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Information on EC 3.5.1.5 - urease and Organism(s) Canavalia ensiformis and UniProt Accession P07374
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3.5.1.5 ureaseIUBMB Comments
A nickel protein.
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Word Map
- 3.5.1.5
-
pylory
- helicobacter
- gastric
- ulcer
-
endoscopy
- gastritis
-
eradication
-
breath
- gastrointestinal
- duodenal
-
peptic
- stomach
- ammonia
- catalase
- mucosa
-
serology
- clarithromycin
- nitrate
- nickel
- amoxicillin
-
pylori-positive
- antrum
-
dyspeptic
- omeprazole
- metronidazole
-
giemsa
- proteus
-
anti-h
- invertase
- mirabilis
-
amend
- campylobacter
-
stool
-
gastroduodenal
-
bismuth
-
nitrification
- nutrition
- lansoprazole
- medicine
- synthesis
-
antisecretory
-
pylori-infected
-
sydney
- drug development
-
manure
-
compost
- analysis
- sucrase
- thiourea
-
pylori-induced
- ranitidine
-
per-protocol
- industry
- food industry
-
intention-to-treat
- biotechnology
-
gastroscopy
-
e-test
The taxonomic range for the selected organisms is: Canavalia ensiformis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
urease, jack bean urease, canatoxin, acid urease, jbure-ii, embryo-specific soybean urease, urea amidohydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Arthritogenic cationic 19 kDa antigen
-
-
-
-
canatoxin
-
presence of a family of urease related genes in Canavalia ensiformis with at least three members: canatoxin, JBU and JBURE-II
JBU
JBURE-II
Urea amidohydrolase
urease
-
-
JBU
presence of a family of urease related genes in Canavalia ensiformis with at least three members: canatoxin, JBU and JBURE-II
JBURE-II
family of urease related genes in Canavalia ensiformis with at least three members: canatoxin, JBU and JBURE-II
Urea amidohydrolase
-
-
-
-
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
-
-
-
-
carboxylic acid amide hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-
SYSTEMATIC NAME
IUBMB Comments
urea amidohydrolase
A nickel protein.
CAS REGISTRY NUMBER
COMMENTARY
9002-13-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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
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
?
-
-
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
-
-
?
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
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
?
-
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ni2+
Ni2+
Nickel
Ni2+
metal-dependent enzyme that contains nickel at its active site
Nickel
-
enzyme contains 2 gatom of nickel per 96600 g of protein
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
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-[(2-acetylanilino)methylidene]-8-methyl-2H-pyrido[1,2-a]-pyrimidine-2,4-dione
54% inhibition at 0.01 mM
3-[(2-fluoroanilino)methylidene]-8-methyl-2H-pyrido[1,2-a]-pyrimidine-2,4-dione
44% inhibition at 0.01 mM
3-[(3-acetylanilino)methylidene]-8-methyl-2H-pyrido[1,2-a]-pyrimidine-2,4-dione
28% inhibition at 0.01 mM
3-[(3-fluoroanilino)methylidene]-8-methyl-2H-pyrido[1,2-a]-pyrimidine-2,4-dione
3% inhibition at 0.01 mM
3-[(4-acetylanilino)methylidene]-8-methyl-2H-pyrido[1,2-a]pyrimidine-2,4-dione
5% inhibition at 0.01 mM
3-[(4-fluoroanilino)methylidene]-8-methyl-2H-pyrido[1,2-a]pyrimidine-2,4-dione
21% inhibition at 0.01 mM
3-[(mesitylamino)methylidene]-8-methyl-2H-pyrido[1,2-a]pyrimidine-2,4-dione
-
4-(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
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-[(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-pyrrol-3-yl)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)methyl]-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
competitive inhibition
4-hydroxy-3-[1-(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)pentyl]-2H-chromen-2-one
competitive inhibition
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-nitro-N'-[[8-methyl-2,4-dioxo-2H-pyrido[1,2-a]pyrimidin-3(4H)-ylidene]methyl] benzohydrazide
60% inhibition at 0.01 mM
7-methoxy-6'-O-coumaroylaloesin
0.5 mM, 30°C, pH 6.8, 93.5% inhibition
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
aloe emodin 11-O-alpha-D-rhamnopyranoside
0.5 mM, 30°C, pH 6.8, 53.6% inhibition
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
catechol
irreversibly inactivates the enzyme with a complex radical-based autocatalytic multistep mechanism
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-(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
-
(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
-
-
(2S)-2-(dimethylamino)-3-ethoxypropane-1-thiol
-
noncompetitive, 50% inhibition at 0.100 mM
(E)-1-(3-nitrobenzylidene)thiosemicarbazide
-
competitive mechanism of inhibition
(R)-4-methoxydalbergione
-
50% inhibition at 0.067 mM, isolated from roots of Ranunculus repens
(R)-dalbergiophenol
-
50% inhibition at 0.035 mM, isolated from roots of Ranunculus repens
2,4,6-trimethyl-N-([1-[(2,4,6-trimethylphenyl)sulfonyl]piperidin-4-yl]methyl)benzenesulfonamide
-
50% inhibition at 0.038 mM
2-[(2S,4R)-2-(4-fluorophenyl)-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
-
-
2-[(2S,4R)-2-phenyl-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
-
-
2-[2-(1,3-benzodioxol-5-yl)-2,3-dihydro-1,5-benzothiazepin-4-yl]phenol
-
-
3,3'-[(1E)-1-phenylprop-1-ene-3,3-diyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(3,4,5-trimethoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(3,4-dimethoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(3-ethoxy-4-hydroxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[[4-(1-methylethyl)phenyl]methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[[4-(dimethylamino)phenyl]methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3-methyl-N-[[1-(3-methylbut-2-en-1-yl)piperidin-4-yl]methyl]but-2-en-1-amine
-
50% inhibition at 0.063 mM
3-phenoxy-N-[[1-(3-phenoxypropyl)piperidin-4-yl]methyl]propan-1-amine
-
50% inhibition at 0.043 mM
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-benzoyl-5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)phenyl benzoate
-
pH 8.2, IC50: 0.234 mM
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-amino-5-pyridin-4-yl-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 8.2, IC50: 0.163 mM
4-methyl-N-([1-[(4-methylphenyl)sulfonyl]piperidin-4-yl]methyl)benzenesulfonamide
-
50% inhibition at 0.042 mM
4-nitro-N-([1-[(4-nitrophenyl)sulfonyl]piperidin-4-yl]methyl)benzenesulfonamide
-
50% inhibition at 0.032 mM
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-(4-chlorophenyl)-4-(2,4-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
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-pyridin-4-yl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: above 0.2 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: 0.095 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: 0.093 mM
5-[4-(benzyloxy)phenyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.41 mM
5-[4-(tert-butyl-dimethyl-silanyloxy)-phenyl]-3H-[1,3,4]oxadiazole-2-thione
-
pH 8.2, IC50: 0.244 mM
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
-
-
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'-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
-
-
Cd2+
-
inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+
chloro(2-[[(2-[[2-(hydroxy-kappaO)ethyl]amino-kappaN]ethyl)imino-kappaN]methyl]-4-nitrophenolato-kappaO)copper
-
-
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
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 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-[(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-[[(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
N-dimethyl-S-methyl-L-cysteine
-
noncompetitive, 50% inhibition at 0.078 mM
Ni2+
-
inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+
Pb2+
-
inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+
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
Zn2+
-
inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+
Thiourea
halogenated substituted thiourea derivatives are slightly less active than methoxy substituted compounds
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+
phenylphosphorodiamidate
-
