Information on EC 1.7.3.3 - factor-independent urate hydroxylase

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

EC NUMBER
COMMENTARY hide
1.7.3.3
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RECOMMENDED NAME
GeneOntology No.
factor-independent urate hydroxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
urate + O2 + H2O = 5-hydroxyisourate + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
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reduction
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additional information
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the enzyme catalyzes the degradation of urate to [S]-allantoin through 5-hydroxyisourate as a metastable intermediate
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
urate degradation to allantoin I
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allantoin degradation
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Purine metabolism
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Caffeine metabolism
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
urate:oxygen oxidoreductase
This enzyme was previously thought to be a copper protein, but it is now known that the enzymes from soy bean (Glycine max), the mould Aspergillus flavus and Bacillus subtilis contains no copper nor any other transition-metal ion. The 5-hydroxyisourate formed decomposes spontaneously to form allantoin and CO2, although there is an enzyme-catalysed pathway in which EC 3.5.2.17, hydroxyisourate hydrolase, catalyses the first step. The enzyme is different from EC 1.14.13.113 (FAD-dependent urate hydroxylase).
CAS REGISTRY NUMBER
COMMENTARY hide
9002-12-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
Aedes aegypti NH-Rockefeller
NH-Rockefeller strain
UniProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
FERM BP-360
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
TB-90
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Manually annotated by BRENDA team
subspecies subtilis LMD 69.3
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain ZZJ4-1
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
prawn
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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1020474 A+, 1020476 A+, 1021176 A+, 1040430 A+, 1040431 A+, 1040432 A+, 1040434 A+, 1040440 A+, 1040494 A+, 1058772 A+, 1082599 A+, 1192551 A+, 1192752 A+, 1203160 A+, 1263718 A+, 1288595 A+, 1512965 A+, 1513073 A+, 1572945 A+, 1599116 A+, 1676032 A+, 1735870 A+, 1757167 A+, 1757172 A+, 1757174 A+, 1757182 A+, 1757195 A+, 1757209 A+, 1757210 A+, 1757220 A+, 1757239 A+, 1757269 A+, 1757291 A+, 2262818 A+, 2262832 A+, 2262841 A+, 2506308 A+, 2538826 A+, 2630809 A+, 2688259 A+, 2791536 A+, 2806985 A+, 2807008 A+, 2807038 A+, 2807044 A+, 2807082 A+, 2807085 A+, 2807095 A+, 2807141 A+, 2807149 A+, 2807166 A+, 2807175 A+, 391343 A+, 689164 A+, 1020441 A++, 1023511 A++, 1040309 A++, 1040314 A++, 1040318 A++, 1040328 A++, 1040336 A++, 1040349 A++, 1040350 A++, 1040353 A++, 1040360 A++, 1040361 A++, 1040364 A++, 1040365 A++, 1040379 A++, 1040403 A++, 1040404 A++, 1040412 A++, 1720884 A++, 1732067 A++, 1732088 A++, 1732089 A++, 1757163 A++, 1757165 A++, 1757180 A++, 1757197 A++, 2210043 A++, 2253445 A++, 2262727 A++, 2262730 A++, 2262740 A++, 2262747 A++, 2262748 A++, 2262862 A++, 2365421 A++, 246671 A++, 2607275 A++, 2765205 A++, 2806975 A++, 2806993 A++, 2807061 A++, 394130 A++, 394131 A++, 394152 A++, 394171 A++, 394186 A++, 711515 A++, 1083298 A++, 1203169 A++, 1302382 A++, 1368299 A++, 1375399 A++, 1378384 A++, 1569177 A++, 1684725 A++, 1684855 A++, 1732112 A++, 1734969 A++, 1734979 A++, 1735879 A++, 1735880 A++, 1735881 A++, 1735890 A++, 1735919 A++, 1757159 A++, 1757161 A++, 1757162 A++, 1757171 A++, 1757179 A++, 1757190 A++, 1757192 A++, 1757194 A++, 1757222 A++, 1757228 A++, 1757230 A++, 2248698 A++, 2262734 A++, 2262755 A++, 2611092 A++, 2630593 A++, 2780109 A++, 2806956 A++, 2806957 A++, 2806963 A++, 2806996 A++, 2807007 A++, 2807017 A++, 2807018 A++, 2807032 A++, 2807143 A++, 2807170 A++, 657736 A++, 1040471 A+++, 1040502 A+++, 1040306 A++++, 1040308 A++++, 1040323 A++++, 1040325 A++++, 1040326 A++++, 1040331 A++++, 1040333 A++++, 1040337 A++++, 1040339 A++++, 1040345 A++++, 1040347 A++++, 1040348 A++++, 1040351 A++++, 1040352 A++++, 1040356 A++++, 1040394 A++++, 1040398 A++++, 1040399 A++++, 394133 A++++, 675091 A++++
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
salmon
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
shark
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Automatic Mining of ENzyme DAta
shrimp
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Automatic Mining of ENzyme DAta
squirrel
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
trout
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
yeast-like fungi
endosymbiont of Nilaparvata lugens
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Manually annotated by BRENDA team
yeasts
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Automatic Mining of ENzyme DAta
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-hydroxyisourate + O2
(S)-allantoin + H2O2 + CO2
show the reaction diagram
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?
