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Information on EC 3.5.1.5 - urease
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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
- ulcer
-
endoscopy
-
eradication
- gastritis
-
breath
- gastrointestinal
- mucosa
- ammonia
- duodenal
- stomach
-
peptic
- antral
- catalase
-
serology
-
dyspeptic
- metronidazole
- amoxicillin
-
pylori-positive
- nitrate
- clarithromycin
- omeprazole
- nickel
- campylobacter
-
gastroduodenal
-
bismuth
- mirabilis
-
anti-h
-
giemsa
-
microbiological
- corpus
-
stool
- proteus
- invertase
- ranitidine
- food industry
-
nitrification
-
manure
-
compost
- nutrition
-
gastroenterology
-
pylori-induced
- felis
-
antisecretory
- calculi
-
sydney
- lansoprazole
- synthesis
- medicine
- biotechnology
- drug development
- analysis
-
intention-to-treat
-
amend
-
pylori-infected
-
epigastric
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
jack bean urease, canatoxin, acid urease, jbure-ii, embryo-specific soybean urease, urea amidohydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid urease
Arthritogenic cationic 19 kDa antigen
-
-
-
-
canatoxin
-
presence of a family of urease related genes in Canavalia ensiformis with at least three members: canatoxin, JBU and JBURE-II
JBU
JBURE-II
Urea amidohydrolase
urease
JBU
presence of a family of urease related genes in Canavalia ensiformis with at least three members: canatoxin, JBU and JBURE-II
JBURE-II
family of urease related genes in Canavalia ensiformis with at least three members: canatoxin, JBU and JBURE-II
Urea amidohydrolase
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-
-
-
urease
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
urea + H2O = CO2 + 2 NH3
active site contains three ionazable groups with pKa-values of 5.3, 6.6 and 9.0 that participate both in catalysis and substrate binding
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urea + H2O = CO2 + 2 NH3
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
condensation
-
-
-
-
carboxylic acid amide hydrolysis
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
urea amidohydrolase
A nickel protein.
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CAS REGISTRY NUMBER
COMMENTARY
9002-13-5
-
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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
hydroxyurea
HCO3- + NH4+ + NH2OH
-
using kinetic isotope effects it is shown that hydroxyurea exhibits biphasic kinetics with a rapid burst phase, followed by a very slow plateau phase. The plateau phase is attributed to irreversible substrate inhibition. The product, hydroxylamine, is shown to be a weak but reversible inhibitor of urease, it is not the cause of the plateau phase
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-
?
urea + H2O
?
urea can be utilized as a nitrogen source via a urease-dependent pathway, the ureolysis can protect the organism against environmental acidification at physiologically relevant pH values. Therefor, urease can confer to Actinomyces naeslundii critical selective advantages over nonureolytic organisms in dental plaque
-
-
?
urea + H2O
?
bacterium strain SL100
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urease may be a virulence factor during colonization of the stomach
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-
-
urea + H2O
?
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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
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-
?
urea + H2O
?
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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
?
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enzyme is induced by urea and short-chain amides, repressed by excess ammonia
-
-
?
urea + H2O
?
-
expression increases 10fold upon nitrogen deprivation, the enzyme is involved in nitrogen aquisition by the bacterium
-
-
?
urea + H2O
?
-
urease is a critical virulence factor in urinary tract infection
-
-
?
urea + H2O
CO2 + 2 NH3
-
-
-
-
?
urea + H2O
CO2 + NH3
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-
-
-
?
urea + H2O
CO2 + NH3
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reverse reaction in water-organic solvent mixtures, the nature of the nonaqueous component of the solvent effects both the rate of the reaction and the position of the equilibrium
-
r
urea + H2O
CO2 + NH3
-
reverse reaction in water-organic solvent mixtures, the nature of the nonaqueous component of the solvent effects both the rate of the reaction and the position of the equilibrium
-
r
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
?
-
-
insecticidal activity of the jack bean ureases JBU and canatoxin. JBU and canatoxin are able to induce activation of rabbit blood platelets
-
-
-
additional information
?
-
-
insecticidal activity of the jack bean ureases JBU and canatoxin. JBU is slightly less toxic than canatoxin. JBU isnot lethal to mice or rats when given intraperitoneally. JBU and canatoxin are able to induce activation of rabbit blood platelets
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-
-
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. Ureases probably contribute to the plant arsenal of defense compounds against predators and phytopathogens
-
-
-
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. Ureases probably contribute to the plant arsenal of defense compounds against predators and phytopathogens
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-
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additional information
?
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-
Cotton seed urease displays low ureolytic activity but exhibits potent antifungal properties at sub-micromolar concentrations against different phytopathogenic fungi. The antifungal effect of cotton urease persists after treatment with an irreversible inhibitor of its enzyme activity. The data suggest an important role of the protein in plant defense
-
-
-
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
?
-
by incubating the enzyme (50 U/L) at 20°C for 60 h, about 95.8% of urea in rice wine is removed
-
-
-
additional information
?
-
by incubating the enzyme (50 U/L) at 20°C for 60 h, about 95.8% of urea in rice wine is removed
-
-
-
additional information
?
