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5-hydroxyisourate + O2
(S)-allantoin + H2O2 + CO2
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
uric acid + O2 + H2O
5-hydroxyisourate + H2O2
-
purine degradation
-
-
?
additional information
?
-
urate + O2 + H2O

5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
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
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
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
-
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
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
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
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
JX083378
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
JX083378
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
yeast-like fungi
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
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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1,3,7-Trimethylxanthine
-
i.e. caffeine, slight
2,9-Dimethyl-1,10-phenanthroline
3,7-Dimethylxanthine
-
i.e. theobromine, slight
5,5'-dithiobis(2-nitrobenzoate)
-
-
beta-mercaptoethanol
-
about 60% residual activity after 1 h incubation with 0.5 mM beta-mercaptoethanol at pH 8.5 and 25ưC
Biguanidine salts
-
inactivation is pH-dependent: slightly inhibitory below pH 10, rapid inactivation at high pH
Ca2+
JX083378
1 mM, 20% residual activity
D-sorbitol
-
about 70% residual activity after 1 h incubation with 0.5 mM D-sorbitol at pH 8.5 and 25ưC
Dicyandiamide
-
inactivation is pH-dependent: small below pH 10, rapid increase at high pH
diethyldithiocarbamic acid
-
-
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
inosine 5'-monophosphate
-
-
Li+
-
18.5% inhibition at 1 mM
phosphate
-
no inactivation by phosphate, in presence of borate or dithiothreitol
Salicylhydroxamic acid
-
-
sodium deoxycholate
-
about 90% residual activity after 1 h incubation with 0.5 mM sodium deoxycholate at pH 8.5 and 25ưC
Tween-80
-
0.5% w/v, 61% residual activity
ZnCl2
-
1 mM, 91% inhibition
2,2'-dipyridyl

-
weak
2,9-Dimethyl-1,10-phenanthroline

-
neo-cuproin
2,9-Dimethyl-1,10-phenanthroline
-
0.1 mM, 64% residual activity
5-Azaorotate

-
-
8-Azaxanthine

substrate analogue
8-Azaxanthine
-
potent inhibitor
8-Azaxanthine
competitive inhibitor, binding structure, overview
8-Azaxanthine
-
substrate analogue binds in the active site of the enzyme
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
9-methyluric acid

-
substrate analogue
9-methyluric acid
-
competitive versus urate
adenine

-
weak
adenine
negligible inhibition at 0.5 mM at pH 9.2
Ag+

-
-
Ag+
-
95% inhibition at 1 mM
allantoin

-
weak
CN-

-
-
CN-
the presence of residue Phe159 enhances the interaction energy of the anion with the urate pi system
Co2+

-
-
Cu2+

-
enzyme contains copper, inhibited by excessive addition of Cu2+, 98% inhibition by 1 mM CuCl2, 97% inhibition by 1 mM CuSO4
Cu2+
2 mM, complete inactivation
Cu2+
-
1 mM, 15% residual activity
Cu2+
strong inhibition at 0.2 mM, negligible inhibition at 0.005 mM
Cu2+
-
1 mM, about 50% inhibition
EDTA

-
20 mM, 1% residual activity
EDTA
JX083378
1 mM, complete loss of activity
Fe2+

-
-
Fe2+
strong inhibition at 0.2 mM, negligible inhibition at 0.005 mM
Fe2+
JX083378
1 mM, 70% residual activity
Fe3+

-
-
Fe3+
-
1 mM, 36% residual activity
glutamine

-
weak
Hg2+

-
-
Hg2+
-
1 mM, 2% residual activity
Hg2+
-
98% inhibition at 1 mM
hypoxanthine

-
-
hypoxanthine
negligible inhibition at 0.5 mM at pH 9.2
Mg2+

-
1 mM: not
Mg2+
-
1 mM, about 30% inhibition; 1 mM, about 50% inhibition
Mn2+

-
-
N-ethylmaleimide

-
-
neocuproin

-
-
NH4+

-
weak
Ni2+

-
-
Ni2+
-
1 mM, about 50% inhibition; 1 mM, about 70% inhibition
Ni2+
JX083378
1 mM, 60% residual activity
o-phenanthroline

-
weak
o-phenanthroline
-
2 mM, 4% residual activity
o-phenanthroline
-
99% inhibition at 2 mM
oxonate

-
-
oxonate
-
0.025 mM 90% inhibition
oxonate
-
0.025 mM 90% inhibition
oxonate
-
0.025 mM 90% inhibition
p-chloromercuribenzoate

-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
slight effect
pyrazinoate

-
channel activity completely disappears
pyrazinoate
-
channel activity completely disappears
SDS

-
purified uricase retains 82% of its original activity after incubation with 0.5% SDS for 6 h
SDS
-
49% inhibition at 0.5% w/v
Trichloropurine