the inhibitor is able to thoroughly protect the flap cysteines from the further reaction with disulfides, this apparently resulting from the closed conformation of the flap. The inhibitor may be regarded as the most suitable inhibitor for active-site protection experiments in inhibition studies of urease
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
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
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
-
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
-
a series of carbazole substituted aminopyrimidines are synthesized and screened for their in vitro urease inhibition and antimicrobial activity, overview
-
additional information
-
synthesis and in vitro urease inhibitory activity of N,N'-disubstituted thioureas, overview. no inhibition by 24 and 36
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.165
Urea
pH 7.0, 25°C, urease encapsulated in chitosan nickel ferrite beads
0.168
Urea
pH 7.0, 25°C, urease encapsulated in chitosan-magnetite beads
0.172
Urea
pH 7.0, 25°C, urease encapsulated in chitosan-coated alginate-magnetite
0.181
Urea
pH 7.0, 25°C, urease encapsulated in chitosan-coated alginate-nickel
3.2
Urea
-
free enzyme or enzyme bound to membrane modified with NaOH + ethylendiamine and H2O2
4.2
Urea
-
soluble urease, 37°C, pH not specified in the publication, Vmax: 200 micromol/min/mg
8.81
Urea
-
immobilized urease, 37°C, pH not specified in the publication, Vmax: 43.48 micromol/min/mg
additional information
additional information
steady-state kinetics analysis
-
additional information
additional information
-
steady-state kinetics analysis
-
additional information
Urea
a combined temperature-pH study of urease kinetics is performed at eight pHs between 5.0 and 8.3 in noninteracting biological buffers (MES and HEPES), at each pH at five temperatures between 15°C and 35°C. The analysis of the determined kinetic parameters KM and vmax shows that even though both the thermodynamic and activation parameters of the urease reaction are little pH-dependent
additional information
additional information
-
kinetic analysis of enzyme immobilized on acrylonitrile copolymer membranes chemically modified by different methods. KM-value of enzyme bound to membrane modified with NaOH + ethylendiamine and H2O2 is equal to that of free enzyme
-
additional information
additional information
-
steady-state kinetics analysis
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pH-variation study on steady-state kinetic parameters
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000000003
2-[4-(2-methylpropyl)phenyl]-N-[(2,4,6-trimethylphenyl)carbamothioyl]propanamide
pH 8.2, 37°C, mixed-type inhibition
0.0000000025
2-[4-(2-methylpropyl)phenyl]-N-[(3-nitrophenyl)carbamothioyl]propanamide
pH 8.2, 37°C, mixed-type inhibition
0.0215
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
pH 6.8, 30°C
0.0659
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
pH 6.8, 30°C
0.0629 - 0.068
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(1H-indol-3-yl)methyl]-2H-chromen-2-one
0.0533
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(1H-pyrrol-3-yl)methyl]-2H-chromen-2-one
pH 6.8, 30°C
0.0193
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(3-methoxyphenyl)methyl]-2H-chromen-2-one
pH 6.8, 30°C
0.071
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(pyridin-4-yl)methyl]-2H-chromen-2-one
pH 6.8, 30°C
0.015
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)methyl]-2H-chromen-2-one
pH 6.8, 30°C
0.0594
4-hydroxy-3-[1-(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)ethyl]-2H-chromen-2-one
pH 6.8, 30°C
0.075
4-hydroxy-3-[1-(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)pentyl]-2H-chromen-2-one
pH 6.8, 30°C
0.0000000012
N-[(2,3-dichlorophenyl)carbamothioyl]-2-[4-(2-methylpropyl)phenyl]propanamide
pH 8.2, 37°C, competitive inhibition, irreversible
0.00091
(E)-1-(3,4,5-trimethoxybenzylidene)thiosemicarbazide
-
pH 8.2, 37°C
0.000122
(E)-1-(4-(N,N-dimethylamino)benzylidene)thiosemicarbazide
-
pH 8.2, 37°C
0.00043
(E)-2-((E)-but-2-enylidene)hydrazinecarbothioamide
-
pH 8.2, 37°C
0.000127
(E)-2-(2,3-dihydroxybenzylidene)hydrazinecarbothioamide
-
pH 8.2, 37°C
0.000152
(E)-2-(2-(benzyloxy)benzylidene)hydrazinecarbothioamide
-
pH 8.2, 37°C
0.000191
(E)-2-(3-(benzyloxy)-4-methoxybenzylidene)hydrazinecarbothioamide
-
pH 8.2, 37°C
0.000134
(E)-2-(4-hydroxy-3,5-dimethoxybenzylidene)hydrazinecarbothioamide
-
pH 8.2, 37°C
0.000391
(E)-2-(4-hydroxybenzylidene)hydrazinecarbothioamide
-
pH 8.2, 37°C
0.0185
1-(5-chloro-2-methylphenyl)-3-(3-chlorophenyl)thiourea
-
pH 6.8, 30°C
0.0629
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(1H-indol-3-yl)methyl]-2H-chromen-2-one
pH 6.8, 30°C
0.068
4-hydroxy-3-[(4-hydroxy-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)(1H-indol-3-yl)methyl]-2H-chromen-2-one
pH 6.8, 30°C
additional information
additional information
inhibition kinetics analysis
-
additional information
additional information
-
inhibition kinetics analysis
-
additional information
additional information
inhibition kinetics, modeling, overview
-
additional information
additional information
-
inhibition kinetics analysis
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0368
(2R,3S)-2-(3,4-dihydroxyphenyl)-3,4-dihydro-2H-1-benzopyran-3,5,7-triol
Canavalia ensiformis
30°C, pH 6.8
0.00197
2,3-dichloro-N'-(2,3-dichlorobenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00266
2,3-dichloro-N'-(3,5-dichlorobenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00272
2,3-dichloro-N'-(3,5-dimethylbenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00735
2,3-dichloro-N'-(3-chlorobenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00501
2,4-dichloro-N'-(2,4-dichlorobenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00465
2,4-dichloro-N'-(3,5-dichlorobenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.019
2-chloro-N'-(3-chlorobenzoyl)-4-methylbenzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.0137
2-iodo-N'-(3-methylbenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.000235
2-[4-(2-methylpropyl)phenyl]-N-[(3-nitrophenyl)carbamothioyl]propanamide
Canavalia ensiformis
pH 8.2, 37°C, mixed-type inhibition
0.000235
2-[4-(2-methylpropyl)phenyl]-N-[(4-sulfamoylphenyl)carbamothioyl]propanamide
Canavalia ensiformis
pH 8.2, 37°C
0.0167
3,5-dichloro-N'-(3-chlorobenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00971
3,5-dichloro-N'-(3-methylbenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00182
3,5-dichloro-N'-(4-chlorobenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00087
3,5-dichloro-N'-(4-methoxybenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00213
3,5-dichloro-N'-(4-methylbenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.0131
3-chloro-N'-(3-chlorobenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.0089
3-chloro-N'-(3-methylbenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00915
3-chloro-N'-(3-nitrobenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00462
3-chloro-N'-(4-methylbenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00907
3-methyl-N'-(3-methylbenzoyl)benzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.021
8-methyl-2H-pyrido[1,2-a]pyrimidine-2,4(3H)-dione
Canavalia ensiformis
pH not specified in the publication, 25°C
0.0432
Acetohydroxamic acid
Canavalia ensiformis
pH and temperature not specified in the publication
0.00028
ethyl 4-[3-(2,4-dichlorobenzoyl)thioureido]benzoate
Canavalia ensiformis
pH 8.2, 37°C
0.00035
ethyl 4-[3-(2-bromobenzoyl)thioureido]benzoate
Canavalia ensiformis
pH 8.2, 37°C
0.00073
ethyl 4-[3-(2-fluorobenzoyl)thioureido]benzoate
Canavalia ensiformis
pH 8.2, 37°C
0.00013
ethyl 4-[3-(3,4-dimethoxybenzoyl)thioureido]benzoate
Canavalia ensiformis
pH 8.2, 37°C
0.00026
ethyl 4-[3-(3-chlorobenzoyl)thioureido]benzoate
Canavalia ensiformis
pH 8.2, 37°C
0.00047
ethyl 4-[3-(3-methoxybenzoyl)thioureido]benzoate
Canavalia ensiformis
pH 8.2, 37°C
0.0017
ethyl 4-[3-(3-methylbenzoyl)thioureido]benzoate
Canavalia ensiformis
pH 8.2, 37°C
0.00021
ethyl 4-[3-(4-methoxybenzoyl)thioureido]benzoate
Canavalia ensiformis
pH 8.2, 37°C
0.00067
ethyl 4-[3-(4-methylbenzoyl)thioureido]benzoate
Canavalia ensiformis
pH 8.2, 37°C
0.00912
N'-(2,3-dichlorobenzoyl)-3,4,5-trimethoxybenzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH8, 37°C, 30 min.
