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Enzyme Nomenclature
Information on EC 1.7.3.3 - factor-independent urate hydroxylase
for references in articles please use BRENDA:EC1.7.3.3
Word Map on EC 1.7.3.3
- 1.7.3.3
- hyperuricemia
- peroxisomal
- renal
- xanthine
- allopurinol
- purine
- catalase
- allantoin
- gout
-
hematologic
-
oxonic
- hypoxanthine
- allantoinase
- hyperkalemia
-
prophylaxis
- flavus
-
amperometric
-
ureide
-
pegylated
- febuxostat
-
hypocalcemia
- hyperphosphatemia
-
urate-lowering
-
uricosuric
-
phosphotungstate
- methemoglobinemia
-
hominoid
- pimecrolimus
- benzbromarone
- utilis
-
nodule-specific
- microbodies
-
hypouricemic
-
tophi
- medicine
- analysis
- drug development
-
darbepoetin
- synthesis
- pharmacology
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
1.7.3.3
-
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RECOMMENDED NAME
GeneOntology No.
factor-independent urate hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
urate + O2 + H2O = 5-hydroxyisourate + H2O2
-
-
-
-
urate + O2 + H2O = 5-hydroxyisourate + H2O2
catalytic mechanism, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
additional information
-
the enzyme catalyzes the degradation of urate to [S]-allantoin through 5-hydroxyisourate as a metastable intermediate
oxidation
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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).
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CAS REGISTRY NUMBER
COMMENTARY
9002-12-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene of a clinical isolate. The nucleotide sequence is identical to the coding sequence of gene puuD of Pseudomonas aeruginosa PAO1
UniProt
-
-
-
-
SwissProt
-
-
-
gene of a clinical isolate. The nucleotide sequence is identical to the coding sequence of gene puuD of Pseudomonas aeruginosa PAO1
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
ancestral uricases have steadily decreased in activity since the last common ancestor of mammals gave rise to descendent primate lineages. This progressive decrease is correlated with physiological function and (potential) adaptation. Analysis of the 3D distribution of amino acid replacements as they accumulated during evolutionary history
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
uric acid + O2 + H2O
5-hydroxyisourate + H2O2
-
purine degradation
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
ureide pathway
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
enzyme production is induced by addition of uric acid to the culture medium
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
enzyme production is induced by addition of uric acid to the culture medium
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
first step in uric acid degradation
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
purine metabolism
a metastable intermediate, which is further degrades to allantoin
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
urate oxidase catalyzes the hydroxylation of uric acid into the metastable product 5-hydroxyisourate in the presence of molecular oxygen as part of the purine degradation pathway. 5-Hydroxyisourate decays slowly to allantoin, a process independent of oxygen and associated with the release of CO
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
dioxygen-binding site structure, overview
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
substrate binding involves residues Arg176 and Glu228, that hold the substrate, Phe159 closing one end of the cavity below, and the two residues Asn254 and Thr57, forming another tweezers above the mean plane of the ligand that construct a location where efficient electron transfer can take place at a low energy level via the catalytic triad Thr57, Lys10, and His256
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
it is proposed that T69 and K9 form a catalytic diad in which K9 deprotonates T69 to allow it to abstract the proton from the N9 position of the substrate to generate the dianion
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
DQ887577
ureide pathway
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
detection of two discrete enzyme-bound intermediates by single-turnover stopped-flow techniques
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
conversion to allantoin
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
JX083378
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
additional information
?
-
-
anion-pi interactions are present in the active site of the enzyme and are energetically favorable
-
-
-
additional information
?
-
-
enzyme catalyzes the oxidation of uric acid to a more soluble and easily excreted compound, allantoin
-
-
-
additional information
?
-
-
purine degradation, urate oxidase catalyzes the oxidation of uric acid with poor solubility to produce 5-hydroxyisourate and allantoin
-
-
-
additional information
?
-
-
uricase can function as a voltage-sensitive channel that is highly selective to urate, relative to K+ and Cl-
-
-
-
additional information
?
-
-
rasburicase acts at the end of the purine catabolic pathway, and unlike allopurinol, it does not induce accumulation of xanthine or hypoxanthine
-
-
-
additional information
?