-
by incubating the enzyme (50 U/L) at 20°C for 60 h, about 95.8% of urea in rice wine is removed
-
-
-
additional information
?
-
by incubating the enzyme (50 U/L) at 20°C for 60 h, about 95.8% of urea in rice wine is removed
-
-
-
additional information
?
-
by incubating the enzyme (50 U/L) at 20°C for 60 h, about 95.8% of urea in rice wine is removed
-
-
-
additional information
?
-
by incubating the enzyme (50 U/L) at 20°C for 60 h, about 95.8% of urea in rice wine is removed
-
-
-
additional information
?
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platelet aggregation induced by Bacillus pasteurii urease is mediated by lipoxygenase-derived eicosanoids and secretion of ADP from the platelets through a calcium-dependent mechanism
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-
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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
?
Q9Z395
urea can be utilized as a nitrogen source via a urease-dependent pathway, the ureolysis can protect the organism against environmental acidification at physiologically relevant pH values. Therefor, urease can confer to Actinomyces naeslundii critical selective advantages over nonureolytic organisms in dental plaque
-
-
?
urea + H2O
?
bacterium strain SL100
-
urease may be a virulence factor during colonization of the stomach
-
-
-
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
?
-
enzyme is induced by urea and short-chain amides, repressed by excess ammonia
-
-
?
urea + H2O
?
-
expression increases 10fold upon nitrogen deprivation, the enzyme is involved in nitrogen aquisition by the bacterium
-
-
?
urea + H2O
?
-
urease is a critical virulence factor in urinary tract infection
-
-
?
additional information
?
-
-
insecticidal activity of the jack bean ureases JBU and canatoxin. JBU and canatoxin are able to induce activation of rabbit blood platelets
-
-
-
additional information
?
-
-
insecticidal activity of the jack bean ureases JBU and canatoxin. JBU is slightly less toxic than canatoxin. JBU isnot lethal to mice or rats when given intraperitoneally. JBU and canatoxin are able to induce activation of rabbit blood platelets
-
-
-
additional information
?
-
P07374
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. Ureases probably contribute to the plant arsenal of defense compounds against predators and phytopathogens
-
-
-
additional information
?
-
Q7XAC5
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. Ureases probably contribute to the plant arsenal of defense compounds against predators and phytopathogens
-
-
-
additional information
?
-
-
Cotton seed urease displays low ureolytic activity but exhibits potent antifungal properties at sub-micromolar concentrations against different phytopathogenic fungi. The antifungal effect of cotton urease persists after treatment with an irreversible inhibitor of its enzyme activity. The data suggest an important role of the protein in plant defense
-
-
-
additional information
?
-
Q84F75
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
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-
-
additional information
?
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B3XPZ2
by incubating the enzyme (50 U/L) at 20°C for 60 h, about 95.8% of urea in rice wine is removed
-
-
-
additional information
?
-
B3XPZ3
by incubating the enzyme (50 U/L) at 20°C for 60 h, about 95.8% of urea in rice wine is removed
-
-
-
additional information
?
-
B3XPZ4
by incubating the enzyme (50 U/L) at 20°C for 60 h, about 95.8% of urea in rice wine is removed
-
-
-
additional information
?
-
B3XPZ2
by incubating the enzyme (50 U/L) at 20°C for 60 h, about 95.8% of urea in rice wine is removed
-
-
-
additional information
?
-
B3XPZ3
by incubating the enzyme (50 U/L) at 20°C for 60 h, about 95.8% of urea in rice wine is removed
-
-
-
additional information
?
-
B3XPZ4
by incubating the enzyme (50 U/L) at 20°C for 60 h, about 95.8% of urea in rice wine is removed
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
-
maximum activity at 18-23% NaCl at 50°C, loses activity irreversibly in the absence of NaCl
Ni2+
Nickel
Ni2+
-
soybean urease is inactive when soybean cell cultures are grown in the absence of nickel
Ni2+
urease activation: apoprotein (UreABC)3 + 6 Ni2+
Nickel
-
nickel metalloenzyme; study of nickel environment in the enzyme
Nickel
-
enzyme contains 2 gatom of nickel per 96600 g of protein; nickel metalloenzyme
Nickel
-
contains 0.8 gatom of nickel per 67000 g of protein; contains 1 atom of nickel per subunit; nickel metalloenzyme
Nickel
-
nickel metalloenzyme; 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
-
nickel metalloenzyme; partial activation of the apoprotein in presence of Ni(II) and CO2, incubation with Ni alone leads to the formation of inactive proteins
