1.17.3.2: xanthine oxidase
This is an abbreviated version!
For detailed information about xanthine oxidase, go to the full flat file.
Word Map on EC 1.17.3.2
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1.17.3.2
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allopurinol
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uric
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dismutase
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catalase
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sod
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xx
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endothelial
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malondialdehyde
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hyperuricemia
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reperfusion
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gout
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ischemia
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purine
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artery
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karyotype
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turner
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myocardial
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gsh
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pulmonary
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myeloperoxidase
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ischemia-reperfusion
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gonad
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hermaphrodite
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oxypurinol
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thiobarbituric
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urate
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spin
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tbars
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chemiluminescence
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dysgenesis
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molybdenum
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gsh-px
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sex-determining
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caffeine
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x-chromosome
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oxygen-derived
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tungsten
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acid-reactive
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masculinization
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fenton
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sex-reversed
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hypouricemic
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monosomy
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feminization
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drug development
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diagnostics
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urate-lowering
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synthesis
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self-fertilizing
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biotechnology
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medicine
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radical-generating
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cyp2a6
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oxidase-derived
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pharmacology
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nondisjunction
- 1.17.3.2
- allopurinol
-
uric
- dismutase
- catalase
- sod
- xx
- endothelial
- malondialdehyde
-
hyperuricemia
-
reperfusion
- gout
- ischemia
- purine
- artery
- karyotype
-
turner
- myocardial
- gsh
- pulmonary
- myeloperoxidase
-
ischemia-reperfusion
- gonad
-
hermaphrodite
- oxypurinol
-
thiobarbituric
- urate
-
spin
-
tbars
-
chemiluminescence
- dysgenesis
- molybdenum
- gsh-px
-
sex-determining
- caffeine
-
x-chromosome
-
oxygen-derived
- tungsten
-
acid-reactive
-
masculinization
-
fenton
-
sex-reversed
-
hypouricemic
-
monosomy
-
feminization
- drug development
- diagnostics
-
urate-lowering
- synthesis
-
self-fertilizing
- biotechnology
- medicine
-
radical-generating
- cyp2a6
-
oxidase-derived
- pharmacology
-
nondisjunction
Reaction
Synonyms
AXOR, EC 1.1.3.22, EC 1.2.3.2, EC 1.2.3.2., hypoxanthine oxidase, hypoxanthine-xanthine oxidase, hypoxanthine:oxygen oxidoreductase, More, oxidase, xanthine, Schardinger enzyme, xanthine dehydrogenase/oxidase, xanthine oxidase, xanthine oxidoreductase, xanthine: oxygen oxidoreductase, xanthine:O2 oxidoreductase, xanthine:oxygen oxidoreductase, xanthine:xanthine oxidase, XnOx, XO, XOD, XOR
ECTree
1.17.3.2 xanthine oxidaseAdvanced search results
results (
results (KM Value
KM Value on EC 1.17.3.2 - xanthine oxidase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.17
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
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-
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0.0451
3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
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substrate and inhibitor compound
0.0649
5-chloro-6-[(2-iminopyrrolidin-1-yl)methyl]-3H-pyrimidin-4-one
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substrate and inhibitor compound
0.0497
O2
untreated C-terminally truncated enzyme mutant, pH 7.8, 25°C
0.0537
O2
DTT-treated C-terminally truncated enzyme mutant, pH 7.8, 25°C
0.129
O2
xanthine oxidoreductase mutant W335A/F336L treated with dithiothreitol, pH 7.8, 25°C
0.0552
xanthine
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pH not specified in the publication, temperature not specified in the publication, mutant E802Q
0.0644
xanthine
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pH not specified in the publication, temperature not specified in the publication, wild-type enzyme
additional information
additional information
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enzyme kinetics at all pH values studied is non-hyperbolic, and the use of the Michaelis-Menten equation is not adequate
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additional information
additional information
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detailed kinetics of wild-type in comparison to mutant enzymes, overview
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additional information
additional information
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steady-state kinetics analysis of wild-type and mutant enzymes with hypoxanthine of xanthine, and of mutant enzymes with benzaldehyde or 4-(dimethyamino)cinnamaldehyde as aldehyde oxidase substrates, overview
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additional information
additional information
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in vitro steady-state kinetic studies, kinetics with cofactor cytochrome C, overview
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additional information
additional information
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steady-state kinetics study of enzyme activity in the presence of Cu2+ and with different pre-incubation times, KM values of 0.0096-0.020 mM, overview
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additional information
additional information
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kinetic analysis, Michaelis-Menten model, detailed overview. Binding of a 6-formylpterin at one of the two xanthine oxidase active sites slows down the turnover rate of xanthine at the adjacent active site and converts the V-[S] plot from substrate inhibition kinetic pattern to a classical Michaelis-Menten hyperbolic saturation pattern. In contrast, binding of xanthine at an active site accelerates the turnover rate of 6-formylpterin at the neighboring active site
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additional information
additional information
steady-state and reductive half-reaction rapid kinetics at pH 7.0 and pH 8.5, overview
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additional information
additional information
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thermodynamics and kinetics of xanthine oxidase in the presence of pyridine, Km for xanthine is increased 4.8fold and Vmax is reduced 1.8fold at 0.5% pyridine, overview
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additional information
additional information
Michaelis-Menten and Lineweaver-Burk kinetics
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additional information
additional information
pH-dependent steady-state kinetics and reductive half-reaction, stopped flow kinetics, kinetic analysis of wild-type and mutant xanthine dehydrogenases, detailed overview. kred, the limiting rate constant for reduction at high [xanthine], is significantly compromised in the mutant variant E232Q, a result that is inconsistent with Glu232 being neutral in the active site of the wild-type enzyme. The ionized Glu232 of wild-type enzyme plays an important role in catalysis by discriminating against the monoanionic form of substrate, effectively increasing the pKa of the substrate by two pH units and ensuring that at physiological pH the neutral form of the substrate predominates in the Michaelis complex. The product release is principally rate-limiting in catalysis. The disparity in rate constants for the chemical step of the reaction and product release is not as great in the bacterial enzyme as compared with the vertebrate forms. The faster turnover observed with the bacterial enzyme is due to a faster rate constant for product release than is seen with the vertebrate enzyme
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additional information
additional information
steady-state kinetics of DTT-treated and untreated C-terminally truncated enzyme mutant
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