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Information on EC 3.5.1.5 - urease and Organism(s) Helicobacter pylori and UniProt Accession P14916
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3.5.1.5 ureaseIUBMB Comments
A nickel protein.
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Word Map
- 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
The taxonomic range for the selected organisms is: Helicobacter pylori
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
urease, jack bean urease, canatoxin, acid urease, jbure-ii, embryo-specific soybean urease, urea amidohydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Arthritogenic cationic 19 kDa antigen
-
-
-
-
Urea amidohydrolase
Urea amidohydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
-
-
-
-
carboxylic acid amide hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-
SYSTEMATIC NAME
IUBMB Comments
urea amidohydrolase
A nickel protein.
CAS REGISTRY NUMBER
COMMENTARY
9002-13-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
urea + H2O
?
-
urease is an important antigen and appears critical for colonization and virulence
-
-
?
urea + H2O
?
-
urease protects Helicobacter pylori against the acidic environment of the stomach, the enzyme acts as cytotoxin, with human gastric cells especially susceptible to its activity and disrups cell tight junctions in such a manner that the cells remain viable but an ionic flow between the cells occurs
-
-
?
urea + H2O
?
-
virulence factor since the ammonium ion produced from urea may by responsible for tissue injury and/or survival of the organism in the gastric environment
-
-
?
urea + H2O
CO2 + NH3
-
role for urease and urease-derived ammonia in megasome formation and survival of Helicobacter pylori in murine peritoneal macrophages and J774 cells
-
-
?
additional information
?
-
the urease impairs growth of selected phytopathogenic fungi at sub-micromolar concentrations. This antifungal property of ureases is not affected by treatment of the proteins with an irreversible inhibitor of the ureolytic activity
-
-
?
additional information
?
-
-
the urease impairs growth of selected phytopathogenic fungi at sub-micromolar concentrations. This antifungal property of ureases is not affected by treatment of the proteins with an irreversible inhibitor of the ureolytic activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
urea + H2O
CO2 + NH3
-
role for urease and urease-derived ammonia in megasome formation and survival of Helicobacter pylori in murine peritoneal macrophages and J774 cells
-
-
?
urea + H2O
?
-
urease is an important antigen and appears critical for colonization and virulence
-
-
?
urea + H2O
?
-
urease protects Helicobacter pylori against the acidic environment of the stomach, the enzyme acts as cytotoxin, with human gastric cells especially susceptible to its activity and disrups cell tight junctions in such a manner that the cells remain viable but an ionic flow between the cells occurs
-
-
?
urea + H2O
?
-
virulence factor since the ammonium ion produced from urea may by responsible for tissue injury and/or survival of the organism in the gastric environment
-
-
?
additional information
?
-
the urease impairs growth of selected phytopathogenic fungi at sub-micromolar concentrations. This antifungal property of ureases is not affected by treatment of the proteins with an irreversible inhibitor of the ureolytic activity
-
-
?
additional information
?
