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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

Reaction

Urate
+
O2
 +
H2O
=
5-hydroxyisourate
 +
H2O2

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

ECTree

     1 Oxidoreductases
         1.7 Acting on other nitrogenous compounds as donors
             1.7.3 With oxygen as acceptor
                1.7.3.3 factor-independent urate hydroxylase

General Stability

General Stability on EC 1.7.3.3 - factor-independent urate hydroxylase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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)
-
borate stabilizes
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
-
EDTA stabilizes
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