urate + O2 + H2O
5-hydroxyisourate + H2O2
show the reaction diagram
uric acid + O2 + H2O
5-hydroxyisourate + H2O2
show the reaction diagram
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purine degradation
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
urate + O2 + H2O
5-hydroxyisourate + H2O2
show the reaction diagram
uric acid + O2 + H2O
5-hydroxyisourate + H2O2
show the reaction diagram
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purine degradation
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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strong activation at 10 mM
CaCl2
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enhances activity
Co2+
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copper
Cu2+
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enzyme contains copper, inhibited by excessive addition of Cu2+
Fe3+
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activates
K+
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slight activation at 10 mM
Mg2+
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strong activation at 10 mM
Mn2+
2 mM, 170% of initial activity
Na+
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slight activation at 10 mM
NaCl
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enhances activity
NH4Cl
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slight activation at 10 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3,7-Trimethylxanthine
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i.e. caffeine, slight
2,2'-dipyridyl
2,9-Dimethyl-1,10-phenanthroline
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neo-cuproin
2-Hydroxypurine
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3,7-Dimethylxanthine
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i.e. theobromine, slight
3-Methyluric acid
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5,5'-dithiobis(2-nitrobenzoate)
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5-Azaorotate
7-Methyluric acid
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8-Azaxanthine
8-nitroxanthine
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9-methyluric acid
adenine
Allantoic acid
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weak
allantoin
Amelide
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arginine
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weak
aspartic acid
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slight
beta-mercaptoethanol
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about 60% residual activity after 1 h incubation with 0.5 mM beta-mercaptoethanol at pH 8.5 and 25C
Biguanidine salts
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inactivation is pH-dependent: slightly inhibitory below pH 10, rapid inactivation at high pH
Cyanurate
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D-sorbitol
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about 70% residual activity after 1 h incubation with 0.5 mM D-sorbitol at pH 8.5 and 25C
Dicyandiamide
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inactivation is pH-dependent: small below pH 10, rapid increase at high pH
diethyldithiocarbamic acid
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glutamine
glyoxylic acid
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weak
Guanidinium salts
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inactivation is pH-dependent: slightly inhibitory below pH 10, rapid inactivation at high pH
hydroxylamine
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Hydroxypurines
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hypoxanthine
inosine 5'-monophosphate
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iodoacetate
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low effect
Li+
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18.5% inhibition at 1 mM
N-ethylmaleimide
neocuproin
o-Iodosobenzoate
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o-phenanthroline
oxonate
Oxopurines
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p-chloromercuribenzoate
phosphate
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no inactivation by phosphate, in presence of borate or dithiothreitol
pyrazinoate
Salicylhydroxamic acid
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SDS
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49% inhibition at 0.5% w/v
Sodium deoxycholate
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about 90% residual activity after 1 h incubation with 0.5 mM sodium deoxycholate at pH 8.5 and 25C
Thiourea
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slight
Trichloropurine
Urate
xanthine
ZnCl2
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1 mM, 91% inhibition
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
uric acid
DQ887577
uric acid (0.3%) is an inducer for uricase production, concentrations higher than 0.3% do not enhance the enzyme productivity
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.029 - 0.061
O2
0.0000135 - 1.05
Urate
0.00588 - 1.5
uric acid
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.01 - 18.1
Urate
31.3
uric acid
Glycine max
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
510 - 2620
Urate
710
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0021
8-nitroxanthine
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competitive inhibitor versus urate at pH 8.0
