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Information on EC 1.17.3.2 - xanthine oxidase and Organism(s) Homo sapiens and UniProt Accession P47989

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EC Tree
     1 Oxidoreductases
         1.17 Acting on CH or CH2 groups
             1.17.3 With oxygen as acceptor
                1.17.3.2 xanthine oxidase
IUBMB Comments
An iron-molybdenum flavoprotein (FAD) containing [2Fe-2S] centres. Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1, aldehyde oxidase. Under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 O2.- + 2 H+. The mammalian enzyme predominantly exists as an NAD-dependent dehydrogenase (EC 1.17.1.4, xanthine dehydrogenase). During purification the enzyme is largely converted to the O2-dependent xanthine oxidase form (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [4,5,7,10] [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo [4,6,10].
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Homo sapiens
UNIPROT: P47989
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
xo, hypoxanthine-xanthine oxidase, xanthine:xanthine oxidase, xanthine:oxygen oxidoreductase, xanthine oxygen oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hypoxanthine oxidase
-
-
-
-
hypoxanthine-xanthine oxidase
-
-
-
-
hypoxanthine:oxygen oxidoreductase
-
-
-
-
oxidase, xanthine
-
-
-
-
Schardinger enzyme
-
-
-
-
xanthine oxidoreductase
xanthine: oxygen oxidoreductase
-
-
xanthine:O2 oxidoreductase
-
-
-
-
xanthine:xanthine oxidase
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
xanthine + H2O + O2 = urate + H2O2
show the reaction diagram
hydrogen-bonding arrangement of the substrate-bound complex at the active site, and proposed mechanism of the purine oxidation reaction by XOR
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
-
reduction
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
xanthine:oxygen oxidoreductase
An iron-molybdenum flavoprotein (FAD) containing [2Fe-2S] centres. Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1, aldehyde oxidase. Under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 O2.- + 2 H+. The mammalian enzyme predominantly exists as an NAD-dependent dehydrogenase (EC 1.17.1.4, xanthine dehydrogenase). During purification the enzyme is largely converted to the O2-dependent xanthine oxidase form (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [4,5,7,10] [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo [4,6,10].
CAS REGISTRY NUMBER
COMMENTARY hide
9002-17-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
?
1-methylxanthine + H2O + O2
1-methylurate + H2O2
show the reaction diagram
-
-
-
-
?
6'-deoxyacyclovir + H2O + O2
acyclovir + H2O2
show the reaction diagram
-
prodrug of the antiviral agent acyclovir
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
show the reaction diagram
adenine + H2O + O2
6-amino-7,9-dihydropurin-8-one + H2O2
show the reaction diagram
-
-
-
?
allopurinol + H2O + O2
?
show the reaction diagram
-
-
-
-
?
allopurinol + H2O + O2
oxypurinol + H2O2
show the reaction diagram
-
allopurinol is a substrate and a competitive inhibitor for xanthine oxidase, it binds irreversibly at the active site reducing molybdenum VI to IV
-
-
?
benzaldehyde + H2O + O2
benzoate + H2O2
show the reaction diagram
-
-
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
?
formycin B + H2O + O2
?
show the reaction diagram
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
N-methylnicotinamide + H2O + O2
?
show the reaction diagram
-
poor oxidation reaction
-
-
r
N1-methylnicotinamide + H2O + O2
?
show the reaction diagram
-
-
-
-
?
pteridine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
purine + H2O + O2
7,9-dihydropurin-8-one + H2O2
show the reaction diagram
-
purine and derivatives
-
?
purine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
?