0.0123
N'-(2,4-dichlorobenzoyl)pyridine-3-carbohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.0133
N'-(2-ethoxybenzoyl)pyridine-3-carbohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.0147
N'-(3-chlorobenzoyl)pyridine-3-carbohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.0105
N'-(3-methylbenzoyl)pyridine-3-carbohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00383
N'-(4-chlorobenzoyl)pyridine-3-carbohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00164
N'-(4-methoxybenzoyl)-3,5-dimethylbenzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
-
0.00987
N'-(4-methylbenzoyl)pyridine-3-carbohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00948
N'-benzoyl-2,3-dichlorobenzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.0053
N'-benzoyl-2,4-dichlorobenzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.0127
N'-benzoyl-3-methylbenzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00932
N'-benzoyl-4-chlorobenzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00963
N'-benzoyl-4-methoxybenzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.0136
N'-benzoyl-4-methylbenzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00678
N'-benzoylbenzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00964
N'-benzoylpyridine-3-carbohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.000212
N-(benzylcarbamothioyl)-2-[4-(2-methylpropyl)phenyl]propanamide
Canavalia ensiformis
pH 8.2, 37°C
0.000225
N-[(2,3-dichlorophenyl)carbamothioyl]-2-[4-(2-methylpropyl)phenyl]propanamide
Canavalia ensiformis
pH 8.2, 37°C, competitive inhibition, irreversible
0.000211
N-[(2,4-dinitrophenyl)carbamothioyl]-2-[4-(2-methylpropyl)phenyl]propanamide
Canavalia ensiformis
pH 8.2, 37°C
0.00021
N-[(3,5-dinitrophenyl)carbamothioyl]-2-[4-(2-methylpropyl)phenyl]propanamide
Canavalia ensiformis
pH 8.2, 37°C
0.000209
N-[(4-bromophenyl)carbamothioyl]-2-[4-(2-methylpropyl)phenyl]propanamide
Canavalia ensiformis
pH 8.2, 37°C
0.000218
N-[(4-chlorophenyl)carbamothioyl]-2-[4-(2-methylpropyl)phenyl]propanamide
Canavalia ensiformis
pH 8.2, 37°C
0.000215
N-[(4-methoxyphenyl)carbamothioyl]-2-[4-(2-methylpropyl)phenyl]propanamide
Canavalia ensiformis
pH 8.2, 37°C
0.1
(2-[[(2-[[2-(hydroxy-kappaO)ethyl]amino-kappaN]ethyl)imino-kappaN]methyl]-4-nitrophenolato-kappaO)(methoxymethanolato-kappaO)zinc
Canavalia ensiformis
-
value above 0.1, pH and temperature not specified in the publication
0.0224
(2-[[(2-[[2-(hydroxy-kappaO)ethyl]amino-kappaN]ethyl)imino-kappaN]methyl]-4-nitrophenolato-kappaO)(nitrato-kappaO)copper
Canavalia ensiformis
-
pH and temperature not specified in the publication
0.03251
(2E)-3-(1,3-benzodioxol-5-yl)-1-(2-hydroxyphenyl)prop-2-en-1-one
Canavalia ensiformis
-
-
0.000989
(E)-1-(3,4,5-trimethoxybenzylidene)thiosemicarbazide
Canavalia ensiformis
-
pH 8.2, 37°C
0.000127
(E)-1-(4-(N,N-dimethylamino)benzylidene)thiosemicarbazide
Canavalia ensiformis
-
pH 8.2, 37°C
0.000746
(E)-2-((E)-but-2-enylidene)hydrazinecarbothioamide
Canavalia ensiformis
-
pH 8.2, 37°C
0.00022
(E)-2-(2,3-dihydroxybenzylidene)hydrazinecarbothioamide
Canavalia ensiformis
-
pH 8.2, 37°C
0.000263
(E)-2-(2-(benzyloxy)benzylidene)hydrazinecarbothioamide
Canavalia ensiformis
-
pH 8.2, 37°C
0.00033
(E)-2-(3-(benzyloxy)-4-methoxybenzylidene)hydrazinecarbothioamide
Canavalia ensiformis
-
pH 8.2, 37°C
0.000233
(E)-2-(4-hydroxy-3,5-dimethoxybenzylidene)hydrazinecarbothioamide
Canavalia ensiformis
-
pH 8.2, 37°C
0.000682
(E)-2-(4-hydroxybenzylidene)hydrazinecarbothioamide
Canavalia ensiformis
-
pH 8.2, 37°C
0.04096
1-(3-chlorophenyl)-3-(2,6-dichlorophenyl)thiourea
Canavalia ensiformis
-
pH 6.8, 30°C
0.01103
1-(3-chlorophenyl)-3-(3,4-dichlorophenyl)thiourea
Canavalia ensiformis
-
pH 6.8, 30°C
0.0159
1-(3-chlorophenyl)-3-(3-methylpyridin-2-yl)thiourea
Canavalia ensiformis
-
pH 6.8, 30°C
0.02303
1-(3-chlorophenyl)-3-(pyridin-3-ylmethyl)thiourea
Canavalia ensiformis
-
pH 6.8, 30°C
0.0201
1-(5-chloro-2-methylphenyl)-3-(3-chlorophenyl)thiourea
Canavalia ensiformis
-
pH 6.8, 30°C
0.133
2,2'-bi-1,3,4-oxadiazole-5,5'(4H,4'H)-dithione
Canavalia ensiformis
-
pH 8.2, IC50: 0.133 mM
0.09374
2-[(2S,4R)-2-(4-fluorophenyl)-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
Canavalia ensiformis
-
-
0.09121
2-[(2S,4R)-2-phenyl-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
Canavalia ensiformis
-
-
0.01907
2-[2-(1,3-benzodioxol-5-yl)-2,3-dihydro-1,5-benzothiazepin-4-yl]phenol
Canavalia ensiformis
-
-
0.086
4-(2,3-dimethylphenyl)-5-phenyl-2,4-dihydro-3H-1,2,4-triazole-3-thione
Canavalia ensiformis
-
pH 6.8, 30°C
0.0194
4-(2,4-dichlorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.0402
4-(2,4-difluorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.0456
4-(2,4-dimethylphenyl)-5-(3-nitrophenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
Canavalia ensiformis
-
pH 6.8, 30°C
0.0281
4-(2,5-dichlorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.0232
4-(3,4-dichlorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.0452
4-(3,4-difluorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.0307
4-(3,4-dimethoxyphenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.0837
4-(3-aminophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.234
4-(4-benzoyl-5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)phenyl benzoate
Canavalia ensiformis
-
pH 8.2, IC50: 0.234 mM
0.032
4-(4-bromophenyl)-5-[hydroxy(phenyl)methyl]-2,4-dihydro-3H-1,2,4-triazole-3-thione
Canavalia ensiformis
-
pH and temperature not specified in the publlication
0.0951
4-(4-bromophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.0182
4-(4-chlorophenyl)-5-[hydroxy(phenyl)methyl]-2,4-dihydro-3H-1,2,4-triazole-3-thione
Canavalia ensiformis
-
pH and temperature not specified in the publlication
0.1
4-(4-chlorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
Canavalia ensiformis
-
above, pH 6.8, 30°C
0.1
4-(4-fluorophenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
Canavalia ensiformis
-
