Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5-hydroxyisourate + O2
(S)-allantoin + H2O2 + CO2
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
urate + O2 + H2O
allantoin + 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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
yeast-like fungi
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
5-hydroxyisourate + H2O2
-
-
-
-
?
urate + O2 + H2O
allantoin + H2O2
-
-
-
-
?
urate + O2 + H2O
allantoin + H2O2
-
-
-
?
urate + O2 + H2O
allantoin + H2O2
nanozyme
-
-
-
-
?
urate + O2 + H2O
allantoin + H2O2
-
-
-
-
?
urate + O2 + H2O
allantoin + 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-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CaCl2
-
enhances activity
K+
slight activation at 10 mM
NH4Cl
slight activation at 10 mM
Zn2+
-
105% activity at 1 mM
Ca2+
-
111% activity at 1 mM
Ca2+
strong activation at 10 mM
Ca2+
-
enzyme activity is strongly enhanced in presence of 1 mM Ca2+
copper
-
contains 0.2 mol copper per mol enzyme protein
copper
-
negligible amount of copper
copper
-
neither copper nor iron detected
copper
-
copper : uricase ratio is 1 : 7
copper
-
enzyme contains 0.15 mol of copper
copper
-
copper : uricase ratio is 1 : 1
Cu2+
-
enzyme contains copper, inhibited by excessive addition of Cu2+
Cu2+
-
enzyme activity is strongly enhanced in presence of 1 mM Cu2+
Cu2+
JX083378
1 mM, 140% of initial activity
Fe2+
-
109% activity at 1 mM
Fe2+
-
enzyme activity is strongly enhanced in presence of 1 mM Fe2+
Iron
-
slight stimulation
Iron
-
contains 0.1 mol iron per mol enzyme
Iron
-
neither copper nor iron detected
Iron
-
contains nearly one mol per mol of enzyme
Iron
-
iron : uricase ratio is 1 : 50
Iron
-
enzyme contains less than 0.05 mol of iron
Mg2+
-
123% activity at 1 mM
Mg2+
-
1 mM, 138% of initial activity
Mg2+
strong activation at 10 mM
Mn2+
-
108% activity at 1 mM
Mn2+
2 mM, 170% of initial activity
Na+
slight activation at 10 mM
Na+
-
enzyme activity is strongly enhanced in presence of 1 mM Na+
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
additional information
-
Mn2+, Mg2+, and K+ do not have much effect on the enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,3,7-Trimethylxanthine
-
i.e. caffeine, slight
2,9-Dimethyl-1,10-phenanthroline
2-mercaptoethanol
-
62.98% residual activity at 20% (v/v)
3,7-Dimethylxanthine
-
i.e. theobromine, slight
5,5'-dithiobis(2-nitrobenzoate)
-
-
acetaldehyde
-
complete inhibition at 20% (v/v)
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
diethyldithiocarbamic acid
-
-
dithiothreitol
-
94.93% residual activity at 20% (v/v)
ethanol
-
71.97% residual activity at 20% (v/v)
Guanidinium salts
-
inactivation is pH-dependent: slightly inhibitory below pH 10, rapid inactivation at high pH
inosine 5'-monophosphate
-
-
K+
-
88.69% residual activity at 1 mM
Li+
-
18.5% inhibition at 1 mM
methanol
-
84.55% residual activity at 20% (v/v)
PEG4000
-
68.04% residual activity at 20% (v/v)
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 25°C
Tween 80
-
95.26% residual activity at 20% (v/v)
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+
-
64% residual activity at 1 mM
Ag+
-
95% inhibition at 1 mM
allantoin
-
weak
Ba2+
-
-
Ba2+
-
1 mM Ba2+ partially truncates enzyme activity to near 50%
Ca2+
-
95.32% residual activity at 1 mM
Ca2+
JX083378
1 mM, 20% residual activity
CN-
-
-
CN-
the presence of residue Phe159 enhances the interaction energy of the anion with the urate pi system
Co2+
-
77% residual activity at 1 mM
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+
-
19.82% residual activity at 1 mM
Cu2+
strong inhibition at 0.2 mM, negligible inhibition at 0.005 mM
Cu2+
-
1 mM, about 50% inhibition
EDTA
-
59% residual activity at 1 mM
EDTA
-
20 mM, 1% residual activity
EDTA
-
enzyme activity is completely inhibited in presence of 5 mM EDTA
EDTA
JX083378
1 mM, complete loss of activity
Fe2+
-
6.07% residual activity at 1 mM
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
Fe3+
-
complete inhibition at 1 mM
glutamine
-
weak
H2O2
-
purified uricase retains 72% of its original activity after incubation with 0.5% H2O2 for 6 h
H2O2
-
68.68% residual activity at 0.02 mM
Hg2+
-
66% residual activity at 1 mM
Hg2+
-
