| Primary Identifier | IPR017950 | Type | Active_site |
| Short Name | Urease_AS |
| 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 acarbamated-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. |
