Information on EC 3.5.1.5 - urease

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
3.5.1.5
-
RECOMMENDED NAME
GeneOntology No.
urease
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
urea + H2O = CO2 + 2 NH3
show the reaction diagram
-
-
-
-
urea + H2O = CO2 + 2 NH3
show the reaction diagram
mechanism
-
urea + H2O = CO2 + 2 NH3
show the reaction diagram
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 ACCESSION NO.
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
carboxylic acid amide hydrolysis
-
-
condensation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
Atrazine degradation
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Purine metabolism
-
urea degradation II
-
SYSTEMATIC NAME
IUBMB Comments
urea amidohydrolase
A nickel protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
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
embryo-specific soybean urease
-
-
JBU
Q8H6V8
presence of a family of urease related genes in Canavalia ensiformis with at least three members: canatoxin, JBU and JBURE-II
JBURE-II
Q8H6V8
-
JBURE-II
Q8H6V8
family of urease related genes in Canavalia ensiformis with at least three members: canatoxin, JBU and JBURE-II
Urea amidohydrolase
-
-
-
-
Urea amidohydrolase
-
-
Urea amidohydrolase
-
-
Urea amidohydrolase
-
-
Urea amidohydrolase
-
-
Urea amidohydrolase
Proteus vulgaris CCM 1956
-
-
-
Urea amidohydrolase
-
-
Urea amidohydrolase
Sporosarcina pasteurii CCM 2056
-
-
-
urease
-
-
urease
Q8FZW3
-
urease
Q8FZW3
-
-
urease
P07374
-
urease
P18314 and P18315 and P18316
-
urease
Enterobacter sp. R-SYB082
-
-
-
urease
Helicobacter hepaticus 3B1
-
-
-
urease
-
-
urease
Proteus vulgaris CCM 1956
-
-
-
urease
Sporosarcina pasteurii CCM 2056, Sporosarcina pasteurii CCM 2056T
-
-
-
urease
-
-
urease JBURE-IIb
E6Y5X0
-
CAS REGISTRY NUMBER
COMMENTARY
9002-13-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain WVU45
Uniprot
Manually annotated by BRENDA team
Actinomyces naeslundii WVU45
strain WVU45
Uniprot
Manually annotated by BRENDA team
Arthrobacter mobilis
-
-
-
Manually annotated by BRENDA team
bacterium strain SL100
gram-positive coccoid isolate prototype with an adhesin specific for gastric mucin
-
-
Manually annotated by BRENDA team
urease subunit beta 2; strain 1330, ATCC 23444
UniProt
Manually annotated by BRENDA team
urease subunit beta 2; strain 1330, ATCC 23444
UniProt
Manually annotated by BRENDA team
pigeonpea
-
-
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
i.e. jack bean
-
-
Manually annotated by BRENDA team
subunits alpha, beta, gamma
P18314 and P18315 and P18316
UniProt
Manually annotated by BRENDA team
R-SYB082; strain R-SYB082
-
-
Manually annotated by BRENDA team
Enterobacter sp. R-SYB082
R-SYB082; strain R-SYB082
-
-
Manually annotated by BRENDA team
-
Q7XAC5
Uniprot
Manually annotated by BRENDA team
alpha-subunit
SwissProt
Manually annotated by BRENDA team
beta-subunit
SwissProt
Manually annotated by BRENDA team
enzyme activity does not contribute to acid resistance of strain ATCC 51449, enzyme is acid-independent. Supplementation of medium by nickel leads to tenfold increase in enzyme activity, independent of de novo protein synthesis
-
-
Manually annotated by BRENDA team
Helicobacter hepaticus 3B1
strain 3B1
-
-
Manually annotated by BRENDA team
ATCC 41653
-
-
Manually annotated by BRENDA team
ATCC 43504
-
-
Manually annotated by BRENDA team
enzyme is induced by acid. Supplementation of medium by nickel leads to tenfold increase in enzyme activity, independent of de novo protein synthesis
-
-
Manually annotated by BRENDA team
recombinantly expressed in Escherichia coli
Uniprot
Manually annotated by BRENDA team
Lactobacillus animalis MU-4
MU-4
-
-
Manually annotated by BRENDA team
strain IFO 14511
-
-
Manually annotated by BRENDA team
Lactobacillus fermentum IFO 14511
strain IFO 14511
-
-
Manually annotated by BRENDA team
strain Rt-5
-
-
Manually annotated by BRENDA team
Lactobacillus reuteri RT-5
strain Rt-5
-
-
Manually annotated by BRENDA team
strain PG-98
-
-
Manually annotated by BRENDA team
Lactobacillus ruminis PG-98
strain PG-98
-
-
Manually annotated by BRENDA team
CCM 1956
-
-
Manually annotated by BRENDA team
Proteus vulgaris CCM 1956
CCM 1956
-
-
Manually annotated by BRENDA team
strain E1F1
-
-
Manually annotated by BRENDA team
Rhodobacter capsulatus E1F1
strain E1F1
-
-
Manually annotated by BRENDA team
Sporosarcina pasteurii CCM 2056
CCM 2056
-
-
Manually annotated by BRENDA team
Sporosarcina pasteurii CCM 2056T
-
-
-
Manually annotated by BRENDA team
exhibits high urease activity and is capable of growing in urinary condition by forming robust biofilms
-
-
Manually annotated by BRENDA team
Streptococcus mitior
-
-
-
Manually annotated by BRENDA team
Streptococcus mitior
PG-118
-
-
Manually annotated by BRENDA team
Streptococcus mitior PG-118
PG-118
-
-
Manually annotated by BRENDA team
strain PG-202
-
-
Manually annotated by BRENDA team
Streptococcus salivarius PG-202
strain PG-202
-
-
Manually annotated by BRENDA team
strain TH3996
-
-
Manually annotated by BRENDA team
biovar 1A strain
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
growth studies demonstrate that Edwardsiella ictaluri is unable to grow at pH 5 in the absence of urea but is able to elevate the environmental pH from pH 5 to pH 7 and grow when exogenous urea is available; urease is required for proliferation and virulence and for intracellular replication. Intracellular replication of wild-type Edwardsiella ictaluri is significantly enhanced when urea is present, indicating that urease plays an important role in intracellular survival and replication, possibly through neutralization of the acidic environment of the phagosome
physiological function
-
effects of urease added to rabbit platelets are assessed turbidimetrically. Fluorescein-labelled HPU bound to platelets but not to erythrocytes. HPU induces aggregation of rabbit platelets accompanied by ATP secretion. No correlation is found between platelet activation and ureolytic activity of HPU
physiological function
-
the bacterium typically colonizes the mucosal lining of the stomach, where the increase in pH of the strongly acidic environment allows the bacterium that requires pH 6-8 to grow, to persist in the hostile conditions. Concomitantly it incurs damage to the host tissue, thereby giving rise to gastritis and gastroduodenal ulcers. The damaging factors are ammonia and monochloramine
physiological function
-
ureolytic bacterium responsible for the formation of urinary stones in human
physiological function
-
the biosynthesis of the active metal-bound form of the nickel-dependent enzyme urease involves the formation of a lysine-carbamate functional group concomitantly with the delivery of two Ni2+- ions into the precast active site of the apoenzyme and with GTP hydrolysis. In the urease system, this role is performed by UreG, an accessory protein belonging to the group of homologous P-loop GTPases
metabolism
-
nitrogen metabolism, could be crucial for the pathogen's survival in nutrient-limited microenvironments where urea is the sole nitrogen source
additional information
-
ureases of Canavalia ensiformis are entomotoxic upon the release of internal peptides by insects digestive enzymes
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
Streptococcus mitior
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
Streptococcus mitior
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-, Q9Z395
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
bacterium strain SL100
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
role for urease and urease-derived ammonia in megasome formation and survival of Helicobacter pylori in murine peritoneal macrophages and J774 cells
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
Streptococcus salivarius PG-202, Lactobacillus reuteri RT-5
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
Rhodobacter capsulatus E1F1
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
Lactobacillus fermentum IFO 14511, Lactobacillus ruminis PG-98, Lactobacillus animalis MU-4, Streptococcus mitior PG-118
-
-
-
-
urea + H2O
CO2 + NH3
show the reaction diagram
Enterobacter sp. R-SYB082
-
-
-
-
?
urea + H2O
?
show the reaction diagram
-
expression increases 10fold upon nitrogen deprivation, the enzyme is involved in nitrogen aquisition by the bacterium
-
-
?
urea + H2O
?
show the reaction diagram
-
urease is an important antigen and appears critical for colonization and virulence
-
-
?
urea + H2O
?
show the reaction diagram
bacterium strain SL100
-
urease may be a virulence factor during colonization of the stomach
-
-
-
urea + H2O
?
show the reaction diagram
-
important virulence factor
-
-
?
urea + H2O
?
show the reaction diagram
-
urease protects Helicobacter pylori against the acidic environment of the stomach, the enzyme acts as cytotoxin, with human gastric cells especially susceptible to its activity and disrups cell tight junctions in such a manner that the cells remain viable but an ionic flow between the cells occurs
-
-
?
urea + H2O
?
show the reaction diagram
-
enzyme is induced by urea and short-chain amides, repressed by excess ammonia
-
-
?
urea + H2O
?
show the reaction diagram
-
urease is a critical virulence factor in urinary tract infection
-
-
?
urea + H2O
?
show the reaction diagram
-, Q9Z395
urea can be utilized as a nitrogen source via a urease-dependent pathway, the ureolysis can protect the organism against environmental acidification at physiologically relevant pH values. Therefor, urease can confer to Actinomyces naeslundii critical selective advantages over nonureolytic organisms in dental plaque
-
-
?
urea + H2O
?
show the reaction diagram
-
NH4+ inhibits urease expression
-
-
?
urea + H2O
?
show the reaction diagram
-
virulence factor since the ammonium ion produced from urea may by responsible for tissue injury and/or survival of the organism in the gastric environment
-
-
?
urea + H2O
?
show the reaction diagram
Rhodobacter capsulatus E1F1
-
NH4+ inhibits urease expression
-
-
?
urea + H2O
CO2 + 2 NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + 2 NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + 2 NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + 2 NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + 2 NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + 2 NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + 2 NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + 2 NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + 2 NH3
show the reaction diagram
-
-
-
-
?
urea + H2O
CO2 + 2 NH3
show the reaction diagram
-, Q8FZW3
-
-
-
?
urea + H2O
CO2 + 2 NH3
show the reaction diagram
Q8FZW3
-
-
-
?
urea + H2O
CO2 + 2 NH3
show the reaction diagram
Proteus vulgaris CCM 1956, Sporosarcina pasteurii CCM 2056
-
-
-
-
?
urea + H2O
CO2 + 2 NH3
show the reaction diagram
Enterobacter sp. R-SYB082
-
-
-
-
?
urea + H2O
ammonia + CO2
show the reaction diagram
-
-
-
-
-
urea + H2O
2 NH3 + CO2
show the reaction diagram
-
-
-
-
?
urea + H2O
2 NH3 + CO2
show the reaction diagram
-
-
-
-
?
urea + H2O
2 NH3 + CO2
show the reaction diagram
Sporosarcina pasteurii CCM 2056T
-
-
-
-
?
hydroxyurea
HCO3- + NH4+ + NH2OH
show the reaction diagram
-
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
-
-
?
additional information
?
-
-
Cotton seed urease displays low ureolytic activity but exhibits potent antifungal properties at sub-micromolar concentrations against different phytopathogenic fungi. The antifungal effect of cotton urease persists after treatment with an irreversible inhibitor of its enzyme activity. The data suggest an important role of the protein in plant defense
-
-
-
additional information
?
-
-
insecticidal activity of the jack bean ureases JBU and canatoxin. JBU and canatoxin are able to induce activation of rabbit blood platelets, 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
?
-
Q84F75
the urease impairs growth of selected phytopathogenic fungi at sub-micromolar concentrations. This antifungal property of ureases is not affected by treatment of the proteins with an irreversible inhibitor of the ureolytic activity
-
-
-
additional information
?
-
Q7XAC5
the urease impairs growth of selected phytopathogenic fungi at sub-micromolar concentrations. This antifungal property of ureases is not affected by treatment of the proteins with an irreversible inhibitor of the ureolytic activity. Ureases probably contribute to the plant arsenal of defense compounds against predators and phytopathogens
-
-
-
additional information
?
-
P07374
the urease impairs growth of selected phytopathogenic fungi at sub-micromolar concentrations. This antifungal property of ureases is not affected by treatment of the proteins with an irreversible inhibitor of the ureolytic activity. Ureases probably contribute to the plant arsenal of defense compounds against predators and phytopathogens
-
-
-
additional information
?
-
-
platelet aggregation induced by Bacillus pasteurii urease is mediated by lipoxygenase-derived eicosanoids and secretion of ADP from the platelets through a calcium-dependent mechanism
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
urea + H2O
CO2 + NH3
show the reaction diagram
-
role for urease and urease-derived ammonia in megasome formation and survival of Helicobacter pylori in murine peritoneal macrophages and J774 cells
-
-
?
urea + H2O
?
show the reaction diagram
-
expression increases 10fold upon nitrogen deprivation, the enzyme is involved in nitrogen aquisition by the bacterium
-
-
?
urea + H2O
?
show the reaction diagram
-
urease is an important antigen and appears critical for colonization and virulence
-
-
?
urea + H2O
?
show the reaction diagram
bacterium strain SL100
-
urease may be a virulence factor during colonization of the stomach
-
-
-
urea + H2O
?
show the reaction diagram
-
important virulence factor
-
-
?
urea + H2O
?
show the reaction diagram
-
urease protects Helicobacter pylori against the acidic environment of the stomach, the enzyme acts as cytotoxin, with human gastric cells especially susceptible to its activity and disrups cell tight junctions in such a manner that the cells remain viable but an ionic flow between the cells occurs
-
-
?
urea + H2O
?
show the reaction diagram
-
enzyme is induced by urea and short-chain amides, repressed by excess ammonia
-
-
?
urea + H2O
?
show the reaction diagram
-
urease is a critical virulence factor in urinary tract infection
-
-
?
urea + H2O
?
show the reaction diagram
-, Q9Z395
urea can be utilized as a nitrogen source via a urease-dependent pathway, the ureolysis can protect the organism against environmental acidification at physiologically relevant pH values. Therefor, urease can confer to Actinomyces naeslundii critical selective advantages over nonureolytic organisms in dental plaque
-
-
?
urea + H2O
?
show the reaction diagram
-
NH4+ inhibits urease expression
-
-
?
urea + H2O
?
show the reaction diagram
-
virulence factor since the ammonium ion produced from urea may by responsible for tissue injury and/or survival of the organism in the gastric environment
-
-
?
urea + H2O
?
show the reaction diagram
Rhodobacter capsulatus E1F1
-
NH4+ inhibits urease expression
-
-
?
additional information
?
-
-
Cotton seed urease displays low ureolytic activity but exhibits potent antifungal properties at sub-micromolar concentrations against different phytopathogenic fungi. The antifungal effect of cotton urease persists after treatment with an irreversible inhibitor of its enzyme activity. The data suggest an important role of the protein in plant defense
-
-
-
additional information
?
-
-
insecticidal activity of the jack bean ureases JBU and canatoxin. JBU and canatoxin are able to induce activation of rabbit blood platelets, 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
?
