94280
Urease from Canavalia ensiformis (Jack bean)
powder, ~1 U/mg
Synonym(s):
Jack bean urease, Urea amidohydrolase
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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 (Ure) enzyme is present in the cytosol. It is active at acidic pH and is expressed at 28°C. Urease consists of nickel and is present in archaea, bacteria, unicellular eukaryotes and plants.
Application
Urease from Canavalia ensiformis may be used for urea determination of various samples, such as legumes . It may be useful for the detection of pathogens as well as heavy-metal ions.
Urease from Canavalia ensiformis (Jack bean) has been used in purification and crystallization studies.
Biochem/physiol Actions
Urease catalyzes the hydrolysis of urea into carbon dioxide and ammonia. Urease is involved in nitrogen metabolism and urea degradation. Urease from Canavalia ensiformis binds 2 nickel ions per subunit .
Unit Definition
1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol urea (Cat. No. 51459) per minute at pH 8.0 and 25 °C.
Other Notes
Application in (selective) hydrolysis/condensations; structure.
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
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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R.L. Blakeley et al.
J. Mol. Catal., 23, 263-263 (1984)
M.C.N. Jayasuriya et al.
Anim. Feed Sci. Technol., 8, 271-271 (1983)
Optimisation of isolation and purification of the jack bean enzyme urease by extraction and subsequent crystallization
Weber M, et al.
Food and Bioproducts Processing, 86(1), 43-52 (2008)
Brendan Wallace et al.
Journal of endourology, 37(3), 358-366 (2022-12-24)
Introduction: The pathogenesis of infectious kidney stones is poorly understood. Bacteria have been implicated in promoting infectious stones via urease production; however, there is mounting evidence indicating the relationship is more complex. The aim of our study was to characterize
M J Sculley et al.
Biophysical chemistry, 19(1), 39-47 (1984-01-01)
The use of bifunctional reagents to form cross-links between subunits in protein oligomers and subsequent disruption of noncovalent interactions with SDS allows comment upon the number of subunits and the symmetry in the original assembly. In existing treatments the number
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