1-methylxanthine + H2O + O2
1-methylurate + H2O2
show the reaction diagram
-
-
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
show the reaction diagram
-
an anticancer prodrug, no activation by xanthine oxidase but conversion to the inactive metabolite 6-thiouric acid, catabolism, overview
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
-
?
pteridine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
purine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
flavoprotein
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CoCl2
-
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
Iron
-
iron-molybdenum protein
Molybdenum
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(4'-methoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
-
-
1,2,4-triazolo[1,5-a]pyrimidine
-
poor inhibitor
1-(4'-nitrophenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
-
-
1-(4'-trifluoromethylphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
-
-
1-4-tolyl-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
-
-
2,4-dihydroxy-6-[(E)-2-(4-hydroxyphenyl)ethenyl]benzaldehyde
-
-
2,6-diaminopurine
-
poor inhibitor
2-amino-6-chloropurine
-
poor inhibitor
2-Aminopurine
-
poor inhibitor
2-chloro-6(methylamino)purine
-
competitive
2-hydroxy-4-methoxy-6-[(E)-2-(4-methoxyphenyl)ethenyl]benzaldehyde
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a resveratrol derivative
2-hydroxy-6-[(E)-2-(4-hydroxyphenyl)ethenyl]-4-methoxybenzaldehyde
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a resveratrol derivative
4-(4'-aminopyrazolo[3,4-d]pyrimidin-1-yl)-benzonitrile
-
-
4-Aminopyrazolo[3,4-d]pyrimidine
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competitive
5,6-Dimethylbenzimidazole
-
poor inhibitor
5-amino-1-(4'-carboxyphenyl)-1H-pyrazole-4-carbonitrile
-
-
5-methylbenzimidazole
-
poor inhibitor
5-nitrobenzimidazole
-
-
6-aminopurine
-
-
6-O-methylguanine
-
poor inhibitor
6-thioguanine
-
-
allopurinol
Aminoglutethimide
-
-
apigenin
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-
cyclosporin A
-
-
dithranol
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-
epicatechin
-
-
febuxostat
green tea extract
-
-
-
losartan
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in patients with coronary disease, losartan therapy reduces endothelium-bound xanthine oxidase activity likely contributing to improved endothelial function, enzyme inhibition with losartan does not improve endothelium-dependent vasodilation before
luteolin
-
-
N-(4''-carboxyphenyl)-N-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosyl)pyrazolo[3,4-d] pyrimidine
-
-
N-(4'-carboxyphenyl)-1H-4-aminopyrazolo[3,4-d]pyrimidine
-
-
N-acetyl-L-cysteine
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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
naringenin
-
-
oxypurinol
-
enzyme inhibition with oxypurinol improves endothelium-dependent vasodilation before
quercetin
-
-
resveratrol
-
i.e. 5[(E)-2-(4-hydroxyphenyl)ethenyl]benzene-1,3-diol, found in grapes as well as in other plants, is a natural phytoalexin, which is biosynthesized in response to pathogenic attack or other stress conditions
[4'-(4''-aminopyrazolo[3,4-d]pyrimidin-1''-yl)-benzoylamino]-acetic acid methyl ester
-
-
[4'-(5-amino-4-cyanopyrazol-1-yl)-benzoylamino]-acetic acid methyl ester
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
angiotensin II
-
Ang II substantially increases endothelial enzyme protein levels and enzyme-dependent superoxide production in cultured endothelial cells
apoptotic lymphocyte microparticles
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microparticles are membrane vesicles released during cell activation and apoptosis, they activate reactive oxygen species production by xanthine oxidase in endothelial cells and aorta, inhibition of phosphoinositol 3-kinase enhances the activating effect, xanthine oxidase inhibitors reduce it, overview
-
additional information
-
heat shock, e.g. by infrared light, induces the enzyme and reactive oxygen species production in keratinocytes and skin, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
allopurinol
-
-
0.93
benzaldehyde
-
-
0.55
formycin B
-
-
0.0017 - 0.021
hypoxanthine
48
N-methylnicotinamide
-
-
0.0017 - 0.072