1 mM, 2% residual activity
Hg2+
-
98% inhibition at 1 mM
Hg2+
-
1 mM Hg2+ partially truncates enzyme activity to less than 50%
hypoxanthine
-
-
hypoxanthine
negligible inhibition at 0.5 mM at pH 9.2
KCN
-
enzyme activity is completely inhibited in presence of 5 mM KCN
Mg2+
-
87.99% residual activity at 1 mM
Mg2+
-
1 mM, about 30% inhibition; 1 mM, about 50% inhibition
Mn2+
-
-
N-ethylmaleimide
-
-
Na+
-
69% residual activity at 1 mM
Na+
-
90.92% residual activity at 1 mM
neocuproin
-
-
NH4+
-
weak
Ni2+
-
84.77% residual activity at 1 mM
Ni2+
-
1 mM Ni2+ partially truncates enzyme activity to near 50%
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
competitive inhibitor
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+
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.08
H2O2
25°C, 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, 37°C
0.0064
Urate
mutant A296V, pH 8.6, 25°C
0.0064
Urate
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
0.0085
Urate
wild-type, pH 8.6, 25°C
0.01528
Urate
mutant enzyme S136C, at pH 8.0 and 30°C
0.017
Urate
mutant A89T/G91A7V92M/H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25°C
0.01843
Urate
wild type enzyme, at pH 8.0 and 30°C
0.028
Urate
-
pH 8.0, mutant enzyme D70A
0.03046
Urate
mutant enzyme N289C, at pH 8.0 and 30°C
0.0337
Urate
pH 8.0, 37°C
0.034
Urate
-
pH 8.0, wild-type enzyme
0.03539
Urate
mutant enzyme I27C/N289C, at pH 8.0 and 30°C
0.03919
Urate
mutant enzyme A132C/A225C, at pH 8.0 and 30°C
0.051
Urate
-
pH 8.0, mutant enzyme K9M
0.0676
Urate
-
at pH 9.0 and 42°C
0.075
Urate
-
pH 7.0, 37°C
0.079
Urate
-
pH 8.0, 40°C
0.0927
Urate
nanozyme
-
nanozyme MVSM, at pH 6.0 and 25°C
0.1045
Urate
mutant enzyme K12C/E286C, at pH 7.4, temperature not specified in the publication
0.1268
Urate
mutant enzyme S296C/C302S, at pH 7.4, temperature not specified in the publication
0.1403
Urate
wild type enzyme, at pH 7.4, temperature not specified in the publication
0.17
Urate
-
pH 8.0, mutant enzyme T69A
0.18965
Urate
mutant enzyme D288C, at pH 8.0 and 30°C
0.23
Urate
mutant enzyme V144A, at pH 9.2 and 25°C
0.24
Urate
mutant enzyme V144A, at pH 7.4 and 25°C
0.247
Urate
wild type enzyme, at pH 7.4 and 25°C
0.267
Urate
wild type enzyme, at pH 9.2 and 25°C
0.27
Urate
unmodified enzyme, 50 mM borate buffer, 25°C, pH 9.2
0.27
Urate
mutant L1711I/Y182F/Y187F/A193S, pH 9.2, 27°C
0.28
Urate
JX083378
pH 8.5, 25°C
0.28
Urate
mutant enzyme Y319R, at pH 9.2 and 25°C
0.29
Urate
mutant enzyme Y319R, at pH 7.4 and 25°C
0.293
Urate
mutant enzyme V144A/Y319R, at pH 9.2 and 25°C
0.3
Urate
mutant enzyme V144A/Y319R, at pH 7.4 and 25°C
0.31
Urate
-
pH 8.5, 30°C
0.31
Urate
wild-type, pH 9.2, 27°C
0.5
Urate
-
at pH 9.0 and 30°C
0.547
Urate
-
pH 8.0, mutant enzyme T69A/K9M
0.8
Urate
unmodified enzyme, 50 mM borate buffer, 40°C, 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), 37°C, 20 min
additional information
Urate
-
Km value for degradation of urate crystals is 7 microg/ml, 30°C, pH not specified in the publication
additional information
Urate
-
Km value for degradation of urate crystals is 9 microg/ml, 30°C, pH not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.067
-
wild-type, pH 8.9, 25°C
10.38
mutant enzyme N289C, at pH 8.0 and 30°C
10.45
wild type enzyme, at pH 8.0 and 30°C
10.5
-
in the cell lysate
11.3
mutant enzyme V144A/Y319R, at pH 9.2 and 25°C
11.4
mutant enzyme V144A, at pH 9.2 and 25°C
13.3
-
hypocotyls, 4 d old
15
pH not specified in the publication, temperature not specified in the publication
15.38
mutant enzyme A132C/A225C, at pH 8.0 and 30°C
16.33
-
natural uricase, in 0.1 M borate, pH 8.4
18
-
crude extract, pH 8.0, 37°C
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, 25°C
2.99
mutant A89T/G91A7V92M/H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25°C
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, 37°C
39
-
after 2.1fold purification, pH 8.0, 37°C
4.22
wild-type, pH 8.6, 25°C
4.91
mutant H245L/E252A/M253I/R291K/A296V/A301S/K303R, pH 8.6, 25°C
5.36
-
soluble cell lysate, at pH 9.0 and 42°C
5.68
mutant A296V, pH 8.6, 25°C
5.94
mutant R291K/A296V/A301S/K303R, pH 8.6, 25°C
50.54
-
after 9.43fold purification, at pH 9.0 and 42°C
6.8
wild-type, pH 9.2, 27°C
7.7
-