-
-
uricase can function as a voltage-sensitive channel that is highly selective to urate, relative to K+ and Cl-
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
uric acid + O2 + H2O
5-hydroxyisourate + H2O2
-
purine degradation
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
D0VWQ1
ureide pathway
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
enzyme production is induced by addition of uric acid to the culture medium
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
enzyme production is induced by addition of uric acid to the culture medium
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
first step in uric acid degradation
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
purine metabolism
a metastable intermediate, which is further degrades to allantoin
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
urate oxidase catalyzes the hydroxylation of uric acid into the metastable product 5-hydroxyisourate in the presence of molecular oxygen as part of the purine degradation pathway. 5-Hydroxyisourate decays slowly to allantoin, a process independent of oxygen and associated with the release of CO
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
DQ887577
ureide pathway
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
conversion to allantoin
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
additional information
?
-
-
enzyme catalyzes the oxidation of uric acid to a more soluble and easily excreted compound, allantoin
-
-
-
additional information
?
-
-
purine degradation, urate oxidase catalyzes the oxidation of uric acid with poor solubility to produce 5-hydroxyisourate and allantoin
-
-
-
additional information
?
-
-
rasburicase acts at the end of the purine catabolic pathway, and unlike allopurinol, it does not induce accumulation of xanthine or hypoxanthine
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
UOX is unique among the oxygen-requiring enzymes in the sense that it does not need a cofactor to convert uric acid to 5-hydroxyisourate
-
additional information
-
the catalytic mechanism of UOX does not imply any cofactor
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu2+
Iron
Mg2+
additional information
Cu2+
-
enzyme contains copper, inhibited by excessive addition of Cu2+
additional information
-
the catalytic mechanism of UOX does not imply any metal ion
additional information
-
a metal ion is possibly strongly bound in the enzyme and forms part of the uricase structure
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-mercaptoethanol
-
about 60% residual activity after 1 h incubation with 0.5 mM beta-mercaptoethanol at pH 8.5 and 25°C
Biguanidine salts
-
inactivation is pH-dependent: slightly inhibitory below pH 10, rapid inactivation at high pH
D-sorbitol
-
about 70% residual activity after 1 h incubation with 0.5 mM D-sorbitol at pH 8.5 and 25°C
Dicyandiamide
-
inactivation is pH-dependent: small below pH 10, rapid increase at high pH
Guanidinium salts
-
inactivation is pH-dependent: slightly inhibitory below pH 10, rapid inactivation at high pH
H2O2
-
purified uricase retains 72% of its original activity after incubation with 0.5% H2O2 for 6 h
sodium deoxycholate
-
about 90% residual activity after 1 h incubation with 0.5 mM sodium deoxycholate at pH 8.5 and 25°C
8-Azaxanthine
-
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
CN-
-
the presence of residue Phe159 enhances the interaction energy of the anion with the urate pi system
Cu2+
-
enzyme contains copper, inhibited by excessive addition of Cu2+, 98% inhibition by 1 mM CuCl2, 97% inhibition by 1 mM CuSO4
SDS
-
purified uricase retains 82% of its original activity after incubation with 0.5% SDS for 6 h
additional information
Q17J02
reduced levels of mRNA levels of urate oxidase after knock down of urate oxidase gene expression
-
additional information
-
no inhibition by 1 mM Fe(ClO4)3 or 1 mM AgNO3
-
additional information
-
production of an egg yolk antibody specific to microbial uricase and its inhibitory effects on uricase activity
-
additional information
-
not inhibitory: Tween-20 or Triton X-100 at 0.5% w/v
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
Q17J02