above, pH 6.8, 30°C
0.0954
4-(4-methoxyphenyl)-6-(9-methyl-9H-carbazol-3-yl)-pyrimidin-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.0737
4-(9-methyl-9H-carbazol-3-yl)-6-(2,4,6-trimethoxyphenyl)-pyrimidin-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.0872
4-(9-methyl-9H-carbazol-3-yl)-6-(4-nitrophenyl)-pyrimidin-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.1
4-(9-methyl-9H-carbazol-3-yl)-6-(pyridin-2-yl)-pyrimidin-2-amine
Canavalia ensiformis
-
above, pH 6.8, 30°C
0.1
4-(9-methyl-9H-carbazol-3-yl)-6-(thiophen-2-yl)-pyrimidin-2-amine
Canavalia ensiformis
-
above, pH 6.8, 30°C
0.1
4-(9-methyl-9H-carbazol-3-yl)-6-phenylpyrimidin-2-amine
Canavalia ensiformis
-
above, pH 6.8, 30°C
0.163
4-amino-5-pyridin-4-yl-2,4-dihydro-3H-1,2,4-triazole-3-thione
Canavalia ensiformis
-
pH 8.2, IC50: 0.163 mM
0.214
5-(1-naphthyl)-1,3,4-oxadiazole-2(3H)-thione
Canavalia ensiformis
-
pH 8.2, IC50: 0.214 mM
0.3132
5-(2-chlorophenyl)-N-(2,6-dimethylphenyl)-1,3,4-thiadiazol-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.4596
5-(3-chlorophenyl)-4-(2,4-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
Canavalia ensiformis
-
pH 6.8, 30°C
0.357
5-(3-chlorophenyl)-4-(2,6-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
Canavalia ensiformis
-
pH 6.8, 30°C
0.1708
5-(4-chlorophenyl)-4-(2,4-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
Canavalia ensiformis
-
pH 6.8, 30°C
0.4836
5-(4-chlorophenyl)-N-(2,3-dimethylphenyl)-1,3,4-thiadiazol-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.2147
5-(4-chlorophenyl)-N-(2,6-dimethylphenyl)-1,3,4-thiadiazol-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.124
5-cyclohexyl-1,3,4-oxadiazole-2(3H)-thione
Canavalia ensiformis
-
pH 8.2, IC50: 0.124 mM
0.2
5-pyridin-4-yl-1,3,4-oxadiazole-2(3H)-thione
Canavalia ensiformis
-
pH 8.2, IC50: above 0.2 mM
0.124
5-pyridin-4-yl-1,3,4-thiadiazole-2(3H)-thione
Canavalia ensiformis
-
pH 8.2, IC50: 0.124 mM
0.095
5-[(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)methyl]-1,3,4-oxadiazole-2(3H)-thione
Canavalia ensiformis
-
pH 8.2, IC50: 0.095 mM
0.095
5-[(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)methyl]-1,3,4-thiadiazole-2(3H)-thione
Canavalia ensiformis
-
pH 8.2, IC50: 0.095 mM
0.093
5-[3-(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)propyl]-1,3,4-oxadiazole-2(3H)-thione
Canavalia ensiformis
-
pH 8.2, IC50: 0.093 mM
0.41
5-[4-(benzyloxy)phenyl]-1,3,4-oxadiazole-2(3H)-thione
Canavalia ensiformis
-
pH 8.2, IC50: 0.41 mM
0.244
5-[4-(tert-butyl-dimethyl-silanyloxy)-phenyl]-3H-[1,3,4]oxadiazole-2-thione
Canavalia ensiformis
-
pH 8.2, IC50: 0.244 mM
0.0167
5-[hydroxy(phenyl)methyl]-4-(4-methylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
Canavalia ensiformis
-
pH and temperature not specified in the publlication
0.1317
5-[hydroxy(phenyl)methyl]-4-(4-nitrophenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
Canavalia ensiformis
-
pH and temperature not specified in the publlication
0.09367
7'-hydroxy-2,2'-dioxo-2H,2'H-6,8'-bichromen-7-yl alpha-L-mannopyranoside
Canavalia ensiformis
-
-
0.02939
7'-hydroxy-2,2'-dioxo-3'-[(2-oxo-2H-chromen-7-yl)oxy]-2H,2'H-8,8'-bichromen-7-yl alpha-D-glucopyranoside
Canavalia ensiformis
-
-
0.04
7'-methoxy-2,2'-dioxo-3'-[(2-oxo-2H-chromen-7-yl)oxy]-2H,2'H-8,8'-bichromen-7-yl alpha-D-glucopyranoside
Canavalia ensiformis
-
-
0.0263
7-hydroxy-2,2'-dioxo-2H,2'H-6,8'-bichromen-7'-yl alpha-L-mannopyranoside
Canavalia ensiformis
-
-
0.06191
7-[(7-methoxy-2-oxo-2H-chromen-3-yl)oxy]-2-oxo-2H-chromen-6-yl alpha-D-glucopyranoside
Canavalia ensiformis
-
-
0.0316
8-hydroxy-3-[(6-hydroxy-2-oxo-2H-chromen-7-yl)oxy]-2-oxo-2H-chromen-7-yl beta-D-glucopyranoside
Canavalia ensiformis
-
-
0.02425
chloro(2-[[(2-[[2-(hydroxy-kappaO)ethyl]amino-kappaN]ethyl)imino-kappaN]methyl]-4-nitrophenolato-kappaO)copper
Canavalia ensiformis
-
pH and temperature not specified in the publication
0.03184
methyl 2-amino-4,5,6,7,8,9-hexahydrocycloocta[b]thiophene-3-carboxylate
Canavalia ensiformis
-
pH 8.2, 30°C
0.0093
methyl 2-amino-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
Canavalia ensiformis
-
pH 8.2, 30°C
0.01658
methyl 2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
Canavalia ensiformis
-
pH 8.2, 30°C
0.00504
methyl 2-amino-5,6-dihydro-4H-cyclopenta[b]thiophene-3-carboxylate
Canavalia ensiformis
-
pH 8.2, 30°C
0.01832
methyl 2-[(methoxycarbonyl)amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
Canavalia ensiformis
-
pH 8.2, 30°C
0.00299
methyl 2-[bis(chlorocarbonyl)amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
Canavalia ensiformis
-
pH 8.2, 30°C
0.01242
methyl 2-[[(chloromethoxy)carbonyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
Canavalia ensiformis
-
pH 8.2, 30°C
0.02908
methyl 2-[[(chloromethoxy)carbonyl]amino]-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
Canavalia ensiformis
-
pH 8.2, 30°C
0.01945
methyl 2-[[(dichloromethoxy)carbonyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
Canavalia ensiformis
-
pH 8.2, 30°C
0.01054
methyl 2-[[(methylsulfanyl)carbonothioyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
Canavalia ensiformis
-
pH 8.2, 30°C
0.4261
N-(2,3-dimethylphenyl)-5-phenyl-1,3,4-thiadiazol-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.3982
N-(2,4-dimethylphenyl)-5-(3-nitrophenyl)-1,3,4-thiadiazol-2-amine
Canavalia ensiformis
-
pH 6.8, 30°C
0.0209
tetracosyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
Canavalia ensiformis
-
pH 6.8, 30°C
0.0161
[5-[(4-methylphenyl)amino]-1,3,4-oxadiazol-2-yl](phenyl)methanol
Canavalia ensiformis
-
pH and temperature not specified in the publlication
0.0803
[5-[(4-nitrophenyl)amino]-1,3,4-oxadiazol-2-yl](phenyl)methanol
Canavalia ensiformis
-
pH and temperature not specified in the publlication
0.00623
N'-benzoyl-3-chlorobenzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.00757
N'-benzoyl-3-chlorobenzohydrazide
Canavalia ensiformis
100 mM urea, 1 mM EDTA, 10 mM K2HPO4, 10 mM LiCl2, pH 8, 37°C, 30 min.