xanthine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.33 - 30
hypoxanthine
1.35 - 18.3
xanthine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0196
(4'-methoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
Homo sapiens
-
-
0.0022
1-(4'-nitrophenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
Homo sapiens
-
-
0.00018
1-(4'-trifluoromethylphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
Homo sapiens
-
-
0.0174
1-4-tolyl-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
Homo sapiens
-
-
0.0025
2,4-dihydroxy-6-[(E)-2-(4-hydroxyphenyl)ethenyl]benzaldehyde
Homo sapiens
-
pH 7.8, 25°C
0.0102
2-chloro-6(methylamino)purine
Homo sapiens
-
pH 7.5, 25°C
0.0169
2-hydroxy-4-methoxy-6-[(E)-2-(4-methoxyphenyl)ethenyl]benzaldehyde
Homo sapiens
-
pH 7.8, 25°C
0.0266
2-hydroxy-6-[(E)-2-(4-hydroxyphenyl)ethenyl]-4-methoxybenzaldehyde
Homo sapiens
-
pH 7.8, 25°C
0.0004
4-(4'-aminopyrazolo[3,4-d]pyrimidin-1-yl)-benzonitrile
Homo sapiens
-
-
0.0303
4-Aminopyrazolo[3,4-d]pyrimidine
Homo sapiens
-
pH 7.5, 25°C
0.0361
5-amino-1-(4'-carboxyphenyl)-1H-pyrazole-4-carbonitrile
Homo sapiens
-
-
0.0868
5-nitrobenzimidazole
Homo sapiens
-
pH 7.5, 25°C
0.0109
6-aminopurine
Homo sapiens
-
pH 7.5, 25°C
0.0924
6-thioguanine
Homo sapiens
-
pH 7.5, 25°C
0.0078 - 0.0134
allopurinol
0.0184
N-(4''-carboxyphenyl)-N-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosyl)pyrazolo[3,4-d] pyrimidine
Homo sapiens
-
-
0.081
N-(4'-carboxyphenyl)-1H-4-aminopyrazolo[3,4-d]pyrimidine
Homo sapiens
-
-
0.0139
resveratrol
Homo sapiens
-
pH 7.8, 25°C
0.00008
[4'-(4''-aminopyrazolo[3,4-d]pyrimidin-1''-yl)-benzoylamino]-acetic acid methyl ester
Homo sapiens
-
-
0.0379
[4'-(5-amino-4-cyanopyrazol-1-yl)-benzoylamino]-acetic acid methyl ester
Homo sapiens
-
-
additional information
additional information
Homo sapiens
-
IC50 values for Tamnus communis root extract on cytochrome C reduction by the enzyme, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.04
-
colostrum
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
7
-
assay at
7.4
-
assay at
7.8
-
assay at
8.1
-
assay at
8.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
22
-
assay at room temperature
23
-
assay at
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
low activity
Manually annotated by BRENDA team
-
a lymphoid cell line
Manually annotated by BRENDA team
-
a nasopharyngeal epidermoid tumor cell line
Manually annotated by BRENDA team
-
tumor cell line
Manually annotated by BRENDA team
-
gastric mucosa of Helicobacter pylori positive and negative pediatric patients
Manually annotated by BRENDA team
-
tumor cell line
Manually annotated by BRENDA team
-
tumor cell line
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
vascular
Manually annotated by BRENDA team
-
glioma cell
Manually annotated by BRENDA team
-
glioma cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
enzyme binds to endothelial cells in a partially heparin-reversible manner
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
XDH_HUMAN
1333
0
146424
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
-
2 * 150000, SDS-PAGE
300000
-
gel filtration
310000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 150000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
-
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant mutant E308V, 15mg/ml protein in 5 mM Tris, pH 8.5, containing 1mM sodium salicylate and 0.1mM EDTA, incubation with 5 mM dithiothreitol for 1 h at room temperature, aliquots of 0.005 ml protein solution are mixed with 0.005 ml of 100 mM sodium citrate, pH 5.0, containing 8-11% polyethylene glycol 8000, 5 mM DTT, 1 mM sodium salicylate, 0.1 mM EDTA, and placed on siliconized glass plates, 7 days at 20°C, X-ray diffraction structure determination and analysis at 2.6 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C1318Y
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
D1109T
-
naturally occuring nonsynonymous single nucleotide polymorphism
E308V
-
site-directed mutagenesis, mutant molybdopterin domain structure, overview, the xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site, the E803V mutation almost completely abrogates the activity towards hypoxanthine as a substrate, but the decrease in activity towards purine substrate is not due to large conformational change in the mutant enzyme
