InterPro domain: IPR002019

This entry represents the urease beta subunit. In Helicobacter pylori, the gamma and beta subunits are fused and known (confusingly) as the alpha subunit.

Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, archaea, fungi and plants. Their primary role is to allow the use of external and internally-generated urea as a nitrogen source. The enzyme consists of three subunits, alpha, beta and gamma, which can exist as separate proteins or can be fused on a single protein chain. The alpha-beta-gamma heterotrimer forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel centre complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers [ 1 , 2 , 3 , 4 , 5 ].

1. Plant ureases: roles and regulation. Acta Biochim. Pol. 47, 1189-95
2. Bacterial ureases in infectious diseases. Microbes Infect. 2, 533-42
3. Staying alive overdosed: how does Helicobacter pylori control urease activity? Int. J. Med. Microbiol. 295, 307-15
4. Supramolecular assembly and acid resistance of Helicobacter pylori urease. Nat. Struct. Biol. 8, 505-9
5. Molecular biology of microbial ureases. Microbiol. Rev. 59, 451-80