-
-
Urate

-
above 0.125 mM
Urate
-
substrate inhibition: above 0.120 mM
Urea

-
-
xanthine

-
-
xanthine
-
competitive versus urate, noncompetitive versus O2
xanthine
-
0.05 mM 60-75% inhibition
xanthine
-
0.05 mM 60-75% inhibition
xanthine
-
0.05 mM 60-75% inhibition
Zn2+

-
1 mM, 22% residual activity
Zn2+
-
1 mM, about 35% inhibition; 1 mM, about 50% inhibition
Zn2+
JX083378
1 mM, 60% residual activity
additional information

reduced levels of mRNA levels of urate oxidase after knock down of urate oxidase gene expression
-
additional information
-
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
-
additional information
-
no inhibition by Cu2+, Fe3+, or Zn2+
-
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0.08
H2O2
25ưC, pH not specified in the publication
additional information
Urate
0.029
O2

-
-
0.0000135
Urate

-
mutant enzyme K9M, apparent Km in air-saturated buffer
0.00002
Urate
-
mutant enzyme F179A, apparent Km in air-saturated buffer
0.00156
Urate
-
mutant enzyme F179Y, apparent Km in air-saturated buffer
0.0034
Urate
-
wild type enzyme, apparent Km in air-saturated buffer
0.0047
Urate
GST-uricase fusion protein
0.0053
Urate
GST-free recombinant uricase
0.0062
Urate
-
pH 8.2, 37ưC
0.0064
Urate
mutant A296V, pH 8.6, 25ưC
0.0064
Urate
mutant R291K/A296V/A301S/K303R, pH 8.6, 25ưC
0.0065
Urate
mutant H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25ưC
0.0085
Urate
wild-type, pH 8.6, 25ưC
0.017
Urate
mutant A89T/G91A7V92M/H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25ưC
0.028
Urate
-
pH 8.0, mutant enzyme D70A
0.0337
Urate
pH 8.0, 37ưC
0.034
Urate
-
pH 8.0, wild-type enzyme
0.051
Urate
-
pH 8.0, mutant enzyme K9M
0.075
Urate
-
pH 7.0, 37ưC
0.079
Urate
-
pH 8.0, 40ưC
0.17
Urate
-
pH 8.0, mutant enzyme T69A
0.27
Urate
unmodified enzyme, 50 mM borate buffer, 25ưC, pH 9.2
0.27
Urate
mutant L1711I/Y182F/Y187F/A193S, pH 9.2, 27ưC
0.28
Urate
JX083378
pH 8.5, 25ưC
0.31
Urate
-
pH 8.5, 30ưC
0.31
Urate
wild-type, pH 9.2, 27ưC
0.547
Urate
-
pH 8.0, mutant enzyme T69A/K9M
0.8
Urate
unmodified enzyme, 50 mM borate buffer, 40ưC, pH 9.2
1.05
Urate
-
pH 8.0, mutant enzyme T69V
0.00588
uric acid

-
-
0.014
uric acid
-
enzyme without histidine tag
0.015
uric acid
-
enzyme with histidine tag
0.042
uric acid
-
poly(N-acryloylmorpholine)-OSu-uricase
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), 37ưC, 20 min
additional information
Urate