0.0203
Thiourea
Canavalia ensiformis
pH and temperature not specified in the publication
0.02125
Thiourea
Canavalia ensiformis
pH and temperature not specified in the publication
0.045
Acetohydroxamic acid
Canavalia ensiformis
-
pH and temperature not specified in the publication
additional information
3,3'-(1H-indol-3-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.21
additional information
3,3'-(1H-pyrrol-2-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.33
additional information
3,3'-(2-phenylpropane-1,1-diyl)bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.28
additional information
3,3'-(2E)-but-2-ene-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.36
additional information
3,3'-(3-phenylpropane-1,1-diyl)bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.17
additional information
3,3'-(naphthalen-1-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.07
additional information
3,3'-(pyridin-3-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.45
additional information
3,3'-(pyridin-4-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.23
additional information
3,3'-butane-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.17
additional information
3,3'-ethane-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.20
additional information
3,3'-hexane-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.06
additional information
3,3'-methanediylbis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.82
additional information
3,3'-pentane-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.19
additional information
3,3'-[(1E)-1-phenylprop-1-ene-3,3-diyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.22
additional information
3,3'-[(2-bromophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.13
additional information
3,3'-[(2-chlorophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.07
additional information
3,3'-[(2-methoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.08
additional information
3,3'-[(3,4,5-trimethoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.08
additional information
3,3'-[(3,4-dimethoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.10
additional information
3,3'-[(3-aminophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.12
additional information
3,3'-[(3-chlorophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.13
additional information
3,3'-[(3-ethoxy-4-hydroxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.04
additional information
3,3'-[(3-hydroxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.14
additional information
3,3'-[(3-methoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.25
additional information
3,3'-[(3-nitrophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.09
additional information
3,3'-[(4-hydroxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.13
additional information
3,3'-[(4-methoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.22
additional information
3,3'-[(4-nitrophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.15
additional information
3,3'-[[4-(1-methylethyl)phenyl]methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.08
additional information
3,3'-[[4-(dimethylamino)phenyl]methanediyl]bis(4-hydroxy-2H-chromen-2-one)
Canavalia ensiformis
-
pIC50: 4.09
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8
urease encapsulated in chitosan-coated alginate-magnetite and chitosan-coated alginate-nickel ferrite beads
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression of JBU and JBURE-II genes is induced in seedlings and in leaves treated with abscisic acid, a phytohormone involved in seed maturation and wound reponse
the expression of JBU and JBURE-II genes is induced in seedlings and in leaves treated with abscisic acid, a phytohormone involved in seed maturation and wound reponse
expression of JBU and JBURE-II genes is induced in seedlings and in leaves treated with abscisic acid, a phytohormone involved in seed maturation and wound reponse
the expression of JBU and JBURE-II genes is induced in seedlings and in leaves treated with abscisic acid, a phytohormone involved in seed maturation and wound reponse
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
ureases of Canavalia ensiformis are entomotoxic upon the release of internal peptides by insects digestive enzymes
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). UREA_CANEN
840
0
90748
Swiss-Prot
Mitochondrion (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90000
90770
-
alpha subunit of jack bean urease without Ni2+, method not specified
95000
-
x * 95000, SDS-PAGE, equilibrium sedimentation in presence of guanidinium chloride and 2-mercaptoethanol
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
homohexamer
?
-
x * 95000, SDS-PAGE, equilibrium sedimentation in presence of guanidinium chloride and 2-mercaptoethanol
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
urease is crystallized at 2.05 A resolution. The active-site architecture of JBU is similar to that of bacterial ureases containing a bi-nickel center. JBU has a bound phosphate and covalently modified residue (Cys592) by beta-mercaptoethanol at its active site. By correlating the structural information of JBU with the available biophysical and biochemical data on insecticidal properties of plant ureases, it is hypothesized that the amphipathic beta-hairpin located in the entomotoxic peptide region of plant ureases might form a membrane insertion beta-barrel as found in beta-poreforming toxins
urease is crystallized and the resulting crystals are diffracted to 2.05 A resolution using synchrotron radiation. The crystals belong to the hexagonal space group P6(3)322, with unit-cell parameters a = b = 138.57, c = 198.36 A
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
a significant increase in pH stability is observed for urease-encapsulated magnetic beads compared with the free urease for both acidic and alkaline medium
752526
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
urease-encapsulated magnetic beads protect the stability of 30-45% relative activity at 70°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enhancement of stability of immobilised urease by biocompatible polymer-conjugated magnetic beads for the industrial application based on removal of urea significant increase in pH stability for urease-encapsulated magnetic beads compared with the free urease for both acidic and alkaline medium
interaction with silver nanoparticles result in destabilization of hexameric nature of the enzyme which is otherwise highly stable
urease encapsulated in chitosan nickel ferrite beads shows 50% loss of activity after 18 reuses
urease encapsulated in chitosan-coated alginate-magnetite shows 50% loss of activity after 14 reuses
urease encapsulated in chitosan-coated alginate-nickel ferrite beads shows 50% loss of activity after 14 reuses
urease encapsulated in chitosan-magnetite beads shows 50% loss of activity after 18 reuses
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 162fold from jack bean meal by immobilized metal affinity chromatography using Cu2+ chelated poly(hydroxyethyl methacrylate-N-methacryloyl-(L)-histidine methyl ester) [PHEMAH-Cu2+]-based cryogels, gel resin synthesis and method evaluation and optimization, first- and second-order kinetic constants for enzyme binding, overview. The enzyme can be repeatedly bound and eluted from (PHEMAH)-Cu2+ cryogel with less than 10% loss in column capacity
immobilized metal ion affinity chromatography (Ni2+), purified protein without enzymatic activity, recombinant Escherichia coli cells positive tested for urease activity in a urea segregation agar assay
using acetone precipitation, gel filtration and ion-exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterologous expression of the insecticidal peptide Jaburetox-2Ec, derived from an internal sequence of JBURE-II urease isoform in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
urease is used to calculate the amount of urea in biological solutions in order to remove urea from blood, waste water, fruit juice and foods. Enhancement of stability of immobilised urease by biocompatible polymer-conjugated magnetic beads for industrial application based on removal of urea
industry
enhancement of stability of immobilised urease by biocompatible polymer-conjugated magnetic beads for industrial application based on removal of urea
medicine
a novel immunoconjugate (L-DOS47) is developed and characterized as a therapeutic agent for tumors expressing CEACAM6. The single domain antibody AFAIKL2, which targets CEACAM6, is expressed in the Escherichia coli BL21 (DE3) pT7-7 system. High purity urease is extracted and purified from Jack bean meal. AFAIKL2 is activated using N-succinimidyl [4-iodoacetyl]aminobenzoate (SIAB) as the cross-linker and then conjugated to urease. The specificity and cytotoxicity of L-DOS47 is confirmed by screening in four cell lines (BxPC-3, A549, MCF7, and CEACAM6-transfected H23). BxPC-3, a CEACAM6-expressing cell line is most susceptible to L-DOS47. L-DOS47 is a potential therapeutic agent in human phase I clinical studies for nonsmall cell lung cancer
biotechnology
-
immobilization of urease on arylamine glass beads results in improved thermal, storage and operational stability. Because of inertness of support and stability of immobilized urease, the preparation can find applications in artificial kidney and urea estimation in biological fluids
medicine
-
use of jack bean urease as a model enzyme for Helicobacter pylori urease. Development of organobismuth components without antifungal activity against Saccharomyces cerevisiae but with antibacterial activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Alagna, L.; Hasnain, S.S.; Piggott, B.; Williams, D.J.