G172R
-
naturally occuring nonsynonymous single nucleotide polymorphism
H1221R
-
naturally occuring nonsynonymous single nucleotide polymorphism, the mutant variant shows about twofold increased activity compared to the wild-type enzyme
I703V
-
naturally occuring single nucleotide polymorphism, the mutant variant shows abput twofold increased activity compared to the wild-type enzyme
N909K
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
P1150R
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
P555S
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
R149C
-
naturally occuring single nucleotide polymorphism, inactive mutant
R607Q
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
R881M
-
site-directed mutagenesis, the xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site, the R881M mutant lacks activity towards xanthine, but retaines slight activity towards hypoxanthine
T109K
-
naturally occuring single nucleotide polymorphism, inactive mutant
T623I
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
additional information
-
enzyme mutantions can lead to xanthinuria
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
heparin-Sepharose 6B-bound enzyme, half-life: 120 h and 67 h at 4°C and 20°C respectively, free enzyme, 61 h and 45 h at 4°C and 67°C respectively
-
the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from milk by ammonium sulfate fractionation, followed by affinity chromatography on heparin-agarose
-
recombinant wild-type and mutant enzymes from Escherichia coli strain JM109 by anion exchange and hydroxyapatite chromatography, ultrafiltration, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mtant enzymes in Escherichia coli strain JM109
-
gene XO, DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes, genotyping, expression in COS-7 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
the enzyme activity detection in sepsis can be used for a negative prognosis in sepsis diagnosis, overview
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Krenitsky, T.A.; Spector, T.; Hall, W.W.
Xanthine oxidase from human liver: purification and characterization
Arch. Biochem. Biophys.
247
108-119
1986
Homo sapiens
Manually annotated by BRENDA team
Radi, R.; Rubbo, H.; Bush, K.; Freeman, B.A.
Xanthine oxidase binding to glycosaminoglycans: kinetics and superoxide dismutase interactions of immobilized xanthine oxidase-heparin complexes
Arch. Biochem. Biophys.
339
125-135
1997
Homo sapiens
Manually annotated by BRENDA team
Pritsos, C.A.
Cellular distribution, metabolism and regulation of the xanthine oxidoreductase enzyme system
Chem. Biol. Interact.
129
195-208
2000
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Zikakis, J.P.; Dressel, M.A.; Silver, M.R.
Bovine, caprine, and human milk xanthine oxidases: isolation, purification, and characterization
Instrum. Anal. Foods, Recent Prog. (Proc. Symp. Int. Flavor Conf. , 3rd Ed. , Charalambous, G. , Inglett, G. , eds. )
2
243-303
1983
Bos taurus, Canis lupus familiaris, Capra hircus, Cavia porcellus, Oryctolagus cuniculus, Equus asinus, Equus caballus, Erythrocebus patas, Felis catus, Ovis aries, Homo sapiens, Mus musculus, Rattus norvegicus, Erythrocebus patas Patas monkey
-
Manually annotated by BRENDA team
Griguer, C.E.; Oliva, C.R.; Kelley, E.E.; Giles, G.I.; Lancaster, J.R.; Gillespie, G.Y.
Xanthine oxidase-dependent regulation of hypoxia-inducible factor in cancer cells
Cancer Res.
66
2257-2263
2006
Homo sapiens
Manually annotated by BRENDA team
Yamaguchi, Y.; Matsumura, T.; Ichida, K.; Okamoto, K.; Nishino, T.
Human Xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: roles of active site residues in binding and activation of purine substrate
J. Biochem.
141
513-524
2007
Homo sapiens
Manually annotated by BRENDA team
Kalra, S.; Paul, M.K.; Balaram, H.; Mukhopadhyay, A.K.
Application of HPLC to study the kinetics of a branched bi-enzyme system consisting of hypoxanthine-guanine phosphoribosyltransferase and xanthine oxidase - an important biochemical system to evaluate the efficiency of the anticancer drug 6-mercaptopurine
J. Chromatogr. B
850
7-14
2007
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Akcam, M.; Elmas, O.; Yilmaz, A.; Caglar, S.; Artan, R.; Gelen, T.; Aliciguezel, Y.
