LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | Urease (urea amidohydrolase, ) a nickel-binding enzyme that catalyses the hydrolysis of urea to form ammonia and carbamate [ ]. It is mainly found in plant seeds, microorganisms and invertebrates. In plants, urease is a hexamer of identical chains, but the subunit composition of urease from different sources varies []; in bacteria [] it consists of either two or three different subunits (alpha, beta and gamma).Urease binds two nickel ions per subunit; four histidine, an aspartate and a carbamated-lysine serve as ligands to these metals; an additional histidine is involved in the catalytic mechanism [ ]. The urease domain forms an (alpha beta)(8) barrel structure with structural similarity to other metal-dependent hydrolases, such as adenosine and AMP deaminase (see ) and phosphotriesterase see ). Urease is unique among nickel metalloenzymes in that it catalyses a hydrolysis rather than a redox reaction. 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 Klebsiella alpha subunit. Jack bean (Canavalia ensiformis) urease has a fused gamma-beta-alpha organisation ( ). This entry describes the C-terminal domain of urease alpha subunit UreC (designated beta or UreB in Helicobacter species).Urease ( ) belongs to MEROPS peptidase family M38 (clan MJ). |
| Short Name | Urease_asu_c |