1 h after feeding with ammonium chloride highest expression of urate oxidase in fat body, 6 h after feeding with ammonium chloride highest expression of urate oxidase in malpighian tubules; in fat body 3fold increased expression towards end of blood meal digestion; in malpighian tubule expression induced in response to a blood meal, maximum level 24 h after feeding
-
additional information
-
dithiothreitol treatment leads to an insignificant change in specific activity below 1%
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Urate
-
Km value for degradation of urate crystals is 7 microg/ml, 30°C, pH not specified in the publication; Km value for degradation of urate crystals is 9 microg/ml, 30°C, pH not specified in the publication
0.0064
Urate
mutant A296V, pH 8.6, 25°C; mutant R291K/A296V/A301S/K303R, pH 8.6, 25°C
0.0065
Urate
mutant H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25°C
0.017
Urate
mutant A89T/G91A7V92M/H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25°C
0.05
uric acid
-
native uricase, monomethoxypoly(ethylene glycol) N-leucine-OSu-uricase and branched monomethoxypoly(ethylene glycol) N-leucine-OSu-uricase
0.25
uric acid
DQ887577
0.1 M sodium borate, pH 8.5 containing 2 mM uric acid, 30 mM 4-aminoantipyrine, 1.5% phenol and peroxidase (15 U/ml), 37°C, 20 min
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.7
Urate
mutant A89T/G91A7V92M/H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25°C
15.5
Urate
mutant H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
510
Urate
mutant A89T/G91A7V92M/H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25°C
2390
Urate
mutant H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
1-methylurate, 3-methylurate, 7-methylurate do not inhibit significantly
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.49
-
urate oxidase including p-azido-L-phenylalanine instead of Phe at position 281, in 0.1 M borate, pH 8.4
2.99
mutant A89T/G91A7V92M/H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25°C
4.91
mutant H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25°C
8.26
-
urate oxidase including p-azido-L-phenylalanine instead of Phe at position 170, in 0.1 M borate, pH 8.4
15
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
among the parameters investigated in shaking flask cultures, the pH value of medium and inoculum size has great influence on the recombinant uricase production, the maximum extracellular uricase yield of 2.6 U/ml is obtained in shaking flask culture; at pH 5.5, the extracellular uricase production reaches top of 7.5 U/ml at 58 h, when fermentation is performed at pH 6.5 for 62 h, 14.5 U/ml of extracellular uricase and 23.3 U/ml of intracellular uricase are produced, the total specific uricase production at pH 6.5 is 1.7times of that at pH 5.5; in high density fermentation in YPG medium at 37°C, extracellular uricase activity increases significantly during the first 40 h, highest extracellular uricase level of 52.3 U/ml is obtained after 58 h of induction, as well as the intracellular activity of 60.3 U/ml, after 86 h of fermentation and 58 h of induction, a total uricase activity of 112600 U/l is obtained, the extracellular and intracellular yields of uricase in high cell density fermentation increased by 3.7fold and 3.5fold compared with the batch fermentation; the combined use of fed-batch culture and pH-controlled strategy increases the expression level of uricase significantly, the extracellular uricase production of 52.3 U/ml (approximately 2.1 g/l of protein) is obtained, which is much higher than that produced by recombinant Escherichia coli strains
additional information
DQ887577
enzyme activity is 0.06 U/ml at pH 4.0; enzyme activity is 0.09 U/ml at pH 4.5; enzyme activity is 0.11 U/ml at pH 5.0; enzyme activity is 0.21 U/ml with potassium nitrate as nitrogen source; enzyme activity is 0.22 U/ml at pH 10.0; enzyme activity is 0.31 U/ml with ammonium sulfate as nitrogen source; enzyme activity is 0.32 U/ml with sodium glutamate as nitrogen source; enzyme activity is 0.37 U/ml at pH 5.5; enzyme activity is 0.42 U/ml at pH 9.5; enzyme activity is 0.45 U/ml with citric acid as carbon source; enzyme activity is 0.46 U/ml with glucose as carbon source; enzyme activity is 0.46 U/ml with peptone as nitrogen source; enzyme activity is 0.47 U/ml at pH 6.0; enzyme activity is 0.47 U/ml with lactose as carbon source; enzyme activity is 0.49 U/ml with starch as carbon source; enzyme activity is 0.57 U/ml at pH 9.0; enzyme activity is 0.57 U/ml with soybean flour as nitrogen source; enzyme activity is 0.63 U/ml at pH 8.5; enzyme activity is 0.65 U/ml with beef extract as nitrogen source; enzyme activity is 0.67 U/ml with sucrose as carbon source; enzyme activity is 0.69 U/ml with yeast extract as nitrogen source; enzyme activity is 0.72 U/ml at pH 8.0; enzyme activity is 0.78 U/ml with maize milk as nitrogen source; enzyme activity is 0.98 U/ml at pH 6.5; enzyme activity is 1.00 U/ml at pH 7.5; enzyme activity is 1.25 U/ml at pH 7.0; when the strain is cultured at 30°C at pH 7.0 for 30-36 h with of 0.6% corn steep liquor as nitrogen source, the uricase activity peaks at 1.25 U/ml