-
Km value for degradation of urate crystals is 7 microg/ml, 30ưC, pH not specified in the publication
additional information
Urate
-
Km value for degradation of urate crystals is 9 microg/ml, 30ưC, pH not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.067
-
wild-type, pH 8.9, 25ưC
10.5
-
in the cell lysate
13.3
-
hypocotyls, 4 d old
15
pH not specified in the publication, temperature not specified in the publication
16.33
-
natural uricase, in 0.1 M borate, pH 8.4
18
-
crude extract, pH 8.0, 37ưC
2.49
-
urate oxidase including p-azido-L-phenylalanine instead of Phe at position 281, in 0.1 M borate, pH 8.4
2.67
-
recombinant strain overexpressing the enzyme, pH 8.9, 25ưC
2.99
mutant A89T/G91A7V92M/H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25ưC
21.5
-
after DEAE Sepharose FF chromatography
25.7
-
after Phenyl-Sepharose FF chromatography
27
-
after HiLoad 26/60 Superdex 75 gel filtration
3.74
-
cotyledons, 4 d old
38.4
recombinant protein, pH 8.0, 37ưC
39
-
after 2.1fold purification, pH 8.0, 37ưC
4.22
wild-type, pH 8.6, 25ưC
4.91
mutant H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25ưC
5.68
mutant A296V, pH 8.6, 25ưC
5.94
mutant R291K/A296V/A301S/K303R, pH 8.6, 25ưC
6.8
wild-type, pH 9.2, 27ưC
8.26
-
urate oxidase including p-azido-L-phenylalanine instead of Phe at position 170, in 0.1 M borate, pH 8.4
8.3
mutant L1711I/Y182F/Y187F/A193S, pH 9.2, 27ưC
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
additional information
-
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
additional information
-
in high density fermentation in YPG medium at 37ưC, 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
additional information
-
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
additional information
-
enzyme activity is 0.06 U/ml at pH 4.0
additional information
DQ887577
enzyme activity is 0.09 U/ml at pH 4.5
additional information
-
enzyme activity is 0.09 U/ml at pH 4.5
additional information
DQ887577
enzyme activity is 0.11 U/ml at pH 5.0
additional information
-
enzyme activity is 0.11 U/ml at pH 5.0
additional information
DQ887577
enzyme activity is 0.21 U/ml with potassium nitrate as nitrogen source
additional information
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enzyme activity is 0.21 U/ml with potassium nitrate as nitrogen source
additional information
DQ887577
enzyme activity is 0.22 U/ml at pH 10.0
additional information
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enzyme activity is 0.22 U/ml at pH 10.0
additional information
DQ887577
enzyme activity is 0.31 U/ml with ammonium sulfate as nitrogen source
additional information
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enzyme activity is 0.31 U/ml with ammonium sulfate as nitrogen source
additional information
DQ887577
enzyme activity is 0.32 U/ml with sodium glutamate as nitrogen source
additional information
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enzyme activity is 0.32 U/ml with sodium glutamate as nitrogen source
additional information
DQ887577
enzyme activity is 0.37 U/ml at pH 5.5
additional information
-
enzyme activity is 0.37 U/ml at pH 5.5
additional information
DQ887577
enzyme activity is 0.42 U/ml at pH 9.5
additional information
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enzyme activity is 0.42 U/ml at pH 9.5
additional information
DQ887577
enzyme activity is 0.45 U/ml with citric acid as carbon source
additional information
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enzyme activity is 0.45 U/ml with citric acid as carbon source
additional information
DQ887577
enzyme activity is 0.46 U/ml with glucose as carbon source
additional information
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enzyme activity is 0.46 U/ml with glucose as carbon source
additional information
DQ887577
enzyme activity is 0.46 U/ml with peptone as nitrogen source
additional information
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enzyme activity is 0.46 U/ml with peptone as nitrogen source
additional information
DQ887577
enzyme activity is 0.47 U/ml at pH 6.0
additional information
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enzyme activity is 0.47 U/ml at pH 6.0
additional information
DQ887577
enzyme activity is 0.47 U/ml with lactose as carbon source
additional information
-
enzyme activity is 0.47 U/ml with lactose as carbon source
additional information
DQ887577
enzyme activity is 0.49 U/ml with starch as carbon source
additional information
-
enzyme activity is 0.49 U/ml with starch as carbon source
additional information
DQ887577
enzyme activity is 0.57 U/ml at pH 9.0
additional information
-
enzyme activity is 0.57 U/ml at pH 9.0
additional information
DQ887577
enzyme activity is 0.57 U/ml with soybean flour as nitrogen source
additional information
-
enzyme activity is 0.57 U/ml with soybean flour as nitrogen source
additional information
DQ887577
enzyme activity is 0.63 U/ml at pH 8.5
additional information
-
enzyme activity is 0.63 U/ml at pH 8.5
additional information
DQ887577
enzyme activity is 0.65 U/ml with beef extract as nitrogen source
additional information
-
enzyme activity is 0.65 U/ml with beef extract as nitrogen source
additional information
DQ887577
enzyme activity is 0.67 U/ml with sucrose as carbon source
additional information
-
enzyme activity is 0.67 U/ml with sucrose as carbon source
additional information
DQ887577
enzyme activity is 0.69 U/ml with yeast extract as nitrogen source
additional information
-
enzyme activity is 0.69 U/ml with yeast extract as nitrogen source
additional information
DQ887577
enzyme activity is 0.72 U/ml at pH 8.0
additional information
-
enzyme activity is 0.72 U/ml at pH 8.0
additional information
DQ887577
enzyme activity is 0.78 U/ml with maize milk as nitrogen source
additional information
-
enzyme activity is 0.78 U/ml with maize milk as nitrogen source
additional information
DQ887577
enzyme activity is 0.98 U/ml at pH 6.5
additional information
-
enzyme activity is 0.98 U/ml at pH 6.5
additional information
DQ887577
enzyme activity is 1.00 U/ml at pH 7.5
additional information
-
enzyme activity is 1.00 U/ml at pH 7.5
additional information
DQ887577
enzyme activity is 1.25 U/ml at pH 7.0
additional information
-
enzyme activity is 1.25 U/ml at pH 7.0
additional information
DQ887577
when the strain is cultured at 30ưC 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
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when the strain is cultured at 30ưC 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
-
-
additional information
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7.1 U/ml predicted optimum activity
additional information
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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
additional information
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rasburicase does not interact with allopurinol, cytarabine, methylprednisolone, methotrexate, mercaptopurine, thioguanine, etoposide, daunorubicin, cyclophosphamide, or vincristine
additional information
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rasburicase maintains the same mechanism of action as the non-recombinant form of urate oxidase, but simply shows a significantly lower reaction rate
additional information
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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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