crude extract, at pH 7.5 and 30°C
7.88
mutant enzyme S136C, at pH 8.0 and 30°C
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, 27°C
87
-
after 11.3fold purification, at pH 7.5 and 30°C
9
wild type enzyme, at pH 9.2 and 25°C
9.2
mutant enzyme Y319R, at pH 9.2 and 25°C
9.38
mutant enzyme D288C, at pH 8.0 and 30°C
9.75
mutant enzyme I27C/N289C, at pH 8.0 and 30°C
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 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
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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 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
-
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
-
-
additional information
-
7.1 U/ml predicted optimum activity
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
additional information
-
rasburicase does not interact with allopurinol, cytarabine, methylprednisolone, methotrexate, mercaptopurine, thioguanine, etoposide, daunorubicin, cyclophosphamide, or vincristine
additional information
-
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
-
repeated use of rasburicase increases risk of hypersensitivity reactions: skin rashes (1.4%), urticaria, bronchospasm (1%), dyspnea, hypoxemia, and anaphylactic shock (1%)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
102000
-
polyacrylamide disc electrophoresis
114000 - 128000
-
PAGE, gel filtration
115000 - 123000
-
PAGE, gel filtration
120000 - 140000
-
PAGE, gel filtration
136300 - 141600
-
ultracentrifugation
137000
-
for the homotetramer, determined by neutron crystallographic analysis
144000
native enzyme, gel filtration
145000 - 150000
-
gel filtration
151000
-
Sephadex G-200 gel filtration
18000
-
x * 39700, isoform UI, x * 3050, isoform UII, x * 55300, isoform UIII, x * 18000, isoform UIV, SDS-PAGE
30000
-
alpha4, 4 * 30000, SDS-PAGE
32000 - 35000
-
SDS-PAGE, gel filtration
32880
yeast-like fungi
-
deduced from nucleotide sequence of cDNA
33270
-
determination of nucleotide sequence of cDNA and calculation of corresponding amino acid sequence
33750
-
4 * 33750, X-ray crystallography
33858
-
4 * 33858, calculation from nucleotide sequence
34160
x * 34160, MALDI-TOF
35000
-
alpha2beta2, 2 * 35000 + 2 * 37000, SDS-PAGE
35050
-
deduced from nucleotide sequence of cDNA
35052
-
alpha4, 4 * 35052, calculated from deduced amino acid sequence
35060
-
MALDI-TOF mass spectrometry
35780
MALDI-TOF mass spectrometry
35790
calculated from amino acid sequence
39000
-
alpha2beta2, 2 * 36000 + 2 * 39000, SDS-PAGE
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
58680
-
MALDI-TOF mass spectrometry
58900
-
calculated from amino acid sequence
60000
-
about 60000 Da, SDS-PAGE
62000
x * 62000, rasburicase, SDS-PAGE
70000 - 76000
-
gel filtration
98000
-
x * 98000, uricase-MBP fusion protein
100000
-
gel filtration
120000
gel filtration
120000
-
gel filtration, equilibrium sedimentation
120000 - 122000
-
-
120000 - 122000
-
PAGE, gel filtration
124000
-
PAGE
125000
-
PAGE
125000
-
short-column meniscus depletion sedimentation equilibrium
128000
-
-
135000
-
-
32000
-
alpha4, 4 * 32000, SDS-PAGE
32000
-
alpha3, 3 * 32000, SDS-PAGE
33000
-
x * 33000, SDS-PAGE
33000
-
4 * 33000, SDS-PAGE
33000
-
alpha4, 4 * 33000, SDS-PAGE
34000
-
SDS-PAGE
34000
-
recombinant uricase determined by SDS-PAGE
34000
-
x * 34000, SDS-PAGE
36000
-
4 * 36000, SDS-PAGE
36000
-
alpha2beta2, 2 * 36000 + 2 * 39000, SDS-PAGE
36000
-
4 * 36000, SDS-PAGE and matrix-assisted laser-desorption ionization-time-of-flight mass spectrometry
37000
-
alpha6, 6 * 37000, SDS-PAGE
37000
-
alpha2beta2, 2 * 35000 + 2 * 37000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hexamer
-
alpha6, 6 * 37000, SDS-PAGE
trimer
-
alpha3, 3 * 32000, SDS-PAGE
?
-
x * 35000, SDS-PAGE
?
x * 62000, rasburicase, SDS-PAGE
?
-
x * 39700, isoform UI, x * 3050, isoform UII, x * 55300, isoform UIII, x * 18000, isoform UIV, SDS-PAGE
?
-
x * 34400, calculated from amino acid sequence
?
-
x * 35000, SDS-PAGE
-
?
-
x * 34400, calculated from amino acid sequence
-
?
-
x * 34500, SDS-PAGE
-
?
-
x * 98000, uricase-MBP fusion protein
?
-
x * 33500, SDS-PAGE
-
?
-
x * 34000, SDS-PAGE
-
?
-
x * 42000, SDS-PAGE
-
?
-
x * 58000, SDS-PAGE
-
?
JX083378
x * 48000, SDS-PAGE
?