Nickel
-
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 metalloenzyme
Nickel
-
contains about 6 Ni2+ ions per urease molecule; nickel metalloenzyme
Nickel
-
His320 of subunit C is essential for urea hydrolysis and Ni2+ binding within the native enzyme; nickel metalloenzyme
Nickel
-
nickel metalloenzyme; 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
Nickel
-
each of the 4 subunits contains 1 atom of nickel; nickel metalloenzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2-[[(2-[[2-(hydroxy-kappaO)ethyl]amino-kappaN]ethyl)imino-kappaN]methyl]-4-nitrophenolato-kappaO)(methoxymethanolato-kappaO)zinc
-
-
(2-[[(2-[[2-(hydroxy-kappaO)ethyl]amino-kappaN]ethyl)imino-kappaN]methyl]-4-nitrophenolato-kappaO)(nitrato-kappaO)copper
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-
(E)-1-(3-nitrobenzylidene)thiosemicarbazide
-
competitive mechanism of inhibition
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
1-benzyl-2-ethyl-6,6-dimethyl-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
1-benzyl-2-ethyl-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
1-ethoxy-2-ethyl-6,6-dimethyl-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
1-ethoxy-2-ethyl-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
2,4,4',6-tetrahydroxy-3-methoxyphenyldeoxybenzoin
-
0.4 mg/ml, 17% inhibition
2,4,6-trimethyl-N-([1-[(2,4,6-trimethylphenyl)sulfonyl]piperidin-4-yl]methyl)benzenesulfonamide
-
50% inhibition at 0.038 mM
2-(4-hydroxyphenyl)-1-(2,4,6-trihydroxy-3-methoxyphenyl)ethanone oxime
-
-
2-ethyl-1-(2-phenylethyl)-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
2-ethyl-1-(4-methoxycyclohexyl)-6,6-dimethyl-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
2-ethyl-1-(4-methoxyphenyl)-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
2-ethyl-6-[2-(ethylsulfanyl)propyl]-1-(4-methoxyphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
2-thioxo-5-(2,3,4-trihydroxybenzylidene)dihydro-4,6(1H,5H)-pyrimidinedione
-
-
2-[(1E)-N-(allyloxy)butanimidoyl]-5,5-dimethylcyclohexane-1,3-dione
-
chelator of the nickel atom in enzyme metallocenter
2-[(1E)-N-ethoxybutanimidoyl]-5,5-dimethylcyclohexane-1,3-dione
-
chelator of the nickel atom in enzyme metallocenter
2-[(2S,4R)-2-(4-fluorophenyl)-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
-
-
2-[(2S,4R)-2-phenyl-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
-
-
2-[2-(1,3-benzodioxol-5-yl)-2,3-dihydro-1,5-benzothiazepin-4-yl]phenol
-
-
3,3'-[(1E)-1-phenylprop-1-ene-3,3-diyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(3,4,5-trimethoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(3,4-dimethoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(3-ethoxy-4-hydroxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[[4-(1-methylethyl)phenyl]methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[[4-(dimethylamino)phenyl]methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3-methyl-N-[[1-(3-methylbut-2-en-1-yl)piperidin-4-yl]methyl]but-2-en-1-amine
-
50% inhibition at 0.063 mM
3-phenoxy-N-[[1-(3-phenoxypropyl)piperidin-4-yl]methyl]propan-1-amine
-
50% inhibition at 0.043 mM
3-[(2-acetylanilino)methylidene]-8-methyl-2H-pyrido[1,2-a]-pyrimidine-2,4-dione
-
54% inhibition at 0.01 mM
3-[(2-fluoroanilino)methylidene]-8-methyl-2H-pyrido[1,2-a]-pyrimidine-2,4-dione
-
44% inhibition at 0.01 mM
3-[(3-acetylanilino)methylidene]-8-methyl-2H-pyrido[1,2-a]-pyrimidine-2,4-dione
-
28% inhibition at 0.01 mM
3-[(3-fluoroanilino)methylidene]-8-methyl-2H-pyrido[1,2-a]-pyrimidine-2,4-dione
-
3% inhibition at 0.01 mM
3-[(4-acetylanilino)methylidene]-8-methyl-2H-pyrido[1,2-a]pyrimidine-2,4-dione
-
5% inhibition at 0.01 mM
3-[(4-fluoroanilino)methylidene]-8-methyl-2H-pyrido[1,2-a]pyrimidine-2,4-dione
-
21% inhibition at 0.01 mM
3-[(mesitylamino)methylidene]-8-methyl-2H-pyrido[1,2-a]pyrimidine-2,4-dione
-
-
4-(2,3-dimethylphenyl)-5-phenyl-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
4-(2,4-dichlorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
-
-
4-(2,4-difluorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
-
-
4-(2,4-dimethylphenyl)-5-(3-nitrophenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
4-(2,5-dichlorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
-
-
4-(3,4-dichlorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
-
-
4-(3,4-difluorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
-
-
4-(3,4-dimethoxyphenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
-
-
4-(4-bromophenyl)-5-[hydroxy(phenyl)methyl]-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
4-(4-chlorophenyl)-5-[hydroxy(phenyl)methyl]-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
4-(9-methyl-9H-carbazol-3-yl)-6-(2,4,6-trimethoxyphenyl)-pyrimidin-2-amine
-
-
4-bromo-N'-[[8-methyl-2,4-dioxo-2H-pyrido[1,2-a]pyrimidin-3(4H)-ylidene]methyl]benzohydrazide
