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Information on EC 1.17.3.2 - xanthine oxidase and Organism(s) Bos taurus and UniProt Accession P80457

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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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Bos taurus
UNIPROT: P80457
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The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
hide
xanthine
+
H2O
+
O2
=
urate
+
H2O2
+
+
=
+
Synonyms
xo, hypoxanthine-xanthine oxidase, xanthine:xanthine oxidase, xanthine:oxygen oxidoreductase, xanthine oxygen oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hypoxanthine oxidase
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hypoxanthine-xanthine oxidase
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hypoxanthine:oxygen oxidoreductase
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oxidase, xanthine
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Schardinger enzyme
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xanthine oxidase
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xanthine oxidoreductase
xanthine:O2 oxidoreductase
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xanthine:xanthine oxidase
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XnOx
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-
additional information
-
XOR can adopt its XOR xanthone oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
xanthine + H2O + O2 = urate + H2O2
show the reaction diagram
reaction mechanism for xanthine oxidase, overview. Catalysis is initiated by base-assisted nucleophilic attack of the equatorial Mo-OH on the C-8 carbon of xanthine with concomitant hydride transfer from C-8 to Mo=S, which simultaneously results in reduction of Mo(VI) to Mo(IV). Reoxidation of the molybdenum center occurs by electron transfer to the other redox-active centers of the enzyme, accompanied by deprotonation of the Mo-SH bond and displacement of bound product by hydroxide from solvent to regenerate the Mo-OH group
xanthine + H2O + O2 = urate + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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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
6,8-dihydroxypurine + H2O + O2
? + H2O2
show the reaction diagram
6,8-dihydroxypurine binding structure, overview
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
hypoxanthine binding structure, overview
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages + H2O + O2
?
show the reaction diagram
-
-
-
-
r
1,3-dimethylxanthine + H2O + O2
1,3-dimethylurate + H2O2
show the reaction diagram
-
-
-
-
?
1,7-dimethylxanthine + H2O + O2
1,7-dimethylurate + H2o2
show the reaction diagram
-
-
-
-
?
1-methyl-2-hydroxypurine + H2O + O2
1-methyl-2-hydroxy-7,9-dihydropurin-8-one + H2O2
show the reaction diagram
-
-
-
?
1-methylxanthine + H2O + O2
1-methylurate + H2O2
show the reaction diagram
2,3-dihydroxybenzaldehyde + H2O + O2
2,3-dihydroxybenzoate + H2O2
show the reaction diagram
-
-
-
?
2,5-dihydroxybenzaldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
?
2,6-diaminopurine + H2O + O2
2,6-diamino-7,9-dihydro-8H-purin-8-one
show the reaction diagram
-
-
-
-
?
2-amino-4-hydroxypterin + H2O + O2
? + H2O2
show the reaction diagram
-
substrate inhibition kinetic pattern
-
-
?
2-amino-6-chloro-purine + H2O + O2
2-amino-6-chloro-7,9-dihydro-purin-8-one + H2O2
show the reaction diagram
-
-
-
-
?
2-hydroxybenzaldehyde + H2O + O2
2-hydroxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
2-mercaptopurine + H2O + O2
8-hydroxy-2-mercaptopurine + H2O2
show the reaction diagram
-
no conversion to 2-thioxanthine
-
-
?
2-methoxybenzaldehyde + H2O + O2
2-methoxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
2-methylbenzaldehyde + H2O + O2
2-methylbenzoate + H2O2
show the reaction diagram
-
-
-
-
?
2-nitrobenzaldehyde + H2O + O2
2-nitrobenzoate + H2O2
show the reaction diagram
-
-
-
-
?
2-oxo-6-methylpurine + H2O + O2
? + H2O2
show the reaction diagram
-
low activity
-
-
?
2-thioxanthine + H2O + O2
2-thiourate + H2O2
show the reaction diagram
-
-
-
-
?