-
x * 48000, SDS-PAGE
-
dimer
-
at pH 8.8 the enzyme associates to form a dimer of about 68000
dimer
-
at pH 8.8 the enzyme associates to form a dimer of about 10000
heterotetramer
-
alpha2beta2, 2 * 36000 + 2 * 39000, SDS-PAGE
heterotetramer
-
alpha2beta2, 2 * 35000 + 2 * 37000, SDS-PAGE
homotetramer
-
-
homotetramer
4 * 34000, 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
-
4 * 34000, SDS-PAGE
homotetramer
x-ray crystallography
homotetramer
-
4 * 33750, X-ray crystallography
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
-
determined by X-ray crystallography, formed by crystallographic symmetry operations
homotetramer
4 * 36400, calculated from amino acid sequence
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 *35 000, SDS-PAGE
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
-
monomer
-
1 * 70000-76000, SDS-PAGE
monomer
-
native enzyme at pH 7.5 is a monomer with MW 32000-35000
monomer
-
native enzyme at pH 7.5 is a monomer with MW 50000
tetramer
-
4 * 33000, SDS-PAGE
tetramer
-
4 * 33858, calculation from nucleotide sequence
tetramer
-
4 * 33000, SDS-PAGE
-
tetramer
-
4 * 33858, calculation from nucleotide sequence
-
tetramer
-
4 * 36000, SDS-PAGE
tetramer
-
alpha4, 4 * 32000-34000, SDS-PAGE
tetramer
-
alpha4, 4 * 30000, SDS-PAGE
tetramer
-
alpha4, 4 * 35052, calculated from deduced amino acid sequence
tetramer
crystallization data
tetramer
-
4 * 36000, SDS-PAGE and matrix-assisted laser-desorption ionization-time-of-flight mass spectrometry
tetramer
-
crystallization data
-
tetramer
-
alpha4, 4 * 33000, SDS-PAGE
tetramer
-
alpha4, 4 * 32000, SDS-PAGE
tetramer
-
alpha4, 4 * 32000-34000, SDS-PAGE
tetramer
-
alpha4, 4 * 32000-34000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
mutant enzyme K12C/E286C, sitting drop vapor diffusion method, using 12% (w/v) polyethylene glycol 3350 and 0.1 M sodium malonate (pH 5.0)
crystallization of large proteins in the presence of polyethylene glycol
-
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)
-
enzyme in complex with substrate urate and inhibitor cyanide, X-ray diffraction structure determination and analysis
hanging drop vapour diffusion method
-
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
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
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
sitting drop vapour diffusion method
sitting drop vapour diffusion method using buffered D2O
-
sitting-drop vapour-diffusion method at room temperature
-
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
-
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°
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
K12C/E286C
the mutations introduce disulfide bonds between the subunits and markedly increase the melting temperature (from 61 to 75°C) of the enzyme compared with wild type
S296C/C302S
the mutations introduce disulfide bonds between the subunits and markedly increase the melting temperature (from 61 to 70°C) of the enzyme compared with wild type
D79A
-
the KM-value for urate is 82% of the wild-type value
F179A
-
decreases Vmax by 2 orders of magnitude
F179Y
-
mutation decreases Vmax by 2-fold
T69A
-
mutant enzyme has a maximal velocity of 3% of the wild-type value. Ionization at pH 6.4 that is observed with the wild-type enzyme is absent in the mutant. The KM-value for urate is 5fold higher than that of the wild-type enzyme
T69A/K9M
-
the KM-value for urate is 16.1fold higher than that of the wild-type enzyme
T69V
-
the KM-value for urate is 30.9fold higher than that of the wild-type enzyme
C249S
-
the substitution has no effect on enzymatic activity
C249S/DELTAL302
-
the combination of both mutations increases the enzymatic activity by 8%.Tthe specific activity of the mutant enzyme does not decrease after exposed to 37°C for 20 h
DELTAL302
-
the mutant has improved specific activity (6%) compared with wild type enzyme
A296V
about 50% ioncrease in catalytic efficiency
A89T/G91A7V92M/H245L/E252A/M253I/R291K/A296V/A301S/K303R
replacement with the corresponding residues of human enzyme. About 30% of wild-type catalytic efficiency
H245L/E252A/M253I/R291K/A296V/A301S/K303R
replacement with the corresponding residues of human enzyme. Catalytic efficiency is higher than in wild-type, but below the efficiency of mutant R291K/A296V/A301S/K303R
I115V/H119R/L120F/H245L/E252A/M253I/R291K/A296V/A301S/K303R
replacement with the corresponding residues of human enzyme, complete loss of activity
R119H
complete loss of activity
R291K/A296V/A301S/K303R
replacement with the corresponding residues of human enzyme. About 50% increase in catalytic efficiency
A132C/A225C
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D288C
the mutant shows 0.8fold reduced catalytic efficiency compared to the wild type enzyme
I27C/N289C
the mutant with 0.45fold reduced catalytic efficiency has similar specific activity and production yield to that of wild type but its thermostability is dramatically improved (120fold increase in half-life at 37°C)
N289C
the mutant 0.3fold reduced catalytic efficiency compared to the wild type enzyme
S136C
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D307R
mutant is an inactive homotetramer of lower solubility
E318R
mutant is similar to S314Stop
L171I/Y182F/Y187F/A193S
mutant displays higher activity and lower thermostability
L322D
mutant behaves similar to wild-type
L322R
mutant shows reduced activity and thermal stability at pH 7.4, enhanced stability at pH 9.2
R310E
displays the lowest stability at pH 7.4 or 9.2 among tested mutants and the strongest effects of pH values on thermal stability
S314Stop
mutant is a homotetramer of about 25% activity, 5 % half-life at pH 7.4 but 100 % half-life at pH 9.2
Y249F
thermal stability is reduced by 50fold at pH 7.4, by about 7fold at pH 9.2
Y319F
thermal stability is reduced by one magnitude at pH 7.4, but by 2fold at pH 9.2
Y319F/Y249F
mutant is an inactive homotetramer
Y319R
the mutant shows wild type activity and has much stronger thermostability than the wild type enzyme
D307R
-
mutant is an inactive homotetramer of lower solubility
