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
-
endoscopy
- gastritis
-
eradication
-
breath
- gastrointestinal
- duodenal
-
peptic
- stomach
- ammonia
- catalase
- mucosa
-
serology
- clarithromycin
- nitrate
- nickel
- amoxicillin
-
pylori-positive
- antrum
-
dyspeptic
- omeprazole
- metronidazole
-
giemsa
- proteus
-
anti-h
- invertase
- mirabilis
-
amend
- campylobacter
-
stool
-
gastroduodenal
-
bismuth
-
nitrification
- nutrition
- lansoprazole
- medicine
- synthesis
-
antisecretory
-
pylori-infected
-
sydney
- drug development
-
manure
-
compost
- analysis
- sucrase
- thiourea
-
pylori-induced
- ranitidine
-
per-protocol
- industry
- food industry
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intention-to-treat
- biotechnology
-
gastroscopy
-
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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KM Value
KM Value on EC 3.5.1.5 - urease
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0.165
Urea
pH 7.0, 25°C, urease encapsulated in chitosan nickel ferrite beads
0.168
Urea
pH 7.0, 25°C, urease encapsulated in chitosan-magnetite beads
0.172
Urea
pH 7.0, 25°C, urease encapsulated in chitosan-coated alginate-magnetite
0.181
Urea
pH 7.0, 25°C, urease encapsulated in chitosan-coated alginate-nickel
0.2
Urea
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range Km: 0.2-0.8 mM, pH 8.0, temperature not specified in the publication
0.21
Urea
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pH 6.8, 37°C, Vmax: 1200 micromol/min/mg, in the presence of preservatives PEG or glycerol
1.7
Urea
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pH 5.5, 65°C, Vmax: 7.29 micromol of ammonia/min/mg protein
3.2
Urea
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free enzyme or enzyme bound to membrane modified with NaOH + ethylendiamine and H2O2
4.2
Urea
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soluble urease, 37°C, pH not specified in the publication, Vmax: 200 micromol/min/mg
8.81
Urea
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immobilized urease, 37°C, pH not specified in the publication, Vmax: 43.48 micromol/min/mg
16.21
Urea
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pH and temperature not specified in the publication
additional information
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kinetic analysis of enzyme immobilized on acrylonitrile copolymer membranes chemically modified by different methods. KM-value of enzyme bound to membrane modified with NaOH + ethylendiamine and H2O2 is equal to that of free enzyme
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additional information
additional information
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sigmoid curve at low urea concentration (below 0.1 mM). In the presence of glycerol or PEG (preservatives), the sigmoid pattern changes to a rectangular hyperbola, and urea hydrolysis is consistent with Michaelis-Menten kinetics. Based on the kinetics of urease in the presence of the preservatives, the two forms of urease i.e., (alpha beta)3 and (alpha beta)6 may well exist in Helicobacter pylori. The hyperbolic kinetics adopted by the dissociated form of urease may allow for maximal urea assimilation by Helicobacter pylori under acidic conditions and at low urea concentration
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additional information
additional information
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reaction kinetics and thermodynamics, overview
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additional information
additional information
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steady-state kinetics analysis
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additional information
additional information
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steady-state kinetics analysis
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additional information
additional information
steady-state kinetics analysis
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additional information
additional information
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steady-state kinetics analysis
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additional information
Urea
a combined temperature-pH study of urease kinetics is performed at eight pHs between 5.0 and 8.3 in noninteracting biological buffers (MES and HEPES), at each pH at five temperatures between 15°C and 35°C. The analysis of the determined kinetic parameters KM and vmax shows that even though both the thermodynamic and activation parameters of the urease reaction are little pH-dependent