2-thioxanthine + H2O + O2
2-thiouric acid + H2O2
show the reaction diagram
-
-
-
-
?
3,4-dihydroxybenzaldehyde + H2O + O2
3,4-dihydroxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
3,4-dimethoxybenzaldehyde + H2O + O2
3,4-dimethoxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
3-hydroxy-4-methoxybenzaldehyde + H2O + O2
3-hydroxy-4-methoxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
3-hydroxybenzaldehyde + H2O + O2
3-hydroxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
3-methoxybenzaldehyde + H2O + O2
3-methoxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
3-methylbenzaldehyde + H2O + O2
3-methylbenzoate + H2O2
show the reaction diagram
-
-
-
-
?
3-methylhypoxanthine + H2O + O2
3-methylxanthine + H2O2
show the reaction diagram
-
-
-
?
3-methylxanthine + H2O + O2
3-methylurate + H2O2
show the reaction diagram
-
-
-
-
?
3-nitrobenzaldehyde + H2O + O2
3-nitrobenzoate + H2O2
show the reaction diagram
-
-
-
-
?
4-hydroxy-3-methoxybenzaldehyde + H2O + O2
4-hydroxy-3-methoxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
4-hydroxybenzaldehyde + H2O + O2
4-hydroxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
4-hydroxyphenylglycoaldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
?
4-methoxybenzaldehyde + H2O + O2
4-methoxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
4-methylbenzaldehyde + H2O + O2
4-methylbenzoate + H2O2
show the reaction diagram
-
-
-
-
?
4-nitrobenzaldehyde + H2O + O2
4-nitrobenzoate + H2O2
show the reaction diagram
-
-
-
-
?
5-chloro-6-[(2-iminopyrrolidin-1-yl)methyl]-3H-pyrimidin-4-one + H2O + O2
?
show the reaction diagram
-
-
-
-
?
6,8-dihydroxypurine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
6-amino-5-bromo-1H-pyrimidin-2-one + H2O + O2
?
show the reaction diagram
-
-
-
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?
6-amino-5-bromo-3H-pyrimidin-4-one + H2O + O2
?
show the reaction diagram
-
-
-
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?
6-amino-5-bromopyrimidine + H2O + O2
?
show the reaction diagram
-
-
-
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?
6-cyanopurine + H2O + O2
6-cyano-7,9-dihydropurine-8-one
show the reaction diagram
-
-
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?
6-formylpterin + H2O + O2
?
show the reaction diagram
-
-
-
-
?
6-formylpterin + H2O + O2
? + H2O2
show the reaction diagram
-
-
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
show the reaction diagram
6-mercaptopurine + H2O + O2
?
show the reaction diagram
-
an anticancer drug
-
-
?
6-thioxanthine + H2O + O2
6-thiourate + H2O2
show the reaction diagram
6-thioxanthine + H2O + O2
6-thiouric acid + H2O2
show the reaction diagram
-
-
-
-
?
7-alkylpteridin-4-one + H2O + O2
7-alkyllumazine + H2O2
show the reaction diagram
-
-
-
?
7-methylxanthine + H2O + O2
7-methylurate + H2O2
show the reaction diagram
-
-
-
-
?
7-phenylpteridin-4-one + H2O + O2
7-phenyllumazine + H2O2
show the reaction diagram
-
-
-
?
7H-pyrrolo[2,3-d]pyrimidin-2(1H)-one + H2O + O2
?
show the reaction diagram
-
-
-
-
?
7H-pyrrolo[2,3-d]pyrimidin-4(3H)-one + H2O + O2
?
show the reaction diagram
-
-
-
-
?