The nickel ion environment in jack bean urease
Biochem. J.
220
591-595
1984
Canavalia ensiformis
Dixon, N.E.; Blakeley, R.L.; Zerner, B.
Jack bean urease (EC 3.5.1.5). I. A simple dry ashing procedure for the microdetermination of trace metals in proteins. The nickel content of urease
Can. J. Biochem.
58
469-473
1979
Canavalia ensiformis
Dixon, N.E.; Gazzola, C.; Asher, C.J.; Lee, D.S.W.; Blakeley, R.L.; Zerner, B.
Jack bean urease (EC 3.5.1.5). II. The relationship between nickel, enzymatic activity, and the abnormal ultraviolet spectrum. The nickel content of jack bean
Can. J. Biochem.
58
474-480
1980
Canavalia ensiformis
Dixon, N.E.; Blakeley, R.L.; Zerner, B.
Jack bean urease (EC 3.5.1.5). III. The involvement of active-site nickel ion in inhibition by beta-mercaptoethanol, phosphoramidate, and fluoride
Can. J. Biochem.
58
481-488
1979
Canavalia ensiformis
Butler, L.G.; Reithel, F.J.
Urease-catalyzed urea synthesis
Arch. Biochem. Biophys.
178
43-50
1977
Canavalia ensiformis
Dixon, N.E.; Gazzola, C.; Blakeley, R.L.; Zerner, B.
Metal ions in enzymes using ammonia or amides
Science
191
1144-1150
1976
Sporosarcina pasteurii, Canavalia ensiformis, Cornu aspersum, Otala lactea, Proteus mirabilis
Butler, L.G.
Synthesis of urea with urease in water-organic solvent mixtures
Methods Enzymol.
136
234-238
1987
Canavalia ensiformis
-
Houimel, M.; Mach, J.P.; Corthesy-Theulaz, I.; Fisch, I.
New inhibitors of Helicobacter pylori urease holoenzyme selected from phage-displayed peptide libraries
Eur. J. Biochem.
262
774-780
1999
Sporosarcina pasteurii, Canavalia ensiformis, Helicobacter pylori
Amtul, Z.; Rasheed, M.; Choudhary, M.I.; Rosanna, S.; Khan, K.M.; Atta Ur, R.
Kinetics of novel competitive inhibitors of urease enzymes by a focused library of oxadiazoles/thiadiazoles and triazoles
Biochem. Biophys. Res. Commun.
319
1053-1063
2004
Sporosarcina pasteurii, Canavalia ensiformis, Proteus mirabilis
Tanaka, T.; Kawase, M.; Tani, S.
alpha-Hydroxyketones as inhibitors of urease
Bioorg. Med. Chem.
12
501-505
2004
Canavalia ensiformis
Amtul, Z.; Kausar, N.; Follmer, C.; Rozmahel, R.F.; Atta-Ur-Rahman, R.F.; Kazmi, S.A.; Shekhani, M.S.; Eriksen, J.L.; Khan, K.M.; Choudhary, M.I.
Cysteine based novel noncompetitive inhibitors of urease(s)- distinctive inhibition susceptibility of microbial and plant ureases
Bioorg. Med. Chem.
14
6737-6744
2006
Sporosarcina pasteurii, Canavalia ensiformis, Proteus mirabilis
Murafuji, T.; Azuma, T.; Miyoshi, Y.; Ishibashi, M.; Rahman, A.F.; Migita, K.; Sugihara, Y.; Mikata, Y.
Inhibition of jack bean urease by organobismuth compounds
Bioorg. Med. Chem. Lett.
16
1510-1513
2006
Canavalia ensiformis
Khan, W.N.; Lodhi, M.A.; Ali, I.; Azhar-Ul-Haq, I.; Malik, A.; Bilal, S.; Gul, R.; Choudhary, M.I.
New natural urease inhibitors from Ranunculus repens
J. Enzyme Inhib. Med. Chem.
21
17-19
2006
Sporosarcina pasteurii, Canavalia ensiformis
Godjevargova, T.; Gabrovska, K.
Kinetic parameters of urease immobilized on modified acrylonitrile copolymer membranes in the presence and absence of Cu(II) ions
Macromol. Biosci.
5
459-466
2005
Canavalia ensiformis
Khan, K.M.; Saify, Z.S.; Arif Lodhi, M.; Butt, N.; Perveen, S.; Maharvi, G.M.; Choudhary, M.I.; Atta-Ur-Rahman, M.I.
Piperidines: a new class of urease inhibitors
Nat. Prod. Res.
20
523-530
2006
Canavalia ensiformis
Krajewska, B.; Ciurli, S.
Jack bean (Canavalia ensiformis) urease. Probing acid-base groups of the active site by pH variation
Plant Physiol. Biochem.
43
651-658
2005
Canavalia ensiformis
Krajewska, B.; Zaborska, W.
Jack bean urease: the effect of active-site binding inhibitors on the reactivity of enzyme thiol groups
Bioorg. Chem.
35
355-365
2007
Canavalia ensiformis
Sivapriya, K.; Suguna, P.; Banerjee, A.; Saravanan, V.; Rao, D.N.; Chandrasekaran, S.
Facile one-pot synthesis of thio and selenourea derivatives: a new class of potent urease inhibitors
Bioorg. Med. Chem. Lett.
17
6387-6391
2007
Canavalia ensiformis
Dominguez, M.J.; Sanmartin, C.; Font, M.; Palop, J.A.; San Francisco, S.; Urrutia, O.; Houdusse, F.; Garcia-Mina, J.M.
Design, synthesis, and biological evaluation of phosphoramide derivatives as urease inhibitors
J. Agric. Food Chem.
56
3721-3731
2008
Canavalia ensiformis
Ayaz, M.; Lodhi, M.A.; Riaz, M.; Ul-haq, A.; Malik, A.; Choudhary, M.I.
Novel urease inhibitors from Daphne oleoids
J. Enzyme Inhib. Med. Chem.
21
527-529
2006
Sporosarcina pasteurii, Canavalia ensiformis
Kot, M.; Zaborska, W.
Inhibition of jack bean urease by tetrachloro-o-benzoquinone and tetrachloro-p-benzoquinone
J. Enzyme Inhib. Med. Chem.
21
537-542
2006
Canavalia ensiformis
Kot, M.