-
Q84F75
the urease impairs growth of selected phytopathogenic fungi at sub-micromolar concentrations. This antifungal property of ureases is not affected by treatment of the proteins with an irreversible inhibitor of the ureolytic activity
-
-
-
additional information
?
-
Q7XAC5
the urease impairs growth of selected phytopathogenic fungi at sub-micromolar concentrations. This antifungal property of ureases is not affected by treatment of the proteins with an irreversible inhibitor of the ureolytic activity. Ureases probably contribute to the plant arsenal of defense compounds against predators and phytopathogens
-
-
-
additional information
?
-
P07374
the urease impairs growth of selected phytopathogenic fungi at sub-micromolar concentrations. This antifungal property of ureases is not affected by treatment of the proteins with an irreversible inhibitor of the ureolytic activity. Ureases probably contribute to the plant arsenal of defense compounds against predators and phytopathogens
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
enhances activity
K+
-
assay with 200 mM KCl
Mg2+
-
enhances activity
Ni2+
-
soybean urease is inactive when soybean cell cultures are grown in the absence of nickel
Ni2+
P18314 and P18315 and P18316
urease activation: apoprotein (UreABC)3 + 6 Ni2+
Ni2+
-
activity is dependent on Ni in the medium
Ni2+
-
required for activity
Ni2+
-
required for activity
Ni2+
E6Y5X0
metallocenter, nickel-dependent
Nickel
-
each of the 4 subunits contains 1 atom of nickel; nickel metalloenzyme
Nickel
-
nickel metalloenzyme; specifically required for ureolysis and cannot be replaced by another metal, 0.5 mol of nickel is firmly bound to 1 mol of enzyme protein
Nickel
-
contains 0.8 gatom of nickel per 67000 g of protein; contains 1 atom of nickel per subunit; nickel metalloenzyme
Nickel
-
nickel metalloenzyme; study of nickel environment in the enzyme
Nickel
-
enzyme contains 2 gatom of nickel per 96600 g of protein; nickel metalloenzyme
Nickel
bacterium strain SL100
-
nickel metalloenzyme
Nickel
-
His320 of subunit C is essential for urea hydrolysis and Ni2+ binding within the native enzyme; nickel metalloenzyme
Nickel
-
enzyme contains 4.09 atoms of nickel per molecule
Nickel
-
dinuclear nickel active site
Nickel
-
nickel metalloenzyme; wild-type enzyme contains 4.6 atoms of nickel per molecule of urease, the nickel content of the mutant enzymes C319A, C319S, C319D and C319Y is lower
Nickel
-
nickel metalloenzyme; partial activation of the apoprotein in presence of Ni(II) and CO2, incubation with Ni alone leads to the formation of inactive proteins
Nickel
-
contains about 6 Ni2+ ions per urease molecule; nickel metalloenzyme
Nickel
-
addition of Ni to purified apourease does not yield active enzyme, the apoenzyme is very slowly activated in vivo by addition of Ni2+ ions to Ni-free cell cultures, apourease activation is an energy-dependent process that is deactivated by cell disruption; nickel metalloenzyme
Nickel
-
contains 200 ng nickel per mg of protein; nickel metalloenzyme
Nickel
-
nickel-containing metalloenzymel
Mn2+
-
enhances activity
additional information
-
urease apoprotein binds numerous metal ions
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2-[[(2-[[2-(hydroxy-kappaO)ethyl]amino-kappaN]ethyl)imino-kappaN]methyl]-4-nitrophenolato-kappaO)(methoxymethanolato-kappaO)zinc
-
-
(2-[[(2-[[2-(hydroxy-kappaO)ethyl]amino-kappaN]ethyl)imino-kappaN]methyl]-4-nitrophenolato-kappaO)(nitrato-kappaO)copper
-
-
(2E)-3-(1,3-benzodioxol-5-yl)-1-(2-hydroxyphenyl)prop-2-en-1-one
-
-
(2S)-2-(dimethylamino)-3-(ethylthio)propan-1-ol
-
noncompetitive, 50% inhibition at 0.040 mM
(2S)-2-(dimethylamino)-3-(ethylthio)propan-1-ol
-
noncompetitive, 50% inhibition at 0.029 mM
(2S)-2-(dimethylamino)-3-ethoxypropane-1-thiol
-
noncompetitive, 50% inhibition at 0.100 mM
(2S)-2-(dimethylamino)-3-ethoxypropane-1-thiol
-
noncompetitive, 50% inhibition at 0.031 mM
(2S)-2-(dimethylamino)-3-ethoxypropane-1-thiol
-
noncompetitive, 50% inhibition at 0.020 mM
(2S)-2-(dimethylamino)-3-mercaptopropan-1-ol
-
noncompetitive, 50% inhibition at 0.022 mM
(2S)-2-(dimethylamino)-3-mercaptopropan-1-ol
-
noncompetitive, 50% inhibition at 0.025 mM
(2S)-2-(dimethylamino)-3-methoxypropane-1-thiol
-
noncompetitive, 50% inhibition at 0.035 mM
(2S)-2-(dimethylamino)-3-methoxypropane-1-thiol
-
noncompetitive, 50% inhibition at 0.036 mM
(aminomethyl)methylphosphinic acid
-
-
(aminomethyl)phosphonic acid
-
-
(E)-1-((E)-3-phenylallylidene)thiosemicarbazide
-
-
-
(E)-1-(2-chlorobenzylidene)thiosemicarbazide
-
-
-
(E)-1-(3,4,5-trimethoxybenzylidene)thiosemicarbazide
-
-
-
(E)-1-(3-bromobenzylidene)thiosemicarbazide
-
-
-
(E)-1-(3-chlorobenzylidene)thiosemicarbazide
-
-
-
(E)-1-(3-methoxybenzylidene)thiosemicarbazide
-
-
-
(E)-1-(3-nitrobenzylidene)thiosemicarbazide
-
competitive mechanism of inhibition
-
(E)-1-(4-(N,N-dimethylamino)benzylidene)thiosemicarbazide
-
-
-
(E)-1-(4-bromobenzylidene)thiosemicarbazide
-
-
-
(E)-1-(4-chlorobenzylidene)thiosemicarbazide
-
-
-
(E)-1-(4-methoxybenzylidene)thiosemicarbazide
-
-
-
(E)-1-(4-nitrobenzylidene)thiosemicarbazide
-
-
-
(E)-2-((E)-but-2-enylidene) hydrazinecarbothioamide
-
-
-
(E)-2-(2,3-dihydroxybenzylidene)hydrazinecarbothioamide
-
-
-
(E)-2-(2-(benzyloxy)benzylidene)hydrazinecarbothioamide
-
-
-
(E)-2-(3-(benzyloxy)-4-methoxybenzylidene)hydrazinecarbothioamide
-
-
-
(E)-2-(4-hydroxy-3,5-dimethoxybenzylidene)hydrazinecarbothioamide
-
-
-
(E)-2-(4-hydroxybenzylidene)hydrazinecarbothioamide
-
-
-
(R)-4-methoxydalbergione
-
50% inhibition at 0.067 mM, isolated from roots of Ranunculus repens
(R)-4-methoxydalbergione
-
50% inhibition at 0.059 mM, isolated from roots of Ranunculus repens
(R)-dalbergiophenol
-
50% inhibition at 0.035 mM, isolated from roots of Ranunculus repens
(R)-dalbergiophenol
-
50% inhibition at 0.025 mM, isolated from roots of Ranunculus repens
([[(benzyloxy)carbonyl]amino]methyl)methylphosphinothioic O-acid
-
-
1'-(trifluoroacetyl)-1,4'-bipiperidine
-
50% inhibition at 0.061 mM
1,1-dimethyl-3-[(1S)-1-naphthalen-1-ylethyl]selenourea
-
-
1,10-phenanthroline
-
5 mM, 67% inhibition
1,4-Naphthoquinone
-
-
1-(2,4-dihydroxyphenyl)-2-(4-fluorophenyl)ethanone oxime
-
-
1-(2,4-dihydroxyphenyl)-2-(4-hydroxyphenyl)ethanone
-
0.4 mg/ml, 16% inhibition
1-(2,4-dihydroxyphenyl)-2-(4-methoxyphenyl)ethanone oxime
-
-
1-(2-hydroxy-4,6-dimethoxyphenyl)-2-(4-methoxyphenyl)ethanone oxime
-
-
1-(3,4-dihydroxyphenyl)-2-(4-hydroxyphenyl)ethanone
-
0.4 mg/ml, 39% inhibition
1-(3,4-dihydroxyphenyl)-2-(4-hydroxyphenyl)ethanone oxime
-
-
1-benzyl-2-ethyl-6,6-dimethyl-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
1-benzyl-2-ethyl-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
1-cyclohexyl-3,3-dimethyl-1-(1-methylethyl)selenourea
-
-
1-ethoxy-2-ethyl-6,6-dimethyl-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
1-ethoxy-2-ethyl-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
2,2'-bi-1,3,4-oxadiazole-5,5'(4H,4'H)-dithione
-
pH 8.2, IC50: 0.133 mM
2,2'-bi-1,3,4-oxadiazole-5,5'(4H,4'H)-dithione
-
pH 8.2, IC50: below 0.125 mM
2,2'-bi-1,3,4-oxadiazole-5,5'(4H,4'H)-dithione
-
-
2,2'-bi-1,3,4-thiadiazole-5,5'(4H,4'H)-dithione
-
pH 8.2, IC50: 0.5 mM
2,2'-bi-1,3,4-thiadiazole-5,5'(4H,4'H)-dithione
-
-
2,2'-thenoin
-
IC50: 0.18 mM
2,3,4,4'-tetrahydroxydeoxybenzoin
-
0.4 mg/ml, 51% inhibition
2,3,4-trihydroxy-4'-methoxydeoxybenzoin
-
0.4 mg/ml, 44% inhibition
2,4,4',6-tetrahydroxy-3-methoxyphenyldeoxybenzoin
-
0.4 mg/ml, 17% inhibition
2,4,6-trihydroxy-9H-xanthen-9-one
-
-
2,4,6-trimethyl-N-([1-[(2,4,6-trimethylphenyl)sulfonyl]piperidin-4-yl]methyl)benzenesulfonamide
-
50% inhibition at 0.038 mM
2,4-dihydroxy-40-methoxydeoxybenzoin
-
0.4 mg/ml, 14% inhibition
-
2,4-dihydroxyacetophenone
-
0.4 mg/ml, 14% inhibition
2,4-diphenyl-2,3-dihydro-1,5-benzothiazepine
-
-
2-(1-amino-2-(4-hydroxyphenyl)ethyl)-4-methoxybenzene-1,3,5-triol
-
-
2-(1-amino-2-(4-hydroxyphenyl)ethyl)benzene-1,3,5-triol
-
-
2-(4-fluorophenyl)-1-(2,3,4-trihydroxyphenyl)ethanone oxime
-
-
2-(4-hydroxyphenyl)-1-(2,3,4-trihydroxyphenyl)ethanone oxime
-
-
2-(4-hydroxyphenyl)-1-(2,4,6-trihydroxy-3-methoxyphenyl)ethanone oxime
-
-
2-(4-hydroxyphenyl)-1-(2,4,6-trihydroxyphenyl)ethanone oxime
-
-
2-(4-methoxyphenyl)-1-(2,3,4-trimethoxyphenyl)ethanamine
-
-
2-(4-methylphenyl)-4-phenyl-2,3-dihydro-1,5-benzothiazepine
-
-
2-(4-nitrophenyl)-4-phenyl-2,3-dihydro-1,5-benzothiazepine
-
-
2-ethyl-1-(2-phenylethyl)-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
2-ethyl-1-(4-methoxycyclohexyl)-6,6-dimethyl-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
2-ethyl-1-(4-methoxyphenyl)-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
2-ethyl-6-[2-(ethylsulfanyl)propyl]-1-(4-methoxyphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
reversible and competitive inhibitor
2-hydroxy-1-phenylethanone
-
IC50: 0.47 mM
2-mercaptoethanol
-
-
2-mercaptoethanol
-
-
2-[(1E)-N-(allyloxy)butanimidoyl]-5,5-dimethylcyclohexane-1,3-dione
-
chelator of the nickel atom in enzyme metallocenter
2-[(1E)-N-ethoxybutanimidoyl]-5,5-dimethylcyclohexane-1,3-dione
-
chelator of the nickel atom in enzyme metallocenter
2-[(2S,4R)-2-(4-fluorophenyl)-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
-
-
2-[(2S,4R)-2-phenyl-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
-
-
2-[2-(1,3-benzodioxol-5-yl)-2,3-dihydro-1,5-benzothiazepin-4-yl]phenol
-
-
2-[2-(3,4-dimethoxyphenyl)ethyl]phenol
-
-
3,3'-(1H-indol-3-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-(1H-pyrrol-2-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-(2-bromobenzylidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(2-chlorobenzylidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(2-methoxybenzylidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(2-phenylpropane-1,1-diyl)bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-(2-phenylpropylidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(2-pyridyl-methylene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(2-pyrolidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(2E)-but-2-ene-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-(3-chlorobenzylidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(3-cinnamylidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(3-hydroxybenzylidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(3-indolidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(3-methoxybenzylidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(3-phenylpropane-1,1-diyl)bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-(4-hydroxybenzylidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(4-methoxybenzylidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(4-nitrobenzylidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(crotonalidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(dihydrocinnamylidene)-bis-(4-hydroxycoumarin)
-
-
3,3'-(naphthalen-1-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-(pyridin-3-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-(pyridin-4-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-butane-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-ethane-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-ethylidenebis-(4-hydroxycoumarin)
-
-
3,3'-hexane-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-methanediylbis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-methylenebis-(4-hydroxycoumarin)
-
-
3,3'-n-butylidene-bis(4-hydroxycoumarin)
-
-
3,3'-n-hexylidene-bis(4-hydroxycoumarin)
-
-
3,3'-n-pentylidene-bis(4-hydroxycoumarin)
-
-
3,3'-pentane-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(1E)-1-phenylprop-1-ene-3,3-diyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(2-bromophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(2-chlorophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(2-methoxyphenyl)methanediyl]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-aminophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(3-chlorophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(3-ethoxy-4-hydroxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(3-hydroxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(3-methoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(3-nitrophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(4-hydroxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(4-methoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
-
3,3'-[(4-nitrophenyl)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)
-
-
3,4,5-trihydroxy-9H-xanthen-9-one
-
-
3,4,5-Trihydroxybenzoate
-
50% inhibition at 0.032 mM
3,4,5-Trihydroxybenzoate
-
50% inhibition at 0.022 mM
3,4-Dihydroxyacetophenone
-
0.4 mg/ml, 41% inhibition
3,5-dimethylphenyl diamidophosphate
-
-
3-(4-bromobenzyl)-1,1-dimethylselenourea
-
-
3-(4-bromophenyl)-1,1-dimethylthiourea
-
-
3-dodecyl-1,1-dimethylthiourea
-
-
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-(1-amino-2-(4-fluorophenyl)ethyl)benzene-1,2,3-triol
