Member database | PROSITE profiles |
PROSITE profiles type | domain |
Short name | UREASE_3 |
Description
Urease (EC 3.5.1.5) is a nickel-binding enzyme that catalyzes the hydrolysis
of urea to carbon dioxide and ammonia
[3]. 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
[1], 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
[2]. The urease domain forms an (alpha
beta)(8) barrel structure with structural similarity to other
metal-dependent hydrolases, such as adenosine and AMP deaminase and phosphotriesterase.
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.
References
1.Microbial ureases: significance, regulation, and molecular characterization. Mobley HL, Hausinger RP. Microbiol. Rev. 53, 85-108, (1989). View articlePMID: 2651866
2.The crystal structure of urease from Klebsiella aerogenes. Jabri E, Carr MB, Hausinger RP, Karplus PA. Science 268, 998-1004, (1995). View articlePMID: 7754395
3.The structure of jack bean urease. The complete amino acid sequence, limited proteolysis and reactive cysteine residues. Takishima K, Suga T, Mamiya G. Eur. J. Biochem. 175, 151-65, (1988). View articlePMID: 3402446
Integrated to
External Links
Representative structure
4ep8: Initial Urease Structure for Radiation Damage Experiment at 100 K