rUrease 5 mg

Recombinant Urease. Each mg of protein contains 345µg Potassium Phosphate and 25µg EDTA Na2.

Urease (EC 3.5.1.5) is an enzyme that catalyzes the hydrolysis of urea into carbon dioxide and ammonia. The reaction occurs as follows: (NH2)2CO + H2O = CO2 + 2NH3. Urease is found in bacteria, yeast and several higher plants. Characteristics: Active site metal: nickel(II). This enzyme is a mutant Urease from microorganism source, showing shifted substrate affinity to urea. The subunit structure is very similar to well known microbial urease. It is composed of multi-subunits and shows a more complex protein structure (alpha 2 Beta 4 Gamma 4) as compared to plant urease. The enzyme comprises of three different subunits to make complete fully active form, 60.3 kD a subunit, 11.7 kD b subunit and 11.1 kD g subunit respectively. rUrease is genetically designed unique mutant with a higher Km to urea, which makes it a suited material to kinetic urea assay with wide measurable range. Enzymatic specificity: urea and hydroxyurea; Inhibitors: heavy metals. 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 (a12b12). 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.