-
R310E
-
displays the lowest stability at pH 7.4 or 9.2 among tested mutants and the strongest effects of pH values on thermal stability
-
Y249F
-
thermal stability is reduced by 50fold at pH 7.4, by about 7fold at pH 9.2
-
Y319F
-
thermal stability is reduced by one magnitude at pH 7.4, but by 2fold at pH 9.2
-
synthesis
-
expression of baboon uricase gene attached with Trx and hexahistidine tags in Escherichia coli Rosetta (DE3). The final yield of mature baboon uricase is 136.0 mg/l with enzyme activity of 17.93 U/mg
K9M
-
mutant enzyme has a maximal velocity of 0.4% of the wild-type value. Ionization at pH 6.4 that is observed with the wild-type enzyme is absent in the mutant. The KM-value for urate is 1.5fold higher than that of the wild-type enzyme
K9M
-
mutant is not able to generate the dianion of urate and is decreased in activity by over 200-fold
V144A
mutant displays higher activity and consistent thermostability
V144A
the mutant has about 25% increase of the activity against wild type
V144A/Y319R
the mutant has about 25% increase of the activity against wild type
V144A/Y319R
the mutant shows an approximately 4 week lagging phase before the exponential activity decrease, an apparent half-life of activity nearly 3folds of mutant V144A, but comparable activity
additional information
-
thioredoxin urate oxidase fusion protein
additional information
-
uricase covalently linked to monomethoxypoly(ethylene glycol) N-leucine-OSu, branched monomethoxypoly(ethylene glycol) N-leucine-OSu or poly(N-acryloylmorpholine)-OSu last longer in blood
additional information
the folding of the C-terminal residues is crucial for thermal stability. When positive charge on residue R3 is eliminated, the mutants become inactive dimers
additional information
-
the folding of the C-terminal residues is crucial for thermal stability. When positive charge on residue R3 is eliminated, the mutants become inactive dimers
-
additional information
the recombinantly expressed porcine enzyme, with a C-terminal sequence from baboon uricase, is applicated to patients with refractory gout, due to a mutation in the uricase gene, by intravenous injection in a PEG-bound form, pharmacokinetics and pharmacodynamics, safety, and efficacy of the treatment in a clinical trial, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10
-
45°C, 30 min, 30% loss of activity
394146
11
-
25°C, 18 h, about 60% loss of activity
701416
12
-
22°C, 30 min, 55% loss of activity
394156
6 - 10
-
the purified enzyme remains stable over a wide range of pH between 6.0-10.0 for 2 h
764830
6 - 11
-
35°C, 1 h, stable
394144
6.5 - 10.5
-
22°C, 30 min, immobilized enzyme, stable
394156
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
7 - 11
-
10 min, stable
394178
7 - 9.5
-
in case of uricase entrapped in lipid vesicles, the remaining activity keeps more than 90% during the pH of 7.0-9.5, and the maximum remaining activity is 98.04% at pH 8.0 when incubated at 40°C or 40 min. For the free uricase, the maximum remaining activity is 86.59% at pH 8.5 when incubated at 40°C or 40 min
712197
7.4
-
37°C, stable for 4 days, in presence of 30 microM oxonate stable for 22 days, with exponential decrease of activity thereafter
743752
8 - 11
-
4°C, 60 days, 35% loss of activity
394132
8 - 9
-
45°C, 30 min, stable
394146
9.2
-
37°C, stable for 12 days, in presence of 30 microM oxonate stable for 22 days, with exponential decrease of activity thereafter
743752
additional information
-
uricase activity in 50 h culture broth with pH values of 5.5 and 6.0 decreases more rapidly than that in cultures with pH values of 6.5 and 7.0, at pH 5.5, about 78% of initial uricase activity is lost within 25 h, under the same conditions, more than 85% of initial uricase activity remains in culture broth of pH 6.5 and 7.0, uricase activity in 66 h culture broth with pH 7.0 degrades much more rapidly than that in samples from 50 h culture, while for pH 6.5, the uricase is still stable, loss of uricase activity is caused by the degradation in acidic environment by proteases secreted by the host cells or releases from host cell lyses, low pH may cause instability of uricase
695795
6
-
45°C, 30 min, 40% loss of activity
394146
6
-
25°C, 18 h, about 60% loss of activity
701416
7 - 10
-
-
743753
7 - 10
-
purified enzyme, 25°C, 18 h, stable
701416
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0 - 70
-
the enzyme remains stable (more than 90% activity) for 30 min at 0-20°C. The activity drops to about 60, 50, 40, less than 30, and less than 20% after 30 min at 30, 40, 50, 60, and 70°C, respectively. At 40°C, the enzyme shows about 80% activity after 5 min, about 65% activity after 10 min, about 50% activity after 20-40 min, and about 30% activity after 50-60 min
10 - 80
-
about 80% relative activity at 10°C, about 85% relative activity at 20-30°C, about 90% relative activity at 37°C, about 40% relative activity at 40°C, about 30% relative activity at 50°C, about 20% relative activity at 60°C, about 10% relative activity at 70°C, and no activity at 80°C after 30 min incubation
100
-
35% relative activity at 100°C
18 - 20
-
2 days, 70% loss of activity
30 - 40
-
enzyme activity is diminished 60% when it is incubated at 30°C for 10 min. After 5 min at 40°C, there is a 25% decline in enzyme activity. The enzyme loses almost 60% of its original activity after 40 min at 40°C, whereas more than 50% of enzyme activity is preserved in the presence of lactose. Half-life at 40°C is almost 38 min and addition of raffinose does not change the half-life, whereas the presence of lactose has remarkable impact on enzyme half-life (46 min). Lactose notably enhances the melting temperature from 27 to 37°C
35 - 60
-
the enzyme is stable at 35ºC for 1 h and thermally inactivated at 60°C after 1 h. Rising temperature up to 40°C diminishes the enzyme activity to 83% and 80% after 45 and 60 min, respectively
52
-
uricase covalently linked to monomethoxypoly(ethylene glycol) N-leucine-OSu-uricase and branched monomethoxypoly(ethylene glycol) N-leucine-OSu-uricase 50% loss of activity
