3.5.1.5: urease
This is an abbreviated version!
For detailed information about urease, go to the full flat file.
Word Map on EC 3.5.1.5
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3.5.1.5
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pylory
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helicobacter
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gastric
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ulcer
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endoscopy
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gastritis
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eradication
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breath
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gastrointestinal
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duodenal
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peptic
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stomach
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ammonia
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catalase
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mucosa
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serology
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clarithromycin
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nitrate
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nickel
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amoxicillin
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pylori-positive
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antrum
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dyspeptic
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omeprazole
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metronidazole
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giemsa
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proteus
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anti-h
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invertase
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mirabilis
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amend
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campylobacter
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stool
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gastroduodenal
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bismuth
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nitrification
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nutrition
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lansoprazole
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medicine
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synthesis
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antisecretory
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pylori-infected
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sydney
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drug development
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manure
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compost
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analysis
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sucrase
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thiourea
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pylori-induced
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ranitidine
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per-protocol
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industry
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food industry
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intention-to-treat
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biotechnology
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gastroscopy
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e-test
- 3.5.1.5
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pylory
- helicobacter
- gastric
- ulcer
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endoscopy
- gastritis
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eradication
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breath
- gastrointestinal
- duodenal
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peptic
- stomach
- ammonia
- catalase
- mucosa
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serology
- clarithromycin
- nitrate
- nickel
- amoxicillin
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pylori-positive
- antrum
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dyspeptic
- omeprazole
- metronidazole
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giemsa
- proteus
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anti-h
- invertase
- mirabilis
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amend
- campylobacter
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stool
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gastroduodenal
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bismuth
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nitrification
- nutrition
- lansoprazole
- medicine
- synthesis
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antisecretory
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pylori-infected
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sydney
- drug development
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manure
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compost
- analysis
- sucrase
- thiourea
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pylori-induced
- ranitidine
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per-protocol
- industry
- food industry
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intention-to-treat
- biotechnology
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gastroscopy
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e-test
Reaction
Synonyms
acid urease, Arthritogenic cationic 19 kDa antigen, BPU, canatoxin, embryo-specific soybean urease, Eu1, Eu4, HPU, jack bean urease, JBU, JBURE-II, More, PMU, urea amido hydrolase, Urea amidohydrolase, urease, urease JBURE-IIb, UreC
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Application
Application on EC 3.5.1.5 - urease
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analysis
biotechnology
drug development
food industry
industry
enhancement of stability of immobilised urease by biocompatible polymer-conjugated magnetic beads for industrial application based on removal of urea
medicine
nutrition
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urea is estimated in different blood samples with the help of agar-immobilized urease and the results are consistent with those from clinical pathology laboratory through an autoanalyzer
analysis
urease is used to calculate the amount of urea in biological solutions in order to remove urea from blood, waste water, fruit juice and foods. Enhancement of stability of immobilised urease by biocompatible polymer-conjugated magnetic beads for industrial application based on removal of urea