Myeloperoxidase, xanthine oxidase and superoxide dismutase in the gastric mucosa of Helicobacter pylori positive and negative pediatric patients
Mol. Cell. Biochem.
290
125-130
2006
Homo sapiens
Manually annotated by BRENDA team
Landmesser, U.; Spiekermann, S.; Preuss, C.; Sorrentino, S.; Fischer, D.; Manes, C.; Mueller, M.; Drexler, H.
Angiotensin II induces endothelial xanthine oxidase activation: role for endothelial dysfunction in patients with coronary disease
Arterioscler. Thromb. Vasc. Biol.
27
943-948
2007
Homo sapiens
Manually annotated by BRENDA team
Begas, E.; Kouvaras, E.; Tsakalof, A.; Papakosta, S.; Asprodini, E.K.
In vivo evaluation of CYP1A2, CYP2A6, NAT-2 and xanthine oxidase activities in a Greek population sample by the RP-HPLC monitoring of caffeine metabolic ratios
Biomed. Chromatogr.
21
190-200
2007
Homo sapiens
Manually annotated by BRENDA team
Hsieh, J.F.; Wu, S.H.; Yang, Y.L.; Choong, K.F.; Chen, S.T.
The screening and characterization of 6-aminopurine-based xanthine oxidase inhibitors
Bioorg. Med. Chem.
15
3450-3456
2007
Homo sapiens
Manually annotated by BRENDA team
George, J.; Struthers, A.D.
The role of urate and xanthine oxidase inhibitors in cardiovascular disease
Cardiovasc. Ther.
26
59-64
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Huang, X.F.; Li, H.Q.; Shi, L.; Xue, J.Y.; Ruan, B.F.; Zhu, H.L.
Synthesis of resveratrol analogues, and evaluation of their cytotoxic and xanthine oxidase inhibitory activities
Chem. Biodivers.
5
636-642
2008
Homo sapiens
Manually annotated by BRENDA team
Luchtemberg, M.N.; Petronilho, F.; Constantino, L.; Gelain, D.P.; Andrades, M.; Ritter, C.; Moreira, J.C.; Streck, E.L.; Dal-Pizzol, F.
Xanthine oxidase activity in patients with sepsis
Clin. Biochem.
41
1186-1190
2008
Homo sapiens
Manually annotated by BRENDA team
Gupta, S.; Rodrigues, L.M.; Esteves, A.P.; Oliveira-Campos, A.M.; Nascimento, M.S.; Nazareth, N.; Cidade, H.; Neves, M.P.; Fernandes, E.; Pinto, M.; Cerqueira, N.M.; Bras, N.
Synthesis of N-aryl-5-amino-4-cyanopyrazole derivatives as potent xanthine oxidase inhibitors
Eur. J. Med. Chem.
43
771-780
2008
Homo sapiens
Manually annotated by BRENDA team
Shin, M.H.; Moon, Y.J.; Seo, J.E.; Lee, Y.; Kim, K.H.; Chung, J.H.
Reactive oxygen species produced by NADPH oxidase, xanthine oxidase, and mitochondrial electron transport system mediate heat shock-induced MMP-1 and MMP-9 expression
Free Radic. Biol. Med.
44
635-645
2008
Homo sapiens
Manually annotated by BRENDA team
Aranda, R.; Domenech, E.; Rus, A.D.; Real, J.T.; Sastre, J.; Vina, J.; Pallardo, F.V.
Age-related increase in xanthine oxidase activity in human plasma and rat tissues
Free Radic. Res.
41
1195-1200
2007
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Khosravan, R.; Kukulka, M.J.; Wu, J.T.; Joseph-Ridge, N.; Vernillet, L.
The effect of age and gender on pharmacokinetics, pharmacodynamics, and safety of febuxostat, a novel nonpurine selective inhibitor of xanthine oxidase
J. Clin. Pharmacol.
48
1014-1024
2008
Homo sapiens
Manually annotated by BRENDA team
Matesanz, N.; Lafuente, N.; Azcutia, V.; Martin, D.; Cuadrado, A.; Nevado, J.; Rodriguez-Manas, L.; Sanchez-Ferrer, C.F.; Peiro, C.