55
-
uricase entrapped in lipid vesicles at enzyme concentrations of 0.005 and 0.1 mg/ml shows no loss of activity after 5 h at 55°C. Uricase entrapped in lipid vesicles at enzyme concentrations of 0.01 mg/ml shows about 35% loss of activity after 5 h at 55°C. Uricase entrapped in lipid vesicles at enzyme concentrations of 0.005 mg/ml shows about 50% loss of activity after 5 h at 55°C. The free uricase at 0.005 mg/ml is rapidly deactivated to about 30% of the initial activity within an incubation time of 2 h, while more than 70% of the initial enzyme activity remains for the uricase at 0.1 mg/ml in the identical incubation time
60 - 61
-
native uricase and poly(N-acryloylmorpholine)-OSu-uricase 50% loss of activity
75
DQ887577
enzyme is thermostable, after heat treatment at 75°C for 45 min, the uricase retains about 100% of its initial activity
80
DQ887577
70% of initial activity remains after 45 min at 80°C
37
12 h, 50% residual activity, complete loss of activity after 54 h
37
-
the specific activity of wild type enzyme decreases to 90% after exposed to 37°C for 20h
40
-
below pH 9.5, 2 h, very slow loss of activity in absence or presence of Cu2+
40
-
10 min, stable below
40
-
30 min, stable below
40
-
the enzyme retains 79.75% of activity when incubated at 40°C for 90 h. After incubation of the enzyme for 15 min at 40 and 45°C, the retained activities are 95.55% and 74.55%, respectivelyThe retained activity decreases significantly when the incubation temperature is above 55°C
40
at 40°C in sodium borate buffer at pH 9.2, the unmodified uricase shows a thermo-inactivation half-life of about 40 h. Modification of the uricase by monomethoxy-poly(ethylene glycol)-350 slightly enhances its thermostability, and modification by monomethoxy-poly(ethylene glycol)-5000 increases its thermo-inactivation half-life to over 85 h at 40°C in sodium borate buffer at pH 9.2
45
-
after 5 min 50% of initial activity
45
the enzyme retains almost 100% activity after 2 min at 45°C, however, at higher temperatures the activity is rapidly lost
50
-
10 min, stable
50
-
pH 7.8, 10 min, stable below
60
-
10 min, stable
60
-
30 min, about 40% loss of activity
60
-
10 min, 55% loss of activity
60
-
pH 7.8, 10 min, 50% loss of activity
65
pH 9.2, half-life 8 min
65
-
30 min, the purified enzyme retains 98.9% of its original activity
70
-
stable up to
70
-
30 min, the purified enzyme retains 64% of its original activity
70
-
the enzyme retains 100% of activity at temperature up to 70°C for 45 min. Increasing the temperature beyond 80°C starts reducing the stability of enzyme to 15 min rather than 30 or 45 min time period. At 100°C the enzyme activity is considerably decreased at all-time points tested
additional information
thermal deactivation of recombinant UOX at neutral pH is associated with the loss of intersubunit hydrogen bonds, subunit is unstable at room temperature and unfolds rapidly at 100°C, tetramer has significantly higher stability than its subunit
additional information
-
thermal deactivation of recombinant UOX at neutral pH is associated with the loss of intersubunit hydrogen bonds, subunit is unstable at room temperature and unfolds rapidly at 100°C, tetramer has significantly higher stability than its subunit
additional information
-
thermal inactivation rises steeply as CuSO4 concentration rises from 0.025 to 0.175 mM and as the pH of the medium exceedes 9.5
additional information
-
the main phase of thermal inactivation follows an irreversible two-state mechanism, with loss of about 20% of the helical structure, loss of the majority of the tertiary structure, and partial exposure of tryptophan residues to solution being approximately concurrent with activity loss. This process results in the formation of aggregated molten globules. In addition, a rapid reversible denaturation phase occurs that is not completely coupled to the main phase. Enzyme inactivation is inhibited by the presence of glycerol and trimethylamine oxide. NaCl destabilizes the enzyme at elevated temperature
additional information
-
kinetic analysis of the thermoinactivation process. The equivalent number of the artificial weakest noncovalent interaction primarily determines the plateau period of stability. Kinetics rather than thermodynamics for homotetramer dissociation determines the thermoinactivation process
additional information
-
the molecular structure of enzyme has a reversible change at a temperature between 30°C and 60°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a dextrin-uricase conjugate is more resistant to simulated physiological conditions and trypsin
-
after modification with monomethoxy-poly(ethylene glycol)-5000, the recombinant intracellular uricase shows residual activity of about 65%
ammonium sulfate protects from inactivation at low pH
-
at 37°C, pH 7.4 half-life is about 3 weeks
at 37°C, pH 9.2 half-life is about 6 weeks
at the physiological pH, significant increase of enzyme activity is found for the uricase entrapped in the lipid vesicles (1.8times that of free uricase) at their respective optimum pH. Free uricase shows rapid decrease in its enzymatic activity with a half life of less than 20 min when incubated with trypsin. Uricase entrapped in the lipid vesicles gradually loses its activity but still 50% of the original activity remains after 60 min (remaining activity is 7.32% in case of free uricase)
-
conjugated uricases are more stable to trypsin digestion
-
Cu2+ inactivates at low temperature, uric acid prevents inactivation
-
dithiothreitol effect of treatment with dithiothreitol on extraction and purification
-
dithiothreitol prevents polymerization and stabilizes throughout purification
-
dithiothreitol stabilization
-
enzyme biosensor entrapped in poly(vinyl alcohol) N-methyl-4(4'-formylstyryl) pyridinium methosulfate acetal is stable for 48 h and maintains 90% activity until 5 days
-
Fe3+ partially protects against inactivation at low pH or at low ionic strength, stimulates reactivation
-
frozen enzyme retains complete activity
-