additional information
-
enzyme activity is 0.06 U/ml at pH 4.0; enzyme activity is 0.09 U/ml at pH 4.5; enzyme activity is 0.11 U/ml at pH 5.0; enzyme activity is 0.21 U/ml with potassium nitrate as nitrogen source; enzyme activity is 0.22 U/ml at pH 10.0; enzyme activity is 0.31 U/ml with ammonium sulfate as nitrogen source; enzyme activity is 0.32 U/ml with sodium glutamate as nitrogen source; enzyme activity is 0.37 U/ml at pH 5.5; enzyme activity is 0.42 U/ml at pH 9.5; enzyme activity is 0.45 U/ml with citric acid as carbon source; enzyme activity is 0.46 U/ml with glucose as carbon source; enzyme activity is 0.46 U/ml with peptone as nitrogen source; enzyme activity is 0.47 U/ml at pH 6.0; enzyme activity is 0.47 U/ml with lactose as carbon source; enzyme activity is 0.49 U/ml with starch as carbon source; enzyme activity is 0.57 U/ml at pH 9.0; enzyme activity is 0.57 U/ml with soybean flour as nitrogen source; enzyme activity is 0.63 U/ml at pH 8.5; enzyme activity is 0.65 U/ml with beef extract as nitrogen source; enzyme activity is 0.67 U/ml with sucrose as carbon source; enzyme activity is 0.69 U/ml with yeast extract as nitrogen source; enzyme activity is 0.72 U/ml at pH 8.0; enzyme activity is 0.78 U/ml with maize milk as nitrogen source; enzyme activity is 0.98 U/ml at pH 6.5; enzyme activity is 1.00 U/ml at pH 7.5; enzyme activity is 1.25 U/ml at pH 7.0; when the strain is cultured at 30°C at pH 7.0 for 30-36 h with of 0.6% corn steep liquor as nitrogen source, the uricase activity peaks at 1.25 U/ml
additional information
-
rasburicase causes enzymatic degradation of uric acid within blood, plasma and serum samples at room temperature, the genetic absence of this molecule in humans and its proteic nature together with poor accuracy in purifi cation and a slow production process confer a high immunogenicity to the compound, leading to elevated rate of hypersensivity reactions; rasburicase does not interact with allopurinol, cytarabine, methylprednisolone, methotrexate, mercaptopurine, thioguanine, etoposide, daunorubicin, cyclophosphamide, or vincristine; rasburicase maintains the same mechanism of action as the non-recombinant form of urate oxidase, but simply shows a significantly lower reaction rate; repeated use of rasburicase increases risk of hypersensitivity reactions: skin rashes (1.4%), urticaria, bronchospasm (1%), dyspnea, hypoxemia, and anaphylactic shock (1%)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
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
8.5
8.9
9.2
9.5
9.2
-
the unmodified uricase has a pH optimum of slightly below pH 9.2 which is not altered by modification with NHS esters of monomethoxy-poly(ethylene glycol)-5000 or monomethoxy-poly(ethylene glycol)-350
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
-
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
-
pH 6.5: about 40% of maximal activity, pH 10.0: about 50% of maximal activity
7 - 11
-
pH 7: about 50% of activity maximum, pH 11: about 40% of activity maximum
8 - 10.2
-
pH 8.0: about 35% of activity maximum, pH 10.2: about 55% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
37
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
-
20°C: about 70% of activity maximum; 50°C: about 60% of activity maximum
20 - 70
-
free uricase shows at least 50% relative activity between 20 and 70°C
20 - 50
-
20°C: about 60% of activity maximum; 50°C: about 50% of activity maximum
20 - 55
-
20°C: about 80% of maximal activity, maximal activity at 30°C, 55°C: about 55% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
isoelectric focusing presents a trail of pI values between 6.55 and 7.6
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
