Urease enzyme from Helicobacter pylori

Urease enzyme from Helicobacter pylori is a multi-subunit, nickel-dependent metalloenzyme essential for the bacterium’s survival in the acidic environment of the human stomach[3][5][6]. The enzyme rapidly hydrolyzes urea, which diffuses into the bacterial cytoplasm via a specialized proton-gated urea channel, forming ammonia and carbon dioxide[7]. The ammonia produced locally neutralizes gastric acid, allowing H. pylori to maintain intracellular and periplasmic pH homeostasis, which is vital for colonization and persistent infection[6][8]. Structurally, H. pylori urease is a dodecameric assembly containing 12 UreA and 12 UreB subunits, with the active site featuring two nickel ions bridged by a carbamylated lysine and surrounded by several histidines and an aspartate[1][7]. Maturation and activation of the enzyme require several accessory proteins (UreD, UreE, UreF, UreG, and UreH), responsible for nickel insertion and proper folding[2][3]. Because urease is both essential for gastric colonization and unique to H. pylori among stomach bacteria, it is a major target for diagnostic tests and drug development, and its inhibition is a validated strategy for eradicating H. pylori infection and ameliorating gastritis, ulcers, and some gastric cancers[1][7][6].

Other names

UreaseH. pylori ureaseHelicobacter pylori urease

Inhibition of urease active site, disruption of nickel binding or incorporation into the enzyme, and inhibition of urea hydrolysis, reducing ammonia production and acid resistance.