-
-
-
4-(1-amino-2-(4-fluorophenyl)ethyl)benzene-1,3-diol
-
-
4-(1-amino-2-(4-hydroxyphenyl)ethyl)benzene-1,2,3-triol
-
-
4-(1-amino-2-(4-hydroxyphenyl)ethyl)benzene-1,2-diol
-
-
4-(1-amino-2-(4-methoxyphenyl)ethyl)benzene-1,3-diol
-
-
4-(2,3-dimethylphenyl)-5-phenyl-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
-
4-(2,4-dimethylphenyl)-5-(3-nitrophenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
-
4-(4-benzoyl-5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)phenyl benzoate
-
pH 8.2, IC50: 0.234 mM
4-(4-benzoyl-5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)phenyl benzoate
-
-
4-(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-(benzyloxy)phenyl diamidophosphate
-
-
4-(p-hydroxyphenethyl)pyrogallol
-
0.4 mg/ml, 94.5% inhibition
4-amino-5-(4-hydroxyphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 8.2, IC50: below 0.125 mM
4-amino-5-(4-hydroxyphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
4-amino-5-pyridin-4-yl-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 8.2, IC50: 0.163 mM
4-amino-5-pyridin-4-yl-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
4-bromophenylboronic acid
-
competitive
4-bromophenylboronic acid
-
competitive inhibition
4-butylbenzene-1,2,3-triol
-
-
4-butylbenzene-1,2-diol
-
-
4-decylbenzene-1,2,3-triol
-
-
4-dodecylbenzene-1,2,3-triol
-
-
4-ethylbenzene-1,2,3-triol
-
-
4-ethylbenzene-1,2-diol
-
-
4-hexylbenzene-1,2,3-triol
-
-
4-hexylbenzene-1,2-diol
-
-
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
4-nitrophenyl diamidophosphate
-
-
4-octylbenzene-1,2,3-triol
-
-
4-octylbenzene-1,2-diol
-
-
4-tetradecylbenzene-1,2,3-triol
-
-
4-[2-(3,4-diethoxyphenyl)ethyl]benzene-1,2,3-triol
-
-
4-[2-(3,4-dimethoxyphenyl)ethyl]benzene-1,2,3-triol
-
-
4-[2-(3,4-dimethoxyphenyl)ethyl]benzene-1,2-diol
-
-
4-[2-(3,4-dimethoxyphenyl)ethyl]phenol
-
-
4-[2-(3-bromophenyl)ethyl]benzene-1,2,3-triol
-
-
4-[2-(3-bromophenyl)ethyl]benzene-1,2-diol
-
-
4-[2-(3-chlorophenyl)ethyl]-1,2-dimethoxybenzene
-
-
4-[2-(3-chlorophenyl)ethyl]benzene-1,2,3-triol
-
-
4-[2-(3-chlorophenyl)ethyl]benzene-1,2-diol
-
-
4-[2-(4-bromophenyl)ethyl]benzene-1,2,3-triol
-
-
4-[2-(4-chlorophenyl)ethyl]-1,2-dimethoxybenzene
-
-
4-[2-(4-chlorophenyl)ethyl]benzene-1,2,3-triol
-
-
4-[2-(4-chlorophenyl)ethyl]benzene-1,2-diol
-
-
4-[2-(4-fluorophenyl)ethyl]benzene-1,2,3-triol
-
-
4-[2-(4-fluorophenyl)ethyl]benzene-1,2-diol
-
-
4-[2-(4-hydroxyphenyl)ethyl]benzene-1,2,3-triol
-
-
4-[2-(4-hydroxyphenyl)ethyl]benzene-1,2-diol
-
-
5-(1-naphthyl)-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.214 mM
5-(1-naphthyl)-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
5-(1-naphthyl)-1,3,4-oxadiazole-2(3H)-thione
-
-
5-(2-chlorophenyl)-N-(2,6-dimethylphenyl)-1,3,4-thiadiazol-2-amine
-
-
-
5-(3-chlorophenyl)-4-(2,4-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
-
5-(3-chlorophenyl)-4-(2,6-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
-
5-(3-hydroxyphenyl)-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
5-(3-hydroxyphenyl)-1,3,4-oxadiazole-2(3H)-thione
-
-
5-(4-chlorophenyl)-4-(2,4-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
-
5-(4-chlorophenyl)-N-(2,3-dimethylphenyl)-1,3,4-thiadiazol-2-amine
-
-
-
5-(4-chlorophenyl)-N-(2,6-dimethylphenyl)-1,3,4-thiadiazol-2-amine
-
-
-
5-(4-hydroxyphenyl)-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.5 mM
5-(4-hydroxyphenyl)-1,3,4-oxadiazole-2(3H)-thione
-
-
5-(4-hydroxyphenyl)-1,3,4-thiadiazole-2(3H)-thione
-
-
5-(4-propoxyphenyl)-3-propyl-1,3,4-thiadiazole-2(3H)-thione
-
-
5-benzhydryl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.95 mM
5-benzhydryl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.25 mM
5-benzhydryl-1,3,4-oxadiazole-2(3H)-thione
-
-
5-benzhydryl-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
5-benzhydryl-1,3,4-thiadiazole-2(3H)-thione
-
-
5-benzyl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
5-benzyl-1,3,4-oxadiazole-2(3H)-thione
-
-
5-cyclohexyl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.124 mM
5-cyclohexyl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.125 mM
5-cyclohexyl-1,3,4-oxadiazole-2(3H)-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-phenyl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
5-phenyl-1,3,4-oxadiazole-2(3H)-thione
-
-
5-phenyl-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.29 mM
5-phenyl-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.25 mM
5-phenyl-1,3,4-thiadiazole-2(3H)-thione
-
-
5-pyridin-4-yl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: above 0.2 mM
5-pyridin-4-yl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
5-pyridin-4-yl-1,3,4-oxadiazole-2(3H)-thione
-
-
5-pyridin-4-yl-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.124 mM
5-pyridin-4-yl-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
5-pyridin-4-yl-1,3,4-thiadiazole-2(3H)-thione
-
-
5-[(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)methyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.095 mM
5-[(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)methyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.5 mM
5-[(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)methyl]-1,3,4-oxadiazole-2(3H)-thione
-
-
5-[(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)methyl]-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.095 mM
5-[(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)methyl]-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.5 mM
5-[(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)methyl]-1,3,4-thiadiazole-2(3H)-thione
-
-
5-[3-(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)propyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.093 mM
5-[3-(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)propyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
5-[3-(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)propyl]-1,3,4-oxadiazole-2(3H)-thione
-
-
5-[3-(benzyloxy)phenyl]-1,3,4-oxadiazole-2(3H)-thione
-
-
5-[4-(benzyloxy)phenyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.41 mM
5-[4-(benzyloxy)phenyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.5 mM
5-[4-(benzyloxy)phenyl]-1,3,4-oxadiazole-2(3H)-thione
-
-
5-[4-(tert-butyl-dimethyl-silanyloxy)-phenyl]-3H-[1,3,4]oxadiazole-2-thione
-
pH 8.2, IC50: 0.244 mM
5-[4-(tert-butyl-dimethyl-silanyloxy)-phenyl]-3H-[1,3,4]oxadiazole-2-thione
-
-
5-[4-(tert-butyl-dimethyl-silanyloxy)-phenyl]-3H-[1,3,4]thiadiazole-2-thione
-
-
5-[hydroxy(phenyl)methyl]-4-(4-methylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
5-[hydroxy(phenyl)methyl]-4-(4-nitrophenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
-
6-(1-hydroxy-2-(4-methoxyphenyl)ethyl)-2,3-dimethoxyphenol
-
0.4 mg/ml, 42% inhibition
7'-hydroxy-2,2'-dioxo-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
-
-
7,8,4'-trihydroxyisoflavone
-
0.4 mg/ml, 81.7% inhibition
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
-
-
Acetohydroxamate
-
10 mM, 88% inhibition
Acetohydroxamate
-
10 mM, 92% inhibition
Acetohydroxamate
-
reversible
Acetohydroxamate
-
-
Acetohydroxamic acid
-
IC50: 0.005 mM
Acetohydroxamic acid
-
-
Acetohydroxamic acid
Q8FZW3
-
Acetohydroxamic acid
-
-
Acetohydroxamic acid
-
inhibits urease activity and biofilm formation in a dose-dependent manner
Acetohydroxamic acid
-
-
acetol
-
IC50: 2.9 mM
Ag+
-
time-dependent inhibition studies exhibit biphasic kinetics with heavy metal ions
aminomethyl(P-methyl)phosphinic acid
-
-
-
beta-(o-methoxyphenyl)-gamma,gamma-bis(8-quinolinoxy)germa-gamma-lactone
-
inhibition occurrs in a noncompetitive and concentration-dependent manner. Highly selective in inhibiting the growth of Proteus mirabilis at moderate concentrations. Potential to be developed as antimicrobial agents against Proteus mirabilis infection
beta-(o-methylphenyl)-gamma,gamma-bis(8-quinolinoxy)germa-gamma-lactone
-
inhibition occurrs in a noncompetitive and concentration-dependent manner. Highly selective in inhibiting the growth of Proteus mirabilis at moderate concentrations. Potential to be developed as antimicrobial agents against Proteus mirabilis infection
Boric acid
-
competitive, maximal inhibition at pH 5.0, minimal inhibition at pH 10.0
Boric acid
-
competitive, pH-variation study of inhibition constant
Boric acid
-
inhibits urease activity and biofilm formation in a dose-dependent manner
Boric acid
-
competitive inhibition
butylboronic acid
-
competitive
butylboronic acid
-
competitive inhibition
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
-
-
citrate buffer
-
-
Co2+
-
1 mM, 39% loss of activity
Cu2+
-
1 mM, complete inactivation
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
cyanide
-
1.0 mM, 32% inhibition
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
EDTA
-
5 mM, 70% inhibition
Fe2+
-
1 mM, 42% loss of activity
-
furoin
-
IC50: 0.36 mM
gallacetophenone
-
0.4 mg/ml, 38% inhibition
Hg2+
-
1 mM, complete inactivation
Hg2+
-
time-dependent inhibition studies exhibit biphasic kinetics with heavy metal ions
hydroxamic acid
-
1.0 mM, 64% inhibition
hydroxylamine
-
50 mM 23% inhibition
hydroxylamine
-
50 mM, 31% inhibition
Hydroxyurea
-
10 mM, 71% inhibition
Hydroxyurea
-
10 mM, 67% inhibition
Hydroxyurea
-
reversible
Hydroxyurea
-
IC50: 0.1 mM
Hydroxyurea
Q8FZW3
-
Hydroxyurea
-
inhibits urease activity and biofilm formation in a dose-dependent manner
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
L-aspartyl-4-hydroxamate
-
50 m, 19% inhibition
-
L-aspartyl-4-hydroxamate
-
50 mM, 43% inhibition
-
L-glutamine
-
50 mM, 14% inhibition
L-glutamyl-5-hydroxamate
-
50 mM, 34% inhibition
-
L-Gly hydroxamate
-
1 mM, 97% inhibition
L-Gly hydroxamate
-
1 mM, 94% inhibition
mercaptoethylamine
-
inactivates enzyme irreversibly
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-amino-4,5,6,7,8,9-hexahydrocycloocta[b]thiophene-3-carboxylate
-
-
methyl 2-amino-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
-
methyl 2-amino-4-methylthiophene-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-[[(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
methyl[(methylamino)methyl]phosphinic acid
-
-
methyl[(methylamino)methyl]phosphinic acid
-
-
methyl[(methylamino)methyl]phosphinic acid
-
-
N-(1,3-benzothiazol-2-yl)phosphoric triamide
-
-
N-(2,3-dimethylphenyl)-5-phenyl-1,3,4-thiadiazol-2-amine
-
-
-
N-(2,4-dimethylphenyl)-5-(3-nitrophenyl)-1,3,4-thiadiazol-2-amine
-
-
-
N-(2-methoxy-4-nitrophenyl)phosphoric triamide
-
-
N-(2-nitrophenyl)phosphoric triamide
-
-
N-(2-phenylethyl)phosphoric triamide
-
-
N-(2-phenylethyl)phosphorothioic triamide
-
-
N-(3-methoxyphenyl)phosphoric triamide
-
-
N-(3-methylpyridin-2-yl)phosphorothioic triamide
-
-
N-(3-morpholin-2-ylpropyl)phosphoric triamide
-
-
N-(3-nitropyridin-2-yl)phosphoric triamide
-
-
N-(4-cyclohexylphenyl)phosphoric triamide
-
-
N-(4-methoxy-1,3-benzothiazol-2-yl)phosphoric triamide
-
-
N-(4-methyl-1,3-benzothiazol-2-yl)phosphoric triamide
-
-
N-(4-methyl-2-nitrophenyl)phosphoric triamide
-
-
N-(4-nitrophenyl)phosphoric triamide
-
-
N-(4-phenoxyphenyl)phosphoric triamide
-
-
N-(6-ethoxy-1,3-benzothiazol-2-yl)phosphoric triamide
-
-
N-(6-fluoro-1,3-benzothiazol-2-yl)phosphoric triamide
-
-
N-(N'-benzyloxycarbonylglycyl)aminomethyl(P-methyl)phosphinothioic acid
-
-
N-1,3-benzothiazol-2-ylphosphoric triamide
-
-
N-1,3-benzothiazol-2-ylphosphorothioic triamide
-
-
N-adamant-1-ylphosphoric triamide
-
-
N-benzyloxycarbonylaminomethyl(P-methyl)phosphinic acid
-
-
N-dimethyl-L-cysteine
-
noncompetitive, 50% inhibition at 0.058 mM
N-dimethyl-L-cysteine
-
noncompetitive, 50% inhibition at 0.05 mM
N-dimethyl-L-cysteine
-
noncompetitive, 50% inhibition at 0.01 mM
N-dimethyl-S-methyl-L-cysteine
-
noncompetitive, 50% inhibition at 0.078 mM
N-dimethyl-S-methyl-L-cysteine
-
noncompetitive, 50% inhibition at 0.05 mM
N-dimethyl-S-methyl-L-cysteine
-
noncompetitive, 50% inhibition at 0.110 mM
N-ethylmaleimide
-
irreversible inactivation
N-glycyl-aminomethyl(P-methyl)phosphinic acid
-
-
N-hydroxyacetamide
-
-
N-n-butylphosphoric triamide
-
-
N-n-butylthiophosphoric triamide
-
-
N-naphthalen-1-ylphosphoric triamide
-
-
N-phenylphosphoric triamide
-
-
N-[2-(4-fluorophenyl)ethyl]phosphoric triamide
-
-
N-[2-(difluoromethoxy)phenyl]phosphoric triamide
-
-
N-[2-(trifluoromethoxy)phenyl]phosphoric triamide
-
-
N-[4-(benzyloxy)phenyl]phosphoric triamide
-
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-phenylalaninamide
-
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-serinamide
-
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-valinamide
-
-
N2-[(benzyloxy)carbonyl]-N-[[hydroxy(methyl)phosphoryl]methyl]glycinamide
-
-
NEM
-
0.1 mM, complete inhibition
Ni2+
-
1 mM, 26% loss of activity
Ni2+
-
inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+
O-benzyl-N-[[hydroxy(methyl)phosphoryl]methyl]-L-serinamide
-
-
O-[4-(benzyloxy)phenyl] diamidothiophosphate
-
-
p-benzoquinone
-
-