-
23% inhibition at 0.01 mM
4-chloro-N'-[[8-methyl-2,4-dioxo-2H-pyrido[1,2-a]pyrimidin-3(4H)-ylidene]methyl]benzohydrazide
-
14% inhibition at 0.01 mM
4-hydroxy-3-[(2E)-1-(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)-3-phenylprop-2-en-1-yl]-2H-chromen-2-one
4-hydroxy-3-[(2E)-1-(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)but-2-en-1-yl]-2H-chromen-2-one
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(1H-indol-3-yl)methyl]-2H-chromen-2-one
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(1H-pyrrol-3-yl)methyl]-2H-chromen-2-one
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(3-methoxyphenyl)methyl]-2H-chromen-2-one
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(pyridin-4-yl)methyl]-2H-chromen-2-one
4-hydroxy-N'-[[8-methyl-2,4-dioxo-2H-pyrido[1,2-a]pyrimidin-3(4H)-ylidene]methyl]benzohydrazide
-
22% inhibition at 0.01 mM
4-methyl-N-([1-[(4-methylphenyl)sulfonyl]piperidin-4-yl]methyl)benzenesulfonamide
-
50% inhibition at 0.042 mM
4-nitro-N'-[[8-methyl-2,4-dioxo-2H-pyrido[1,2-a]pyrimidin-3(4H)-ylidene]methyl] benzohydrazide
-
60% inhibition at 0.01 mM
4-nitro-N-([1-[(4-nitrophenyl)sulfonyl]piperidin-4-yl]methyl)benzenesulfonamide
-
50% inhibition at 0.032 mM
5-(1,4-dihydro-9-anthracenylmethylene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(1H-indol-3-ylmethylene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(2,4-dihydroxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(2-bromo-4,5-dimethoxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(2-hydroxy-3-methoxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(2-hydroxy-5-methoxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(2-methylbenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(3,4-dihydroxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(3,4-dimethoxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(3,5-dibromo-4-hydroxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(3,5-dichloro-2-hydroxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(3-chlorophenyl)-4-(2,4-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
5-(3-chlorophenyl)-4-(2,6-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
5-(3-hydroxy-4-methoxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(4-bromo-2,5-dimethoxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(4-chlorophenyl)-4-(2,4-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
5-(4-ethoxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(4-hydroxy-3,5-dimethoxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(4-hydroxy-3-iodo-5-methoxybenzylidene)-2-thioxodihydro-4,6(1H,5H) pyrimidinedione
-
-
5-(4-pyridinylmethylene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(4-[[4,6-dioxo-2-thioxotetrahydro-5(2H)pyrimidinylidene]methyl]-benzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-hydroxy-1,4-naphthoquinone
-
5-hydroxy-1,4-naphthoquinone, juglone, acts as a strong, time and concentration dependent inactivator of urease. The reactivation of juglone-modified urease shows the participation of reversible and irreversible contribution in the inactivation. In the presence of an excess of DTT, urease inactivated by juglone regains 70% of its activity. The reversible inactivation is attributed to oxidation of the essential urease thiols by reactive oxygen species (ROS) realizing during reduction of juglone to seminaphthoquinone. The irreversible contribution in the inhibition is assumed as an arylation of urease thiol groups by juglone
5-[(2-hydroxy-1-naphthyl)methylene]-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-[(5-methyl-2-furyl)methylene]-2-thioxodihydro-4,6(1H,5H)pyrimidinedione
-
-
5-[(6-bromo-4-chloro-2-oxo-2H-chromen-3-yl)methylene]-2-thioxodihydro 4,6(1H,5H)-pyrimidinedione
-
-
5-[(6-methyl-2-pyridinyl)methylene]-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-[4(dimethylamino) benzylidene]-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-[4-(methylsulfanyl)benzylidene]-2-thioxodihydro-4,6(1H,5H) pyrimidinedione
-
-
5-[4-(tert-butyl-dimethyl-silanyloxy)-phenyl]-3H-[1,3,4]thiadiazole-2-thione
-
-
5-[hydroxy(phenyl)methyl]-4-(4-methylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
5-[hydroxy(phenyl)methyl]-4-(4-nitrophenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
6-(1-hydroxy-2-(4-methoxyphenyl)ethyl)-2,3-dimethoxyphenol
-
0.4 mg/ml, 42% inhibition
7'-hydroxy-2,2'-dioxo-3'-[(2-oxo-2H-chromen-7-yl)oxy]-2H,2'H-8,8'-bichromen-7-yl alpha-D-glucopyranoside
7'-methoxy-2,2'-dioxo-3'-[(2-oxo-2H-chromen-7-yl)oxy]-2H,2'H-8,8'-bichromen-7-yl alpha-D-glucopyranoside
8-hydroxy-3-[(6-hydroxy-2-oxo-2H-chromen-7-yl)oxy]-2-oxo-2H-chromen-7-yl beta-D-glucopyranoside
8-methyl-2H-pyrido[1,2-a]pyrimidine-2,4(3H)-dione
-
26% inhibition at 0.01 mM