-
-
the urease impairs growth of selected phytopathogenic fungi at sub-micromolar concentrations. This antifungal property of ureases is not affected by treatment of the proteins with an irreversible inhibitor of the ureolytic activity
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ni2+
Nickel
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-[(4-[[5-(2-bromophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
-
3-[(4-[[5-(2-chlorophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
-
3-[(4-[[5-(2-fluorophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
-
3-[(4-[[5-(3-bromophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
-
3-[(4-[[5-(3-chlorophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
-
3-[(4-[[5-(3-fluorophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
-
3-[(4-[[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
-
3-[(4-[[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
-
3-[(4-[[5-(4-fluorophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
-
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)(4-[[5-(2-methoxyphenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)methyl]-2H-1-benzopyran-2-one
-
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)(4-[[5-(2-methylphenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)methyl]-2H-1-benzopyran-2-one
-
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)(4-[[5-(3-methoxyphenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)methyl]-2H-1-benzopyran-2-one
-
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)(4-[[5-(3-methylphenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)methyl]-2H-1-benzopyran-2-one
-
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)(4-[[5-(3-nitrophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)methyl]-2H-1-benzopyran-2-one
-
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)(4-[[5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)methyl]-2H-1-benzopyran-2-one
-
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)(4-[[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)methyl]-2H-1-benzopyran-2-one
-
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)[4-([5-[4-(trifluoromethyl)phenyl]-1,3,4-thiadiazol-2-yl]amino)phenyl]methyl]-2H-1-benzopyran-2-one
-
hydroxamic acid
hydroxamic acids are strong inhibitors of urease due to their chelating ability. They bind the Ni(II) centers present in the active site of urease in their anionic form via the (O,O) coordination mode. The Ni(II) centers of the urease active site are electrophilic in nature. This is responsible for appreciable charge transfer from the nucleophilic oxygen centers of the hydroxamate ligand to the Ni(II) centers when they bind in the active site. Hydroxamic acids with hydrophobic groups attached to them are more potent inhibitors of urease because they can easily penetrate the hydrophobic environment surrounding the active site. The -CONHO-x01moiety of the hydroxamic acid is also found to be absolutely necessary for chelation and inhibition of urease
hydroxy[3-(5-[4-[(4-hydroxy-2-oxo-2H-1-benzopyran-3-yl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]anilino]-1,3,4-thiadiazol-2-yl)phenyl]oxoammonium
-
1-(2,4-dihydroxyphenyl)-2-(4-hydroxyphenyl)ethanone
-
0.4 mg/ml, 16% inhibition
1-(3,4-dihydroxyphenyl)-2-(4-hydroxyphenyl)ethanone
-
0.4 mg/ml, 39% inhibition
2,4,4',6-tetrahydroxy-3-methoxyphenyldeoxybenzoin
-
0.4 mg/ml, 17% inhibition
2-(4-hydroxyphenyl)-1-(2,4,6-trihydroxy-3-methoxyphenyl)ethanone oxime
-
-
6-(1-hydroxy-2-(4-methoxyphenyl)ethyl)-2,3-dimethoxyphenol
-
0.4 mg/ml, 42% inhibition
copper(II) complex [CuClL1]*CH3OH
-
L2 is the deprotonated form of 4-bromo-N'-(2-hydroxy-5-methoxybenzylidene)benzohydrazide
copper(II) complex [CuClL2]*CH3OH
-
L3 is the deprotonated form of N'-(2-hydroxy-5-methoxybenzylidene)-3-methylbenzohydrazide
copper(II) complex [CuL1(NCS)]
-
L1 is the deprotonated form of N'-(2-hydroxybenzylidene)-3-methylbenzohydrazide. NCS is N-chlorsuccinimide
copper(II) complex [CuL3(NCS)]*CH3OH
-
L4 is the deprotonated form of 2-chloro-N'-(2-hydroxy-5-methoxybenzylidene)benzohydrazide
copper(II) complex [CuL4(NCS)]*0.4H2O
-
L5 is the dianionic form of N'-(2-hydroxybenzylidene)-3-methylbenzohydrazide
Hpn protein
-
synthesis and purifcation of the 7 kDa protein, the synthetic nickel-binding histidine-rich protein designated Hpn is capable of abrogating urease activity of live Heicobacter pylori in liquid cultures due to inhibition of nickel uptake into cells
-
oxovanadium complex [VOL(AHA)]
-
reaction of N'-(3-bromo-2-hydroxybenzylidene)-4-methoxybenzohydrazide and acetohydroxamic acid with VO(acac)2 in methanol gives the complex [VOL(AHA)]. The benzohydrazone ligand, in its dianionic form, coordinates to V atom through the phenolate oxygen, imino nitrogen and enolate oxygen. The acetohydroxamic acid coordinates to V atom through the carbonyl oxygen and deprotonated hydroxyl oxygen. The V atom is in octahedral coordination. The percent inhibition at concentration of 0.1 mM/l on Helicobacter pylori urease is 78% for the oxovanadium complex
peptides
