|PROSITE documentation PDOC00133 [for PROSITE entry PS00145]|
Urease (EC 22.214.171.124) is a nickel-binding enzyme that catalyzes 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 identical chains. In bacteria , it consists of either two or three different subunits (α, β and γ).
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 (α β)(8) barrel structure (see <PDB:2KAU>) with structural similarity to other metal-dependent hydrolases, such as adenosine and AMP deaminase (see <PDOC00419>) and phosphotriesterase (see <PDOC01026>).
As signatures for this enzyme, we selected a region that contains two histidines that bind one of the nickel ions and the region of the active site histidine. We also developed a profile that covers the whole urease domain.Last update:
April 2008 / Text revised; profile added.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Takishima K., Suga T., Mamiya G.|
|Title||The structure of jack bean urease. The complete amino acid sequence, limited proteolysis and reactive cysteine residues.|
|Source||Eur. J. Biochem. 175:151-165(1988).|
|2||Authors||Mobley H.L.T., Hausinger R.P.|
|Title||Microbial ureases: significance, regulation, and molecular characterization.|
|Source||Microbiol. Rev. 53:85-108(1989).|
|3||Authors||Jabri E., Carr M.B., Hausinger R.P., Karplus P.A.|
|Title||The crystal structure of urease from Klebsiella aerogenes.|