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
-
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
-
gastroscopy
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e-test
- 3.5.1.5
-
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
-
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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Metals Ions
Metals Ions on EC 3.5.1.5 - urease
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NaCl
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maximum activity at 18-23% NaCl at 50°C, loses activity irreversibly in the absence of NaCl
Ni2+
Nickel
Ni2+
metal-dependent enzyme that contains nickel at its active site
Ni2+
-
soybean urease is inactive when soybean cell cultures are grown in the absence of nickel
Ni2+
urease activation: apoprotein (UreABC)3 + 6 Ni2+
Ni2+
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the nickel-containing enzyme requires four accessory proteins for proper active site metalation. The metallochaperone UreE delivers nickel to UreG, a GTPase that forms a UreD/UreF/UreG complex, which binds to urease apoprotein via UreD. A molecular tunnel in UreD is a direct facilitator of nickel transfer into urease
Ni2+
Ni2+ is essential to urease activation, best at 0.5 mM. Urease is inhibited at high concentration of Ni2+
Nickel
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enzyme contains 2 gatom of nickel per 96600 g of protein
Nickel
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partial activation of the apoprotein in presence of Ni(II) and CO2, incubation with Ni alone leads to the formation of inactive proteins
Nickel
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addition of Ni to purified apourease does not yield active enzyme, the apoenzyme is very slowly activated in vivo by addition of Ni2+ ions to Ni-free cell cultures, apourease activation is an energy-dependent process that is deactivated by cell disruption
Nickel
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wild-type enzyme contains 4.6 atoms of nickel per molecule of urease, the nickel content of the mutant enzymes C319A, C319S, C319D and C319Y is lower
Nickel
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His320 of subunit C is essential for urea hydrolysis and Ni2+ binding within the native enzyme
Nickel
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specifically required for ureolysis and cannot be replaced by another metal, 0.5 mol of nickel is firmly bound to 1 mol of enzyme protein