p-chloromercuribenzene sulfonate
-
0.1 mM, complete inhibition
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
0.5 mM, 90% inhibition
p-hydroxymercuribenzoate
-
-
Pb2+
-
inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+
PCMB
-
0.1 mM, complete loss of activity
Peptides
-
TFLPQPRCSALLRYLSEDGVIVPS and YDFYWW, no inhibition of the enzyme from Bacillus pasteurii and Canavalia ensiformis
Phenylboronic acid
-
competitive
Phenylboronic acid
-
competitive inhibition
phenylphosphoramidate
-
-
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
phenylphosphorodiamidate
-
-
Phenylurea
-
weak non-competitive
psi-tectorigenin
-
0.4 mg/ml, 36% inhibition
quercetin-4-O-beta-D-glucopyranoside
-
-
-
S-ethyl-L-cysteine
-
noncompetitive, 50% inhibition at 0.035 mM
S-ethyl-L-cysteine
-
noncompetitive, 50% inhibition at 0.030 mM
Selenourea
-
50 mM, 80% inhibition
Semicarbazide
-
50 mM, 48% inhibition
Semicarbazide
-
50 mM, 31% inhibition
Semicarbazide
-
competitive
tetrachloro-o-benzoquinone
-
no recovery of urease activity bound in the urease-inhibitor complex after dilution or addition of dithiothreitol
tetrachloro-p-benzoquinone
-
-
tetracosyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
-
-
Thiourea
-
50 mM, 26% inhibition
Thiourea
-
50% inhibition at 0.015 mM
Thiourea
-
50% inhibition at 0.021 mM
Thiourea
Q8FZW3
-
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+
-
1 mM, 36% loss of activity
Zn2+
-
inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+
[(acetylamino)methyl]methylphosphinic acid
-
-
[(acetylamino)methyl]phosphonic acid
-
-
[(benzylamino)methyl]methylphosphinic acid
-
-
[(dimethylamino)methyl]methylphosphinic acid
-
-
[(dimethylamino)methyl]phosphonic acid
-
-
[(methylamino)methyl]phosphonic acid
-
-
[5-[(4-methylphenyl)amino]-1,3,4-oxadiazol-2-yl](phenyl)methanol
-
-
[5-[(4-nitrophenyl)amino]-1,3,4-oxadiazol-2-yl](phenyl)methanol
-
-
[[benzyl(methyl)amino]methyl]phosphonic acid
-
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
-
slight stimulation
glycerol
-
optimum concentration: 15%
n-octylglucoside
-
optimum concentration: 0.1%
Ni2+
-
supplementation of growth medium by nickel leads to tenfold increase in enzyme activity, induction occuring at post-translational level
Ni2+
-
supplementation of growth medium by nickel leads to tenfold increase in enzyme activity
PEG
-
optimum concentration: 0.5%
SDS
-
optimum concentration: 0.02%
Triton X-100
-
optimum concentration: 0.05%
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0195
-
Urea
-
; 35C, pH 4.5
0.11
-
Urea
-
pH 8.4, temperature not specified in the publication
0.16
-
Urea
-
-
0.2
-
Urea
-
range Km: 0.2-0.8 mM, pH 8.0, temperature not specified in the publication
0.21
-
Urea
-
pH 6.8, 37C, Vmax: 1200 micromol/min/mg, in the presence of preservatives PEG or glycerol
0.45
-
Urea
-
pH 5.5
0.5
-
Urea
-
pH 5.5
0.5
-
Urea
-
pH 8.8
0.83
-
Urea
-
-
0.9
-
Urea
-
pH 8.8
1.03
-
Urea
-
pH 8.2, temperature not specified in the publication
1.33
-
Urea
-
pH 8.5, temperature not specified in the publication
1.4
-
Urea
-
mutant betaH41A
1.5
-
Urea
-
mutant betaH39A
1.6
-
Urea
-
mutant alphah312A
1.66
-
Urea
-
pH 6.8, 37C
1.66
-
Urea
-
pH and temperature not specified in the publication
1.7
-
Urea
bacterium strain SL100
-
-
1.7
-
Urea
-
pH 5.5, 65C, Vmax: 7.29 micromol of ammonia/min/mg protein
1.9
-
Urea
-
mutant gammaH96A
2
-
Urea
-
mutant alphaH321A
2
-
Urea
Streptococcus mitior
-
pH 4.5, temperature not specified in the publication
2.2
-
Urea
-
pH 8, temperature not specified in the publication
2.3
-
Urea
-
wild-type enzyme
2.4
-
Urea
-
wild-type enzyme
2.5
-
Urea
-
pH 6.9, temperature not specified in the publication
2.7
-
Urea
-
mutant R336Q
2.7
-
Urea
-
soluble urease, Vmax: 285 micromol/min/mg
2.7
-
Urea
-
pH 2, temperature not specified in the publication
2.7
-
Urea
-
estimated value, pH 7.0, 37C
2.8
-
Urea
-
pH 7.0, 37C; pH 7.5, temperature not specified in the publication; pH 7.75, temperature not specified in the publication
2.8
-
Urea
-
pH 2, temperature not specified in the publication
2.9
-
Urea
-
wild-type enzyme
2.9
-
Urea
-
pH 7.0, 38C
3
-
Urea
Arthrobacter mobilis
-
pH 4.2, temperature not specified in the publication
3
-
Urea
-
pH 8.0, temperature not specified in the publication
3
-
Urea
-
pH 7.3, temperature not specified in the publication
3.2
-
Urea
-
free enzyme or enzyme bound to membrane modified with NaOH + ethylendiamine and H2O2
3.23
-
Urea
-
soluble enzyme
3.35
-
Urea
-
soluble enzyme
3.43
-
Urea
-
arylamine glass-immobilized urease
3.55
-
Urea
-
alkylamine glass-immobilized urease
3.6
-
Urea
-
mutant D221N
3.92
-
Urea
-
chitosan-immobilized urease, Vmax: 265 micromol/min/mg
4.1
-
Urea
-
pH 8.0, temperature not specified in the publication
4.2
-
Urea
-
soluble urease, 37C, pH not specified in the publication, Vmax: 200 micromol/min/mg
4.5
-
Urea
-
pH and temperature not specified in the publication
5
-
Urea
-
mutant 319A
5.07
-
Urea
-
agar-immobilized enzyme
5.4
-
Urea
-
mutant C319D
5.6
-
Urea
Q8FZW3
by hyperbolic regression, Lineweaver-Burk: 5.24 mM
5.6
-
Urea
-
pH 7.0, temperature not specified in the publication
5.88
-
Urea
-
alginate-immobilized urease, Vmax: 282 micromol/min/mg
7.4
-
Urea
-
mutant H320N
8.3
-
Urea
-
mutant alphaH320A
8.81
-
Urea
-
immobilized urease, 37C, pH not specified in the publication, Vmax: 43.48 micromol/min/mg
9.3
-
Urea
-
pH and temperature not specified in the publication
9.5
-
Urea
-
pH 6, temperature not specified in the publication
10.5
-
Urea
-
pH 7.5, temperature not specified in the publication
10.6
-
Urea
-
mutant H320Q
10.9
-
Urea
-
mutant H320A
11.3
-
Urea
-
mutant C319S
12.5
-
Urea
-
pH 7.6, temperature not specified in the publication
13
-
Urea
-
pH 7.5, temperature not specified in the publication
17.3
-
Urea
-
pH 8.0, temperature not specified in the publication
17.6
-
Urea
-
partially purified enzyme, pH 7.0, 37C
18
72
Urea
-
value depends on pH and type of buffer
24
-
Urea
-
mutant D221A
32
-
Urea
-
pH 7.0, temperature not specified in the publication
34
-
Urea
-
pH 7.0, temperature not specified in the publication
175
-
Urea
-
mutant H219N
227
-
Urea
-
mutant H219Q
1100
-
Urea
-
mutant alphaH219A
2090
-
Urea
-
mutant H219A
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
-
sigmoid curve at low urea concentration (below 0.1 mM). In the presence of glycerol or PEG (preservatives), the sigmoid pattern changes to a rectangular hyperbola, and urea hydrolysis is consistent with Michaelis-Menten kinetics. Based on the kinetics of urease in the presence of the preservatives, the two forms of urease i.e., (alpha beta)3 and (alpha beta)6 may well exist in Helicobacter pylori. The hyperbolic kinetics adopted by the dissociated form of urease may allow for maximal urea assimilation by Helicobacter pylori under acidic conditions and at low urea concentration
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.06
-
Urea
-
mutant H320N
0.068
-
Urea
-
mutant H320A
0.33
-
Urea
-
mutant H320Q
0.62
-
Urea
-
mutant R336Q
1.7
-
Urea
-
mutant D221A
60
-
Urea
-
mutant D221N
194
-
Urea
-
mutant H219A
322
-
Urea
-
mutant H219N
1860
-
Urea
-
mutant H219Q
2970
-
Urea
-
wild-type enzyme
3500
-
Urea
-
pH 7.0, 37C
5913
-
Urea
-
pH 7.0, 38C
additional information
-
additional information
-
pH-variation study on steady-state kinetic parameters
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1250
-
Urea
-
pH 7.0, 37C
17751
2000
-
Urea
-
pH 7.0, 38C
17751
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.017
-
(2S)-2-(dimethylamino)-3-(ethylthio)propan-1-ol
-
pH 8.2
0.018
-
(2S)-2-(dimethylamino)-3-(ethylthio)propan-1-ol
-
pH 5.0
0.002
-
(2S)-2-(dimethylamino)-3-ethoxypropane-1-thiol
-
pH 8.2
0.055
-
(2S)-2-(dimethylamino)-3-ethoxypropane-1-thiol
-
pH 5.0
0.002
-
(2S)-2-(dimethylamino)-3-mercaptopropan-1-ol
-
pH 8.2
0.013
-
(2S)-2-(dimethylamino)-3-mercaptopropan-1-ol
-
pH 5.0
0.002
-
(2S)-2-(dimethylamino)-3-methoxypropane-1-thiol
-
pH 8.2
0.019
-
(2S)-2-(dimethylamino)-3-methoxypropane-1-thiol
-
pH 5.0
0.34
-
(aminomethyl)methylphosphinic acid
-
pH 7.0, 37C
0.24
-
(aminomethyl)phosphonic acid
-
pH 7.0, 37C
0.314
-
(aminomethyl)phosphonic acid
-
pH 7.0, 37C
0.000407
-
(E)-1-((E)-3-phenylallylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.00017
-
(E)-1-(2-chlorobenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.00091
-
(E)-1-(3,4,5-trimethoxybenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.00067
-
(E)-1-(3-bromobenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000625
-
(E)-1-(3-chlorobenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000127
-
(E)-1-(3-methoxybenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
9e-05
-
(E)-1-(3-nitrobenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000122
-
(E)-1-(4-(N,N-dimethylamino)benzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.00077
-
(E)-1-(4-bromobenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000398
-
(E)-1-(4-chlorobenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000807
-
(E)-1-(4-methoxybenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000497
-
(E)-1-(4-nitrobenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.00043
-
(E)-2-((E)-but-2-enylidene) hydrazinecarbothioamide
-
pH 8.2, 37C
-
0.000127
-
(E)-2-(2,3-dihydroxybenzylidene)hydrazinecarbothioamide
-
pH 8.2, 37C
-
0.000152
-
(E)-2-(2-(benzyloxy)benzylidene)hydrazinecarbothioamide
-
pH 8.2, 37C
-
0.000191
-
(E)-2-(3-(benzyloxy)-4-methoxybenzylidene)hydrazinecarbothioamide
-
pH 8.2, 37C
-
0.000134
-
(E)-2-(4-hydroxy-3,5-dimethoxybenzylidene)hydrazinecarbothioamide
-
pH 8.2, 37C
-
0.000391
-
(E)-2-(4-hydroxybenzylidene)hydrazinecarbothioamide
-
pH 8.2, 37C
-
0.014
-
([[(benzyloxy)carbonyl]amino]methyl)methylphosphinothioic O-acid
-
-
0.0175
-
([[(benzyloxy)carbonyl]amino]methyl)methylphosphinothioic O-acid
-
-
9.4e-05
-
1,1-dimethyl-3-[(1S)-1-naphthalen-1-ylethyl]selenourea
-
-
0.358
-
1-benzyl-2-ethyl-6,6-dimethyl-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
pH 3.85, 36C
0.106
-
1-benzyl-2-ethyl-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
pH 3.85, 36C
0.754
-
1-benzyl-2-ethyl-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
pH 3.85, 36C
2.5e-05
-
1-cyclohexyl-3,3-dimethyl-1-(1-methylethyl)selenourea
-
-
0.446
-
1-ethoxy-2-ethyl-6,6-dimethyl-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
pH 3.85, 36C
0.566
-
1-ethoxy-2-ethyl-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
pH 3.85, 36C
0.02
-
2,2'-bi-1,3,4-oxadiazole-5,5'(4H,4'H)-dithione
-
pH 5.0, 30C
0.03
-
2,2'-bi-1,3,4-oxadiazole-5,5'(4H,4'H)-dithione
-
pH 8.2, 30C
0.002
-
2,2'-bi-1,3,4-thiadiazole-5,5'(4H,4'H)-dithione
-
pH 5.0, 30C
0.005
-
2,2'-bi-1,3,4-thiadiazole-5,5'(4H,4'H)-dithione
-
pH 8.2, 30C
0.169
-
2-ethyl-1-(2-phenylethyl)-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
pH 3.85, 36C
0.0293
-
2-ethyl-1-(4-methoxycyclohexyl)-6,6-dimethyl-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
pH 3.85, 36C
0.0495
-
2-ethyl-1-(4-methoxyphenyl)-6-(2,4,6-trimethylphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
pH 3.85, 36C
0.0817
-
2-ethyl-6-[2-(ethylsulfanyl)propyl]-1-(4-methoxyphenyl)-1,5,6,7-tetrahydro-4H-benzimidazol-4-one
-
pH 3.85, 36C
0.0059
-
2-[(1E)-N-(allyloxy)butanimidoyl]-5,5-dimethylcyclohexane-1,3-dione
-
-
0.0086
-
2-[(1E)-N-ethoxybutanimidoyl]-5,5-dimethylcyclohexane-1,3-dione
-
-
0.000135
-
3-(4-bromobenzyl)-1,1-dimethylselenourea
-
-
0.000255
-
3-(4-bromophenyl)-1,1-dimethylthiourea
-
-
0.000124
-
3-dodecyl-1,1-dimethylthiourea
-
-
0.04
-
4-(4-benzoyl-5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)phenyl benzoate
-
pH 5.0, 30C
0.29
-
4-(4-benzoyl-5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)phenyl benzoate
-
pH 8.2, 30C
0.29
-
4-amino-5-(4-hydroxyphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 8.2, 30C
0.31
-
4-amino-5-(4-hydroxyphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 5.0, 30C
0.2
-
4-amino-5-pyridin-4-yl-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 8.2, 30C
0.24
-
4-amino-5-pyridin-4-yl-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 5.0, 30C
0.22
-
4-bromophenylboronic acid
-
pH 7.0, 37C
0.3
-
4-bromophenylboronic acid
-
pH 7.3, 27C
0.13
-
5-(1-naphthyl)-1,3,4-oxadiazole-2(3H)-thione
-
pH 5.0, 30C; pH 8.2, 30C
0.15
-
5-(3-hydroxyphenyl)-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, 30C
0.16
-
5-(3-hydroxyphenyl)-1,3,4-oxadiazole-2(3H)-thione
-
pH 5.0, 30C
0.05
-
5-(4-hydroxyphenyl)-1,3,4-oxadiazole-2(3H)-thione
-
pH 5.0, 30C; pH 8.2, 30C
0.002
-
5-(4-hydroxyphenyl)-1,3,4-thiadiazole-2(3H)-thione
-
pH 5.0, 30C; pH 8.2, 30C
0.06
-
5-(4-propoxyphenyl)-3-propyl-1,3,4-thiadiazole-2(3H)-thione
-
pH 5.0, 30C
0.19
-
5-(4-propoxyphenyl)-3-propyl-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, 30C
0.04
-
5-benzhydryl-1,3,4-oxadiazole-2(3H)-thione
-
pH 5.0, 30C
0.11
-
5-benzhydryl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, 30C
0.06
-
5-benzhydryl-1,3,4-thiadiazole-2(3H)-thione
-
