InterPro domain: IPR008221

Urease (urea amidohydrolase, 3.5.1.5 ) catalyses the hydrolysis of urea to form ammonia and carbamate. The subunit composition of urease from different sources varies [ 1 ], but each holoenzyme consists of four structural domains [ 2 ]: three structural domains and a nickel-binding catalytic domain common to amidohydrolases [ 3 ]. Urease is unique among nickel metalloenzymes in that it catalyses a hydrolysis rather than a redox reaction. In Klebsiella aerogenes, the domains are found in an alpha subunit (with the C-terminal two-thirds representing the catalytic domain and the N-terminal one-third representing one of the structural domains); a beta subunit, and a gamma subunit. In Helicobacter pylori, the gamma and beta domains are fused and called the alpha subunit. The catalytic subunit (called beta or B) has the same organisation as the K. aerogenes alpha subunit. Jack bean (Canavalia ensiformis) urease has a fused gamma-beta-alpha organisation.

This group represents the gamma-beta-alpha type.

1. Molecular biology of microbial ureases. Microbiol. Rev. 59, 451-80
2. The crystal structure of urease from Klebsiella aerogenes. Science 268, 998-1004
3. An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. Proteins 28, 72-82