0.008
oxonate
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unmodified enzyme, 50 mM borate buffer, 25C, pH 9.2
0.041 - 4.5
xanthine
additional information
additional information
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1-methylurate, 3-methylurate, 7-methylurate do not inhibit significantly
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.067
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wild-type, pH 8.9, 25C
2.49
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urate oxidase including p-azido-L-phenylalanine instead of Phe at position 281, in 0.1 M borate, pH 8.4
2.67
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recombinant strain overexpressing the enzyme, pH 8.9, 25C
2.99
mutant A89T/G91A7V92M/H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25C
3.74
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cotyledons, 4 d old
4.22
wild-type, pH 8.6, 25C
4.91
mutant H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25C
5.32
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purified enzyme
5.68
mutant A296V, pH 8.6, 25C
5.94
mutant R291K/A296V/A301S/K303R, pH 8.6, 25C
8.26
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urate oxidase including p-azido-L-phenylalanine instead of Phe at position 170, in 0.1 M borate, pH 8.4
9.35
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male rats
10.5
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in the cell lysate
13.3
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hypocotyls, 4 d old
15.3
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female
15.4
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roots, 4 d old
16.33
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natural uricase, in 0.1 M borate, pH 8.4
18
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crude extract, pH 8.0, 37C
21.5
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after DEAE Sepharose FF chromatography
25.7
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after Phenyl-Sepharose FF chromatography
27
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after HiLoad 26/60 Superdex 75 gel filtration
38.4
recombinant protein, pH 8.0, 37C
39
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after 2.1fold purification, pH 8.0, 37C
1790
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nodules, 21 d old
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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yield of recombinant uricase is significantly improved by the combined use of a high cell-density cultivation technique and a pH control strategy of switching culture pH from 5.5 to 6.5 in the induction phase
7
DQ887577
optimal pH for uricase production in culture flasks
8 - 8.5
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borate and phosphate buffer
8.5 - 9.3
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8.6
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free enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
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free uricase shows at least 50% relative activity between pH 6.5 and 9.5, around pH 7.5, free uricase remains 81.16% of its maximum activity, while the uricase loaded in the lipid vesicles remains almost the same high activity (178.26%) as its optimum activity (179.72%)
6.5 - 11
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pH 6.5: about 40% of maximal activity, pH 10.0: about 50% of maximal activity
7 - 11
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pH 7: about 50% of activity maximum, pH 11: about 40% of activity maximum
7.4 - 9.6
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50% of activity maximum at pH 7.4 and pH 9.6, free enzyme
7.5 - 8.5
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8 - 10.2
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pH 8.0: about 35% of activity maximum, pH 10.2: about 55% of activity maximum
8 - 11
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50% of activity maximum at pH 8 and pH 11, immobilized enzyme
8.5 - 10.5
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50% of activity maximum at pH 8.5 and pH 10.5
8.5 - 9.5
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8.6 - 9.5
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
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20C: about 70% of activity maximum; 50C: about 60% of activity maximum
20 - 70
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free uricase shows at least 50% relative activity between 20 and 70C
20 - 50
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20C: about 60% of activity maximum; 50C: about 50% of activity maximum
20 - 55
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20C: about 80% of maximal activity, maximal activity at 30C, 55C: about 55% of maximal activity
35 - 60
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.96
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isoelectric focusing, pH gradient 3.5-9.5
7.6
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isoelectric focusing, rasburicase
8.46
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determined by means of P/ACE 5000
9.38
calculation from nucleotide sequence
additional information
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isoelectric focusing presents a trail of pI values between 6.55 and 7.6