| Type: | Active_site | Name: | Urease active site |
| Description: | Urease (urea amidohydrolase, ) is a nickel-binding enzyme that catalyses the hydrolysis of urea to carbon dioxide and ammonia []. Historically, it was the first enzyme to be crystallized (in 1926). It is mainly found in plant seeds, microorganisms and invertebrates. In plants, urease is a hexamer of identicalchains. 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 isinvolved in the catalytic mechanism []. The urease domain forms an (alphabeta)(8) barrel structure with structural similarity to other metal-dependent hydrolases, such as adenosine and AMP deaminase and phosphotriesterase.This entry represents a conserved region that contains the active site histidine. | Short Name: | Urease_AS |