8-methyl-3-[(2-sulfanylanilino)methylidene]-2H-pyrido[1,2-a]pyrimidine-2,4-dione
-
73% inhibition at 0.01 mM
8-methyl-3-[[(4-methyl-2-pyridinyl)amino]methylidene]-2Hpyrido[1,2-]pyrimidine-2,4-dione
-
20% inhibition at 0.01 mM
8-methyl-3-[[(5-methyl-2-pyridinyl)amino] methylidene]-2H-pyrido[1,2-]pyrimidine-2,4-dione
-
48% inhibition at 0.01 mM
8-methyl-3-[[(5-nitro-2-pyridinyl)amino] methylidene]-2H-pyrido[1,2-a]pyrimidine-2,4-dione
-
36% inhibition at 0.01 mM
Allicin
-
from garlic, inhibits the biofilm formation and urease activity in vitro in both prelysed and intact cells. A higher concentration of allicin is needed to inhibit the established biofilms
beta-(o-methoxyphenyl)-gamma,gamma-bis(8-quinolinoxy)germa-gamma-lactone
-
inhibition occurrs in a noncompetitive and concentration-dependent manner. Highly selective in inhibiting the growth of Proteus mirabilis at moderate concentrations. Potential to be developed as antimicrobial agents against Proteus mirabilis infection
beta-(o-methylphenyl)-gamma,gamma-bis(8-quinolinoxy)germa-gamma-lactone
-
inhibition occurrs in a noncompetitive and concentration-dependent manner. Highly selective in inhibiting the growth of Proteus mirabilis at moderate concentrations. Potential to be developed as antimicrobial agents against Proteus mirabilis infection
chloro(2-[[(2-[[2-(hydroxy-kappaO)ethyl]amino-kappaN]ethyl)imino-kappaN]methyl]-4-nitrophenolato-kappaO)copper
-
-
citrate
binding of the ligand to the active site involves stabilizing interactions, such as a carboxylate group that binds the nickel ions at the active site and several hydrogen bonds with the surrounding residues
dehydroascorbic acid
-
inhibitory action of dehydroascorbic acid is revealed in the presence of Fe3+ ions and found to be primarily mediated by H2O2. The resulting inhibition by dehydroascorbic acid -Fe3+ consists of enzyme thiol oxidation and its effectiveness grew with increasing pH
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
-
iodoacetamide
-
phosphate protects wild-type enzyme from inactivation, does not affect inactivation of C319S urease
L-ascorbic acid
-
in an unbuffered system L-ascorbic acid inactivates urease in a biphasic manner by denaturation brought about by ascorbic acid-lowered pH. In a buffered system neither ascorbic acid nor dehydroascorbic acid themselves are inhibitors of urease
methyl (7E)-7-[4,4-dimethyl-3-(3-methylisoxazol-5-yl)-2,6-dioxocyclohexyl]-7-(ethoxyimino)heptanoate
-
chelator of the nickel atom in enzyme metallocenter
methyl 2-[[(chloromethoxy)carbonyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
methyl 2-[[(chloromethoxy)carbonyl]amino]-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
methyl 2-[[(dichloromethoxy)carbonyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
methyl 2-[[(methylsulfanyl)carbonothioyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
methyl 3-(4-[[(3-methoxy-3-oxopropyl)amino]methyl]piperidin-1-yl)propanoate
-
50% inhibition at 0.019 mM
methyl 5-[(1E)-N-(allyloxy)butanimidoyl]-2,2-dimethyl-4,6-dioxocyclohexanecarboxylate
-
chelator of the nickel atom in enzyme metallocenter
methyl 5-[(1E)-N-ethoxybutanimidoyl]-2,2-dimethyl-4,6-dioxocyclohexanecarboxylate
-
chelator of the nickel atom in enzyme metallocenter
methyl 5-[(1E)-N-ethoxyethanimidoyl]-2,2-dimethyl-4,6-dioxocyclohexanecarboxylate
-
chelator of the nickel atom in enzyme metallocenter
N'-[[8-methyl-2,4-dioxo-2H-pyrido[1,2-a]pyrimidin-3(4H)-ylidene]methyl]-benzo-hydrazide
-
13% inhibition at 0.01 mM
Pb2+
-
inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+
peptides
-
TFLPQPRCSALLRYLSEDGVIVPS and YDFYWW, no inhibition of the enzyme from Bacillus pasteurii and Canavalia ensiformis
tetrachloro-o-benzoquinone
-
no recovery of urease activity bound in the urease-inhibitor complex after dilution or addition of dithiothreitol
triphenylbismuth difluoride
-
first-order rate constant for inactivation 0.00158 per s
tris(2,4,6-trimethylphenyl)bismuth
-
first-order rate constant for inactivation 0.0027 per s
tris(4-fluorophenyl)bismuth dichloride
-
first-order rate constant for inactivation 0.00158 per s
tris(4-fluorophenyl)bismuth difluoride
-
first-order rate constant for inactivation 0.00259 per s
tris(4-methylphenyl)bismuth dichloride
-
first-order rate constant for inactivation 0.00259 per s
(2S)-2-(dimethylamino)-3-(ethylthio)propan-1-ol
-
noncompetitive, 50% inhibition at 0.040 mM
(2S)-2-(dimethylamino)-3-(ethylthio)propan-1-ol
-
noncompetitive, 50% inhibition at 0.029 mM
(2S)-2-(dimethylamino)-3-ethoxypropane-1-thiol
-
noncompetitive, 50% inhibition at 0.100 mM
(2S)-2-(dimethylamino)-3-ethoxypropane-1-thiol
-
noncompetitive, 50% inhibition at 0.031 mM
(2S)-2-(dimethylamino)-3-ethoxypropane-1-thiol
-
noncompetitive, 50% inhibition at 0.020 mM
(2S)-2-(dimethylamino)-3-mercaptopropan-1-ol