7H-pyrrolo[2,3-d]pyrimidine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
acetaldehyde + H2O + O2
acetic acid + H2O2
show the reaction diagram
adenine + H2O + O2
6-amino-7,9-dihydropurin-8-one + H2O2
show the reaction diagram
-
-
-
?
adenine + H2O + O2
? + H2O2
show the reaction diagram
-
substrate inhibition kinetic pattern
-
-
?
aldehyde + indophenol
?
show the reaction diagram
-
-
-
-
r
allopurinol + H2O + O2
?
show the reaction diagram
-
-
-
-
?
allopurinol + H2O + O2
oxypurinol + H2O2
show the reaction diagram
-
-
allopurinol is a conventional substrate that generates superoxide radicals during its oxidation
-
?
benzaldehyde + H2O + O2
benzoate + H2O2
show the reaction diagram
-
-
-
-
?
butanal + H2O + O2
butanoate + 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
-
?
dibromoacetonitrile + H2O + O2
?
show the reaction diagram
-
-
-
-
r
formaldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
r
FYX-051 + O2 + H2O
?
show the reaction diagram
-
the structure of bovine XOR exposed to the slow-reacting substrate FYX-051 shows a covalent intermediate of the hydroxylation reaction, in which the hydroxyl oxygen bridged the molybdenumatom and the acceptor carbon atom of the aromatic ring of the substrate
-
-
?
glyceraldehyde-3-phosphate + H2O + O2
?
show the reaction diagram
-
-
-
-
?
glyceryl trinitrate + 2,3-dihydroxybenzaldehyde
?
show the reaction diagram
-
-
-
-
?
glyceryl trinitrate + NADH
? + NAD+ + H2O
show the reaction diagram
-
-
further reaction of organic nitrite with thiols or ascorbate leads to generation of NO or nitrosothiols
-
?
glyceryl trinitrate + xanthine
urate + ?
show the reaction diagram
-
-
-
-
?
guanine + H2O + O2
2-amino-7,9-dihydro-1H-purine-6,8-dione + H2O2
show the reaction diagram
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
indole-3-acetaldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
?
indole-3-aldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
?
isosorbide dinitrate + 2,3-dihydroxybenzaldehyde
?
show the reaction diagram
-
-
-
-
?
isosorbide dinitrate + NADH
? + NAD+ + H2O
show the reaction diagram
-
-
further reaction of organic nitrite with thiols or ascorbate leads to generation of NO or nitrosothiols
-
?
isosorbide dinitrate + xanthine
urate + ?
show the reaction diagram
-
-
-
-
?
lumazine + H2O + O2
? + H2O2
show the reaction diagram
-
classical Michaelis-Menten hyperbolic saturation kinetic pattern
-
-
?
N1-methylnicotinamide + H2O + O2
?
show the reaction diagram
-
-
-
-
?
NADH + H2O + O2
NAD+ + H2O2
show the reaction diagram
NADPH + indophenol
?
show the reaction diagram
-
-
-
-
r
nitrate + 2,3-dihydroxybenzaldehyde
nitrite + ?
show the reaction diagram
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
show the reaction diagram
nitrate + xanthine
nitrite + urate + ?
show the reaction diagram
-
-
-
-
?
nitrite + 2,3-dihydroxybenzaldehyde
NO + ?
show the reaction diagram
-
NO generation occurs under aerobic conditions and is regulated by O2 tension, pH, nitrite, and reducing substrate concentrations
-
-
?
nitrite + NADH
NO + NAD+ + H2O
show the reaction diagram
nitrite + O2 + hypoxanthine
peroxynitrite + ?
show the reaction diagram
-
-
-
-
?
nitrite + O2 + pterin
peroxynitrite + ?
show the reaction diagram
-
-
-
-
?
nitrite + xanthine
NO + ?
show the reaction diagram
o-hydroxybenzaldehyde + H2O + O2
o-hydroxybenzoate + H2O2
show the reaction diagram
-
-
-
?
organic nitrate + NADH
organic nitrite + NAD+ + H2O
show the reaction diagram
-
organic nitrite is the initial product in the process of xanthine oxidase mediated organic nitrate biotransformation and is the precursor of NO and nitrosothiols, serving as the link between organic nitrate and soluble guanylyl cyclase
-
-
?
