1.7.3.3: factor-independent urate hydroxylase
This is an abbreviated version!
For detailed information about factor-independent urate hydroxylase, go to the full flat file.
Word Map on EC 1.7.3.3
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1.7.3.3
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hyperuricemia
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peroxisomal
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xanthine
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allopurinol
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gout
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purine
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catalase
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allantoin
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biosensors
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electrode
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hematologic
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creatinine
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oxonic
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febuxostat
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allantoinase
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hyperkalemia
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hypoxanthine
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prophylaxis
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flavus
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hyperphosphatemia
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urate-lowering
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ureide
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methemoglobinemia
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pegylated
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amperometric
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uricosuric
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hypocalcemia
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tophi
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benzbromarone
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hominoid
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phosphotungstate
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microbodies
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hypouricemic
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probenecid
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utilis
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pimecrolimus
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pharmacology
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medicine
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analysis
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synthesis
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weight-based
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nodule-specific
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miocene
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drug development
- 1.7.3.3
- hyperuricemia
- peroxisomal
- xanthine
- allopurinol
- gout
- purine
- catalase
- allantoin
-
biosensors
-
electrode
-
hematologic
- creatinine
-
oxonic
- febuxostat
- allantoinase
- hyperkalemia
- hypoxanthine
-
prophylaxis
- flavus
- hyperphosphatemia
-
urate-lowering
-
ureide
- methemoglobinemia
-
pegylated
-
amperometric
-
uricosuric
-
hypocalcemia
-
tophi
- benzbromarone
-
hominoid
-
phosphotungstate
- microbodies
-
hypouricemic
- probenecid
- utilis
- pimecrolimus
- pharmacology
- medicine
- analysis
- synthesis
-
weight-based
-
nodule-specific
-
miocene
- drug development
Reaction
Synonyms
AaUO, AgUOX, dHU-wPU, ELITEK, Fasturtec, MVSM, N-35, Nodule specific uricase, Nodulin 35, Nodulin 35 homolog, Non-symbiotic uricase, oxidase, urate, Pucl, Rasburicase, Uaz, Uox, Urate oxidase, urate oxidoreductase, UriA, uric acid oxidase, uricase, uricase II, Uricoenzyme, Uricozyme
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Temperature Stability
Temperature Stability on EC 1.7.3.3 - factor-independent urate hydroxylase
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0 - 70
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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
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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
30 - 40
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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
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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
37
40
45
50
52
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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
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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
60 - 61
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native uricase and poly(N-acryloylmorpholine)-OSu-uricase 50% loss of activity
65
70
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
additional information
12 h, 50% residual activity, complete loss of activity after 54 h
37
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the specific activity of wild type enzyme decreases to 90% after exposed to 37°C for 20h
40
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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
the enzyme retains almost 100% activity after 2 min at 45°C, however, at higher temperatures the activity is rapidly lost
70
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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
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
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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
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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
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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
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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
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the molecular structure of enzyme has a reversible change at a temperature between 30°C and 60°C