LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Domain |
| Description | Urease (urea amidohydrolase, ) catalyses the hydrolysis of urea to form ammonia and carbamate. The subunit composition of urease from different sources varies [ ], but each holoenzyme consists of four structural domains []: three structural domains and a nickel-binding catalytic domain common to amidohydrolases []. 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 ( ). The N-terminal domain is a composite domain and plays a major trimer stabilising role by contacting the catalytic domain of the symmetry related alpha-subunit [ ]. |
| Short Name | Urease_alpha_N_dom |