pH 5.0, 30C
0.12
-
5-benzhydryl-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, 30C
0.14
-
5-benzyl-1,3,4-oxadiazole-2(3H)-thione
-
pH 5.0, 30C
0.17
-
5-benzyl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, 30C
0.09
-
5-cyclohexyl-1,3,4-oxadiazole-2(3H)-thione
-
pH 5.0, 30C
0.1
-
5-cyclohexyl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, 30C
0.16
-
5-phenyl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, 30C
0.19
-
5-phenyl-1,3,4-oxadiazole-2(3H)-thione
-
pH 5.0, 30C
0.02
-
5-phenyl-1,3,4-thiadiazole-2(3H)-thione
-
pH 5.0, 30C
0.1
-
5-phenyl-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, 30C
0.09
-
5-pyridin-4-yl-1,3,4-oxadiazole-2(3H)-thione
-
pH 5.0, 30C; pH 8.2, 30C
0.11
-
5-pyridin-4-yl-1,3,4-thiadiazole-2(3H)-thione
-
pH 5.0, 30C; pH 8.2, 30C
0.005
-
5-[(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)methyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 5.0, 30C; pH 8.2, 30C
0.005
-
5-[(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)methyl]-1,3,4-thiadiazole-2(3H)-thione
-
pH 5.0, 30C
0.008
-
5-[(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)methyl]-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, 30C
0.006
-
5-[3-(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)propyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 5.0, 30C
0.01
-
5-[3-(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)propyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, 30C
0.09
-
5-[3-(benzyloxy)phenyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, 30C
0.16
-
5-[3-(benzyloxy)phenyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 5.0, 30C
0.69
-
5-[4-(benzyloxy)phenyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 5.0, 30C
0.85
-
5-[4-(benzyloxy)phenyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, 30C
0.23
-
5-[4-(tert-butyl-dimethyl-silanyloxy)-phenyl]-3H-[1,3,4]oxadiazole-2-thione
-
pH 5.0, 30C; pH 8.2, 30C
0.15
-
5-[4-(tert-butyl-dimethyl-silanyloxy)-phenyl]-3H-[1,3,4]thiadiazole-2-thione
-
pH 5.0, 30C
0.25
-
5-[4-(tert-butyl-dimethyl-silanyloxy)-phenyl]-3H-[1,3,4]thiadiazole-2-thione
-
pH 8.2, 30C
0.77
-
Acetohydroxamic acid
Q8FZW3
competitive
0.34
-
aminomethyl(P-methyl)phosphinic acid
-
-
-
0.425
-
aminomethyl(P-methyl)phosphinic acid
-
-
-
0.2
-
Boric acid
-
pH 7.0, 37C
0.35
-
Boric acid
-
pH 7.3, 27C
1.5
-
butylboronic acid
-
pH 7.0, 37C
1.8
-
butylboronic acid
-
pH 7.3, 27C
1.04
-
Hydroxyurea
Q8FZW3
competitive
0.0054
-
methyl (7E)-7-[4,4-dimethyl-3-(3-methylisoxazol-5-yl)-2,6-dioxocyclohexyl]-7-(ethoxyimino)heptanoate
-
-
0.0049
-
methyl 5-[(1E)-N-(allyloxy)butanimidoyl]-2,2-dimethyl-4,6-dioxocyclohexanecarboxylate
-
-
0.0027
-
methyl 5-[(1E)-N-ethoxybutanimidoyl]-2,2-dimethyl-4,6-dioxocyclohexanecarboxylate
-
pH 4.95, 36C
0.0041
-
methyl 5-[(1E)-N-ethoxyethanimidoyl]-2,2-dimethyl-4,6-dioxocyclohexanecarboxylate
-
-
0.018
-
methyl[(methylamino)methyl]phosphinic acid
-
-
0.018
-
methyl[(methylamino)methyl]phosphinic acid
-
pH 7.0, 37C
0.027
-
methyl[(methylamino)methyl]phosphinic acid
-
-
0.224
-
methyl[(methylamino)methyl]phosphinic acid
-
pH 7.0, 37C
0.00017
-
N-(N'-benzyloxycarbonylglycyl)aminomethyl(P-methyl)phosphinothioic acid
-
-
0.00045
-
N-(N'-benzyloxycarbonylglycyl)aminomethyl(P-methyl)phosphinothioic acid
-
-
0.043
-
N-benzyloxycarbonylaminomethyl(P-methyl)phosphinic acid
-
-
0.065
-
N-benzyloxycarbonylaminomethyl(P-methyl)phosphinic acid
-
-
0.002
-
N-dimethyl-L-cysteine
-
pH 8.2
0.009
-
N-dimethyl-L-cysteine
-
pH 5.0
0.006
-
N-dimethyl-S-methyl-L-cysteine
-
pH 5.0
0.008
-
N-dimethyl-S-methyl-L-cysteine
-
pH 8.2
7
-
N-ethylmaleimide
-
Ki(fast), pH 6.4
7.5
-
N-ethylmaleimide
-
Ki(slow), pH 6.4
0.021
-
N-glycyl-aminomethyl(P-methyl)phosphinic acid
-
-
0.03
-
N-glycyl-aminomethyl(P-methyl)phosphinic acid
-
-
0.176
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-phenylalaninamide
-
-
0.215
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-phenylalaninamide
-
-
0.037
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-serinamide
-
-
0.041
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-serinamide
-
-
0.12
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-valinamide
-
-
0.208
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-valinamide
-
-
0.135
-
N2-[(benzyloxy)carbonyl]-N-[[hydroxy(methyl)phosphoryl]methyl]glycinamide
-
-
0.178
-
N2-[(benzyloxy)carbonyl]-N-[[hydroxy(methyl)phosphoryl]methyl]glycinamide
-
-
1.3
-
NaF
-
pH 7.0, 37C
0.025
-
O-benzyl-N-[[hydroxy(methyl)phosphoryl]methyl]-L-serinamide
-
-
0.0326
-
O-benzyl-N-[[hydroxy(methyl)phosphoryl]methyl]-L-serinamide
-
-
2
-
Phenylboronic acid
-
pH 7.0, 37C
2.5
-
Phenylboronic acid
-
pH 7.3, 27C
0.011
-
S-ethyl-L-cysteine
-
pH 5.0
0.014
-
S-ethyl-L-cysteine
-
pH 8.2
0.0024
-
tetrachloro-o-benzoquinone
-
-
0.00045
-
tetrachloro-p-benzoquinone
-
-
0.0196
-
Thiourea
-
pH 8.2, 37C
26.12
-
Thiourea
Q8FZW3
competitive
0.095
-
[(acetylamino)methyl]methylphosphinic acid
-
pH 7.0, 37C
0.295
-
[(acetylamino)methyl]methylphosphinic acid
-
pH 7.0, 37C
0.148
-
[(acetylamino)methyl]phosphonic acid
-
pH 7.0, 37C
0.072
-
[(benzylamino)methyl]methylphosphinic acid
-
pH 7.0, 37C
0.571
-
[(benzylamino)methyl]methylphosphinic acid
-
pH 7.0, 37C
0.00062
-
[(dimethylamino)methyl]methylphosphinic acid
-
pH 7.0, 37C
0.0037
-
[(dimethylamino)methyl]methylphosphinic acid
-
pH 7.0, 37C
0.013
-
[(dimethylamino)methyl]phosphonic acid
-
pH 7.0, 37C
0.021
-
[(dimethylamino)methyl]phosphonic acid
-
pH 7.0, 37C
0.07
-
[(methylamino)methyl]phosphonic acid
-
pH 7.0, 37C
0.204
-
[(methylamino)methyl]phosphonic acid
-
pH 7.0, 37C
0.115
-
[[benzyl(methyl)amino]methyl]phosphonic acid
-
pH 7.0, 37C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
(2-[[(2-[[2-(hydroxy-kappaO)ethyl]amino-kappaN]ethyl)imino-kappaN]methyl]-4-nitrophenolato-kappaO)(methoxymethanolato-kappaO)zinc
-
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
-
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
-
-
1.1
-
(aminomethyl)methylphosphinic acid
-
pH 7.0, 37C
0.432
-
(aminomethyl)phosphonic acid
-
pH 7.0, 37C
0.7
-
(aminomethyl)phosphonic acid
-
pH 7.0, 37C
0.000457
-
(E)-1-((E)-3-phenylallylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000215
-
(E)-1-(2-chlorobenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000989
-
(E)-1-(3,4,5-trimethoxybenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000767
-
(E)-1-(3-bromobenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.00067
-
(E)-1-(3-chlorobenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000177
-
(E)-1-(3-methoxybenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000102
-
(E)-1-(3-nitrobenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000127
-
(E)-1-(4-(N,N-dimethylamino)benzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000707
-
(E)-1-(4-bromobenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.00041
-
(E)-1-(4-chlorobenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000887
-
(E)-1-(4-methoxybenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000547
-
(E)-1-(4-nitrobenzylidene)thiosemicarbazide
-
pH 8.2, 37C
-
0.000746
-
(E)-2-((E)-but-2-enylidene) hydrazinecarbothioamide
-
pH 8.2, 37C
-
0.00022
-
(E)-2-(2,3-dihydroxybenzylidene)hydrazinecarbothioamide
-
pH 8.2, 37C
-
0.000263
-
(E)-2-(2-(benzyloxy)benzylidene)hydrazinecarbothioamide
-
pH 8.2, 37C
-
0.00033
-
(E)-2-(3-(benzyloxy)-4-methoxybenzylidene)hydrazinecarbothioamide
-
pH 8.2, 37C
-
0.000233
-
(E)-2-(4-hydroxy-3,5-dimethoxybenzylidene)hydrazinecarbothioamide
-
pH 8.2, 37C
-
0.000682
-
(E)-2-(4-hydroxybenzylidene)hydrazinecarbothioamide
-
pH 8.2, 37C
-
0.002
0.003
(Hg2)2+
-
-
0.112
-
([[(benzyloxy)carbonyl]amino]methyl)methylphosphinothioic O-acid
-
-
0.158
-
([[(benzyloxy)carbonyl]amino]methyl)methylphosphinothioic O-acid
-
-
0.03
-
1,4-Naphthoquinone
-
pH 7.7, temperature not provided
0.125
-
2,2'-bi-1,3,4-oxadiazole-5,5'(4H,4'H)-dithione
-
pH 8.2, IC50: below 0.125 mM
0.133
-
2,2'-bi-1,3,4-oxadiazole-5,5'(4H,4'H)-dithione
-
pH 8.2, IC50: 0.133 mM
0.5
-
2,2'-bi-1,3,4-thiadiazole-5,5'(4H,4'H)-dithione
-
pH 8.2, IC50: 0.5 mM
0.18
-
2,2'-thenoin
-
IC50: 0.18 mM
0.138
-
2,4,6-trihydroxy-9H-xanthen-9-one
-
pH 6.8, 30C
0.02631
-
2,4-diphenyl-2,3-dihydro-1,5-benzothiazepine
-
-
0.02465
-
2-(4-methylphenyl)-4-phenyl-2,3-dihydro-1,5-benzothiazepine
-
-
0.03671
-
2-(4-nitrophenyl)-4-phenyl-2,3-dihydro-1,5-benzothiazepine
-
-
0.47
-
2-hydroxy-1-phenylethanone
-
IC50: 0.47 mM
0.09374
-
2-[(2S,4R)-2-(4-fluorophenyl)-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
-
-
0.09121
-
2-[(2S,4R)-2-phenyl-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
-
-
0.01907
-
2-[2-(1,3-benzodioxol-5-yl)-2,3-dihydro-1,5-benzothiazepin-4-yl]phenol
-
-
0.07385
-
3,3'-(2-bromobenzylidene)-bis-(4-hydroxycoumarin)
-
-
0.08453
-
3,3'-(2-chlorobenzylidene)-bis-(4-hydroxycoumarin)
-
-
0.05218
-
3,3'-(2-phenylpropylidene)-bis-(4-hydroxycoumarin)
-
-
0.03503
-
3,3'-(2-pyridyl-methylene)-bis-(4-hydroxycoumarin)
-
-
0.07293
-
3,3'-(3-chlorobenzylidene)-bis-(4-hydroxycoumarin)
-
-
0.05906
-
3,3'-(3-cinnamylidene)-bis-(4-hydroxycoumarin)
-
-
0.07191
-
3,3'-(3-hydroxybenzylidene)-bis-(4-hydroxycoumarin)
-
-
0.04841
-
3,3'-(3-indolidene)-bis-(4-hydroxycoumarin)
-
-
0.07368
-
3,3'-(4-hydroxybenzylidene)-bis-(4-hydroxycoumarin)
-
-
0.0553
-
3,3'-(4-methoxybenzylidene)-bis-(4-hydroxycoumarin)
-
-
0.06501
-
3,3'-(4-nitrobenzylidene)-bis-(4-hydroxycoumarin)
-
-
0.04292
-
3,3'-(crotonalidene)-bis-(4-hydroxycoumarin)
-
-
0.01501
-
3,3'-methylenebis-(4-hydroxycoumarin)
-
-
0.06639
-
3,3'-n-butylidene-bis(4-hydroxycoumarin)
-
-
0.08632
-
3,3'-n-hexylidene-bis(4-hydroxycoumarin)
-
-
0.037
-
3,4,5-trihydroxy-9H-xanthen-9-one
-
pH 6.8, 30C
2.5e-05
-
3,5-dimethylphenyl diamidophosphate
-
-
0.011
-
4-(1-amino-2-(4-hydroxyphenyl)ethyl)benzene-1,2,3-triol
-
-
0.047
-
4-(1-amino-2-(4-hydroxyphenyl)ethyl)benzene-1,2-diol
-
-
0.086
-
4-(2,3-dimethylphenyl)-5-phenyl-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 6.8, 30C
-
0.0456
-
4-(2,4-dimethylphenyl)-5-(3-nitrophenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 6.8, 30C
-
0.234
-
4-(4-benzoyl-5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)phenyl benzoate
-
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
-
pH and temperature not specified in the publlication
0.0182
-
4-(4-chlorophenyl)-5-[hydroxy(phenyl)methyl]-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH and temperature not specified in the publlication
1.6e-05
-
4-(benzyloxy)phenyl diamidophosphate
-
-
0.03
-
4-(p-hydroxyphenethyl)pyrogallol
-
-
0.125
-
4-amino-5-(4-hydroxyphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 8.2, IC50: below 0.125 mM
0.163
-
4-amino-5-pyridin-4-yl-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 8.2, IC50: 0.163 mM
0.079
-
4-butylbenzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0079
-
4-butylbenzene-1,2-diol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.124
-
4-decylbenzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.168
-
4-dodecylbenzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.034
-
4-ethylbenzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0049
-
4-ethylbenzene-1,2-diol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.091
-
4-hexylbenzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0123
-
4-hexylbenzene-1,2-diol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
6.3e-05
-
4-nitrophenyl diamidophosphate
-
-
0.103
-
4-octylbenzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.058
-
4-octylbenzene-1,2-diol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.25
-
4-tetradecylbenzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.069
-
4-[2-(3,4-diethoxyphenyl)ethyl]benzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.071
-
4-[2-(3,4-dimethoxyphenyl)ethyl]benzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0227
-
4-[2-(3,4-dimethoxyphenyl)ethyl]benzene-1,2-diol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.204
-
4-[2-(3,4-dimethoxyphenyl)ethyl]phenol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.052
-
4-[2-(3-bromophenyl)ethyl]benzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0169
-
4-[2-(3-bromophenyl)ethyl]benzene-1,2-diol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.235
-
4-[2-(3-chlorophenyl)ethyl]-1,2-dimethoxybenzene
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.05
-
4-[2-(3-chlorophenyl)ethyl]benzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0157
-
4-[2-(3-chlorophenyl)ethyl]benzene-1,2-diol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.048
-
4-[2-(4-bromophenyl)ethyl]benzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.254
-
4-[2-(4-chlorophenyl)ethyl]-1,2-dimethoxybenzene
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.047
-
4-[2-(4-chlorophenyl)ethyl]benzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0083
-
4-[2-(4-chlorophenyl)ethyl]benzene-1,2-diol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.043
-
