3.5.1.5: urease
This is an abbreviated version!
For detailed information about urease, go to the full flat file.
Word Map on EC 3.5.1.5
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3.5.1.5
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pylory
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helicobacter
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gastric
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ulcer
-
endoscopy
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gastritis
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eradication
-
breath
-
gastrointestinal
-
duodenal
-
peptic
-
stomach
-
ammonia
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catalase
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mucosa
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serology
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clarithromycin
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nitrate
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nickel
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amoxicillin
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pylori-positive
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antrum
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dyspeptic
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omeprazole
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metronidazole
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giemsa
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proteus
-
anti-h
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invertase
-
mirabilis
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amend
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campylobacter
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stool
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gastroduodenal
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bismuth
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nitrification
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nutrition
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lansoprazole
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medicine
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synthesis
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antisecretory
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pylori-infected
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sydney
-
drug development
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manure
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compost
-
analysis
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sucrase
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thiourea
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pylori-induced
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ranitidine
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per-protocol
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industry
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food industry
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intention-to-treat
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biotechnology
-
gastroscopy
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e-test
- 3.5.1.5
-
pylory
- helicobacter
- gastric
- ulcer
-
endoscopy
- gastritis
-
eradication
-
breath
- gastrointestinal
- duodenal
-
peptic
- stomach
- ammonia
- catalase
- mucosa
-
serology
- clarithromycin
- nitrate
- nickel
- amoxicillin
-
pylori-positive
- antrum
-
dyspeptic
- omeprazole
- metronidazole
-
giemsa
- proteus
-
anti-h
- invertase
- mirabilis
-
amend
- campylobacter
-
stool
-
gastroduodenal
-
bismuth
-
nitrification
- nutrition
- lansoprazole
- medicine
- synthesis
-
antisecretory
-
pylori-infected
-
sydney
- drug development
-
manure
-
compost
- analysis
- sucrase
- thiourea
-
pylori-induced
- ranitidine
-
per-protocol
- industry
- food industry
-
intention-to-treat
- biotechnology
-
gastroscopy
-
e-test
Reaction
Synonyms
acid urease, Arthritogenic cationic 19 kDa antigen, BPU, canatoxin, embryo-specific soybean urease, Eu1, Eu4, HPU, jack bean urease, JBU, JBURE-II, More, PMU, urea amido hydrolase, Urea amidohydrolase, urease, urease JBURE-IIb, UreC
ECTree
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Inhibitors
Inhibitors on EC 3.5.1.5 - urease
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(2-[[(2-[[2-(hydroxy-kappaO)ethyl]amino-kappaN]ethyl)imino-kappaN]methyl]-4-nitrophenolato-kappaO)(methoxymethanolato-kappaO)zinc
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(2-[[(2-[[2-(hydroxy-kappaO)ethyl]amino-kappaN]ethyl)imino-kappaN]methyl]-4-nitrophenolato-kappaO)(nitrato-kappaO)copper
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(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
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competitive mechanism of inhibition
1-(2,4-dihydroxyphenyl)-2-(4-hydroxyphenyl)ethanone
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0.4 mg/ml, 16% inhibition
1-(3,4-dihydroxyphenyl)-2-(4-hydroxyphenyl)ethanone
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0.4 mg/ml, 39% inhibition
1-benzyl-2-ethyl-6,6-dimethyl-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
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reversible and competitive inhibitor
1-benzyl-2-ethyl-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
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reversible and competitive inhibitor
1-ethoxy-2-ethyl-6,6-dimethyl-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
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reversible and competitive inhibitor
1-ethoxy-2-ethyl-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
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reversible and competitive inhibitor
2,4,4',6-tetrahydroxy-3-methoxyphenyldeoxybenzoin
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0.4 mg/ml, 17% inhibition
2,4,6-trimethyl-N-([1-[(2,4,6-trimethylphenyl)sulfonyl]piperidin-4-yl]methyl)benzenesulfonamide
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50% inhibition at 0.038 mM
2-(4-hydroxyphenyl)-1-(2,4,6-trihydroxy-3-methoxyphenyl)ethanone oxime
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-
2-ethyl-1-(2-phenylethyl)-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
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reversible and competitive inhibitor
2-ethyl-1-(4-methoxycyclohexyl)-6,6-dimethyl-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
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reversible and competitive inhibitor
2-ethyl-1-(4-methoxyphenyl)-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
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reversible and competitive inhibitor
2-ethyl-6-[2-(ethylsulfanyl)propyl]-1-(4-methoxyphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
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reversible and competitive inhibitor
2-thioxo-5-(2,3,4-trihydroxybenzylidene)dihydro-4,6(1H,5H)-pyrimidinedione
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2-[(1E)-N-(allyloxy)butanimidoyl]-5,5-dimethylcyclohexane-1,3-dione
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chelator of the nickel atom in enzyme metallocenter
2-[(1E)-N-ethoxybutanimidoyl]-5,5-dimethylcyclohexane-1,3-dione
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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
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2-[(2S,4R)-2-phenyl-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
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2-[2-(1,3-benzodioxol-5-yl)-2,3-dihydro-1,5-benzothiazepin-4-yl]phenol
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2-[4-(2-methylpropyl)phenyl]-N-[(2,4,6-trimethylphenyl)carbamothioyl]propanamide
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2-[4-(2-methylpropyl)phenyl]-N-[(3-nitrophenyl)carbamothioyl]propanamide
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2-[4-(2-methylpropyl)phenyl]-N-[(4-sulfamoylphenyl)carbamothioyl]propanamide
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3,3'-[(1E)-1-phenylprop-1-ene-3,3-diyl]bis(4-hydroxy-2H-chromen-2-one)
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3,3'-[(3,4,5-trimethoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
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3,3'-[(3,4-dimethoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
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3,3'-[(3-ethoxy-4-hydroxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
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3,3'-[[4-(1-methylethyl)phenyl]methanediyl]bis(4-hydroxy-2H-chromen-2-one)
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3,3'-[[4-(dimethylamino)phenyl]methanediyl]bis(4-hydroxy-2H-chromen-2-one)
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3-methyl-N-[[1-(3-methylbut-2-en-1-yl)piperidin-4-yl]methyl]but-2-en-1-amine
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50% inhibition at 0.063 mM
3-phenoxy-N-[[1-(3-phenoxypropyl)piperidin-4-yl]methyl]propan-1-amine
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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
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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
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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
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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
