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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
- helicobacter
-
pylory
- gastric
- ulcer
-
endoscopy
-
eradication
- gastritis
-
breath
- duodenal
-
peptic
- gastrointestinal
- catalase
- stomach
- ammonia
- mucosa
-
serology
- metronidazole
- clarithromycin
- antrum
- nickel
- omeprazole
- nitrate
- amoxicillin
-
dyspeptic
-
pylori-positive
- mirabilis
- proteus
-
gastroduodenal
-
bismuth
-
giemsa
-
anti-h
- invertase
-
amend
- campylobacter
-
stool
-
manure
- industry
-
e-test
-
gastroscopy
-
sydney
-
pylori-infected
-
antisecretory
- synthesis
-
pylori-induced
- lansoprazole
- medicine
- biotechnology
- food industry
-
nitrification
- drug development
- sucrase
- analysis
- thiourea
-
compost
- nutrition
-
per-protocol
-
intention-to-treat
- ranitidine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
acid urease, Arthritogenic cationic 19 kDa antigen, BPU, canatoxin, embryo-specific soybean urease, Eu1, Eu4, HPU, jack bean urease, JBU, 
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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
UreC
additional information
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
-
-
-
-
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
-
urea + H2O = CO2 + 2 NH3
-
-
-
-
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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
-
-
?
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
?
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
-
-
?
urea + H2O
CO2 + NH3
-
-
-
-
?
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
-
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 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
?
-
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
?
-
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
-
-
?
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
?
-
-
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
?
-
-
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
?
-
Limosilactobacillus reuteri CICC6124
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
?
-
Limosilactobacillus reuteri CICC6124
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
?
-
Limosilactobacillus reuteri CICC6124
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
?
-
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
Providencia rettgeri CGMCC 8326
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
Providencia rettgeri CGMCC 8326
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
Providencia rettgeri JN-B815
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
Providencia rettgeri JN-B815
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
-
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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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
?
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
?
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 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
?
-
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
?
-
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
-
-
?
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
?
-
-
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
?
-
-
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
?
-
Limosilactobacillus reuteri CICC6124
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
?
-
Limosilactobacillus reuteri CICC6124
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
?
-
Limosilactobacillus reuteri CICC6124
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
?
-
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
-
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
Providencia rettgeri CGMCC 8326
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
Providencia rettgeri CGMCC 8326
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
Providencia rettgeri JN-B815
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
additional information
?
-
Providencia rettgeri JN-B815
the enzyme exhibits not only urease activity, but also urethanase (EC 3.5.1.75) activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
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+
-
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
-
enzyme contains 2 gatom of nickel per 96600 g of protein
Nickel
-
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
-
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
-
His320 of subunit C is essential for urea hydrolysis and Ni2+ binding within the native enzyme
Nickel
-
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
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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
-
-
(2R,3S)-2-(3,4-dihydroxyphenyl)-3,4-dihydro-2H-1-benzopyran-3,5,7-triol
0.5 mM, 30°C, pH 6.8, 81.5% inhibition
(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
-
-
2-[4-(2-methylpropyl)phenyl]-N-[(2,4,6-trimethylphenyl)carbamothioyl]propanamide
-
2-[4-(2-methylpropyl)phenyl]-N-[(3-nitrophenyl)carbamothioyl]propanamide
-
2-[4-(2-methylpropyl)phenyl]-N-[(4-sulfamoylphenyl)carbamothioyl]propanamide
-
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-[(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
-
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-(methoxymethyl)-5-methylbenzene-1,3-diol
0.5 mM, 30°C, pH 6.8, 91.5% inhibition
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-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
-
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-fluorouridine
-
the combination of 0.3 mM zeatin with the protein inhibitor results in the alleviation of their inhibitory effect on the urease activity
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
7-methoxy-6'-O-coumaroylaloesin
0.5 mM, 30°C, pH 6.8, 93.5% inhibition
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
aloe emodin 11-O-alpha-D-rhamnopyranoside
0.5 mM, 30°C, pH 6.8, 53.6% inhibition
alpha-Amanitin
-
the combination of 0.3 mM zeatin with the protein inhibitor results in the alleviation of their inhibitory effect on the urease activity
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
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
cordycepin
-
the combination of 0.3 mM zeatin with the protein inhibitor results in the alleviation of their inhibitory effect on the urease activity
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
epigallocatechin
strong time-dependent inactivation of urease that is not due to their oxygen sensitivity. Rather, the compound appears to inactivate urease by reacting with a specific Cys residue located on the flexible loop. Substitution of this cysteine by alanine in the C319A variant increases the urease resistance
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
-
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
-
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
N-(2,5-dimethylphenyl)-N'-[3-(trifluoromethyl)phenyl]thiourea
-
N-(2-bromophenyl)-N'-[2-hydroperoxy-5-(trifluoromethyl)phenyl]thiourea
-
N-(2-chloro-4,6-dimethoxyphenyl)-N'-[3-(trifluoromethyl)phenyl]thiourea
-
N-(3,4-dimethylphenyl)-N'-[2-(trifluoromethyl)phenyl]thiourea
-
N-(3,4-dimethylphenyl)-N'-[2-hydroperoxy-5-(trifluoromethyl)phenyl]thiourea
-
N-(3,4-dimethylphenyl)-N'-[3-(trifluoromethyl)phenyl]thiourea
-
N-(3-chlorophenyl)-N'-[2-methoxy-5-(trifluoromethyl)phenyl]thiourea
-
N-(5-chloro-2,4-dimethoxyphenyl)-N'-(3-methoxyphenyl)thiourea
-
N-(5-chloro-2,4-dimethoxyphenyl)-N'-[2-(trifluoromethyl)phenyl]thiourea
-
N-(benzylcarbamothioyl)-2-[4-(2-methylpropyl)phenyl]propanamide
-
N-[(2,3-dichlorophenyl)carbamothioyl]-2-[4-(2-methylpropyl)phenyl]propanamide
-
N-[(2,4-dinitrophenyl)carbamothioyl]-2-[4-(2-methylpropyl)phenyl]propanamide
-
N-[(3,5-dinitrophenyl)carbamothioyl]-2-[4-(2-methylpropyl)phenyl]propanamide
-
N-[(4-bromophenyl)carbamothioyl]-2-[4-(2-methylpropyl)phenyl]propanamide
-
N-[(4-chlorophenyl)carbamothioyl]-2-[4-(2-methylpropyl)phenyl]propanamide
-
N-[(4-methoxyphenyl)carbamothioyl]-2-[4-(2-methylpropyl)phenyl]propanamide
-
N-[3-(methylsulfanyl)phenyl]-N'-[2-(trifluoromethyl)phenyl]thiourea
-
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
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
sulfite
competitive inhibitor. The structure of the urease-sulfite complex, determined at 1.65 A resolution, shows the inhibitor bound to the dinuclear Ni(II) center of urease in a tridentate mode involving bonds between the two Ni(II) ions in the active site and all three oxygen atoms of the inhibitor
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
catechol
irreversibly inactivates the enzyme with a complex radical-based autocatalytic multistep mechanism
catechol
irreversibly inactivates the enzyme with a complex radical-based autocatalytic multistep mechanism
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
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