-
TFLPQPRCSALLRYLSEDGVIVPS and YDFYWW, no inhibition of the enzyme from Bacillus pasteurii and Canavalia ensiformis
additional information
-
enzyme inhibition by flavonoids from tropicaal herb Calopogonium mucunoides,overview. No or poor inhibition by cabreuvin and 7-O-methylpseudobaptigenin
-
additional information
-
evaluation of 3-,6-,7-,9-,12-monohydroxy tetradecanoic acids as enzyme inhibitors in agriculture, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ni2+
-
supplementation of growth medium by nickel leads to tenfold increase in enzyme activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
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
-
0.2
Urea
-
range Km: 0.2-0.8 mM, pH 8.0, temperature not specified in the publication
0.21
Urea
-
pH 6.8, 37°C, Vmax: 1200 micromol/min/mg, in the presence of preservatives PEG or glycerol
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00741
3-[(4-[[5-(2-bromophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.00225
3-[(4-[[5-(2-chlorophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.00029
3-[(4-[[5-(2-fluorophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.01585
3-[(4-[[5-(3-bromophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.01406
3-[(4-[[5-(3-chlorophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.00512
3-[(4-[[5-(3-fluorophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.01397
3-[(4-[[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.00608
3-[(4-[[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.0024
3-[(4-[[5-(4-fluorophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]-4-hydroxy-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.0056
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)(4-[[5-(2-methoxyphenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)methyl]-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.01522
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)(4-[[5-(2-methylphenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)methyl]-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.0153
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)(4-[[5-(3-methoxyphenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)methyl]-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.03844
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)(4-[[5-(3-methylphenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)methyl]-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.01469
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)(4-[[5-(3-nitrophenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)methyl]-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.0105
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)(4-[[5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)methyl]-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.02336
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)(4-[[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]amino]phenyl)methyl]-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.00012
4-hydroxy-3-[(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)[4-([5-[4-(trifluoromethyl)phenyl]-1,3,4-thiadiazol-2-yl]amino)phenyl]methyl]-2H-1-benzopyran-2-one
Helicobacter pylori
30°C, pH not specified in the publication
0.03102
hydroxy[3-(5-[4-[(4-hydroxy-2-oxo-2H-1-benzopyran-3-yl)(4-hydroxy-2-oxo-3,4-dihydro-2H-1-benzopyran-3-yl)methyl]anilino]-1,3,4-thiadiazol-2-yl)phenyl]oxoammonium
Helicobacter pylori
30°C, pH not specified in the publication
0.101
12-hydroxytetradecanoic acid
Helicobacter pylori
-
pH and temperature not specified in the publication
0.227
2-[2-(3,4-dimethoxyphenyl)ethyl]phenol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.1
3-hydroxytetradecanoic acid
Helicobacter pylori
-
pH and temperature not specified in the publication
0.079
4-butylbenzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0079
4-butylbenzene-1,2-diol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.124
4-decylbenzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.168
4-dodecylbenzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.034
4-ethylbenzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0049
4-ethylbenzene-1,2-diol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.091
4-hexylbenzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0123
4-hexylbenzene-1,2-diol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.103
4-octylbenzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.058
4-octylbenzene-1,2-diol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.25
4-tetradecylbenzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.069
4-[2-(3,4-diethoxyphenyl)ethyl]benzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.071
4-[2-(3,4-dimethoxyphenyl)ethyl]benzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0227
4-[2-(3,4-dimethoxyphenyl)ethyl]benzene-1,2-diol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.204
4-[2-(3,4-dimethoxyphenyl)ethyl]phenol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.052
4-[2-(3-bromophenyl)ethyl]benzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0169
