Everything about Urease totally explained
Urease is an
enzyme that
catalyzes the
hydrolysis of
urea into
carbon dioxide and
ammonia. The reaction occurs as follows:
(NH2)2CO + H
2O →
CO2 + 2
NH3
Urea + Water --
urease--> Ammonium Carbonate
In
1926 James Sumner showed that urease is a
protein. Urease is found in
bacteria,
yeast and several higher
plants.
Characteristics:
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 (
). 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 fungusFurther Information
Get more info on 'Urease'.
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