propanal + H2O + O2
propanoate + H2O2
show the reaction diagram
-
-
-
?
pteridine + H2O + O2
?
show the reaction diagram
pterin + H2O + O2
isoxanthopterin + H2O2
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
-
-
-
-
?
pyridine 3-aldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
r
pyridine-2-aldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
?
pyridine-3-aldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
?
pyridine-4-aldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
?
pyrimidine derivatives + H2O + O2
?
show the reaction diagram
salicylaldehyde + H2O + O2
salicylic acid + H2O2
show the reaction diagram
-
-
-
?
succinate semialdehyde + H2O + O2
succinate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
superoxide + urate + ?
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
xanthine + methylene blue + O2
urate + reduced methylene blue
show the reaction diagram
-
-
-
-
?
xanthine + NO2-
uric acid + NO
show the reaction diagram
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
xanthine + thionine + O2
urate + reduced thionine
show the reaction diagram
-
-
-
-
?
xanthopterin + H2O + O2
?
show the reaction diagram
-
-
-
-
?
xanthopterin + H2O + O2
? + H2O2
show the reaction diagram
-
substrate activation kinetic pattern
-
-
?
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
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
show the reaction diagram
-
-
-
-
?
6-mercaptopurine + H2O + O2
?
show the reaction diagram
-
an anticancer drug
-
-
?
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
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
show the reaction diagram
-
reaction can be an important source of NO production in ischemic tissues
-
-
?
nitrite + NADH
NO + NAD+ + H2O
show the reaction diagram
-
reaction can be an important source of NO production in ischemic tissues
-
-
?
organic nitrate + NADH
organic nitrite + NAD+ + H2O
show the reaction diagram
-
organic nitrite is the initial product in the process of xanthine oxidase mediated organic nitrate biotransformation and is the precursor of NO and nitrosothiols, serving as the link between organic nitrate and soluble guanylyl cyclase
-
-
?
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
?
-
-
during inflammatory conditions, reversible oxidation of critical cysteine residues or limited proteolysis converts xanthine dehydrogenase, XDH, EC 1.17.1.4, to xanthine oxidase, XO, which reduces O2 to superoxide and H2O2. Conversion to XO, however, is not requisite for reactive oxygen species production, as XDH displays partial oxidase activity. Xanthine oxidoreductase generates proinflammatory oxidants and secondary nitrating species, with inhibition of XOR proving beneficial in a variety of disorders
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
molybdenum cofactor
dioxothiomolybdenum cofactor
molybdenum cofactor
molybdopterin
-
one cofactor per subunit, oxidation of xanthine takes place at this center, electrons are rapidly distributed to the other centers by intramolecular electron transfer
NAD+
-
-
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
Cu2+
-
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
Mo4+
-
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(3-(furan-2-yl)-4,5-dihydro-5-(pyridin-4-yl)pyrazol-1-yl)ethanone
-
2,4-dichloro-6-(2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazolin-5-yl)phenol
-
2-(3-phenyl-1H-pyrazol-5-yl)aniline
-
2-(4-chlorophenyl)-5-(3,4-dimethoxyphenyl)-5,6-dihydropyrazolo[1,5-c]quinazoline
-
2-hydroxy-6-methylpurine
interacts with Arg880 in both active sites of the enzyme dimer, binding structure, overview
2-methoxy-4-(2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazolin-5-yl)phenol
-
2-phenylpyrazolo[1,5-c]quinazoline
-
2-[3-(4-chlorophenyl)-1H-pyrazol-5-yl]aniline
-
3,4-dihydroxyphenyl dodecanoate
sigmoidal inhibition of superoxide anion formation
3,4-dihydroxyphenyl octanoate
-
4-(2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazolin-5-yl)benzonitrile
-
4-(2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazolin-5-yl)phenol
-
4-[2-(4-chlorophenyl)-5,6-dihydropyrazolo[1,5-c]quinazolin-5-yl]-2-methoxyphenol