4-[2-(3-bromophenyl)ethyl]benzene-1,2-diol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.235
4-[2-(3-chlorophenyl)ethyl]-1,2-dimethoxybenzene
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.05
4-[2-(3-chlorophenyl)ethyl]benzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0157
4-[2-(3-chlorophenyl)ethyl]benzene-1,2-diol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.048
4-[2-(4-bromophenyl)ethyl]benzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.254
4-[2-(4-chlorophenyl)ethyl]-1,2-dimethoxybenzene
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.047
4-[2-(4-chlorophenyl)ethyl]benzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0083
4-[2-(4-chlorophenyl)ethyl]benzene-1,2-diol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.043
4-[2-(4-fluorophenyl)ethyl]benzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0062
4-[2-(4-fluorophenyl)ethyl]benzene-1,2-diol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.032
4-[2-(4-hydroxyphenyl)ethyl]benzene-1,2,3-triol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0015
4-[2-(4-hydroxyphenyl)ethyl]benzene-1,2-diol
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.07
6-hydroxytetradecanoic acid
Helicobacter pylori
-
pH and temperature not specified in the publication
0.0079
7-hydroxy-3-(4-hydroxyphenyl)-4H-1-benzopyran-4-one
Helicobacter pylori
-
pH 8.2, 30°C
0.09
7-hydroxytetradecanoic acid
Helicobacter pylori
-
pH and temperature not specified in the publication
0.083
9-hydroxytetradecanoic acid
Helicobacter pylori
-
pH and temperature not specified in the publication
0.0084
N'-(2-bromobenzylidene)-2-(4-nitrophenoxy)acetohydrazide
Helicobacter pylori
-
23°C, pH not specified in the publication
0.0202
N'-(4-nitrobenzylidene)-2-(4-nitrophenoxy)acetohydrazide
Helicobacter pylori
-
23°C, pH not specified in the publication
0.0172
N-hydroxyacetamide
Helicobacter pylori
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 10
-
pH 4.5: about 45% of maximal activity, pH 10.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
effects of urease added to rabbit platelets are assessed turbidimetrically. Fluorescein-labelled HPU bound to platelets but not to erythrocytes. HPU induces aggregation of rabbit platelets accompanied by ATP secretion. No correlation is found between platelet activation and ureolytic activity of HPU
physiological function
-
the bacterium typically colonizes the mucosal lining of the stomach, where the increase in pH of the strongly acidic environment allows the bacterium that requires pH 6-8 to grow, to persist in the hostile conditions. Concomitantly it incurs damage to the host tissue, thereby giving rise to gastritis and gastroduodenal ulcers. The damaging factors are ammonia and monochloramine
physiological function
-
the biosynthesis of the active metal-bound form of the nickel-dependent enzyme urease involves the formation of a lysine-carbamate functional group concomitantly with the delivery of two Ni2+- ions into the precast active site of the apoenzyme and with GTP hydrolysis. In the urease system, this role is performed by UreG, an accessory protein belonging to the group of homologous P-loop GTPases
physiological function
-
neutralization of acid by ammonia is essential for gastric Helicobacter pylori colonization
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
-
SDS-PAGE, subunits of the purified urease are shown to be stoichiometrically equal, with estimated molecular masses of 63 kDa and 29kDa
63000
-
SDS-PAGE, subunits of the purified urease are shown to be stoichiometrically equal, with estimated molecular masses of 63 kDa and 29kDa
64300
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dodecamer
the enzyme consists of a spherical assembly composed of four (alphabeta)3 units having three-fold symmetry. It has a dodecameric ((alphabeta)3)4 architecture
hexamer
hexamer
-
purified enzyme may be a hexameric aggregate, consistent with the reported stoichiometry of (29-63 kDa) * 6 of Helicobacter pylori
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stability at 4°C is enhanced by addition of glycerol or 2-mercaptoethanol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using ammonium sulfate precipitation, dialysis, and anion exchange chromatography
-
using NH4(SO4)2 precipitation, phenyl-Sepharose column chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
drug development
-
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
-
urease is considered a first line target for drug development and vaccination against Helicobacter pylori infection
medicine
-
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
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Houimel, M.; Mach, J.P.; Corthesy-Theulaz, I.; Fisch, I.
New inhibitors of Helicobacter pylori urease holoenzyme selected from phage-displayed peptide libraries
Eur. J. Biochem.
262
774-780
1999
Sporosarcina pasteurii, Canavalia ensiformis, Helicobacter pylori
Perez-Perez, G.I.; Gower, C.B.; Blaser, M.J.
Effects of cations on Helicobacter pylori urease activity, release, and stability
Infect. Immun.