half-life of wild-type at pH 7.4, 37°C is 22 days, half-life of mutant L1711I/Y182F/Y187F/A193S is 0.3 days
lactose has protective effects on enzyme stability
-
little loss of activity by freeze-drying
-
lower stability in solutions of phosphate buffer than in borate buffer
-
proteolytic digestion by endopeptidases cause rapid loss of activity, exopeptidases have slight effect
Repeated freezing and thawing has no effect
-
stability of immobilized enzyme depends on the time of stirring during immobilization and on the quantity of enzyme used
-
stable against oxidants and SDS
-
the stability of the enzyme increases up to 4.9fold in the presence of 12% (w/v) of glycerol and sucrose. The effect of sorbitol on enzyme stability is negligible in the presence of glycerol and sucrose. In the presence of 20% (w/v) glycerol, sorbitol, and sucrose, the enzyme has the highest stability
-
unusually resistant to guanidinium chloride
-
unusually resistant to SDS
-
urate oxidase from female rat livers is more stable than enzyme from male rat livers
-
urea, 4 M, several h without loss of activity
-
uricase is reversibly inactivated in solutions of low ionic strength (like during dialysis against water). After incubation for 2 h in 100 mM sodium chloride in water at 4°C, the dialysis-inactivated uricase shows about 70% of the maximal specific activity. After incubation for 2 h in 100 mM Tris-HCl pH 8.0 plus 100 mM NaCl at 4°C, the dialysis-inactivated uricase shows about 90% of the maximal specific activity. After pre-incubation for 0.5 h in sodim borate plus 100 mM NACL at 25°C followed by the direct addition of urate to measure its activity, the dialysis-inactivated uricase shows about 80% of the maximal specific activity
borate stabilizes
-
EDTA stabilizes
-
proteolytic digestion by endopeptidases cause rapid loss of activity, exopeptidases have slight effect
-
proteolytic digestion by endopeptidases cause rapid loss of activity, exopeptidases have slight effect
-
proteolytic digestion by endopeptidases cause rapid loss of activity, exopeptidases have slight effect
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-12°C, 0.10 mol/l Tris/HCl buffer (pH 8.0), 8 months, less than 20% loss of activity, enzyme remains stable
-
-15°C, 100 mM borate buffer, pH 8.0, containing 100 mM or more ammonium sulfate
-
-20°C and 4°C, mutant enzyme I27C/N289C, 60 days, almost no loss of activity
-20°C, 72 h, no loss of activity
-20°C, purified enzyme, 72 h, 20% loss of activity
-
0-4°C, crystals in (NH4)2SO4 solution, 3 months, stable
-
37°C, mutant enzyme I27C/N289C, 15 days, almost no loss of activity
37°C, purified enzyme, 12 h and 48 h, 50% and 100% loss of activity
-
3°C, 0.15% sodium carbonate, several weeks, stable
-
4°C, 0.10 mol/l Tris/HCl buffer (pH 8.0), 10 weeks, less than 20% loss of activity
-
4°C, 100 mM Tris-HCl buffer, pH 9.5, 90% of activity after 5 days
yeast-like fungi
-
4°C, 20 mM phosphate buffer, pH 7.8, for at least 1 month
-
4°C, 7 days, 40% loss of activity
-
4°C, 72 h, no loss of activity
4°C, free uricase in borate buffer (pH 8.5), 28 days, 70% loss of activity
-
4°C, purified enzyme, 72 h, 20% loss of activity
-
4°C, uricase in lipid vesicles in borate buffer (pH 8.5), 28 days, no loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a plasmid containing the AgUOX gene is introduced into the expression host cell Escherichia coli DH1
complete cDNA and genomic DNA fragment coding for urate oxidase is isolated and characterized, heterologous expression in Escherichia coli
developing of a method for genetically incorporating p-azido-L-phenylalanine into target protein in Escherichia coli in a site-specific manner utilizing a tyrosyl suppressor tRNA/aminoacyl-tRNA synthetase system, substitution of p-azido-L-phenylalanine for F170 or F281 in urate oxidase, optimization of the system by adding a Shine-Dalgarno sequence and tandem suppressor tRNA in order to increase the expression levels of tyrosyl suppressor tRNA and aminoacyl-tRNA synthetase
-
expressed in Chinese hamster ovary cells
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3)
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli by combination of small ubiquitin-related modifier protein and maltose-binding protein to achieve the soluble expression of chimeric enzyme
-
expressed in Saccharomyces cerevisiae
expression in Escherichia coli
expression in Escherichia coli DH5alpha
yeast-like fungi
-
expression in Escherichia coli MC1061
-
expression in Escherichia coli RR1
-
expression in Escherichia coli, Escherichia coli harboring pUOD1 produces 20fold higher uricase than the original Arthrobacter strain, even without an inducer
-
expression in Saccharomyces cerevisiae
overexpression in Escherichia coli JM109
-
overexpression in Pichia angusta
-
uricase production by the recombinant Hansenula polymorpha strain MU200 harboring Candida utilis uricase gene under the control of methanol oxidase promoter using Saccharomyces cerevisiae alpha-factor signal peptide as the secretory sequence
-
using the recombinant DNA technique, enzyme is obtained from a genetically modified Saccharomyces cerevisiae strain that expresses urate oxidase cDNA, cloned from a strain of Aspergillus flavus
-
-
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Saccharomyces cerevisiae
-
expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Saccharomyces cerevisiae
-
expression in Saccharomyces cerevisiae
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
drug development
-
urate oxidase has the potential to be a therapeutic target for the treatment of gout
pharmacology
-
urate oxidase is a potential therapeutic protein in the prevention and treatment of tumor lysis syndrome and hyperuricemia. However, its severe immunogenicity limits its clinical application. Engineering site-specific modifications of keto groups in urate oxidase by using evolved Methanocaldococcus jannaschii aminoacyl-tRNA synthetase(s)/suppressor tRNA pairs reduces its antigenicity. The mutated uricase exhibits decreased antigenic properties, while its catalytic activities remain unchanged