4-[2-(4-fluorophenyl)ethyl]benzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0062
-
4-[2-(4-fluorophenyl)ethyl]benzene-1,2-diol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.032
-
4-[2-(4-hydroxyphenyl)ethyl]benzene-1,2,3-triol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0015
-
4-[2-(4-hydroxyphenyl)ethyl]benzene-1,2-diol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.125
-
5-(1-naphthyl)-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
0.214
-
5-(1-naphthyl)-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.214 mM
0.3132
-
5-(2-chlorophenyl)-N-(2,6-dimethylphenyl)-1,3,4-thiadiazol-2-amine
-
pH 6.8, 30C
-
0.4596
-
5-(3-chlorophenyl)-4-(2,4-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 6.8, 30C
-
0.357
-
5-(3-chlorophenyl)-4-(2,6-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 6.8, 30C
-
0.125
-
5-(3-hydroxyphenyl)-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
0.1708
-
5-(4-chlorophenyl)-4-(2,4-dimethylphenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
-
pH 6.8, 30C
-
0.4836
-
5-(4-chlorophenyl)-N-(2,3-dimethylphenyl)-1,3,4-thiadiazol-2-amine
-
pH 6.8, 30C
-
0.2147
-
5-(4-chlorophenyl)-N-(2,6-dimethylphenyl)-1,3,4-thiadiazol-2-amine
-
pH 6.8, 30C
-
0.5
-
5-(4-hydroxyphenyl)-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.5 mM
0.25
-
5-benzhydryl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.25 mM
0.95
-
5-benzhydryl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.95 mM
0.125
-
5-benzhydryl-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
0.125
-
5-benzyl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
0.124
-
5-cyclohexyl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.124 mM
0.125
-
5-cyclohexyl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.125 mM
0.025
-
5-hydroxy-1,4-naphthoquinone
-
pH 7.7, temperature not provided
0.125
-
5-phenyl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
0.25
-
5-phenyl-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.25 mM
0.29
-
5-phenyl-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.29 mM
0.125
-
5-pyridin-4-yl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
0.2
-
5-pyridin-4-yl-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: above 0.2 mM
0.124
-
5-pyridin-4-yl-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.124 mM
0.125
-
5-pyridin-4-yl-1,3,4-thiadiazole-2(3H)-thione
-
pH 8.2, IC50: below 0.125 mM
0.095
-
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
0.5
-
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
0.095
-
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
0.5
-
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
0.093
-
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
0.125
-
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
0.41
-
5-[4-(benzyloxy)phenyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.41 mM
0.5
-
5-[4-(benzyloxy)phenyl]-1,3,4-oxadiazole-2(3H)-thione
-
pH 8.2, IC50: 0.5 mM
0.244
-
5-[4-(tert-butyl-dimethyl-silanyloxy)-phenyl]-3H-[1,3,4]oxadiazole-2-thione
-
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
-
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
-
pH and temperature not specified in the publlication
0.01506
-
7'-hydroxy-2,2'-dioxo-2H,2'H-6,8'-bichromen-7-yl alpha-L-mannopyranoside
-
-
0.09367
-
7'-hydroxy-2,2'-dioxo-2H,2'H-6,8'-bichromen-7-yl alpha-L-mannopyranoside
-
-
0.02417
-
7'-hydroxy-2,2'-dioxo-3'-[(2-oxo-2H-chromen-7-yl)oxy]-2H,2'H-8,8'-bichromen-7-yl alpha-D-glucopyranoside
-
-
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
-
-
0.03762
-
7'-methoxy-2,2'-dioxo-3'-[(2-oxo-2H-chromen-7-yl)oxy]-2H,2'H-8,8'-bichromen-7-yl alpha-D-glucopyranoside
-
-
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
-
-
0.14
-
7,8,4'-trihydroxyisoflavone
-
-
0.02205
-
7-hydroxy-2,2'-dioxo-2H,2'H-6,8'-bichromen-7'-yl alpha-L-mannopyranoside
-
-
0.0263
-
7-hydroxy-2,2'-dioxo-2H,2'H-6,8'-bichromen-7'-yl alpha-L-mannopyranoside
-
-
0.05527
-
7-[(7-methoxy-2-oxo-2H-chromen-3-yl)oxy]-2-oxo-2H-chromen-6-yl alpha-D-glucopyranoside
-
-
0.06191
-
7-[(7-methoxy-2-oxo-2H-chromen-3-yl)oxy]-2-oxo-2H-chromen-6-yl alpha-D-glucopyranoside
-
-
0.02901
-
8-hydroxy-3-[(6-hydroxy-2-oxo-2H-chromen-7-yl)oxy]-2-oxo-2H-chromen-7-yl beta-D-glucopyranoside
-
-
0.0316
-
8-hydroxy-3-[(6-hydroxy-2-oxo-2H-chromen-7-yl)oxy]-2-oxo-2H-chromen-7-yl beta-D-glucopyranoside
-
-
0.005
-
Acetohydroxamic acid
-
IC50: 0.005 mM
0.017
-
Acetohydroxamic acid
-
-
0.02221
-
Acetohydroxamic acid
-
pH 8.2, 30C
0.0241
-
Acetohydroxamic acid
-
pH 8.2, 30C
0.045
-
Acetohydroxamic acid
-
pH and temperature not specified in the publication
2.9
-
acetol
-
IC50: 2.9 mM
2.3e-08
-
Ag+
-
pH 7.0, 37C
0.002
0.003
Ag+
-
-
1.1
-
aminomethyl(P-methyl)phosphinic acid
-
-
-
2.53
-
aminomethyl(P-methyl)phosphinic acid
-
-
-
0.14
-
avicularin
-
pH 6.0, 37C
0.031
-
beta-(o-methoxyphenyl)-gamma,gamma-bis(8-quinolinoxy)germa-gamma-lactone
-
-
0.02425
-
chloro(2-[[(2-[[2-(hydroxy-kappaO)ethyl]amino-kappaN]ethyl)imino-kappaN]methyl]-4-nitrophenolato-kappaO)copper
-
pH and temperature not specified in the publication
0.002
0.003
Cu2+
-
-
0.0033
-
Cu2+
-
pH 7.0, 37C
0.36
-
furoin
-
IC50: 0.36 mM
0.12
-
guaijaverin
-
pH 6.0, 37C
7.1e-05
-
Hg2+
-
pH 7.0, 37C
0.002
0.003
Hg2+
-
-
0.1
-
Hydroxyurea
-
IC50: 0.1 mM
0.16
-
isoquercitrin
-
pH 6.0, 37C
0.02801
-
methyl 2-amino-4,5,6,7,8,9-hexahydrocycloocta[b]thiophene-3-carboxylate
-
pH 8.2, 30C
0.03184
-
methyl 2-amino-4,5,6,7,8,9-hexahydrocycloocta[b]thiophene-3-carboxylate
-
pH 8.2, 30C
0.00534
-
methyl 2-amino-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
pH 8.2, 30C
0.0093
-
methyl 2-amino-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
pH 8.2, 30C
0.00083
-
methyl 2-amino-4-methylthiophene-3-carboxylate
-
pH 8.2, 30C
0.00281
-
methyl 2-amino-4-methylthiophene-3-carboxylate
-
pH 8.2, 30C
0.01107
-
methyl 2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
-
pH 8.2, 30C
0.01658
-
methyl 2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
-
pH 8.2, 30C
0.00213
-
methyl 2-amino-5,6-dihydro-4H-cyclopenta[b]thiophene-3-carboxylate
-
pH 8.2, 30C
0.00504
-
methyl 2-amino-5,6-dihydro-4H-cyclopenta[b]thiophene-3-carboxylate
-
pH 8.2, 30C
0.01832
-
methyl 2-[(methoxycarbonyl)amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
pH 8.2, 30C
0.02495
-
methyl 2-[(methoxycarbonyl)amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
pH 8.2, 30C
0.00077
-
methyl 2-[bis(chlorocarbonyl)amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
pH 8.2, 30C
0.00299
-
methyl 2-[bis(chlorocarbonyl)amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
pH 8.2, 30C
0.00635
-
methyl 2-[[(chloromethoxy)carbonyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
pH 8.2, 30C
0.01242
-
methyl 2-[[(chloromethoxy)carbonyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
pH 8.2, 30C
0.0271
-
methyl 2-[[(chloromethoxy)carbonyl]amino]-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
-
pH 8.2, 30C
0.02908
-
methyl 2-[[(chloromethoxy)carbonyl]amino]-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
-
pH 8.2, 30C
0.01321
-
methyl 2-[[(dichloromethoxy)carbonyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
pH 8.2, 30C
0.01945
-
methyl 2-[[(dichloromethoxy)carbonyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
pH 8.2, 30C
0.01054
-
methyl 2-[[(methylsulfanyl)carbonothioyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
pH 8.2, 30C
0.01369
-
methyl 2-[[(methylsulfanyl)carbonothioyl]amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylate
-
pH 8.2, 30C
0.06
-
methyl[(methylamino)methyl]phosphinic acid
-
-
0.06
-
methyl[(methylamino)methyl]phosphinic acid
-
pH 7.0, 37C
0.153
-
methyl[(methylamino)methyl]phosphinic acid
-
-
0.884
-
methyl[(methylamino)methyl]phosphinic acid
-
pH 7.0, 37C
0.4261
-
N-(2,3-dimethylphenyl)-5-phenyl-1,3,4-thiadiazol-2-amine
-
pH 6.8, 30C
-
0.3982
-
N-(2,4-dimethylphenyl)-5-(3-nitrophenyl)-1,3,4-thiadiazol-2-amine
-
pH 6.8, 30C
-
2e-05
-
N-(2-methoxy-4-nitrophenyl)phosphoric triamide
-
-
0.003
-
N-(2-nitrophenyl)phosphoric triamide
-
-
1.4e-05
-
N-(2-phenylethyl)phosphoric triamide
-
-
0.01386
-
N-(2-phenylethyl)phosphorothioic triamide
-
-
0.00557
-
N-(3-methoxyphenyl)phosphoric triamide
-
-
0.04255
-
N-(3-methylpyridin-2-yl)phosphorothioic triamide
-
-
0.00071
-
N-(3-morpholin-2-ylpropyl)phosphoric triamide
-
-
7e-05
-
N-(3-nitropyridin-2-yl)phosphoric triamide
-
-
0.04425
-
N-(4-cyclohexylphenyl)phosphoric triamide
-
-
1e-05
-
N-(4-methoxy-1,3-benzothiazol-2-yl)phosphoric triamide
-
-
1e-05
-
N-(4-methyl-1,3-benzothiazol-2-yl)phosphoric triamide
-
-
3e-06
-
N-(4-methyl-2-nitrophenyl)phosphoric triamide
-
-
0.0003
-
N-(4-nitrophenyl)phosphoric triamide
-
-
0.01298
-
N-(4-phenoxyphenyl)phosphoric triamide
-
-
5e-06
-
N-(6-ethoxy-1,3-benzothiazol-2-yl)phosphoric triamide
-
-
5e-06
-
N-(6-fluoro-1,3-benzothiazol-2-yl)phosphoric triamide
-
-
0.0018
-
N-(N'-benzyloxycarbonylglycyl)aminomethyl(P-methyl)phosphinothioic acid
-
-
0.0031
-
N-(N'-benzyloxycarbonylglycyl)aminomethyl(P-methyl)phosphinothioic acid
-
-
2e-06
-
N-1,3-benzothiazol-2-ylphosphoric triamide
-
-
0.00296
-
N-1,3-benzothiazol-2-ylphosphorothioic triamide
-
-
0.00256
-
N-adamant-1-ylphosphoric triamide
-
-
0.123
-
N-benzyloxycarbonylaminomethyl(P-methyl)phosphinic acid
-
-
0.319
-
N-benzyloxycarbonylaminomethyl(P-methyl)phosphinic acid
-
-
0.06
-
N-glycyl-aminomethyl(P-methyl)phosphinic acid
-
-
0.086
-
N-glycyl-aminomethyl(P-methyl)phosphinic acid
-
-
0.0172
-
N-hydroxyacetamide
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
0.0001
-
N-n-butylthiophosphorictriamide
-
-
0.00053
-
N-naphthalen-1-ylphosphoric triamide
-
-
0.00363
-
N-phenylphosphoric triamide
-
-
4.8e-05
-
N-[2-(4-fluorophenyl)ethyl]phosphoric triamide
-
-
2e-05
-
N-[2-(difluoromethoxy)phenyl]phosphoric triamide
-
-
0.075
-
N-[2-(trifluoromethoxy)phenyl]phosphoric triamide
-
-
0.0035
-
N-[4-(benzyloxy)phenyl]phosphoric triamide
-
-
0.6
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-phenylalaninamide
-
-
0.754
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-phenylalaninamide
-
-
0.15
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-serinamide
-
-
0.342
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-serinamide
-
-
0.485
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-valinamide
-
-
0.617
-
N-[[hydroxy(methyl)phosphoryl]methyl]-L-valinamide
-
-
0.45
-
N2-[(benzyloxy)carbonyl]-N-[[hydroxy(methyl)phosphoryl]methyl]glycinamide
-
-
0.64
-
N2-[(benzyloxy)carbonyl]-N-[[hydroxy(methyl)phosphoryl]methyl]glycinamide
-
-
0.08
-
O-benzyl-N-[[hydroxy(methyl)phosphoryl]methyl]-L-serinamide
-
-
0.183
-
O-benzyl-N-[[hydroxy(methyl)phosphoryl]methyl]-L-serinamide
-
-
0.01654
-
O-[4-(benzyloxy)phenyl] diamidothiophosphate
-
-
0.0051
-
p-benzoquinone
-
-
3e-06
-
phenylphosphorodiamidate
-
-
0.08
-
quercetin
-
pH 6.0, 37C
0.19
-
quercetin-4-O-beta-D-glucopyranoside
-
pH 6.0, 37C
-
0.2
-
quercitrin
-
pH 6.0, 37C
0.0209
-
tetracosyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
-
pH 6.8, 30C
0.01506
-
Thiourea
-
-
0.021
-
Thiourea
-
pH 6.8, 30C
0.021
-
Thiourea
-
pH and temperature not specified in the publlication
0.021
-
Thiourea
-
pH 6.8, 30C
0.021
-
Thiourea
-
pH 8.2, 37C
0.0211
-
Thiourea
-
-
0.258
-
[(acetylamino)methyl]methylphosphinic acid
-
pH 7.0, 37C
1.455
-
[(acetylamino)methyl]methylphosphinic acid
-
pH 7.0, 37C
0.463
-
[(acetylamino)methyl]phosphonic acid
-
pH 7.0, 37C
0.256
-
[(benzylamino)methyl]methylphosphinic acid
-
pH 7.0, 37C
1.632
-
[(benzylamino)methyl]methylphosphinic acid
-
pH 7.0, 37C
0.0038
-
[(dimethylamino)methyl]methylphosphinic acid
-
pH 7.0, 37C
0.0144
-
[(dimethylamino)methyl]methylphosphinic acid
-
pH 7.0, 37C
0.049
-
[(dimethylamino)methyl]phosphonic acid
-
pH 7.0, 37C
0.082
-
[(dimethylamino)methyl]phosphonic acid
-
pH 7.0, 37C
0.228
-
[(methylamino)methyl]phosphonic acid
-
pH 7.0, 37C
0.678
-
[(methylamino)methyl]phosphonic acid
-
pH 7.0, 37C
0.0161
-
[5-[(4-methylphenyl)amino]-1,3,4-oxadiazol-2-yl](phenyl)methanol
-
pH and temperature not specified in the publlication
0.0803
-
[5-[(4-nitrophenyl)amino]-1,3,4-oxadiazol-2-yl](phenyl)methanol
-
pH and temperature not specified in the publlication
0.3
-
[[benzyl(methyl)amino]methyl]phosphonic acid
-
pH 7.0, 37C
0.227
-
2-[2-(3,4-dimethoxyphenyl)ethyl]phenol
-
cell free urease preparation, pH not specified in the publication, temperature not specified in the publication
additional information
-
3,3'-(1H-indol-3-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.21
additional information
-
3,3'-(1H-pyrrol-2-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.33
0.08181
-
3,3'-(2-methoxybenzylidene)-bis-(4-hydroxycoumarin)
-
-
additional information
-
3,3'-(2-phenylpropane-1,1-diyl)bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.28
0.04609
-
3,3'-(2-pyrolidene)-bis-(4-hydroxycoumarin)
-
-
additional information
-
3,3'-(2E)-but-2-ene-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.36
0.05978
-
