U0251
Urease from Canavalia ensiformis (Jack bean)
Type C-3, powder, ≥600,000 units/g solid
Synonym(s):
Jack bean urease, Urea amidohydrolase
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About This Item
Recommended Products
biological source
Canavalia ensiformis
Quality Level
type
Type C-3
form
powder
specific activity
≥600,000 units/g solid
mol wt
~544620 Da
purified by
crystallization
storage temp.
−20°C
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General description
Subunit molecular weight: ~90,770
Composed of six subunits with total molecular weight: ~544,620
Composed of six subunits with total molecular weight: ~544,620
Urease is a nickel-dependent metalloenzyme , found in various plants, bacteria, fungi, and algae. It contains two distinct subunits-UreA(26.5 kDa) and UreB (60.3–61.6 kDa).
Biochem/physiol Actions
Urease aids in the bioavailability of nitrogen in plants. It is implicated in defense mechanism and exhibits insecticidal activity. In addition, urease exhibits antifungal activity by retarding growth and affecting membrane integrity of filamentous fungi and yeasts.
Urease was shown to induce vacuolation in Hela cells, an effect dependent on the ability of urease to convert urea to ammonia.
Unit Definition
One micromolar unit will liberate 1.0 μmole of NH3 from urea per min at pH 7.0 at 25 °C. It is equivalent to 1.0 I.U. or 0.054 Sumner unit (1.0 mg ammonia nitrogen in 5 minutes at pH 7.0 at 20 °C)
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Certificates of Analysis (COA)
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T L Cover et al.
Infection and immunity, 59(4), 1264-1270 (1991-04-01)
Concentrated broth culture supernatants from 50 to 60% of Helicobacter pylori strains induce eukaryotic cell vacuolation in vitro. A quantitative assay for cell vacuolation was developed on the basis of the rapid uptake of visibly vacuolated HeLa cells was significantly
Barbara Krajewska et al.
Plant physiology and biochemistry : PPB, 43(7), 651-658 (2005-07-19)
A pH-variation study of jack bean (Canavalia ensiformis) urease steady-state kinetic parameters and of the inhibition constant of boric acid, a urease competitive inhibitor, was performed using both noninhibitory organic (MES, HEPES and CHES) and inhibitory inorganic (phosphate) buffers, in
Yu Hang Fong et al.
PLoS biology, 11(10), e1001678-e1001678 (2013-10-12)
Urease is a metalloenzyme essential for the survival of Helicobacter pylori in acidic gastric environment. Maturation of urease involves carbamylation of Lys219 and insertion of two nickel ions at its active site. This process requires GTP hydrolysis and the formation
Angela R Piovesan et al.
Archives of biochemistry and biophysics, 547, 6-17 (2014-03-04)
Ureases catalyze the hydrolysis of urea into NH3 and CO2. They are synthesized by plants, fungi and bacteria but not by animals. Ureases display biological activities unrelated to their enzymatic activity, i.e., platelet and neutrophil activation, fungus inhibition and insecticidal
Anne H S Martinelli et al.
Biochimica et biophysica acta, 1840(3), 935-944 (2013-11-19)
Ureases are metalloenzymes involved in defense mechanisms in plants. The insecticidal activity of Canavalia ensiformis (jack bean) ureases relies partially on an internal 10kDa peptide generated by enzymatic hydrolysis of the protein within susceptible insects. A recombinant version of this
Articles
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