UreaseHelicobacter Pylori Urease drawn from PDB 1E9Z.
- Active site metal: nickel(II)
- Molecular weight: 480 kDa or 545 kDa for Jack Bean Urease (calculated mass from the amino acid sequence).
- Optimum pH: 7.4
- Optimum Temperature: 60 degrees Celsius
- Enzymatic specificity: urea and hydroxyurea
- Inhibitors: heavy metals
The multi-subunit enzyme usually has a 3:3 (alpha:beta) stoichiometry with a 2-fold symmetric structure (note that the image above gives the structure of the asymmetric unit, one third of the true biological assembly). An exceptional urease is found in Helicobacter pylori, which combines four of the regular six subunit enzymes in an overall tetrahedral assembly of 24 subunits (α12β12). This supra-molecular assembly is thought to confer additional stability for the enzyme in this organism, which functions to produce ammonia in order to neutralise gastric acid. The presence of urease is used in the diagnosis of Helicobacter species.
As diagnostic test
Organisms that produce urease tend to be gastrointestinal or urinary tract pathogens, since urease enables them to neutralize the acid present in these acidic environments.
Urease can be used to remove wine stains from textiles.
Urease-positive pathogens include:
- Helicobacter pylori
- Enteric bacteria including Proteus, Klebsiella and Serratia
- Ureaplasma urealyticum, a relative of the mycoplasma
- Cryptococcus, an opportunistic fungus
Further information might be found on the talk pageor at requests for expansion.
v • d • eCarbon-nitrogen non-peptide hydrolases(EC3.5)
3.5.1 - AmidohydrolasesAsparaginase- Glutaminase- Urease - Biotinidase- Aspartoacylase- Ceramidase-Aspartylglucosaminidase- Fatty acid amide
hydrolase- Histone deacetylase(Sirtuin) 3.5.2
Barbiturase- Beta-lactamase3.5.3 Arginase-
Agmatinase3.5.4 - AminohydrolasesGuanine deaminase- Adenosine deaminase- AMP
deaminase- Inosine monophosphate synthase- DCMP deaminase- GTP cyclohydrolase IOther Nitrilase-