wild-type and PEX5-defective CHO cell lines each stable producing the enzyme
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no uricase is detected in mycelium grown in minimal medium containing NH4Cl as sole nitrogen source. Uricase activity is increased 10fold to 40fold under derepression conditions and is induced by exogenous uric acid
additional information
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activity increases once the haustorium has differentiated after Uromyces phaseoli infection. A up-regulation of urate oxidase gene expression occurs at the post-transcriptional level rather than an overexpression of the urate oxidase gene. A general pathogenic effect and host urate oxidase, and purine pool depauperation
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no activity in liver of New World monkeys, low activity in liver of Old World monkeys
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no activity in liver of New World monkeys, low activity in liver of Old World monkeys
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is mainly localized in the membrane of PEX5-defective mutant cells
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the enzyme is mainly localized in the peroxisomal matrix of wild-type cells
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limited to large peroxisomes in uninfected cells of root nodules of Glycine max inoculated with Bradyrhizobium japonicum
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18000
-
x * 39700, isoform UI, x * 3050, isoform UII, x * 55300, isoform UIII, x * 18000, isoform UIV, SDS-PAGE
32000
33000
33270
-
determination of nucleotide sequence of cDNA and calculation of corresponding amino acid sequence
34000
36000
37000
39700
-
x * 39700, isoform UI, x * 3050, isoform UII, x * 55300, isoform UIII, x * 18000, isoform UIV, SDS-PAGE
55300
-
x * 39700, isoform UI, x * 3050, isoform UII, x * 55300, isoform UIII, x * 18000, isoform UIV, SDS-PAGE
100000
120000 - 122000
124000
125000
128000
137000
-
for the homotetramer, determined by neutron crystallographic analysis
36000
-
4 * 36000, SDS-PAGE and matrix-assisted laser-desorption ionization-time-of-flight mass spectrometry
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterotetramer
homotetramer
monomer
tetramer
?
-
x * 39700, isoform UI, x * 3050, isoform UII, x * 55300, isoform UIII, x * 18000, isoform UIV, SDS-PAGE
homotetramer
determined by X-ray diffraction measurements, the AgUOX-native structure is solved by molecular replacement using the program AmoRe, pairs of dimers are stacked face-to-face to form a tetramer
homotetramer
-
determined by X-ray crystallography, formed by crystallographic symmetry operations
homotetramer
-
determined by gel filtration, tunnel-shaped homotetramer, each of the 4 active sites in UOX is formed by residues from 2 subunits and located at the subunit-subunit interface
homotetramer
-
4 * 000, SDS-PAGE, homotetrameric uricase in water dissociates into inactive homodimers that can form active homotetramers again in solutions of high ionic strength
homotetramer
-
4 * 000, SDS-PAGE, homotetrameric uricase in water dissociates into inactive homodimers that can form active homotetramers again in solutions of high ionic strength
-
tetramer
-
4 * 33000, SDS-PAGE; 4 * 33858, calculation from nucleotide sequence
tetramer
-
4 * 33000, SDS-PAGE; 4 * 33858, calculation from nucleotide sequence
-
tetramer
-
4 * 36000, SDS-PAGE and matrix-assisted laser-desorption ionization-time-of-flight mass spectrometry
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallizations are performed using the hanging-drop vapour-diffusion method at 19.9°C, structures of crystals soaked with the substrate uric acid, the inhibitor 8-azaxanthin and allantoin are determined at 1.9-2.2 A resolution, 2 homotetramers comprise the asymmetric crystallographic unit, each subunit contains 2 T-fold domains of topology, which are usually found in purine- and pterin-binding enzymes, the uric acid substrate is bound tightly to the enzyme by interactions with Arg180, Leu222 and Gln223 from one subunit and with Thr67 and sp68 of the neighbouring subunit in the tetramer
crystallization of large proteins in the presence of polyethylene glycol