Inhibition of jack bean urease by p-benzoquinone: elucidation of the role of thiols and reversibility of the process
J. Enzyme Inhib. Med. Chem.
21
697-701
2006
Canavalia ensiformis
Mulinari, F.; Staniscuaski, F.; Bertholdo-Vargas, L.R.; Postal, M.; Oliveira-Neto, O.B.; Rigden, D.J.; Grossi-de-Sa, M.F.; Carlini, C.R.
Jaburetox-2Ec: An insecticidal peptide derived from an isoform of urease from the plant Canavalia ensiformis
Peptides
28
2042-2050
2007
Canavalia ensiformis (Q8H6V8), Canavalia ensiformis
Follmer, C.
Insights into the role and structure of plant ureases
Phytochemistry
69
18-28
2008
Canavalia ensiformis, Canavalia ensiformis (Q8H6V8), Glycine max
Saburova, E.A.; Tikhonenko, S.A.; Dybovskaya, Y.N.; Sukhorukov, B.I.
Changes in the activity and structure of urease in the interaction with polyelectrolytes
Russ. J. Phys. Chem. A
82
468-474
2008
Canavalia ensiformis
-
Becker-Ritt, A.B.; Martinelli, A.H.; Mitidieri, S.; Feder, V.; Wassermann, G.E.; Santi, L.; Vainstein, M.H.; Oliveira, J.T.; Fiuza, L.M.; Pasquali, G.; Carlini, C.R.
Antifungal activity of plant and bacterial ureases
Toxicon
50
971-983
2007
Canavalia ensiformis (P07374), Glycine max (Q7XAC5), Glycine max, Helicobacter pylori (Q84F75), Helicobacter pylori
Khan, K.M.; Iqbal, S.; Lodhi, M.A.; Maharvi, G.M.; Ullah, Z.; Choudhary, M.I.; Rahman, A.U.; Perveen, S.
Biscoumarin: new class of urease inhibitors; economical synthesis and activity
Bioorg. Med. Chem.
15
1963-1968
2004
Canavalia ensiformis
Zaheer-ul-Haq, K.; Lodhi, M.A.; Ahmad Nawaz, S.; Iqbal, S.; Mohammed Khan, K.; Rode, B.M.; Atta-ur-Rahman, B.M.; Choudhary, M.I.
3D-QSAR CoMFA studies on bis-coumarine analogues as urease inhibitors: a strategic design in anti-urease agents
Bioorg. Med. Chem.
16
3456-3461
2008
Canavalia ensiformis
Font, M.; Dominguez, M.J.; Sanmartin, C.; Palop, J.A.; San-Francisco, S.; Urrutia, O.; Houdusse, F.; Garcia-Mina, J.M.
Structural characteristics of phosphoramide derivatives as urease inhibitors. Requirements for activity
J. Agric. Food Chem.
56
8451-8460
2008
Canavalia ensiformis
Kot, M.; Bicz, A.
Inactivation of jack bean urease by N-ethylmaleimide: pH dependence, reversibility and thiols influence
J. Enzyme Inhib. Med. Chem.
23
514-520
2008
Canavalia ensiformis
Krajewska, B.
Mono- (Ag, Hg) and di- (Cu, Hg) valent metal ions effects on the activity of jack bean urease. Probing the modes of metal binding to the enzyme
J. Enzyme Inhib. Med. Chem.
23
535-542
2008
Canavalia ensiformis
Ansari, F.L.; Wadood, A.; Ullah, A.; Iftikhar, F.; Ul-Haq, Z.
In silico studies of urease inhibitors to explore ligand-enzyme interactions
J. Enzyme Inhib. Med. Chem.
24
151-156
2009
Canavalia ensiformis
Balasubramanian, A.; Ponnuraj, K.
Purification, crystallization and preliminary X-ray analysis of urease from jack bean (Canavalia ensiformis)
Acta Crystallogr. Sect. F
65
949-951
2009
Canavalia ensiformis
Marlier, J.F.; Robins, L.I.; Tucker, K.A.; Rawlings, J.; Anderson, M.A.; Cleland, W.W.
A Kinetic and Isotope Effect Investigation of the Urease-Catalyzed Hydrolysis of Hydroxyurea
Biochemistry
49
8213-8219
2010
Canavalia ensiformis
Kot, M.; Karcz, W.; Zaborska, W.
5-Hydroxy-1,4-naphthoquinone (juglone) and 2-hydroxy-1,4-naphthoquinone (lawsone) influence on jack bean urease activity: Elucidation of the difference in inhibition activity
Bioorg. Chem.
38
132-137
2010
Canavalia ensiformis
Shabana, S.; Kawai, A.; Kai, K.; Akiyama, K.; Hayashi, H.
Inhibitory activity against urease of quercetin glycosides isolated from Allium cepa and Psidium guajava
Biosci. Biotechnol. Biochem.
74
878-880
2010
Canavalia ensiformis
You, Z.L.; Ni, L.L.; Shi, D.H.; Bai, S.
Synthesis, structures, and urease inhibitory activities of three copper(II) and zinc(II) complexes with 2-{[2-(2-hydroxyethylamino)ethylimino]methyl}-4-nitrophenol
Eur. J. Med. Chem.
45
3196-3199
2010
Canavalia ensiformis
Arfan, M.; Ali, M.; Ahmad, H.; Anis, I.; Khan, A.; Choudhary, M.I.; Shah, M.R.
Urease inhibitors from Hypericum oblongifolium WALL
J. Enzyme Inhib. Med. Chem.
25
296-299
2010
Canavalia ensiformis
Akhtar, T.; Hameed, S.; Khan, K.M.; Khan, A.; Choudhary, M.I.
Design, synthesis, and urease inhibition studies of some 1,3,4-oxadiazoles and 1,2,4-triazoles derived from mandelic acid
J. Enzyme Inhib. Med. Chem.
25
572-576
2010
Canavalia ensiformis
Krajewska, B.; Brindell, M.
Urease activity and l-ascorbic acid
J. Enzyme Inhib. Med. Chem.
26
309-318
2011
Canavalia ensiformis
Balasubramanian, A.; Ponnuraj, K.
Crystal structure of the first plant urease from jack bean: 83 years of journey from its first crystal to molecular structure
J. Mol. Biol.
400
274-283
2010
Canavalia ensiformis (P07374), Canavalia ensiformis
Krajewska, B.
Ureases I. Functional, catalytic and kinetic properties: A review
J. Mol. Catal. B
59
9-21
2009
Klebsiella aerogenes, Pseudarthrobacter oxydans, Aspergillus nidulans, Aspergillus niger, Sporosarcina pasteurii, Corynebacterium ammoniagenes, Cajanus cajan, Canavalia ensiformis, Coccidioides immitis, Helicobacter pylori, Limosilactobacillus fermentum, Limosilactobacillus reuteri, Otala lactea, Proteus mirabilis, Providencia rettgeri, Providencia stuartii, Schizosaccharomyces pombe, Selenomonas ruminantium, Staphylococcus saprophyticus, Staphylococcus sp., Staphylococcus xylosus, Streptococcus mitior, Ureaplasma urealyticum, Staphylococcus leei, Brucella suis, Pseudomonas, Klebsiella, Arthrobacter mobilis, Nitellopsis obtusa
-
Khan, K.M.; Wadood, A.; Ali, M.; Zia-Ullah, M.; Ul-Haq, Z.; Lodhi, M.A.; Khan, M.; Perveen, S.; Choudhary, M.I.
Identification of potent urease inhibitors via ligand- and structure-based virtual screening and in vitro assays
J. Mol. Graph. Model.
28
792-798
2010
Sporosarcina pasteurii, Canavalia ensiformis
Mangaldas, K.; Rajput, Y.; Sharma, R.