62
299-302
1994
Helicobacter pylori
Turbett, G.R.; Hoj, P.B.; Horne, R.; Mee, B.J.
Purification and characterization of the urease enzymes of Helicobacter species from humans and animals
Infect. Immun.
60
5259-5266
1992
Helicobacter felis, Helicobacter mustelae, Helicobacter pylori
Segal, E.D.; Shon, J.; Tompkins, L.S.
Characterization of Helicobacter pylori urease mutants
Infect. Immun.
60
1883-1889
1992
Helicobacter pylori
Evans, D.J.; Evans, D.G.; Kirkpatrick, S.S.; Graham, D.Y.
Characterization of the Helicobacter pylori urease and purification of its subunits
Microb. Pathog.
10
15-26
1991
Helicobacter pylori
Agha, A.; Opekun, A.R.; Abudayyeh, S.; Graham, D.Y.
Effect of different organic acids (citric, malic and ascorbic) on intragastric urease activity
Aliment. Pharmacol. Ther.
21
1145-1148
2005
Helicobacter pylori
Belzer, C.; Stoof, J.; Beckwith, C.S.; Kuipers, E.J.; Kusters, J.G.; van Vliet, A.H.
Differential regulation of urease activity in Helicobacter hepaticus and Helicobacter pylori
Microbiology
151
3989-3995
2005
Helicobacter pylori, Helicobacter hepaticus
Xiao, Z.P.; Shi, D.H.; Li, H.Q.; Zhang, L.N.; Xu, C.; Zhu, H.L.
Polyphenols based on isoflavones as inhibitors of Helicobacter pylori urease
Bioorg. Med. Chem.
15
3703-3710
2007
Helicobacter pylori
Schwartz, J.T.; Allen, L.A.
Role of urease in megasome formation and Helicobacter pylori survival in macrophages
J. Leukoc. Biol.
79
1214-1225
2006
Helicobacter pylori
Becker-Ritt, A.B.; Martinelli, A.H.; Mitidieri, S.; Feder, V.; Wassermann, G.E.; Santi, L.; Vainstein, M.H.; Oliveira, J.T.; Fiuza, L.M.; Pasquali, G.; Carlini, C.R.
Antifungal activity of plant and bacterial ureases
Toxicon
50
971-983
2007
Canavalia ensiformis (P07374), Glycine max (Q7XAC5), Glycine max, Helicobacter pylori (Q84F75), Helicobacter pylori
Li, H.Q.; Xiao, Z.P.; Yin-Luo, Z.P.; Yan, T.; Lv, P.C.; Zhu, H.L.
Amines and oximes derived from deoxybenzoins as Helicobacter pylori urease inhibitors
Eur. J. Med. Chem.
44
2246-2251
2009
Helicobacter pylori
Hassani, A.R.; Ordouzadeh, N.; Ghaemi, A.; Amirmozafari, N.; Hamdi, K.; Nazari, R.
In vitro inhibition of Helicobacter pylori urease with non and semi fermented Camellia sinensis
Indian J. Med. Microbiol.
27
30-34
2009
Helicobacter pylori
Wassermann, G.E.; Olivera-Severo, D.; Uberti, A.F.; Carlini, C.R.
Helicobacter pylori urease activates blood platelets through a lipoxygenase-mediated pathway
J. Cell. Mol. Med.
14
2025-2034
2010
Helicobacter pylori
Gang, J.G.; Yun, S.K.; Hwang, S.Y.
Helicobacter pylori urease may exist in two forms: evidence from the kinetic studies
J. Microbiol. Biotechnol.
19
1565-1568
2009
Helicobacter pylori
Krajewska, B.