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crystals of about a few tens of micrometres in size, which is nucleated previously in crystallization batch containing 5% PEG 8000, 100 mM NaCl, 8 mg/ml uox-substrate complex and 100 mM Tris-HCl pH 8.5, are used as seeds and their size and quality are further improved using a temperature-control device, large crystals of Uox, co-crystallized with its substrates analogues 8-azaxanthine, 9-methyluric acid or the natural substrate in the presence of cyanide (0.5-2 mg/ml), and soaks with the natural substrate in the absence of cyanide, diffracting to high resolutions are obtained, in the presence of different inhibitors, the crystal form of Uox has a body-centred orthorhombic symmetry and one of the largest primitive unit-cell volumes (a: 80 A, b: 96 A, c: 106 A)
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enzyme in complex with substrate urate and inhibitor cyanide, X-ray diffraction structure determination and analysis
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ligand-free Uox crystallized with NH4Cl and 15% (w/v) PEG 8000, ligand-free Uox crystallized in water with 10% (w/v) PEG 8000, ligand-free Uox crystallized with NaCl and 15% (w/v) PEG 8000, ligand-free Uox crystallized with (NH4)2SO4 and 15% (w/v) PEG 8000, ligand-free Uox crystallized with NaCl and 8% PEG 8000, ligand-free Uox crystallized with KCl and 10% (w/v) PEG 8000, and Uox complexed with 8-azaxanthine and crystallized with NaCl and 10% (w/v) PEG 8000, in 50 mM Tris buffer pH 8.0
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quantum mechanical/molecular mechanical calculations based on PDB entry 4N9M. The oxidation consists of chemical transformation from 8-hydroxyxythine to an anionic radical via a proton transfer along with an electron transfer, proton transfer to the O2- anion (radical), diradical recombination to form a peroxo intermediate, and dissociation of H2O2 to generate the dehydrourate. Hydration is initiated by the nucleophilic attack of a water molecule on dehydrourate, along with a concerted proton transfer through residue Thr69 in the catalytic site. Hydration is the rate-determining step
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recombinant enzyme in complex with inhibitor 8-azaxanthine in presence of O2 or Cl-, batch technique at room temperature, 10-15 mg/ml protein with an excess of 0.5-2 mg/ml of 8-azaxanthin in 50 mM Tris/HCl, pH 8.5, in the presence of 5-8% w/v PEG 8000 and 0.05 M NaCl, 24-48 h, X-ray diffraction structure determination and analysis at 1.6-1.7 A resolution
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sitting-drop vapour-difusion method. Four different crystal forms of Uox are analyzed. In the presence of uracil and 5,6-diaminouracil crystals usually belong to the trigonal space group P3(1)21, the asymmetric unit of which contains one tetramer of Uox. Chemical oxidation of 5,6-diaminouracil within the protein may occur, leading to the canonical (I222) packing with one subunit per asymmetric unit. Coexistence of two crystal forms, P2(1) with two tetramers per asymmetric unit and I222, is found in the same crystallization drop containing another inhibitor, guanine. A fourth form, P2(1)2(1)2 with one tetramer per asymmetric unit, results in the presence of cymelarsan, an additive
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structure to 1.4 A resolution, showing a homotetramer containing two homodimers. In each homodimer H-bonds are found between residues E311 and Y249 and between Y319 and D257. Electrostatic interaction networks surround D307 plus R310 and intersubunit R3, K312 plus D257, E318 plus K242, and L322 plus R258
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homology modeling of monomeric enzyme. The highly conserved residue Gly290 could interact with Asn262 and His264. Residue substitutions near Gly290 may affect its spatial orientation and result in changes in catalysis.Gly290 is likely to participate in the structure of the active site and to be involved in oxygen-binding
to 1.93 A resolution. Space group P212121 with unit cell parameters a 69.16 A, b 139.31 A, c 256.33 A, and alpha =beta =gamma =90°
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
UOX is deactivated at different protein concentrations at 45°C in 20 mM phosphate containing 0.15 M NaCl, 0.01 mg/ml UOX is deactivated much faster than its counterparts at concentrations of 0.1 and 1.0 mg/ml
700631