-
noncompetitive, 50% inhibition at 0.022 mM
(2S)-2-(dimethylamino)-3-mercaptopropan-1-ol
-
noncompetitive, 50% inhibition at 0.025 mM
(2S)-2-(dimethylamino)-3-methoxypropane-1-thiol
-
noncompetitive, 50% inhibition at 0.035 mM
(2S)-2-(dimethylamino)-3-methoxypropane-1-thiol
-
noncompetitive, 50% inhibition at 0.036 mM
(R)-4-methoxydalbergione
-
50% inhibition at 0.067 mM, isolated from roots of Ranunculus repens
(R)-4-methoxydalbergione
-
50% inhibition at 0.059 mM, isolated from roots of Ranunculus repens
(R)-dalbergiophenol
-
50% inhibition at 0.035 mM, isolated from roots of Ranunculus repens
(R)-dalbergiophenol
-
50% inhibition at 0.025 mM, isolated from roots of Ranunculus repens
2,2'-bi-1,3,4-oxadiazole-5,5'(4H,4'H)-dithione
-
pH 8.2, IC50: below 0.125 mM
4-(4-benzoyl-5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)phenyl benzoate
-
pH 8.2, IC50: 0.234 mM
4-(4-benzoyl-5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)phenyl benzoate
-
-
4-amino-5-(4-hydroxyphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 8.2, IC50: below 0.125 mM
4-amino-5-(4-hydroxyphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
4-amino-5-pyridin-4-yl-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 8.2, IC50: 0.163 mM
4-hydroxy-3-[(2E)-1-(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)-3-phenylprop-2-en-1-yl]-2H-chromen-2-one
-
competitive inhibition
4-hydroxy-3-[(2E)-1-(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)-3-phenylprop-2-en-1-yl]-2H-chromen-2-one
-
competitive inhibition
4-hydroxy-3-[(2E)-1-(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)but-2-en-1-yl]-2H-chromen-2-one
-
competitive inhibition
4-hydroxy-3-[(2E)-1-(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)but-2-en-1-yl]-2H-chromen-2-one
-
uncompetitive inhibition
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(1H-indol-3-yl)methyl]-2H-chromen-2-one
-
competitive inhibition
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(1H-indol-3-yl)methyl]-2H-chromen-2-one
-
competitive inhibition; uncompetitive inhibition
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(1H-pyrrol-3-yl)methyl]-2H-chromen-2-one
-
competitive inhibition
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(1H-pyrrol-3-yl)methyl]-2H-chromen-2-one
-
uncompetitive inhibition
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(3-methoxyphenyl)methyl]-2H-chromen-2-one
-
competitive inhibition
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(3-methoxyphenyl)methyl]-2H-chromen-2-one
-
competitive inhibition
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(pyridin-4-yl)methyl]-2H-chromen-2-one
-
competitive inhibition
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(pyridin-4-yl)methyl]-2H-chromen-2-one
-
noncompetitive inhibition
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)methyl]-2H-chromen-2-one
-
competitive inhibition
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)methyl]-2H-chromen-2-one
-
competitive inhibition, enzyme-ligand interaction analysis, structure, overview
4-hydroxy-3-[1-(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)ethyl]-2H-chromen-2-one
-
competitive inhibition
4-hydroxy-3-[1-(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)ethyl]-2H-chromen-2-one
-
uncompetitive inhibition, enzyme-ligand interaction analysis, structure, overview
4-hydroxy-3-[1-(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)pentyl]-2H-chromen-2-one
-
competitive inhibition
4-hydroxy-3-[1-(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)pentyl]-2H-chromen-2-one
-
competitive inhibition
5-(1-naphthyl)-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
5-(3-hydroxyphenyl)-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
5-pyridin-4-yl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: above 0.2 mM
5-pyridin-4-yl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
5-pyridin-4-yl-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
5-[(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)methyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.095 mM
5-[(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)methyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.5 mM
5-[(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)methyl]-1,3,4-oxadiazole-2(3H)-thione
-
-
5-[(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)methyl]-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.095 mM
5-[(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)methyl]-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.5 mM
5-[(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)methyl]-1,3,4-thiadiazole-2(3H)-thione
-
-
5-[3-(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)propyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.093 mM
