Urease is found in the natural environment (water and soil) and in human body, where its occurrence is connected with protein degradation. It is an enzyme and is capable of urea hydrolysis: one molecule of ammonia and one molecule of carbamate appear in the first step, carbamate spontaneously converts into the second ammonia molecule and carbonic acid in a water solution, and ammonia is protonated. This urea hydrolysis results in pH increase. Urease and ammonia, generated during urea hydrolysis, may be toxic for human tissue and probably have role in long-lasting diseases, like atherosclerosis, urinary tract infections, or rheumatoid arthritis.
Urease can be used to analyze urea concentration in blood, urine, alcoholic beverages, natural water and environmental wastewaters; to analyze heavy metal content in natural waters, wastewaters and soil; to determine creatinine, arginine and IgG; to remove urea from artificial kidney dialyzates, alcohol beverages and fertilizer wastewaters; to control or shift pH for multi-enzyme reaction system; to hydrolyze urea as sources of ammonia or carbon dioxide in special cases, and for the wastewater reclamation for life support systems in space.
[1] Iwona Konieczna, Paulina ?arnowiec, Marek Kwinkowski, Beata Kolesińska, Justyna Fr?czyk, Zbigniew Kamiński, Wies?aw Kaca (2012) Bacterial Urease and its Role in Long-Lasting Human Diseases, Curr Protein Petp Sci., 13, 789-806
[2] Yingjie Qin, Joaquim M. S. Cabral (2002) Review: Properties and Applications of Urease, Biocatalysis and Biotransformation, 20, 1-14
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 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.
Clinical reagent in determination of urea in body fluid.
Subunit molecular weight: ~90,770
Composed of six subunits with total molecular weight: ~544,620
Urease, an enzyme, converts urea into ammonium
carbonate [(NH4)2CO3] that releases ammonia. Thus, the
enzyme activates the hydrolysis of urea. When the
release occurs on or near the soil surface, ammonia is lost
to the air; if it occurs near the seeds, they fail to
germinate, or it proves to be toxic to the roots of young
saplings. Crops can get affected by a high concentration
of ammonia. Soybean, jack beans and a number of fungi
are sources of urease. Its isoelectric point is pH 5.5.
Urease enzyme catalyzes the hydrolysis of urea which
occurs readily in the soils. Large numbers of bacteria,
fungi and actinomycetes in soils possess urease. A small
group of bacteria, known as urea bacteria, have an
exceptional ability to decompose urea. Activity increases
in proportion with the size of the soil microbial
population and the organic matter content. The presence
of relatively fresh plant residues often results in abundant
supplies of urease. The greatest activity of urease is
reported to occur in the rhizosphere, where microbial
activity is high and where it can be excreted from the
plant roots.
Although warm temperature (up to 37°C) favors
urease activity, the hydrolysis of urea occurs at
significant rates at temperatures down to 2°C. The effects
of soil moisture levels on urease activity are generally
small in comparison to the influence of the pH and
temperature. Free ammonia inhibits the enzymatic action
of urease.
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 .