3,3'-(3-methoxybenzylidene)-bis-(4-hydroxycoumarin)
-
-
additional information
-
3,3'-(3-phenylpropane-1,1-diyl)bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.17
0.06728
-
3,3'-(dihydrocinnamylidene)-bis-(4-hydroxycoumarin)
-
-
additional information
-
3,3'-(naphthalen-1-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.07
additional information
-
3,3'-(pyridin-3-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.45
additional information
-
3,3'-(pyridin-4-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.23
additional information
-
3,3'-butane-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.17
additional information
-
3,3'-ethane-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.20
0.0613
-
3,3'-ethylidenebis-(4-hydroxycoumarin)
-
-
additional information
-
3,3'-hexane-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.06
additional information
-
3,3'-methanediylbis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.82
0.08474
-
3,3'-n-pentylidene-bis(4-hydroxycoumarin)
-
-
additional information
-
3,3'-pentane-1,1-diylbis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.19
additional information
-
3,3'-[(1E)-1-phenylprop-1-ene-3,3-diyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.22
additional information
-
3,3'-[(2-bromophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.13
additional information
-
3,3'-[(2-chlorophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.07
additional information
-
3,3'-[(2-methoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.08
additional information
-
3,3'-[(3,4,5-trimethoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.08
additional information
-
3,3'-[(3,4-dimethoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.10
additional information
-
3,3'-[(3-aminophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.12
additional information
-
3,3'-[(3-chlorophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.13
additional information
-
3,3'-[(3-ethoxy-4-hydroxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.04
additional information
-
3,3'-[(3-hydroxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.14
additional information
-
3,3'-[(3-methoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.25
additional information
-
3,3'-[(3-nitrophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.09
additional information
-
3,3'-[(4-hydroxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.13
additional information
-
3,3'-[(4-methoxyphenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.22
additional information
-
3,3'-[(4-nitrophenyl)methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.15
additional information
-
3,3'-[[4-(1-methylethyl)phenyl]methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.08
additional information
-
3,3'-[[4-(dimethylamino)phenyl]methanediyl]bis(4-hydroxy-2H-chromen-2-one)
-
pIC50: 4.09
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.647
-
-
20C, pH 4
0.79
-
-
pH 8.4, temperature not specified in the publication
2.02
-
-
4.04 micromol NH3/min/mg, pH 7.0, temperature not specified in the publication
59.9
-
-
-
60.6
-
-
pH 7.5, temperature not specified in the publication
101.7
-
-
-
219
-
-
pH 7.6, temperature not specified in the publication
220
-
-
pH 2, temperature not specified in the publication
230
-
Streptococcus mitior
-
pH 4.5, temperature not specified in the publication
290
-
-
pH 2, temperature not specified in the publication
440
-
P18314 and P18315 and P18316
G11P (UreB), 1.67 Ni2+/active site
540
-
Q8FZW3
-
540
-
-
pH 7.0, temperature not specified in the publication
664
-
-
-
670
-
-
pH 8.5, temperature not specified in the publication
690
-
-
pH 7.5, temperature not specified in the publication
700
-
-
pH 8.2, temperature not specified in the publication
730
-
-
pH and temperature not specified in the publication
1100
-
-
pH 8, temperature not specified in the publication
1120
-
bacterium strain SL100
-
-
1341
-
-
pH 8.0, temperature not specified in the publication
1573
-
-
pH 7.2, temperature not specified in the publication
1700
-
-
pH 8.0, temperature not specified
1750
-
-
pH 8.0, temperature not specified in the publication
1979
-
-
pH 6, temperature not specified in the publication
2000
-
-
pH 7.5, temperature not specified in the publication
2200
-
P18314 and P18315 and P18316
wild type, 2.1 Ni2+/active site
2370
-
Arthrobacter mobilis
-
pH 4.2, temperature not specified in the publication
2500
-
-
pH 7.75, temperature not specified in the publication
2500
-
-
pH 8.0, temperature not specified in the publication
3120
-
-
pH 7.3, temperature not specified in the publication
3570
-
-
pH 7.0, temperature not specified in the publication
7100
-
-
pH and temperature not specified in the publication
180000
-
-
pH 6.9, temperature not specified in the publication
additional information
-
-
the specific activity of a whole cell acid urease preparation is assessed in model wine solutions at different levels of malic and lactic acids, metabisulfite, ethanol, and pH by performing a central composite design
additional information
-
-
urease activites of Staphylococcus sp. T-02 cells grown in AU medium are higher. When urea is omitted from the AU medium, the overall activity is reduced up to 50%
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.85
-
-
assay at
4.2
-
Arthrobacter mobilis
-
-
4.5
-
Streptococcus mitior
-
-
4.5
-
Streptococcus mitior
-
-
5
-
-
mutant D221A
5.2
-
-
mutant enzymes C319S and C319D
5.5
-
-
and a second higher optimum at pH 9.0
5.5
-
-
and 2 other optima at pH 7.5 and 8.8
5.5
-
-
soluble urease and immobilized urease
6
-
-
in citrate buffer
6
-
-
mutant enzymes H320A, H320N and H320A
6
-
-
assay at
6.1
-
-
assay at
6.2
-
-
alginate-immobilized urease
6.5
-
-
immobilized urease
6.7
-
-
mutant C319A
6.8
-
-
mutant enzyme alphaH320A
6.8
-
-
alkylamine glass-immobilized enzyme
6.8
-
-
assay at
6.8
-
-
assay at
7
-
-
in citrate buffer
7
-
-
arylamine glass-immobilized enzyme
7
-
-
assay at
7
-
-
soluble urease
7
-
-
assay at
7.2
-
-
assay at
7.3
-
-
soluble enzyme
7.3
-
Q8FZW3
-
7.3
-
-
-
7.5
-
-
and 2 other optima at pH 5.5 and pH 8.8
7.5
-
-
agar-immobilized enzyme
7.5
-
-
assay at
7.6
-
-
wild-type enzyme
7.7
-
-
assay at
7.8
-
-
wild-type enzyme
7.9
-
-
chitosan-immobilized urease
8
-
-
-
8
-
-
wild-type enzyme
8
-
-
soluble urease and immobilized urease
8.8
-
-
and 2 lower optima at pH 5.5 and pH 7.5
9
-
-
and a second lower optimum at pH 5.5
9
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
3
-
optimal activity
3
7
-
pH 3.0: about 65% of maximal activity, pH 7.0: anout 75% of maximal activity
4.5
10
-
pH 4.5: about 45% of maximal activity, pH 10.0: about 70% of maximal activity
5
7
-
proteomic analysis with two-dimensional gel electrophoresis shows that urease proteins are expressed at both pH 5 and pH 7, although urease activity is detectable only when urease is grown at pH 5
5
8
-
pH 5.0: about 70% of maximal activity, pH 8.0: about 80% of maximal activity
5.5
8
-
pH 5.5: about 55% of maximal activity, pH 8.0: about 65% of maximal activity
6
8
Q8FZW3
-
6
8.5
-
pH 6.0: about 75% of maximal activity, pH 8.5: about 80% of maximal activity, soluble enzyme
6.9
7.5
-
optimal activity
7
10
-
pH 7.0: about 35% of maximal activity, pH 10.0: about 40% of maximal activity
7
8
-
pH 7.0: about 65% of maximal activity, pH 8.0: about 70% of maximal activity, agar-immobilized enzyme
7
8.5
-
pH 7.0: 52% of maximal activity, pH 8.5: 42% of maximal activity
7
9
-
about 65% of maximal activity at pH 7.0 and 9.0
7.3
9.6
-
50% of maximal activity at pH 7.3 and pH 9.6
8.4
9
-
optimal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
28
35
Q8FZW3
-
28
-
-
assay at
28
-
-
Yersinia enterocolitica biovar 1A grown at 28C (optimum temperature for growth) exhibits higher urease activity than that grown at 37C
30
-
-
soluble urease
30
-
-
assay at
35
50
-
broad temperatur optimum in the range of 35-50C
36
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
38
-
-
assay at
47
-
-
soluble enzyme
60
-
-
agar-immobilized urease
65
-
-
-
65
-
-
optimal assay temperature
65
-
-
soluble urease
75
-
-
chitosan-immobilized urease
77
-
-
urease coupled to the alkylamine glass or arylamine glass
80
-
-
alginate-immobilized urease
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
45
Q8FZW3
-
20
60
-
20C: about 90% of maximal activity, 60C: about 40% of maximal activity, soluble enzyme
25
75
-
25C: about 80% of maximal activity, 75C: about 45% of maximal activity
30
70
-
30C: about 40% of maximal activity, 70C: about 10% of maximal activity
40
70
-
40C: about 50% of maximal activity, 70C: about 80% of maximal activity, agar-immobilized enzyme
40
80
-
about 60% of maximal activity at 40C and at 80C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
Q8FZW3
-
5.6
-
E6Y5X0
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
expression of the urease operon is sensitive to the aspartate concentration in milk and to the cell availability of glutamate, glutamine, and ammonium ions
Manually annotated by BRENDA team
-
soybean contains an ubiquitous urease (encoded by Eu4) that is synthesized in all tissues, as well as an embryo-specific urease (encoded by the gene Eu1) that is confined to the developing embryo and is retained in mature seeds where its activity is roughly 1000fold higher than that of ubiquitous urease
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
additional information
-
optimal pH for urease activity in whole and permeabilized cells and of cell free extracts differs slightly, but is in the range 6.0-7.0. Significant activity is retained at pH 3.0 and 8.0, and, for cell free extracts, at pH 4.0 in the presence of ethanol. Urease production is evaluated in fermentations with pH control (5.25-6.5) and without pH control. Very little urease is produced in absence of urea, which at 5 g/l slows growth significantly in fermentations without pH control, but prevented a decrease in pH below 5.1 and results in higher final biomass. Optimal pH for growth is between 6.0 and 6.5 but specific urease activity is higher for fermentations at low pH at the beginning of the exponential phase. However, a higher total urease activity is obtained at pH 6.0 and 6.5 because of higher biomass
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Rhodobacter capsulatus E1F1
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Brucella abortus (strain 2308)
Helicobacter mustelae (strain ATCC 43772 / LMG 18044 / NCTC 12198 / 12198)
Helicobacter mustelae (strain ATCC 43772 / LMG 18044 / NCTC 12198 / 12198)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
11100
-
-
gamma subunit, method not specified
11700
-
-
beta subunit, method not specified
12000
-
-
gamma subunit, method not specified
14000
-
-
beta subunit, method not specified
20400
-
-
beta subunit, method not specified
21000
-
-
beta subunit, method not specified
26500
-
-
beta subunit, method not specified
29000
-
-
SDS-PAGE, subunits of the purified urease are shown to be stoichiometrically equal, with estimated molecular masses of 63 kDa and 29kDa
30000
-
-
SDS-PAGE, two major bands at 30 kDa and 60 kDa
60000
-
-
SDS-PAGE, two major bands at 30 kDa and 60 kDa
60300
-
-
alpha subunit, method not specified
61000
-
-
alpha subunit, method not specified
61400
-
-
alpha subunit, method not specified
63000
-
-
SDS-PAGE, subunits of the purified urease are shown to be stoichiometrically equal, with estimated molecular masses of 63 kDa and 29kDa
65000
-
-
alpha subunit, method not specified
72400
-
-
alpha subunit, method not specified
90000
-
-
SDS-PAGE
90770
-
-
alpha subunit of jack bean urease without Ni2+, method not specified
113900
-
-
gamma subunit, method not specified
125000
-
-
gel filtration
130000
135000
Q8FZW3
gel filtration
130000
-
-
sucrose density gradient centrifugation
135000
-
-
non-denaturing PAGE
140000
-
-
gel filtration
150000
-
-
gel filtration
157000
-
Q8FZW3
nondenaturing PAGE
174500
-
-
native PAGE
175000
-
-
gel filtration
180000
-
-
sucrose density gradient centrifugation
185000
-
-
gel filtration
185000
-
-
gel filtration
190000
-
-
gel filtration
200000
-
Streptococcus mitior
-
gel filtration
215000
-
-
gel filtration
224000
-
-
gel filtration
230000
-
-
gel filtration
232000
-
-
gel filtration
242000
-
-
gel filtration
260000
-
bacterium strain SL100
-
gel filtration
280000
-
-
urease 1, non-denaturing PAGE
350000
-
-
gel filtration
380000
-
-
non-denaturing PAGE
410000
-
-
non-denaturing PAGE
420000
-
-
non-denaturing PAGE
430000
-
-
gel filtration
480000
-
-
urease 2, non-denaturing PAGE
480000
-
-
gel filtration
545000
-
-
native PAGE
545300
-
-
hexamer with 12 nickel ions included, method not specified
580000
-
-
gel filtration
590000
-
-
hexamer with 12 nickel ions included, sedimentation method
600000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 174000 + x * 179000, SDS-PAGE; x * 179000, SDS-PAGE and treatment with 6.4 mM mercaptoethanol
?
