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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General Information
General Information on EC 1.17.3.2 - xanthine oxidase
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evolution
malfunction
metabolism
physiological function
additional information
analysis of circulating xanthine oxidase activities in marine mammals adapted to tolerate repeated cycles of ischemia/reperfusion associated with diving (bottlenose dolphin, northern elephant seal) in comparison with semiaquatic (river otter) and terrestrial mammals (human, pig), overview
evolution
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analysis of circulating xanthine oxidase activities in marine mammals adapted to tolerate repeated cycles of ischemia/reperfusion associated with diving (bottlenose dolphin, northern elephant seal) in comparison with semiaquatic (river otter) and terrestrial mammals (human, pig), overview
evolution
Lontra longicaudis annectens
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analysis of circulating xanthine oxidase activities in marine mammals adapted to tolerate repeated cycles of ischemia/reperfusion associated with diving (bottlenose dolphin, northern elephant seal) in comparison with semiaquatic (river otter) and terrestrial mammals (human, pig), overview
evolution
analysis of circulating xanthine oxidase activities in marine mammals adapted to tolerate repeated cycles of ischemia/reperfusion associated with diving (bottlenose dolphin, northern elephant seal) in comparison with semiaquatic (river otter) and terrestrial mammals (human, pig), overview
evolution
analysis of circulating xanthine oxidase activities in marine mammals adapted to tolerate repeated cycles of ischemia/reperfusion associated with diving (bottlenose dolphin, northern elephant seal) in comparison with semiaquatic (river otter) and terrestrial mammals (human, pig), overview
malfunction
deletion mutant exhibits less than 1% of the wild-type strain activity towards xanthine and hypoxanthine under inducible conditions and both strains show no activity after cultivation without inducer (adenine)
malfunction
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upregulation of seric XO activity through infection with Ichthyophthirius multifiliis leads to an excessive formation of uric acid, which contributes to oxidative and inflammatory processes. Uric acid induces the release of pro-inflammatory and pro-oxidative mediators, such as nitric oxide (NOx) and reactive oxygen species (ROS), which contribute directly to disease pathogenesis
malfunction
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upregulation of splenic xanthine oxidase activity contributes to disease pathogenesis of Aeromonas caviae infection, as well as whether it may be considered a pathway involved in reactive oxygen species (ROS) and nitric oxide (NO) production. Excessive uric acid induces the release of pro-inflammatory mediators, such as ROS and NOx, which contribute to disease pathophysiology, in spleen tissue they contribute to oxidation and inflammation of the tissue
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the enzyme plays an important role in the metabolism of many xenobiotics and drugs, such as purines and pyrimidines, mercaptopurine and azathioprine, thiazides, pyrazinamide, and acyclovir
metabolism
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xanthine oxidase is a key enzyme in the purine metabolic pathway, catalysing the oxidation of hypoxanthine to uric acid
metabolism
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xanthine oxidase, a key enzyme in purine metabolism, produces reactive oxygen species causing vascular injuries and chronic heart failure
metabolism
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effects of enzyme inhibition in inflammatory macrophages, overview
metabolism
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xanthine oxidase is the key enzyme that catalyzes the oxidation of hypoxanthine to xanthine and then to uric acid
metabolism
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purine nucleoside phosphorylase (PNP) and xanthine oxidase (XO) are key enzymes involved in the purine salvage pathway. PNP metabolizes purine bases to synthetize purine nucleotides whereas XO catalyzes the oxidation of purines to uric acid
metabolism
Lontra longicaudis annectens
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purine nucleoside phosphorylase (PNP) and xanthine oxidase (XO) are key enzymes involved in the purine salvage pathway. PNP metabolizes purine bases to synthetize purine nucleotides whereas XO catalyzes the oxidation of purines to uric acid
metabolism
purine nucleoside phosphorylase (PNP) and xanthine oxidase (XO) are key enzymes involved in the purine salvage pathway. PNP metabolizes purine bases to synthetize purine nucleotides whereas XO catalyzes the oxidation of purines to uric acid
metabolism
purine nucleoside phosphorylase (PNP) and xanthine oxidase (XO) are key enzymes involved in the purine salvage pathway. PNP metabolizes purine bases to synthetize purine nucleotides whereas XO catalyzes the oxidation of purines to uric acid
metabolism
purine nucleoside phosphorylase (PNP) and xanthine oxidase (XO) are key enzymes involved in the purinesalvage pathway. PNP metabolizes purine bases to synthetize purine nucleotides whereas XO catalyzes the oxidation of purines to uric acid
metabolism
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effects of enzyme inhibition in inflammatory macrophages, overview
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xanthine oxidase is a key enzyme that can catalyze the conversion of xanthine to uric acid, causing various diseases in humans
physiological function
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xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation
physiological function
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xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation
physiological function
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xanthine oxidoreductase is a ubiquitous molybdenum-iron-flavo enzyme with a central role in purine catabolism where it catalyzes the oxidation of hypoxanthine to xanthine and of xanthine to uric acid
physiological function
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xanthine oxidase functions not only to hydroxylate xanthine at C-8 to give uric acid, but also hypoxanthine at C-2 to give xanthine in the immediate preceding step of purine catabolism
physiological function
