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
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Subunits
Subunits on EC 1.17.3.2 - xanthine oxidase
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dimer
homodimer
additional information
?
x * 150000, about, C-terminally truncated mutant enzyme DELTAC, SDS-PAGE
dimer
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composed with two different peptides with the mass of 55.5 and 85.5 kDa
dimer
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the two XOD subunits are strongly cooperative in both binding and catalysis
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composed of two identical subunits of about 145 kDa, each being subdivided into three domains: a N-terminal iron-sulfur-binding domain of 20 kDa, a 40 kDa domain harboring a FAD-binding site, and a C-terminal molybdenum cofactor-binding domain of 85 kDa
homodimer
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alpha2, with four redox-active centers in each subunit laid out in discretely folding domains, structure, overview
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comparison of structural alterations of xanthine oxidase leading to xanthine dehydrogenase, EC 1.17.14, activity involving residues R335, R427, W336, and F549, mechanism of transition, overview
additional information
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on polyacrylamide gel electrophoresis in presence of SDS and 2-mercaptoethanol the purified xanthine oxidase is dissociated into one major band of approximately 150000 Da and three bands of 100000 Da, 60000 Da and 40000 Da
additional information
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structural comparison of xanthine dehydrogenase, EC 1.17.1.4, and xanthine oxidase, overview