PS51368

Urease domain profile

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Short nameUREASE_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

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