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immobilization of urease on arylamine glass beads results in improved thermal, storage and operational stability. Because of inertness of support and stability of immobilized urease, the preparation can find applications in artificial kidney and urea estimation in biological fluids
biotechnology
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in food industry immobilisation of acid urease on an inert carrier has the potential advantages of significant cost savings, improved stability or resistance to shear or inhibitory compound inactivation. Purified acid urease preparation is covalently immobilised onto biocompatible porous chitosan beads of different size. The kinetics of urea degradation in a model wine solution using this biocatalyst is of the pseudofirst order with respect to the urea concentration in the liquid bulk, the apparent pseudo-first order kinetic rate constant ranging from about two thirds to one fifth of that pertaining to free acid urease
biotechnology
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soybean (Glycine max) urease is immobilized on alginate and chitosan beads and shows improved stability. This could have a potential role in haemodialysis machines
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3-,6-,7-,9-,12-monohydroxy tetradecanoic acid isomers can be used in agriculture, pharmacy and cosmetic industries due to their excellent antielastase, antiurease and antioxidant activities. Hydroxy fatty acids can be urease inhibitors and anti-Helicobacter pylori agents due to their antiurease activity
drug development
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urease is considered a first line target for drug development and vaccination against Helicobacter pylori infection
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the enzyme is applicable to elimination of urea in Chinese rice wine
food industry
use of recombinant acid urease for enzymatic degradation of urea in rice wine. Ethylcarbamate, a carcinogenic compound, is formed from urea and ethanol in rice wine, therefore enzymatic elimination of urea is always attractive
food industry
Limosilactobacillus reuteri CICC6124
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use of recombinant acid urease for enzymatic degradation of urea in rice wine. Ethylcarbamate, a carcinogenic compound, is formed from urea and ethanol in rice wine, therefore enzymatic elimination of urea is always attractive
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food industry
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the enzyme is applicable to elimination of urea in Chinese rice wine
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enhancement of intragastric enzyme activity is not strictly a function of pH-value, but is related to differential effects of the availability of nickel, which is required for enzyme activity
medicine
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lack of enzyme activity in most enterohaemorrhagic strains is due to a premature stop codon in ureD encoding a chaperone protein of the urease gene cluster
medicine
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use of jack bean urease as a model enzyme for Helicobacter pylori urease. Development of organobismuth components without antifungal activity against Saccharomyces cerevisiae but with antibacterial activity
medicine
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the action of urease in the upper intestinal tract is exploited in a non-invasive urease breath test for the diagnosis of bacterial infections of Helicobacter pylori: 13C- or 14C-labelled urea is ingested, and if the bacterium is present in the stomach, the urea is converted into isotope-labelled carbon dioxide. This is absorbed into the blood and exhaled in the breath, where it is detected by mass spectrometer or scintillation counter
medicine
a novel immunoconjugate (L-DOS47) is developed and characterized as a therapeutic agent for tumors expressing CEACAM6. The single domain antibody AFAIKL2, which targets CEACAM6, is expressed in the Escherichia coli BL21 (DE3) pT7-7 system. High purity urease is extracted and purified from Jack bean meal. AFAIKL2 is activated using N-succinimidyl [4-iodoacetyl]aminobenzoate (SIAB) as the cross-linker and then conjugated to urease. The specificity and cytotoxicity of L-DOS47 is confirmed by screening in four cell lines (BxPC-3, A549, MCF7, and CEACAM6-transfected H23). BxPC-3, a CEACAM6-expressing cell line is most susceptible to L-DOS47. L-DOS47 is a potential therapeutic agent in human phase I clinical studies for nonsmall cell lung cancer
medicine
importance of overall cryptococcal urease inhibition, rather than of its enzymatic activity alone, for the future development of therapeutic tools targeting cryptococcosis
medicine
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site targeted delivery of urease along with chemotherapeutic drugs can be a promising tool for anti-cancer applications. Urease shows its inhibitory effects on cancer cell lines through the generation of toxic ammonia, which in turn increases the pH of the surrounding medium. This increase in extracellular pH, enhances the cytotoxic effect of weak base chemotherapeutic drugs, doxorubicin (0.05 mM) and vinblastine (0.100 mM) in the presence of urease (5 U/ml) and urea (0-4 mM) significantly
medicine
Cryptococcus gattii VGI R265
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importance of overall cryptococcal urease inhibition, rather than of its enzymatic activity alone, for the future development of therapeutic tools targeting cryptococcosis
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medicine
Glutamicibacter creatinolyticus MTCC 5604
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site targeted delivery of urease along with chemotherapeutic drugs can be a promising tool for anti-cancer applications. Urease shows its inhibitory effects on cancer cell lines through the generation of toxic ammonia, which in turn increases the pH of the surrounding medium. This increase in extracellular pH, enhances the cytotoxic effect of weak base chemotherapeutic drugs, doxorubicin (0.05 mM) and vinblastine (0.100 mM) in the presence of urease (5 U/ml) and urea (0-4 mM) significantly
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nutrition
Limosilactobacillus fermentum IFO 14511
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elimination of the urea in alcoholic beverages
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nutrition
Streptococcus mitior PG-118
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elimination of the urea in alcoholic beverages
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