-
x * 67000, SDS-PAGE
?
-
x * 95000, SDS-PAGE, equilibrium sedimentation in presence of guanidinium chloride and 2-mercaptoethanol
?
-
x * 93500, SDS-PAGE
?
-
x + 11000 + x * 11000 + x * 62000, SDS-PAGE
?
-
x * 31000 + x * 66000, SDS-PAGE
?
-
x * 172000, SDS-PAGE
?
Q8FZW3
x * 61054 + x * 11377 + x * 11129, calculated from sequence; x * 66000 + x * 15500 + x * 14000, SDS-PAGE
?
-
x * 65000 (UreA) + x * 32000 (UreB), SDS-PAGE
?
E6Y5X0
x * 90000 (SDS-PAGE), 90059.6 (predicted sequence)
?
-
x * 61054 + x * 11377 + x * 11129, calculated from sequence; x * 66000 + x * 15500 + x * 14000, SDS-PAGE
-
decamer
-
alpha2beta4tau4, 2 * 72000 + 4 * 11000 + 4 * 9000, SDS-PAGE
dimer
-
2 * 90500, SDS-PAGE
dodecamer
-
alpha4beta4gamma4, 4 * 72400 + 4 * 20400, + 4 * 13900, SDS-PAGE
dodecamer
-
((alpha beta)3)4 dodecameric complex, method not specified
hexamer
-
or pentamer, x * 64000 + x * 66000, SDS-PAGE
hexamer
-
x * 38000, SDS-PAGE
hexamer
bacterium strain SL100
-
3 * 21000 + 3 * 65000, SDS-PAGE
hexamer
-
3 * 30200 + 3 * 69300, SDS-PAGE
hexamer
-
3 * 29200 + 3 * 64800, SDS-PAGE
hexamer
-
3 * 30100 + 3 * 64300, SDS-PAGE; 3 * 30400 + 3 * 64300, SDS-PAGE
hexamer
-
alpha2beta2gamma2, 2 * 64000 + 2 * 15500 + 2 * 15000, SDS-PAGE
hexamer
-
6 * 72000, SDS-PAGE
hexamer
-
purified enzyme may be a hexameric aggregate, consistent with the reported stoichiometry of (29-63 kDa) * 6 of Helicobacter pylori
hexamer
Enterobacter sp. R-SYB082
-
6 * 72000, SDS-PAGE
-
homodimer
-
method not specified
homodimer
-
conclusion from native PAGE
homohexamer
-
6 * 90000, SDS-PAGE
homohexamer
-
6 * 72000, SDS-PAGE
homohexamer
-
2 Ni2+/subunit
homohexamer
-
6 * 90770, without Ni ions, method not specified
homohexamer
Enterobacter sp. R-SYB082
-
6 * 72000, SDS-PAGE
-
nonamer
P18314 and P18315 and P18316
(UreABC)3
pentadecamer
-
(alpha,beta,gamma)5, 5 * 65000 + 5 * 21000 + 5 * 12000, SDS-PAGE
pentamer
-
or hexamer, x * 64000 + x * 66000, SDS-PAGE
tetramer
-
4 * 65500, SDS-PAGE
trimer
-
3 * 67000, SDS-PAGE
trimer
-
composed of three distinct subunits, one large (60 kDa) and two small (11 kDa), commonly forming (alpha beta gamma)3 trimers
trimer
-
1 * 61000 + 1 * 11000 + 1 * 14000 composed of three distinct subunits (one large (61 kDa) and two small (11 kDa and 14 kDa)), commonly forming (alpha beta gamma)3 trimers
trimer
-
(alpha beta gamma)5 trimer. Method not specified
trimer
-
(alpha beta gamma)4 trimer, method not specified
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
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
-
crystal structure determined at 2.2 A
-
urease is inactive in the crystalline form, possibly due to conformational restrictions associated with a lid covering the active site
-
wild-type and mutant enzyme
-
crystal structure determined at 2.0 A
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.3
-
bacterium strain SL100
-
30 min, retains most of its activity
2.5
-
-
the amount of viable Yersinia enterocolitica biovar 1A decreases significantly when incubated at pH 2.5 for 2 h. No decrease is observed at this pH in the presence of urea
3
8
Lactobacillus fermentum, Streptococcus mitior
-
37C, 30 min, stable
3
9
-
37C, 30 min, stable
3.5
-
-
22C, 12 h, soluble enzyme retains 5% of its original activity, alkylamine glass-immobilized enzyme and arylamine glass immobilized urease retain 37% and 38%, respectively
4
6
-
; 35C, 30 min, stable
4
8
-
37C, 30 min, stable
4
-
-
enzyme gets irreversibly inactivated at pH 4
5
-
-
and below, nickel is irreversibly removed with concommitant loss of enzyme activity
5
-
-
irreversibly inactivated below pH 5
6
10
-
30C, 2 h, stable
7
10
-
30C, 5 h, stable
7
-
-
in presence of 10 mM EDTA protein-nickel binding remains intact
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
pH 7.3, half-life of soluble enzyme is 21 days, half-life of agar-immobilized enzyme is 53 days
4
-
-
immobilized urease shows improved stability when stored at 4C and t1/2 of urease is found to be 19 days, 80 days and 121 days, respectively for soluble, alginate and chitosan ureases
30
-
-
pH 4, 30 min, stable below
30
-
-
30 min, stable
40
-
-
pH 4, 30 min, stable below
50
-
-
pH 7.5, 10 min, stable below
50
-
Streptococcus mitior
-
pH 4, 30 min, stable below
50
-
-
2 h, 30% loss of activity, wild-type enzyme
50
-
-
very stable below 50C
55
-
-
30 min, 15% loss of activity
60
-
-
pH 7.5, 10 min, 50% loss of activity
60
-
-
pH 4, 30 min, stable below
60
-
-
30 min, stable up to
60
-
-
2 h, 55% loss of activity, wild-type enzyme. 2 h, complete inactivation of mutant enzymes betaH39A and alphaH320A
60
-
-
30 min, about 25% loss of activity
60
-
-
retains more than 80% activity after incubation up to 60C for 15 min
65
-
-
stable up to
70
-
-
1 h, 87% loss of activity, wild-type enzyme, 58% loss of activity of mutant enzyme alphaG312A, complete inactivation of mutant enzymes gammaH96A, betaH39A, betaH41A, alphaH219A, alphaH320A and alphaH321A
70
-
-
30 min, about 55% loss of activity
75
-
-
immobilized urease shows improved stability at 75C. Soluble urease t1/2: 12 min, chitosan-immobilized urease t1/2: 58 min, alginate-immobilized urease t1/2: 43 min
77
-
-
15 min, soluble urease has a residual activity of 22%, alkylamine glass-immobilized enzyme and arylamine glass-immobilized urease retain 96% and 98%, respectively. Even after 90 min of incubation immobilized urease retains 50% of activity
additional information
-
-
Ni substantially increase stability of the intact metalloprotein, Tm = 79C compared with apoenzyme Tm = 62C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unstable during purification in absence of nickel. When 0.005 mM NiSO4 is present during growth and at 0.1 mM in buffers during sonication and purification, the urease is completely stable at room temperature during the purification procedure
bacterium strain SL100
-
dithiothreitol, 50 mM, stabilizes
-
agar-immobilized enzyme showes good mechanical stability
-
the immobilized enzyme is more stable in wet condition than in semi-dry condition and storing it at 4C is more favourable over 27C. There is a tremendous decrease in activity when the immobilized urease is not stored in buffer (i.e. semi-dry condition) and storing it at 4C improves the longevity. Both the alkyl and arylamine-urease in wet condition stored at 4C are further reused (30times) and the residual activity are 40% and 20%, respectively
-
stability at 4C is enhanced by addition of glycerol or 2-mercaptoethanol
-
resistant to denaturation by 4 M urea
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Methanol
-
100% activity
phenol
-
0.01% activity
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 70 days, soluble enzyme loses 90% of its activity, alkylamine-immobilized enzyme loses 15% of the initial activity, the arylamine-immobilized enzyme loses 17% of its activity
-
20C, 50 mM phosphate buffer, pH 7.5, 50% glycerol, 1 mM EDTA, 5 mM 2-mercaptoethanol, about 30% loss of activity after 2 months
-
4C, sodium phosphate buffer, pH 7.2, 1% bovine serum albumin, stable for 20 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
bacterium strain SL100
-
commercial preparation
-
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
E6Y5X0
using acetone precipitation, gel filtration and ion-exchange chromatography
-
wild-type and mutant enzymes C319A, C319S, C319D and C319Y
-
using ammonium sulfate precipitation, dialysis, and anion exchange chromatography
-
using NH4(SO4)2 precipitation, phenyl-Sepharose column chromatography and gel filtration
-
anion exchange chromatography, gel filtration
-
anion-exchange chromatography, hydrophobic interaction chromatography, affinity chromatography (Cellufine Sulphate)
-
large-scale HPLC-based
-
recombinant enzyme from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
urease gene cluster
Q9Z395
heterologous expression of the insecticidal peptide Jaburetox-2Ec, derived from an internal sequence of JBURE-II urease isoform in Escherichia coli
-
His-tagged version expressed in Escherichia coli BL21 STAR (DE3)
E6Y5X0
-
P18314 and P18315 and P18316
expression in Escherichia coli with and without coexpression of the Helicobacter pylori nickel transporter NixA
Q93PJ4, Q93PJ5
recombinantly expressed in Escherichia coli
-
urease gene cluster
-
expression in Escherichia coli and Streptococcus gordonii DL1
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
urease activity of Vibrio parahaemolyticus is intimately related to the transcriptional activity of UreR (transcriptional activator). Two nucleotides located at positions -108 and -66 upstream of the methionine initiation codon for UreR play a critical role for temperature-dependent urease activity in strain TH3996
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
alphaH134A
-
no detectable activity, 53% of the nickel content of wild-type enzyme
alphaH136A
-
no detectable activity, 6% of the nickel content of wild-type enzyme
alphaH219A
-
1.9% of the activity of the wild-type enzyme, 80% of the nickel content of the wild type enzyme, very high Km-value compared to wild-type enzyme
alphaH246A
-
no detectable activity, 21% of the nickel content of wild-type enzyme
alphaH320A
-
normal nickel content, 0.003% of the activity of the wild-type enzyme, unlike wild-type enzyme no inactivation by diethyldicarbonate
alphaH321A
-
activity and nickel content are similar to wild-type enzyme
betaH39A
-
activity and nickel content are similar to wild-type enzyme
betaH41A
-
activity and nickel content are similar to wild-type enzyme
C319A
-
48% of the activity of the wild-type enzyme, nickel content of the mutant is lower than that of the wild-type enzyme, small increase in Km-value; no activity
C319D
-
0.03% of the activity of the wild-type enzyme, nickel content of the mutant is lower than that of the wild-type enzyme, small increase in Km-value
C319S
-
4.5% of the activity of the wild-type enzyme, nickel content of the mutant is lower than that of the wild-type enzyme, small increase in Km-value
D221A
-
low activity, small increase in Km-value and pH 5 optimum
G11P
P18314 and P18315 and P18316
UreB, subunit beta, analysis of urease activation
G18P
P18314 and P18315 and P18316
UreB, subunit beta, analysis of urease activation
gammaH96A
-
activity and nickel content are similar to wild-type enzyme
H219A
-
1000fold increased Km-value over that of the native enzyme
H219H
-
100fold increased Km-value over that of the native enzyme
H219Q
-
100fold increased Km-value over that of the native enzyme
H320A
-
100000fold deficiencies in rates, modest Km changes, disorders in the peptide flap covering their active sites, the pH-optimum is anomalous with optima near pH 6 and shoulders that extend to pH 9
H320N
-
100000fold deficiencies in rates, modest Km changes, disorders in the peptide flap covering their active sites, the pH-optimum is anomalous with optima near pH 6 and shoulders that extend to pH 9
H320Q
-
100000fold deficiencies in rates, modest Km changes, disorders in the peptide flap covering their active sites, the pH-optimum is anomalous with optima near pH 6 and shoulders that extend to pH 9
R336Q
-
0.0001fold decreased catalytic rate with near-normal pH dependence, unaffected Km-value, phenylglyoxal inactivates at over half the rate observed for the native enzyme
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
urea is estimated in different blood samples with the help of agar-immobilized urease and the results are consistent with those from clinical pathology laboratory through an autoanalyzer
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
food industry
-
the enzyme is applicable to elimination of urea in Chinese rice wine
food industry
Enterobacter sp. R-SYB082
-
the enzyme is applicable to elimination of urea in Chinese rice wine
-
medicine
-
lack of enzyme activity in most enterohaemorrhagic strains is due to a premature stop codon in ureD encoding a chaperone protein of the urease gene cluster
biotechnology
-
soybean (Glycine max) urease is immobilized on alginate and chitosan beads and shows improved stability. This could have a potential role in haemodialysis machines
medicine
-
enhancement of intragastric enzyme activity is not strictly a function of pH-value, but is related to differential effects of the availability of nickel, which is required for enzyme activity
medicine
-
the action of urease in the upper intestinal tract is exploited in a non-invasive urease breath test for the diagnosis of bacterial infections of Helicobacter pylori: 13C- or 14C-labelled urea is ingested, and if the bacterium is present in the stomach, the urea is converted into isotope-labelled carbon dioxide. This is absorbed into the blood and exhaled in the breath, where it is detected by mass spectrometer or scintillation counter
nutrition
-
elimination of the urea in alcoholic beverages
nutrition
Lactobacillus animalis MU-4
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elimination of the urea in alcoholic beverages
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biotechnology
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in food industry immobilisation of acid urease on an inert carrier has the potential advantages of significant cost savings, improved stability or resistance to shear or inhibitory compound inactivation. Purified acid urease preparation is covalently immobilised onto biocompatible porous chitosan beads of different size. The kinetics of urea degradation in a model wine solution using this biocatalyst is of the pseudofirst order with respect to the urea concentration in the liquid bulk, the apparent pseudo-first order kinetic rate constant ranging from about two thirds to one fifth of that pertaining to free acid urease
nutrition
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elimination of the urea in alcoholic beverages
synthesis
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production of ammonia
nutrition
Lactobacillus fermentum IFO 14511
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elimination of the urea in alcoholic beverages
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nutrition
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elimination of the urea in alcoholic beverages
nutrition
Lactobacillus reuteri RT-5
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elimination of the urea in alcoholic beverages
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nutrition
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elimination of the urea in alcoholic beverages
nutrition
Lactobacillus ruminis PG-98
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elimination of the urea in alcoholic beverages
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nutrition
Streptococcus mitior
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elimination of the urea in alcoholic beverages
nutrition
Streptococcus mitior PG-118
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elimination of the urea in alcoholic beverages
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nutrition
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elimination of the urea in alcoholic beverages
nutrition
Streptococcus salivarius PG-202
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elimination of the urea in alcoholic beverages
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