analysis
a colorimetric 96-well microtiter plate assay for the determination of urate oxidase activity and its kinetic parameters based on hydrogen peroxide quantitation. The general advantages of the colorimetric assay are easy handling of large amounts of samples at the same time, the possibility of automation, and the need for less material
analysis
-
modified colorimetric assay for uricase activity in flexible 96-well microtiter plates using the uricase/uric acid/horseradish peroxidase/4-aminoantipyrine/3,5-dichloro-2-hydroxybenzene sulfonate colorimetric reaction. The method is much more efficient than the conventional ones and greatly reduces assay time from 4 days to less than 20 h
analysis
-
development of an urate-selective microbial biosensor cells of the recombinant thermotolerant methylotrophic yeast Hansenula polymorpha as biorecognition element. The UOX producing cells are coupled to horseradish peroxidase and immobilized on graphite electrodes by physical entrapment behind a dialysis membrane. A high urate selectivity with a detection limit of about 8 microM is found
analysis
development of a high-throughput screening system of Bacillus fastidiosus uricase mutants, using 96-well plates and monitoring of uric acid by absorbance at 298 nm
analysis
specific activity calculated from the level of total proteins is a favorable index for recognizing an enzyme mutant with small improvement of activity. Uricase mutants whose activities are improved by more than 80% are recognized with higher sensitivity and specificity during screening a library of enzyme mutants expressed in Escherichia coli
analysis
-
uric acid can be detected in human sera with the enzyme with none of the tested uric acid analogs being a competitive substrate
analysis
-
uric acid can be detected in human sera with the enzyme with none of the tested uric acid analogs being a competitive substrate
-
medicine
-
determining the urate concentration in blood and urine
medicine
-
determining the urate concentration in blood and urine
medicine
DQ887577
determination of the urate concentration in blood and urine is required for the diagnosis of gout as urate accumulation is a causative factor of gout in humans
medicine
substitute for allopurinol in the management of gout and hyperuricaemia
medicine
the enzyme might be useful in the treatment of patients with refractory gout, overview
medicine
-
treatment od tumor lysis syndrome, recombinant urate oxidase is effective in reducing uric acid and preventing uric acid accumulation in patients with hematologic malignancies with hyperuricemia or at high risk of developing it, rasburicase represents an effective alternative to allopurinol to promptly reduce uric acid levels, improve patients electrolyte status, and reverse renal insufficiency
medicine
-
urate oxidase is used to reduce toxic urate accumulation during chemotherapy
medicine
-
uricase is an important medical enzyme which can be used to determine urate in clinical analysis, to therapy gout, hyperuricemia, and tumor lysis syndrome
medicine
-
treatment of patients with high risk for tumor lysis syndrome with 0.2 mg/kg intravenously over 30 min, daily, for 4 days leads to 75.3% reduction in plasma uric acid at 4 h as compared to baseline. Recombinant rasburicase that is indigenously developed is effective for prevention and management of hyperuricemia in patients who are at high risk of developing tumor lysis syndrome
medicine
-
oral uricase therapy significantly decreases plasma uric acid concentrations in pigs with chronic kidney disease
medicine
-
the enzyme can be used as biosensor for uric acid measurements in biofluids of sweat and wounds
medicine
-
the enzyme can be used for treating gout disease
medicine
-
the enzyme is used for the treatment of gout and hyperuricemia occurring in tumor lysis syndrome
medicine
-
the enzyme, when engineered as bifunctional protein with uricase and peroxidase activities (constructed by direct fusion of Candida utilis uricase and Vitreoscilla hemoglobin), can be used for evaluation and measurement of uric acid from lyophilized serum
medicine
-
determining the urate concentration in blood and urine
-
medicine
-
the enzyme can be used for treating gout disease
-
synthesis
high-yield expression of uricase in Escherichia coli and establishment of an efficient three-step protein purification protocol. The purity of the recombinant protein is more than 98% and the specific activity is 38.4 IU/mg
synthesis
-
at optimized growth parameters, the crude preparation shows uricase activity of 13.42 U/ml
synthesis
-
at optimized growth parameters, the crude preparation shows uricase activity of 17.7 U/ml
synthesis
expression of the Escherichia-coli-codon-optimized gene as a fusion with the N-terminus of Mxe GyrA intein and chitin-binding domain for simple purification. After purification, the cleavage of the fusion protein is induced by adding DTT. Pure and properly folded uricase is obtained
synthesis
-
optimization of enzyme production from a bacterium isolated in deep litter poultry soil. Up to 306 U/l extracellular enzyme can be obtained
synthesis
-
optimum uricase production is in basal medium containing sucrose as a sole carbon source, uric acid as a nitrogen source at pH 6. Presence of cysteine HCl, cystine and glutamic acid enhances uricase production. Up to 167 U/ml can be obtained
synthesis
-
optimum uricase production is in basal medium containing sucrose as a sole carbon source, uric acid as a nitrogen source at pH 6. Presence of cysteine HCl, cystine and glutamic acid enhances uricase production. Up to 167 U/ml can be obtained
-
synthesis
-
at optimized growth parameters, the crude preparation shows uricase activity of 13.42 U/ml
-
synthesis
-
at optimized growth parameters, the crude preparation shows uricase activity of 17.7 U/ml
-
synthesis
-
at optimized growth parameters, the crude preparation shows uricase activity of 13.42 U/ml
-
synthesis
-
at optimized growth parameters, the crude preparation shows uricase activity of 17.7 U/ml
-