5-[3-(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)propyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
5-[3-(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)propyl]-1,3,4-oxadiazole-2(3H)-thione
-
-
5-[4-(benzyloxy)phenyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.41 mM
5-[4-(benzyloxy)phenyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.5 mM
5-[4-(tert-butyl-dimethyl-silanyloxy)-phenyl]-3H-[1,3,4]oxadiazole-2-thione
-
pH 8.2, IC50: 0.244 mM
5-[4-(tert-butyl-dimethyl-silanyloxy)-phenyl]-3H-[1,3,4]oxadiazole-2-thione
-
-
7'-hydroxy-2,2'-dioxo-2H,2'H-6,8'-bichromen-7-yl alpha-L-mannopyranoside
-
-
7'-hydroxy-2,2'-dioxo-2H,2'H-6,8'-bichromen-7-yl alpha-L-mannopyranoside
-
-
7'-hydroxy-2,2'-dioxo-3'-[(2-oxo-2H-chromen-7-yl)oxy]-2H,2'H-8,8'-bichromen-7-yl alpha-D-glucopyranoside
-
-
7'-hydroxy-2,2'-dioxo-3'-[(2-oxo-2H-chromen-7-yl)oxy]-2H,2'H-8,8'-bichromen-7-yl alpha-D-glucopyranoside
-
-
7'-methoxy-2,2'-dioxo-3'-[(2-oxo-2H-chromen-7-yl)oxy]-2H,2'H-8,8'-bichromen-7-yl alpha-D-glucopyranoside
-
-
7'-methoxy-2,2'-dioxo-3'-[(2-oxo-2H-chromen-7-yl)oxy]-2H,2'H-8,8'-bichromen-7-yl alpha-D-glucopyranoside
-
-
7-hydroxy-2,2'-dioxo-2H,2'H-6,8'-bichromen-7'-yl alpha-L-mannopyranoside
-
-
7-hydroxy-2,2'-dioxo-2H,2'H-6,8'-bichromen-7'-yl alpha-L-mannopyranoside
-
-
7-[(7-methoxy-2-oxo-2H-chromen-3-yl)oxy]-2-oxo-2H-chromen-6-yl alpha-D-glucopyranoside
-
-
7-[(7-methoxy-2-oxo-2H-chromen-3-yl)oxy]-2-oxo-2H-chromen-6-yl alpha-D-glucopyranoside
-
-
8-hydroxy-3-[(6-hydroxy-2-oxo-2H-chromen-7-yl)oxy]-2-oxo-2H-chromen-7-yl beta-D-glucopyranoside
-
-
8-hydroxy-3-[(6-hydroxy-2-oxo-2H-chromen-7-yl)oxy]-2-oxo-2H-chromen-7-yl beta-D-glucopyranoside
-
-
Acetohydroxamic acid
-
inhibits urease activity and biofilm formation in a dose-dependent manner
Ag+
-
time-dependent inhibition studies exhibit biphasic kinetics with heavy metal ions
Boric acid
-
competitive, maximal inhibition at pH 5.0, minimal inhibition at pH 10.0
Boric acid
-
competitive inhibition, which is a reversible reaction with residual activity at lower than 0.25 mM boric acid, maximal inhibition at pH 7.0-9.0 and 30°C. Boric acid binds to the active site of the enzyme
Boric acid
-
inhibits urease activity and biofilm formation in a dose-dependent manner
Cd2+
-
inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+
Cu2+
-
inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+. Enzyme immobilized on membranes modified with NH2NH2/H2SO4, NaOH + ethylenediamine or H2O2 is most sensitive to Cu2+
Cu2+
-
time-dependent inhibition studies exhibit biphasic kinetics with heavy metal ions
fluoride
-
two fluoride anions are coordinated to the Ni(II) ions in the active site, in terminal and bridging positions. One fluoride competitively binds to the Ni(II) ion proposed to coordinate urea in the initial step of the catalytic mechanism, while another fluoride uncompetitively substitutes the Ni(II)-bridging hydroxide, blocking its nucleophilic attack on urea. Kinetic studies on the fluoride-induced inhibition of urease, mixed competitive and predominant uncompetitive mechanism that increases by increasing the pH, and a lesser competitive inhibition that increases by lowering the pH, overview
Hg2+
-
time-dependent inhibition studies exhibit biphasic kinetics with heavy metal ions
Hydroxyurea
-
inhibits urease activity and biofilm formation in a dose-dependent manner
methyl 2-amino-4,5,6,7,8,9-hexahydrocycloocta[b]thiophene-3-carboxylate
-
-
methyl 2-amino-4,5,6,7,8,9-hexahydrocycloocta[b]thiophene-3-carboxylate
-
-
methyl 2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
-
-
methyl 2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
-
-
methyl 2-amino-5,6-dihydro-4H-cyclopenta[b]thiophene-3-carboxylate
-
-
methyl 2-[(methoxycarbonyl)amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
-
methyl 2-[(methoxycarbonyl)amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
-
methyl 2-[bis(chlorocarbonyl)amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
-
methyl 2-[bis(chlorocarbonyl)amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
-
methyl 2-[[(chloromethoxy)carbonyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
-
methyl 2-[[(chloromethoxy)carbonyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
-
methyl 2-[[(chloromethoxy)carbonyl]amino]-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
-
-
methyl 2-[[(chloromethoxy)carbonyl]amino]-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
-
-
methyl 2-[[(dichloromethoxy)carbonyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
-
methyl 2-[[(dichloromethoxy)carbonyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
-
methyl 2-[[(methylsulfanyl)carbonothioyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
-
methyl 2-[[(methylsulfanyl)carbonothioyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
-
