ChemicalBook--->CAS DataBase List--->9002-13-5

9002-13-5

9002-13-5 Structure

9002-13-5 Structure
IdentificationBack Directory
[Name]

UREASE
[CAS]

9002-13-5
[Synonyms]

UREASE
3.5.1.5
EC 3.5.1.5
EC 6.3.4.6
Urease,jack
CRUDE UREASE
IUB: 3.5.1.5
UREASE, SP-OP
UREASE,POWDER
Enzyme urease
jackbeanurease
JACK BEAN MEAL
UREA AMIDOLYASE
UREA AMYDOLYASE
Einecs 232-656-0
Recombinant Urease
UREASE (JACK BEAN)
UREASE (JACK BEANS)
UREA AMIDOHYDROLASE
urea aminohydrolase
JACKBEANMEAL,POWDER
UREASE AMIDOHYDROLASE
UREASE JACK BEAN MEAL
UREASE, FROM JACK BEAN
urease from jack beans
Urease [1000 units/mg]
Urease [>=200 units/mg]
UREASE (ATP-HYDROLYZING)
rUrease, Urea amidohydrolase
UreaseExJackBean(E.C.3.5.1.5)
UREASE TYPE IV FROM JACK BEANS
urease type ix from jack beans
UREASE TYPE VI FROM JACK BEANS
UREASE TYPE VII FROM JACK BEANS
urease type C-3 from jack beans
urease type iii from jack beans
Urease from Jack bean, lyophil.
UREASE FROM JACK BEANS, ~8 U/MG
UREASEFROMLACTOBACILLUSFERMENTUM
UREASE TYPE II-C FROM JACK BEANS
UREASE FROM JACK BEANS, ~35 U/MG
UREASE, HIGH ACTIVITY (JACK BEAN)
Urease, recombinant from bacteria
UREASE-ACTIVE MEAL FROM JACK BEANS
Urease from jack bean min. 220 U/mg
Urease, froM jack bean, 2000 units/Mg
urease type X from bacillus pasteurii
UREASE FROM JACK BEANS APPROX. 8 U/MG
Urease Canavalia ensiformis (Jack bean)
UREASE FROM JACK BEANS APPROX. 60 U/MG
UREASE FROM JACK BEANS, POWDER, ~1 U/MG
UREASE, JACK BEAN MOL. WT. 272000-*54500 0
Urease from Canavalia ensiformis (Jack bean)
urease glycerol solution type iii from*jack beans
UREASE FROM JACK BEANS, LYOPH., POWDER, ~100 U/MG
Urease enzyme preparation from lactobacillus fermentum
UREASE FROM CANAVALIA ENSIFORMIS, ACTIVITY: 3500-4500 UNITS/MG
UREASE TABLETS FROM JACK BEAN MEAL FOR THE DETERMINATION OF UREA
UREASE FROM CANAVALIA ENSIFORMIS, ACTIVITY: LARGER THAN 100000 UNITS/MG
UREASE (FROM JACK BEANS) LYOPHILIZED, 5U/MG FOR THE DETERMINING OF UREA IN SERUM
[EINECS(EC#)]

232-656-0
[Molecular Formula]

N/A
[MDL Number]

MFCD00070858
Chemical PropertiesBack Directory
[Appearance]

powder
[storage temp. ]

2-8°C
[form ]

powder
[color ]

yellow
[Water Solubility ]

It is slightly soluble in water.
[Merck ]

9870
[EPA Substance Registry System]

Urease (9002-13-5)
Hazard InformationBack Directory
[Chemical Properties]

powder
[Uses]

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.
[General Description]

Subunit molecular weight: ~90,770
Composed of six subunits with total molecular weight: ~544,620
[Agricultural Uses]

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.
[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 .
Safety DataBack Directory
[Hazard Codes ]

Xn
[Risk Statements ]

36/37/38-42
[Safety Statements ]

22-24-26-36/37-45-36-23
[WGK Germany ]

1
[RTECS ]

YU1700000
[F ]

10-21
[TSCA ]

Yes
[HS Code ]

35079090
Raw materials And Preparation ProductsBack Directory
[Raw materials]

Jack beans meal
Questions And AnswerBack Directory
[Description]

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.
[References]

[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
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