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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Metals Ions
Metals Ions on EC 1.17.3.2 - xanthine oxidase
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CoCl2
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increased activity of xanthine oxidase in cells exposed to CoCl2 and subsequent increase in reactive oxygen species derived from enzyme activity, which results in accumulation of hypoxia-inducible factor 1alpha. Blockade of enzyme activity by allopurinol, N-acetyl-L-cysteine or siRNA significantly attenuates expression of hypoxia-inducible factor 1alpha and thus the induction of genes such as erythropoietin and vascular endothelial growth factor
Cu2+
Fe2+
Iron
Mo
Mo4+
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the Mo(VI) ion at the active site is reduced to Mo(IV), which then transfers two electrons, via the 2Fe-2S clusters, to the FAD cofactor
Molybdenum
additional information
Cu2+
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Cu2+ either stimulates or inhibits xanthine oxidase activity, depending on metal concentration (inhibition above 0.7 mM) and pre-incubation length, the latter also determining the inhibition type. Cu2+-enzyme complex formation is characterized by modifications in xanthine oxidase electronic absorption bands, intrinsic fluorescence, and alpha-helical and beta-sheet content. Apparent dissociation constant values imply high- and low-affinity Cu2+ binding sites in the vicinity of the enzyme's reactive centers, Cu2+ binding to high-affinity sites causes alterations around xanthine oxidase molybdenum and flavin adenine dinucleotide centers, changes in secondary structure, and moderate activity inhibition, binding to low affinity sites causes alterations around all xanthine oxidase reactive centers including FeS, changes in tertiary structure as reflected by alterations in spectral properties, and drastic activity inhibition. Stimulation is attributed to transient stabilization of xanthine oxidase optimal conformation. Potential role of copper in the regulation of xanthine oxidase activity, binding kinetics, detailed overview
Fe2+
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xanthine oxidase dependent oxidation of ascorbate is markedly increased in presence of iron
Fe2+
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two 2Fe-2S clusters. The Mo(VI) ion at the active site is reduced to Mo(IV), which then transfers two electrons, via the 2Fe-2S clusters, to the FAD cofactor
Iron
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iron-molybdenum protein
Molybdenum
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molybdenum cofactor is a complex between molybdenum and molybdopterin (a 6-alkylpterin with 4-carbon side chain which has an enedithiol at carbon 1' and 2', a hydroxyl at carbon 3', and a terminal phosphate group)
Molybdenum
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an iron-molybdenum protein
Molybdenum
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nitrate reduction to nitrite as well as nitrite reduction to NO occurs at the molybdenum site
Molybdenum
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the enzyme accelerates reaction rate via base-catalyzed chemistry in which a Mo-OH group undertakes nucleophilic attack on the carbon center to be hydroxylated, with concomitant hydride transfer to a catalytically essential Mo=S group in the molybdenum coordination sphere. This chemistry appears to proceed via obligate two-electron chemistry rather than in individual steps to yield a reduced enzyme product complex with product coordinmated to the active site molybdenum by means of the newly introduced hydroxyl group in a sinple end-on fashion
Molybdenum
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the molybdenum center is a pyranopterin-MoVI-OS-OH. The pyranopterin cofactor is coordinated to the metall via an enedithiolate side chain, coordination geometry, overview
Molybdenum
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XOR is a molybdenum-containing enzyme. In the oxidized form of XORs, the Mo(VI) ion is in the center of a square-pyramidal geometry, coordinated by an oxo-ligand at the apical position and one hydroxo and one sulfido ligand at equatorial positions,3a in addition to the two vicinal sulfur ligands contributed by the pterin group, cofactor geometry, overview
Molybdenum
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an iron-molybdenum protein
Molybdenum
XOR is a molybdenum-containing enzyme. In the oxidized form of XORs, the Mo(VI) ion is in the center of a square-pyramidal geometry, coordinated by an oxo-ligand at the apical position and one hydroxo and one sulfido ligand at equatorial positions, in addition to the two vicinal sulfur ligands contributed by the pterin group, cofactor geometry, overview
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the molybdenum center is located in a separate subunit from the Fe/S- and flavin-containing parts of the enzyme