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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
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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
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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
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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
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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
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3-[(mesitylamino)methylidene]-8-methyl-2H-pyrido[1,2-a]pyrimidine-2,4-dione
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4-(2,3-dimethylphenyl)-5-phenyl-2,4-dihydro-3H-1,2,4-triazole-3-thione
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4-(2,4-dichlorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
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4-(2,4-difluorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
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4-(2,4-dimethylphenyl)-5-(3-nitrophenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
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4-(2,5-dichlorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
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4-(3,4-dichlorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
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4-(3,4-difluorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
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4-(3,4-dimethoxyphenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
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4-(4-bromophenyl)-5-[hydroxy(phenyl)methyl]-2,4-dihydro-3H-1,2,4-triazole-3-thione
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4-(4-chlorophenyl)-5-[hydroxy(phenyl)methyl]-2,4-dihydro-3H-1,2,4-triazole-3-thione
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4-(9-methyl-9H-carbazol-3-yl)-6-(2,4,6-trimethoxyphenyl)-pyrimidin-2-amine
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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
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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
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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
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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
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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
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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
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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
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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
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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
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5-(2-hydroxy-5-methoxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
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-
5-(2-methylbenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
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-
5-(3,4-dihydroxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
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-
5-(3,4-dimethoxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
-
-
5-(3,5-dibromo-4-hydroxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
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-
5-(3,5-dichloro-2-hydroxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
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-
5-(3-chlorophenyl)-4-(2,4-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
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5-(3-chlorophenyl)-4-(2,6-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
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5-(3-hydroxy-4-methoxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
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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
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-
5-(4-hydroxy-3,5-dimethoxybenzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
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5-(4-hydroxy-3-iodo-5-methoxybenzylidene)-2-thioxodihydro-4,6(1H,5H) pyrimidinedione
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-
5-(4-pyridinylmethylene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
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5-(4-[[4,6-dioxo-2-thioxotetrahydro-5(2H)pyrimidinylidene]methyl]-benzylidene)-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
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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
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5-[(5-methyl-2-furyl)methylene]-2-thioxodihydro-4,6(1H,5H)pyrimidinedione
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5-[(6-bromo-4-chloro-2-oxo-2H-chromen-3-yl)methylene]-2-thioxodihydro 4,6(1H,5H)-pyrimidinedione
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5-[(6-methyl-2-pyridinyl)methylene]-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
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5-[4(dimethylamino) benzylidene]-2-thioxodihydro-4,6(1H,5H)-pyrimidinedione
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5-[4-(methylsulfanyl)benzylidene]-2-thioxodihydro-4,6(1H,5H) pyrimidinedione
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5-[4-(tert-butyl-dimethyl-silanyloxy)-phenyl]-3H-[1,3,4]thiadiazole-2-thione
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5-[hydroxy(phenyl)methyl]-4-(4-methylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
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5-[hydroxy(phenyl)methyl]-4-(4-nitrophenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
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6-(1-hydroxy-2-(4-methoxyphenyl)ethyl)-2,3-dimethoxyphenol
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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
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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
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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
-
noncompetitive, 50% inhibition at 0.040 mM
(2S)-2-(dimethylamino)-3-(ethylthio)propan-1-ol
-
noncompetitive, 50% inhibition at 0.029 mM
-
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
-
noncompetitive, 50% inhibition at 0.022 mM
(2S)-2-(dimethylamino)-3-mercaptopropan-1-ol
-
noncompetitive, 50% inhibition at 0.025 mM
-
noncompetitive, 50% inhibition at 0.035 mM
(2S)-2-(dimethylamino)-3-methoxypropane-1-thiol
-
noncompetitive, 50% inhibition at 0.036 mM
-
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
-
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
-
pH 8.2, IC50: 0.234 mM
4-(4-benzoyl-5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)phenyl benzoate
-
-
-
pH 8.2, IC50: below 0.125 mM
4-amino-5-(4-hydroxyphenyl)-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
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
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
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
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
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
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
-
pH 8.2, IC50: below 0.125 mM
-
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
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
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-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-[(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
-
-
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
-
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
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 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
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-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-[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]-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-[[(methylsulfanyl)carbonothioyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
-
N-(N'-benzyloxycarbonylglycyl)aminomethyl(P-methyl)phosphinothioic acid
-
-
-
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
-
-
Ni2+
-
inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+
Ni2+
Ni2+ is essential to urease activation, best at 0.5 mM. Urease is inhibited at high concentration of Ni2+
-
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
quercetin
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
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+
-
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
-
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
natural urease inhibitors from Aloe vera resin and Lycium shawii are isolated from the methanol extracts
-
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
caftaric acid, desmosine, kanamycin, and labetalol, each examined at concentrations up to 0.6 mM, show little to no inhibitory activity
-
additional information
-
caftaric acid, desmosine, kanamycin, and labetalol, each examined at concentrations up to 0.6 mM, show little to no inhibitory activity
-
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
-