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
-
peptic
- stomach
- ammonia
- catalase
- mucosa
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serology
- clarithromycin
- nitrate
- nickel
- amoxicillin
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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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3.5.1.5 ureaseAdvanced search results
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results (Engineering
Engineering on EC 3.5.1.5 - urease
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alphaH134A
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no detectable activity, 53% of the nickel content of wild-type enzyme
alphaH136A
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no detectable activity, 6% of the nickel content of wild-type enzyme
alphaH219A
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1.9% of the activity of the wild-type enzyme, 80% of the nickel content of the wild type enzyme, very high Km-value compared to wild-type enzyme
alphaH246A
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no detectable activity, 21% of the nickel content of wild-type enzyme
alphaH320A
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normal nickel content, 0.003% of the activity of the wild-type enzyme, unlike wild-type enzyme no inactivation by diethyldicarbonate
alphaH321A
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activity and nickel content are similar to wild-type enzyme
C319A
C319D
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0.03% of the activity of the wild-type enzyme, nickel content of the mutant is lower than that of the wild-type enzyme, small increase in Km-value
C319S
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4.5% of the activity of the wild-type enzyme, nickel content of the mutant is lower than that of the wild-type enzyme, small increase in Km-value
G11P
UreB, subunit beta, analysis of urease activation
G18P
UreB, subunit beta, analysis of urease activation
H320A
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100000fold deficiencies in rates, modest Km changes, disorders in the peptide flap covering their active sites, the pH-optimum is anomalous with optima near pH 6 and shoulders that extend to pH 9
H320N
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100000fold deficiencies in rates, modest Km changes, disorders in the peptide flap covering their active sites, the pH-optimum is anomalous with optima near pH 6 and shoulders that extend to pH 9
H320Q
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100000fold deficiencies in rates, modest Km changes, disorders in the peptide flap covering their active sites, the pH-optimum is anomalous with optima near pH 6 and shoulders that extend to pH 9
R336Q
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0.0001fold decreased catalytic rate with near-normal pH dependence, unaffected Km-value, phenylglyoxal inactivates at over half the rate observed for the native enzyme
additional information
C319A
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48% of the activity of the wild-type enzyme, nickel content of the mutant is lower than that of the wild-type enzyme, small increase in Km-value
C319A
mutation increases the urease resistance to both epigallocatechin and quercetin
additional information
crosslinked enzyme aggregates of Providencia rettgeri urease (PRU-CLEAs) are prepared using genipin as crosslinking agent, method, overview. Optimal at 0.3 g/l of bovine serum albumin. The aggregates remove urea, but the treatment with PRU-CLEAs reveals no significant change of volatile flavor substances in Chinese rice wine. By using urea as the substrate, the values of Km and Vmax of free urease from Providencia rettgeri JN-B815 are estimated to be 5.99 mmol/l and 840 nmol/min, while those of immobilized urease are 13.54 mmol/l and 940 nmol/min, respectively. By using urethane as the substrate, the Km and Vmax value of free urethanase are determined to be 183.82 mmol/l and 970 nmol/min, while those of immobilized enzyme are 705.78 mmol/l and 650 nmol/min, respectively
additional information
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crosslinked enzyme aggregates of Providencia rettgeri urease (PRU-CLEAs) are prepared using genipin as crosslinking agent, method, overview. Optimal at 0.3 g/l of bovine serum albumin. The aggregates remove urea, but the treatment with PRU-CLEAs reveals no significant change of volatile flavor substances in Chinese rice wine. By using urea as the substrate, the values of Km and Vmax of free urease from Providencia rettgeri JN-B815 are estimated to be 5.99 mmol/l and 840 nmol/min, while those of immobilized urease are 13.54 mmol/l and 940 nmol/min, respectively. By using urethane as the substrate, the Km and Vmax value of free urethanase are determined to be 183.82 mmol/l and 970 nmol/min, while those of immobilized enzyme are 705.78 mmol/l and 650 nmol/min, respectively
additional information
Providencia rettgeri CGMCC 8326
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crosslinked enzyme aggregates of Providencia rettgeri urease (PRU-CLEAs) are prepared using genipin as crosslinking agent, method, overview. Optimal at 0.3 g/l of bovine serum albumin. The aggregates remove urea, but the treatment with PRU-CLEAs reveals no significant change of volatile flavor substances in Chinese rice wine. By using urea as the substrate, the values of Km and Vmax of free urease from Providencia rettgeri JN-B815 are estimated to be 5.99 mmol/l and 840 nmol/min, while those of immobilized urease are 13.54 mmol/l and 940 nmol/min, respectively. By using urethane as the substrate, the Km and Vmax value of free urethanase are determined to be 183.82 mmol/l and 970 nmol/min, while those of immobilized enzyme are 705.78 mmol/l and 650 nmol/min, respectively
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additional information
Providencia rettgeri JN-B815
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crosslinked enzyme aggregates of Providencia rettgeri urease (PRU-CLEAs) are prepared using genipin as crosslinking agent, method, overview. Optimal at 0.3 g/l of bovine serum albumin. The aggregates remove urea, but the treatment with PRU-CLEAs reveals no significant change of volatile flavor substances in Chinese rice wine. By using urea as the substrate, the values of Km and Vmax of free urease from Providencia rettgeri JN-B815 are estimated to be 5.99 mmol/l and 840 nmol/min, while those of immobilized urease are 13.54 mmol/l and 940 nmol/min, respectively. By using urethane as the substrate, the Km and Vmax value of free urethanase are determined to be 183.82 mmol/l and 970 nmol/min, while those of immobilized enzyme are 705.78 mmol/l and 650 nmol/min, respectively
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