mammalian xanthine oxidoreductase can exist in both dehydrogenase and oxidase forms. The C-terminal peptide plays a role in the formation of an intermediate form during the transition between xanthine dehydrogenase and xanthine oxidase. Conversion between the two is implicated in such diverse processes as lactation, anti-bacterial activity, reperfusion injury and a growing number of diseases. The dehydrogenase-oxidase transformation occurs rather readily and the insertion of the C-terminal peptide into the active site cavity of its subunit stabilizes the dehydrogenase form. The intermediate form can be generated (e.g. in endothelial cells) upon interaction of the C-terminal peptide portion of the enzyme with other proteins or the cell membrane. Residues Cys535 and Cys992 are involved in the rapid phase and Cys1316 and Cys1324 in the slow phase of the modification reaction. The irreversible conversion of XDH to XOR by trypsin involves limited proteolysis at the same linker peptide. Triggering events, such as the formation of a disulfide bond between Cys535 and Cys992 or proteolysis of the linker, reorient Phe549 (also a part of the long linker), resulting in disruption of a four amino acid cluster. Arg426 is then released from the cluster and moves the A-loop that blocks the approach of NAD+ to the flavin ring of the FAD moiety, as well as changing the electrostatic environment
physiological function
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xanthine oxidase catalyzes the oxidation of xanthine to uric acid. Uric acid in serum is acts as an anti-oxidant. Xanthine oxidase is a key enzyme in uric acid production. This process generates excessive reactive oxygen species (ROS) that play an important role in atherogenesis. Xanthine oxidase induces foam cell formation in large part through activation of LOX-1/NLRP3 pathway in both vascular smooth muscle cells and THP-1 cells, but uric acid-induced foam cell formation occurs exclusively through the CD36 pathway. Xanthine oxidase enhances the expression of NLRP3, caspase-1, cleaved interleukin-1beta and interleukin-18 in vascular smooth muscle cells and THP-1 cells, while uric acid has no effect
physiological function
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xanthine oxidase is an important enzyme of purine metabolism that catalyzes the hydroxylation of hypoxanthine to xanthine and then xanthine to uric acid. Xanthine oxidase is used in the oxidation of purines and related compounds and plays a role in biochemical reactions such as hydroxylation of purines, pterines, aromatic heterocycles, aliphatic and aromatic aldehydes and also in the detoxification or activation of endogenous compounds and xenobiotics
physiological function
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xanthine oxidoreductase (XOR) is a molybdopterin-containing enzyme that catalyzes the oxidation of hypoxanthine to xanthine, and further generates uric acid from xanthine in the purine metabolic pathway
physiological function
Bacillus pumilus RL-2d
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xanthine oxidase is an important enzyme of purine metabolism that catalyzes the hydroxylation of hypoxanthine to xanthine and then xanthine to uric acid. Xanthine oxidase is used in the oxidation of purines and related compounds and plays a role in biochemical reactions such as hydroxylation of purines, pterines, aromatic heterocycles, aliphatic and aromatic aldehydes and also in the detoxification or activation of endogenous compounds and xenobiotics
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the enzyme also serves as an important biological source of reactive oxygen species that are involved in many pathological processes, such as inflammation, atherosclerosis, cancer, and aging
additional information
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elevated level of blood uric acid, hyperuricemia, is the underlying cause of gout, development of enzyme inhibitors more efficacious, than allopurinol, to treat gout and possibly against cardiovascular diseases, overview
additional information
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elevated level of blood uric acid, hyperuricemia, is the underlying cause of gout, development of enzyme inhibitors more efficacious, than allopurinol, to treat gout and possibly against cardiovascular diseases, overview
additional information
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serum xanthine oxidase activity is correlated with serum uric acid levels, while no correlation is observed for liver xanthine oxidase activity. The serum uric acid levels in mice treated with the flavonoids genistein, apigenin, quercetin, rutin and astilbin are higher than control levels. No statistically significant difference in serum and liver xanthine oxidase activities between normal control mice and hyperuricemic mice
additional information
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the enzyme is regulated by substrates at active sites via cooperative interactions between catalytic subunits. A substrate can regulate the activity of xanthine oxidase via binding at the active sites, or a xanthine oxidase catalytic subunit can simultaneously serve as a regulatory unit
additional information
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xanthine oxidoreductase is implicated in many inflammatory diseases. Inhibition of XOR within the inflammatory mononuclear phagocytes, i.e. MNP, prevents neutrophil recruitment during adoptive transfer demonstrating the role of XOR in MNP-mediated neutrophil recruitment, role of XOR in the inflammatory state of MNP, overview. XOR activity is specifically increased by inflammatory mononuclear phagocyte differentiation. Inhibition of XOR reduces levels of CINC-1 secreted by inflammatory mononuclear phagocytes, and increases levels of SUMO-PPARgamma in the cell lines
additional information
XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4
additional information
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XOR can adopt its XOR xanthone oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4
additional information
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xanthine oxidoreductase is implicated in many inflammatory diseases. Inhibition of XOR within the inflammatory mononuclear phagocytes, i.e. MNP, prevents neutrophil recruitment during adoptive transfer demonstrating the role of XOR in MNP-mediated neutrophil recruitment, role of XOR in the inflammatory state of MNP, overview. XOR activity is specifically increased by inflammatory mononuclear phagocyte differentiation. Inhibition of XOR reduces levels of CINC-1 secreted by inflammatory mononuclear phagocytes, and increases levels of SUMO-PPARgamma in the cell lines
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additional information
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serum xanthine oxidase activity is correlated with serum uric acid levels, while no correlation is observed for liver xanthine oxidase activity. The serum uric acid levels in mice treated with the flavonoids genistein, apigenin, quercetin, rutin and astilbin are higher than control levels. No statistically significant difference in serum and liver xanthine oxidase activities between normal control mice and hyperuricemic mice
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