1.7.3.3: factor-independent urate hydroxylase
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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
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biosensors
-
electrode
-
hematologic
- creatinine
-
oxonic
- febuxostat
- allantoinase
- hyperkalemia
- hypoxanthine
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prophylaxis
- flavus
- hyperphosphatemia
-
urate-lowering
-
ureide
- methemoglobinemia
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pegylated
-
amperometric
-
uricosuric
-
hypocalcemia
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tophi
- benzbromarone
-
hominoid
-
phosphotungstate
- microbodies
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hypouricemic
- probenecid
- utilis
- pimecrolimus
- pharmacology
- medicine
- analysis
- synthesis
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weight-based
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nodule-specific
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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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1.7.3.3 factor-independent urate hydroxylaseAdvanced search results
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results (Application
Application on EC 1.7.3.3 - factor-independent urate hydroxylase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
drug development
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urate oxidase has the potential to be a therapeutic target for the treatment of gout
medicine
pharmacology
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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
synthesis
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
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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
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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
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uric acid can be detected in human sera with the enzyme with none of the tested uric acid analogs being a competitive substrate
analysis
Cytobacillus firmus DWD-33
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uric acid can be detected in human sera with the enzyme with none of the tested uric acid analogs being a competitive substrate
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medicine
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determining the urate concentration in blood and urine
medicine
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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
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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
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urate oxidase is used to reduce toxic urate accumulation during chemotherapy
medicine
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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
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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
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oral uricase therapy significantly decreases plasma uric acid concentrations in pigs with chronic kidney disease
medicine
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the enzyme can be used as biosensor for uric acid measurements in biofluids of sweat and wounds
medicine
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the enzyme is used for the treatment of gout and hyperuricemia occurring in tumor lysis syndrome
medicine
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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
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determining the urate concentration in blood and urine
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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
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at optimized growth parameters, the crude preparation shows uricase activity of 13.42 U/ml
synthesis
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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
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optimization of enzyme production from a bacterium isolated in deep litter poultry soil. Up to 306 U/l extracellular enzyme can be obtained
synthesis
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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
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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
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synthesis
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at optimized growth parameters, the crude preparation shows uricase activity of 13.42 U/ml
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synthesis
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at optimized growth parameters, the crude preparation shows uricase activity of 17.7 U/ml
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synthesis
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at optimized growth parameters, the crude preparation shows uricase activity of 13.42 U/ml
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synthesis
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at optimized growth parameters, the crude preparation shows uricase activity of 17.7 U/ml
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