N-(N'-benzyloxycarbonylglycyl)aminomethyl(P-methyl)phosphinothioic acid
-
-
N-dimethyl-S-methyl-L-cysteine
-
noncompetitive, 50% inhibition at 0.078 mM
N-dimethyl-S-methyl-L-cysteine
-
noncompetitive, 50% inhibition at 0.110 mM
N2-[(benzyloxy)carbonyl]-N-[[hydroxy(methyl)phosphoryl]methyl]glycinamide
-
-
N2-[(benzyloxy)carbonyl]-N-[[hydroxy(methyl)phosphoryl]methyl]glycinamide
-
-
Ni2+
-
inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+
phenylphosphorodiamidate
-
the inhibitor is able to thoroughly protect the flap cysteines from the further reaction with disulfides, this apparently resulting from the closed conformation of the flap. The inhibitor may be regarded as the most suitable inhibitor for active-site protection experiments in inhibition studies of urease
Thiourea
-
halogenated substituted thiourea derivatives are slightly less active than methoxy substituted compounds
Zn2+
-
inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+
additional information
-
not inhibitory: S-ethyl-L-cysteine, (2S)-2-(dimethylamino)-3-(ethylthio)propan-1-ol, (2S)-2-(dimethylamino)-3-mercaptopropan-1-ol, (2S)-2-(dimethylamino)-3-methoxypropane-1-thiol
-
additional information
-
specific cation-binding sites determining the structural dynamics of the enzyme-polyelectrolyte complex play the regulating role in the urease molecule
-
additional information
-
potent urease inhibitory activity of biscoumarins, mechanisms of inhibition using the nickel containing active sites of the enzyme, overview. The compounds competitively inhibit Jack bean urease through interactionwith the nickel metallocentre, as deduced from Michaelis-Menten kinetics, UV-visible absorbance spectroscopic, and molecular docking simulation studies
-
additional information
-
design, synthesis, molecular docking studies and in vitro screening of ethyl 4-(3-benzoylthioureido) benzoates as urease inhibitors, docking study and binding mode analysis, overview. No inhibition by n-propyl gallate and 2-tert-butyl-4-hydroxyanisole. Structure-activity relationship analysis suggests that the urease activity of a particular molecule is apparently governed by the substitution present at aromatic residues
-
additional information
-
synthesis and in vitro urease inhibitory activity of N,N'-disubstituted thioureas, overview. no inhibition by 24 and 36
-
additional information
-
a series of carbazole substituted aminopyrimidines are synthesized and screened for their in vitro urease inhibition and antimicrobial activity, overview
-
additional information
-
synthesis, characterization, and urease inhibition of 5-substituted-8-methyl-2H-pyrido[1,2-a]pyrimidine-2,4(3H)-diones, anilines, amino pyridines and hydrazides derivatives, detailed overview. No inhibition by 5
-
additional information
-
the enzyme is completely inactivated by dialyzing against 10 mM TRis-HCl, 1 mM EDTA, pH 7.6, at 5°C for overnight. No activation occurs after adding solid NaCl to make a 30% solution and incubating for 20 h at 5°C
-
additional information
-
evaluation of 3-,6-,7-,9-,12-monohydroxy tetradecanoic acids as enzyme inhibitors in agriculture, overview
-
additional information
-
enzyme inhibition by flavonoids from tropicaal herb Calopogonium mucunoides,overview. No or poor inhibition by cabreuvin and 7-O-methylpseudobaptigenin
-
additional information
-
potent urease inhibitory activity of biscoumarins, mechanisms of inhibition using the nickel containing active sites of the enzyme, overview. Some of the compounds competitively inhibit Bacillus pasteurii urease through interactionwith the nickel metallocentre, as deduced from Michaelis-Menten kinetics, UV-visible absorbance spectroscopic, and molecular docking simulation studies, some comppounds behave differently. Biscoumarins bind at phenyl ring as the major active pharmacophore
-
additional information
-
synthesis and structure-activity relationship of thiobarbituric acid derivatives as potent inhibitors of urease, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ni2+
-
supplementation of growth medium by nickel leads to tenfold increase in enzyme activity, induction occuring at post-translational level
Ni2+
-
supplementation of growth medium by nickel leads to tenfold increase in enzyme activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
1.7
Urea
-
pH 5.5, 65°C, Vmax: 7.29 micromol of ammonia/min/mg protein
2.8
Urea
-
pH 7.0, 37°C; pH 7.5, temperature not specified in the publication; pH 7.75, temperature not specified in the publication
3.2
Urea
-
free enzyme or enzyme bound to membrane modified with NaOH + ethylendiamine and H2O2
4.2
Urea
-
soluble urease, 37°C, pH not specified in the publication, Vmax: 200 micromol/min/mg
8.81
Urea
-
immobilized urease, 37°C, pH not specified in the publication, Vmax: 43.48 micromol/min/mg