel-dependent metalloenzyme complex that is essential for the survival and pathogenesis of the bacterium within the human stomach [1.1.1, 1.1.2]. It catalyzes the rapid hydrolysis of urea into ammonia and carbon dioxide, a process that neutralizes local gastric acid and creates a hospitable, near-neutral microenvironment for the acid-sensitive organism [1.1.3, 1.1.4]. This neutralization is a prerequisite for H. pylori to colonize the gastric mucosa, where it can lead to chronic inflammation, peptic ulcers, and gastric cancer [1.1.5, 1.5.4]. In addition to its enzymatic function, the protein acts as a potent immunogen and may play a non-catalytic role in protecting the bacterium from host-derived oxidative stress [1.1.5]. Due to its central role in infection, urease is the basis for gold-standard diagnostic tools like the urea breath test and is a major target for the development of novel antimicrobial therapies and vaccines [1.2.2, 1.5.1].

Other names

Urea amidohydrolaseGastric ureaseH. pylori urease

Inhibition of urease enzyme activity to prevent gastric acid neutralization and bacterial survival [1.2.5, 1.3.2].