Urease immobilization on arylamine glass beads and its characterization
J. Plant Biochem. Biotechnol.
19
73-77
2010
Canavalia ensiformis
-
Berlicki, L.; Bochno, M.; Grabowiecka, A.; Bialas, A.; Kosikowska, P.; Kafarski, P.
N-Substituted aminomethanephosphonic and aminomethane-P-methylphosphinic acids as inhibitors of ureases
Amino Acids
42
1937-1945
2012
Sporosarcina pasteurii, Canavalia ensiformis, Sporosarcina pasteurii CCM 2056T
Mulinari, F.; Becker-Ritt, A.B.; Demartini, D.R.; Ligabue-Braun, R.; Staniscuaski, F.; Verli, H.; Fragoso, R.R.; Schroeder, E.K.; Carlini, C.R.; Grossi-de-Sa, M.F.
Characterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease
Biochim. Biophys. Acta
1814
1758-1768
2011
Canavalia ensiformis (E6Y5X0), Canavalia ensiformis
Khan, I.; Ali, S.; Hameed, S.; Rama, N.H.; Hussain, M.T.; Wadood, A.; Uddin, R.; Ul-Haq, Z.; Khan, A.; Ali, S.; Choudhary, M.I.
Synthesis, antioxidant activities and urease inhibition of some new 1,2,4-triazole and 1,3,4-thiadiazole derivatives
Eur. J. Med. Chem.
45
5200-5207
2010
Canavalia ensiformis
Aslam, M.A.; Mahmood, S.U.; Shahid, M.; Saeed, A.; Iqbal, J.
Synthesis, biological assay in vitro and molecular docking studies of new Schiff base derivatives as potential urease inhibitors
Eur. J. Med. Chem.
46
5473-5479
2011
Canavalia ensiformis
Defferrari, M.S.; Demartini, D.R.; Marcelino, T.B.; Pinto, P.M.; Carlini, C.R.
Insecticidal effect of Canavalia ensiformis major urease on nymphs of the milkweed bug Oncopeltus fasciatus and characterization of digestive peptidases
Insect Biochem. Mol. Biol.
41
388-399
2011
Canavalia ensiformis
Lodhi, M.A.; Shams, S.; Choudhary, M.I.; Lodhi, A.; Ul-Haq, Z.; Jalil, S.; Nawaz, S.A.; Khan, K.M.; Iqbal, S.; Rahman, A.U.
Structural basis of binding and rationale for the potent urease inhibitory activity of biscoumarins
BioMed Res. Int.
2014
935039
2014
Sporosarcina pasteurii, Canavalia ensiformis (P07374), Canavalia ensiformis
Saeed, A.; Khan, M.S.; Rafique, H.; Shahid, M.; Iqbal, J.
Design, synthesis, molecular docking studies and in vitro screening of ethyl 4-(3-benzoylthioureido) benzoates as urease inhibitors
Bioorg. Chem.
52
1-7
2014
Canavalia ensiformis (P07374)
Khan, K.M.; Naz, F.; Taha, M.; Khan, A.; Perveen, S.; Choudhary, M.I.; Voelter, W.
Synthesis and in vitro urease inhibitory activity of N,N'-disubstituted thioureas
Eur. J. Med. Chem.
74
314-323
2014
Canavalia ensiformis
Adsul, L.K.; Bandgar, B.P.; Chavan, H.V.; Jalde, S.S.; Dhakane, V.D.; Shirfule, A.L.
Synthesis and biological evaluation of novel series of aminopyrimidine derivatives as urease inhibitors and antimicrobial agents
J. Enzyme Inhib. Med. Chem.
28
1316-1323
2013
Canavalia ensiformis
Du, N.; Sheng, L.; Xu, H.; Song, C.; Chen, S.
Kinetics of competitive inhibition of jack bean urease by boric acid
J. Mol. Catal. B
82
53-58
2012
Canavalia ensiformis (P07374)
-
Tekiner, P.; Percin, I.; Erguen, B.; Yavuz, H.; Aksoez, E.
Purification of urease from jack bean (Canavalia ensiformis) with copper (II) chelated poly(hydroxyethyl methacrylate-N-methacryloyl-(L)-histidine methyl ester) cryogels
J. Mol. Recognit.
25
549-554
2012
Canavalia ensiformis (P07374), Canavalia ensiformis
Rauf, A.; Liaqat, S.; Qureshi, A.; Yaqub, M.; Rehman, A.; Hassan, M.; Chohan, Z.; Nasim, F.; Hadda, T.
Synthesis, characterization, and urease inhibition of 5-substituted-8-methyl-2H-pyrido[1,2-a]pyrimidine-2,4(3H)-diones
Med. Chem. Res.
21
60-74
2012
Canavalia ensiformis (P07374)
-
Dogac, Y.I.; Teke, M.
Synthesis and characterisation of biocompatible polymer-conjugated magnetic beads for enhancement stability of urease
Appl. Biochem. Biotechnol.
179
94-110
2016
Canavalia ensiformis (P07374)
Tian, B.; Wong, W.Y.; Hegmann, E.; Gaspar, K.; Kumar, P.; Chao, H.
Production and characterization of a camelid single domain antibody-urease enzyme conjugate for the treatment of cancer
Bioconjug. Chem.
26
1144-1155
2015
Canavalia ensiformis (P07374), Canavalia ensiformis
Abbas, A.; Ali, B.; Kanwal, B.; Khan, K.M.; Iqbal, J.; Ur Rahman, S.; Zaib, S.; Perveen, S.
Synthesis and in vitro urease inhibitory activity of benzohydrazide derivatives, in silico and kinetic studies
Bioorg. Chem.
82
163-177
2019
Canavalia ensiformis (P07374)
Rehman, N.U.; Khan, A.; Al-Harrasi, A.; Khiat, M.; Hussain, H.; Wadood, A.; Riaz, M.
Natural urease inhibitors from Aloe vera resin and Lycium shawii and their structural-activity relationship and molecular docking study
Bioorg. Chem.
88
102955
2019
Canavalia ensiformis (P07374)
Abdul Fattah, T.; Saeed, A.; Channar, P.A.; Ashraf, Z.; Abbas, Q.; Hassan, M.; Larik, F.A.
Synthesis, enzyme inhibitory kinetics, and computational studies of novel 1-(2-(4-isobutylphenyl) propanoyl)-3-arylthioureas as Jack bean urease inhibitors
Chem. Biol. Drug Des.
91
434-447
2018
Canavalia ensiformis (P07374), Canavalia ensiformis
Rauf, M.K.; Yaseen, S.; Badshah, A.; Zaib, S.; Arshad, R.; Imtiaz-Ud-Din, R.; Tahir, M.N.; Iqbal, J.
Synthesis, characterization and urease inhibition, in vitro anticancer and antileishmanial studies of Ni(II) complexes with N,N,N-trisubstituted thioureas
J. Biol. Inorg. Chem.
20
541-554
2015
Canavalia ensiformis (P07374), Canavalia ensiformis
Mazzei, L.; Cianci, M.; Musiani, F.; Lente, G.; Palombo, M.; Ciurli, S.
Inactivation of urease by catechol kinetics and structure
J. Inorg. Biochem.
166
182-189
2017
Canavalia ensiformis (P07374), Canavalia ensiformis, Sporosarcina pasteurii (P41022), Sporosarcina pasteurii
Krajewska, B.
A combined temperature-pH study of urease kinetics. Assigning pKa values to ionizable groups of the active site involved in the catalytic reaction
J. Mol. Catal. B
124
70-76
2016
Canavalia ensiformis (P07374)
-
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