Xanthine oxidase-derived extracellular superoxide anions stimulate activator protein 1 activity and hypertrophy in human vascular smooth muscle via c-Jun N-terminal kinase and p38 mitogen-activated protein kinases
J. Hypertens.
25
609-618
2007
Homo sapiens
Manually annotated by BRENDA team
Mostefai, H.A.; Agouni, A.; Carusio, N.; Mastronardi, M.L.; Heymes, C.; Henrion, D.; Andriantsitohaina, R.; Martinez, M.C.
Phosphatidylinositol 3-kinase and xanthine oxidase regulate nitric oxide and reactive oxygen species productions by apoptotic lymphocyte microparticles in endothelial cells
J. Immunol.
180
5028-5035
2008
Homo sapiens
Manually annotated by BRENDA team
Kudo, M.; Moteki, T.; Sasaki, T.; Konno, Y.; Ujiie, S.; Onose, A.; Mizugaki, M.; Ishikawa, M.; Hiratsuka, M.
Functional characterization of human xanthine oxidase allelic variants
Pharmacogenet. Genomics
18
243-251
2008
Homo sapiens
Manually annotated by BRENDA team
Mittal, A.; Phillips, A.R.; Loveday, B.; Windsor, J.A.
The potential role for xanthine oxidase inhibition in major intra-abdominal surgery
World J. Surg.
32
288-295
2008
Felis silvestris, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Mukoyoshi, M.; Nishimura, S.; Hoshide, S.; Umeda, S.; Kanou, M.; Taniguchi, K.; Muroga, H.
In vitro drug-drug interaction studies with febuxostat, a novel non-purine selective inhibitor of xanthine oxidase: plasma protein binding, identification of metabolic enzymes and cytochrome P450 inhibition
Xenobiotica
38
496-510
2008
Homo sapiens
Manually annotated by BRENDA team
Iswantini, D.; Darusman, L.; Hidayat, R.
Indonesian Sidaguri (Sida rhombifolia L.) as antigout and inhibition kinetics of flavonoids crude extract on the activity of xanthine oxidase
J. Biol. Sci.
9
504-508
2009
Homo sapiens
-
Manually annotated by BRENDA team
Naoghare, P.K.; Kwon, H.T.; Song, J.M.
On-chip assay for determining the inhibitory effects and modes of action of drugs against xanthine oxidase
J. Pharm. Biomed. Anal.
51
1-6
2010
Homo sapiens
Manually annotated by BRENDA team
Boumerfeg, S.; Baghiani, A.; Messaoudi, D.; Khennouf, S.; Arrar, L.
Antioxidant properties and xanthine oxidase inhibitory effects of Tamus communis L. root extracts
Phytother. Res.
23
283-288
2009
Bos taurus, Ovis aries, Homo sapiens
Manually annotated by BRENDA team
Dai, Y.; Cao, Y.; Zhang, Z.; Vallurupalli, S.; Mehta, J.L.
Xanthine oxidase induces foam cell formation through LOX-1 and NLRP3 activation
Cardiovasc. Drugs Ther.
31
19-27
2017
Homo sapiens
Manually annotated by BRENDA team
Lopez-Cruz, R.I.; Perez-Milicua, M.B.; Crocker, D.E.; Gaxiola-Robles, R.; Bernal-Vertiz, J.A.; de la Rosa, A.; Vazquez-Medina, J.P.; Zenteno-Savin, T.
Purine nucleoside phosphorylase and xanthine oxidase activities in erythrocytes and plasma from marine, semiaquatic and terrestrial mammals
Comp. Biochem. Physiol. A
171
31-35
2014
Tursiops truncatus, Lontra longicaudis annectens, Sus scrofa (F1S3Y7), Mirounga angustirostris (H9A5F8), Mirounga angustirostris, Homo sapiens (P47989), Homo sapiens
Manually annotated by BRENDA team