Ureases I. Functional, catalytic and kinetic properties: A review
J. Mol. Catal. B
59
9-21
2009
Klebsiella aerogenes, Pseudarthrobacter oxydans, Aspergillus nidulans, Aspergillus niger, Sporosarcina pasteurii, Corynebacterium ammoniagenes, Cajanus cajan, Canavalia ensiformis, Coccidioides immitis, Helicobacter pylori, Limosilactobacillus fermentum, Limosilactobacillus reuteri, Otala lactea, Proteus mirabilis, Providencia rettgeri, Providencia stuartii, Schizosaccharomyces pombe, Selenomonas ruminantium, Staphylococcus saprophyticus, Staphylococcus sp., Staphylococcus xylosus, Streptococcus mitior, Ureaplasma urealyticum, Staphylococcus leei, Brucella suis, Pseudomonas, Klebsiella, Arthrobacter mobilis, Nitellopsis obtusa
-
Zambelli, B.; Turano, P.; Musiani, F.; Neyroz, P.; Ciurli, S.
Zn2+-linked dimerization of UreG from Helicobacter pylori, a chaperone involved in nickel trafficking and urease activation
Proteins
74
222-239
2009
Helicobacter pylori
Xiao, Z.P.; Ma, T.W.; Fu, W.C.; Peng, X.C.; Zhang, A.H.; Zhu, H.L.
The synthesis, structure and activity evaluation of pyrogallol and catechol derivatives as Helicobacter pylori urease inhibitors
Eur. J. Med. Chem.
45
5064-5070
2010
Helicobacter pylori
Sokmen, B.B.; Hasdemir, B.; Yusufoglu, A.; Yanardag, R.
Some monohydroxy tetradecanoic acid isomers as novel urease and elastase inhibitors and as new antioxidants
Appl. Biochem. Biotechnol.
172
1358-1364
2014
Helicobacter pylori
Heyl, K.A.; Fischer, A.; Goebel, U.B.; Henklein, P.; Heimesaat, M.M.; Bereswill, S.
Inhibition of Helicobacter pylori urease activity in vivo by the synthetic nickel binding protein Hpn
Eur. J. Microbiol. Immunol. (Bp.)
3
77-80
2013
Helicobacter pylori
Ndemangou, B.; Sielinou, V.T.; Vardamides, J.C.; Ali, M.S.; Lateef, M.; Iqbal, L.; Afza, N.; Nkengfack, A.E.
Urease inhibitory isoflavonoids from different parts of Calopogonium mucunoides (Fabaceae)
J. Enzyme Inhib. Med. Chem.
28
1156-1161
2013
Helicobacter pylori
Sheng, G.H.; Chen, X.F.; Li, J.; Chen, J.; Xu, Y.; Han, Y.W.; Yang, T.; You, Z.; Zhu, H.L.
Synthesis, crystal structures and urease inhibition of N-(2-bromobenzylidene)-2-(4-nitrophenoxy) acetohydrazide and N-(4-nitrobenzylidene)-2-(4-nitrophenoxy)acetohydrazide
Acta Chim. Slov.
62
940-946
2015
Helicobacter pylori, Helicobacter pylori ATCC 43504
Alomari, M.; Taha, M.; Imran, S.; Jamil, W.; Selvaraj, M.; Uddin, N.; Rahim, F.
Design, synthesis, in vitro evaluation, molecular docking and ADME properties studies of hybrid bis-coumarin with thiadiazole as a new inhibitor of urease
Bioorg. Chem.
92
103235
2019
Helicobacter pylori (P14916), Helicobacter pylori ATCC 700392 (P14916)
Qu, D.; Niu, F.; Zhao, X.; Yan, K.X.; Ye, Y.T.; Wang, J.; Zhang, M.; You, Z.
Synthesis, crystal structures, and urease inhibition of an acetohydroxamate-coordinated oxovanadium(V) complex derived from N-(3-bromo-2-hydroxybenzylidene)-4-methoxybenzohydrazide
Bioorg. Med. Chem.
23
1944-1949
2015
Helicobacter pylori, Helicobacter pylori ATCC 43504
Pan, L.; Wang, C.; Yan, K.; Zhao, K.; Sheng, G.; Zhu, H.; Zhao, X.; Qu, D.; Niu, F.; You, Z.
Synthesis, structures and Helicobacter pylori urease inhibitory activity of copper(II) complexes with tridentate aroylhydrazone ligands
J. Inorg. Biochem.
159
22-28
2016
Helicobacter pylori, Helicobacter pylori ATCC 43504
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