-
4-[2-(4-chlorophenyl)-5,6-dihydropyrazolo[1,5-c]quinazolin-5-yl]phenol
-
5-(1H-indol-3-yl)-2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazoline
-
5-(2-nitrophenyl)-2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazoline
-
5-(3,4-dimethoxyphenyl)-2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazoline
-
5-(3-nitrophenyl)-2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazoline
-
allopurinol
alloxanthine
-
apigenin
binding structure, thermodynamic, and kinetic analysis, computational docking
butyl caffeate
competitive inhibition of urate and superoxide anion formation
caffeic acid
catechin
inhibits at lower concentration
chrysin
strong reversible competitive inhibition, inhibition mechanism. Chrysin interacts with the amino acid residues Leu648, Phe649, Glu802, Leu873,Ser876, Glu879, Arg880, Phe1009, Thr1010, Val1011 and Phe1013 located within the active cavity of the enzyme, insertion of chrysin into the active site occupying the catalytic center of xanthine oxidase to avoid the entrance of xanthine and causing conformational changes in the enzyme. Binding structure, thermodynamic, and kinetic analysis, computational docking. Molecular modeling of enzyme-drug interaction
curcumin
-
decyl caffeate
competitive inhibition of urate and superoxide anion formation
decyl gallate
50% inhibition of urate formation at0.097 mM, 50% inhibition of superoxide anion generation at 0.0039 mM
epicatechin
inhibits at lower concentration
febuxostat
-
gallic acid
50% inhibition of urate formation above 0.2 mM, 50% inhibition of superoxide anion generation at 0.0026 mM
heptyl caffeate
competitive inhibition of urate and superoxide anion formation
hexyl caffeate
competitive inhibition of urate and superoxide anion formation
hexyl gallate
50% inhibition of urate formation above 0.2 mM, 50% inhibition of superoxide anion generation at 0.0052 mM
kaempferol
inhibits at lower concentration
menthyl gallate
50% inhibition of urate formation above 0.2 mM, 50% inhibition of superoxide anion generation at 0.0049 mM
methyl caffeate
competitive inhibition of urate and superoxide anion formation
methyl N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-D-tyrosinate
-
methyl N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-L-tyrosinate
-
methyl N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-D-tryptophanate
-
methyl N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-L-alaninate
-
methyl N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-L-phenylalaninate
-
methyl N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-L-tyrosinate
-
methyl N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-3-(1H-inden-3-yl)-D-alaninate
-
methyl N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-D-tyrosinate
-
methyl N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-L-tyrosinate
-
methyl N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-L-alaninate
-
methyl N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-L-phenylalaninate
-
methyl N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-L-tyrosinate
-
N'-[(E)-(2,4,6-trihydroxyphenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(E)-(2-bromophenyl)methylidene]pyridine-3-carbohydrazide
-
N'-[(E)-(2-fluorophenyl)methylidene]pyridine-3-carbohydrazide
-
N'-[(E)-(2-hydroxy-3-methoxyphenyl)methylidene]pyridine-3-carbohydrazide
-
N'-[(E)-(2-hydroxy-3-methoxyphenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(E)-(2-methylphenyl)methylidene]pyridine-3-carbohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]pyridine-3-carbohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(E)-(3,5-dihydroxyphenyl)methylidene]pyridine-3-carbohydrazide
-
N'-[(E)-(3-chlorophenyl)methylidene]pyridine-3-carbohydrazide
-
N'-[(E)-(3-chlorophenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(E)-(3-ethoxy-2-hydroxyphenyl)methylidene]pyridine-3-carbohydrazide
-
N'-[(E)-(3-ethoxy-2-hydroxyphenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(E)-(3-nitrophenyl)methylidene]pyridine-3-carbohydrazide
-
N'-[(E)-(3-nitrophenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(E)-(4-chlorophenyl)methylidene]pyridine-3-carbohydrazide
-
N'-[(E)-(4-chlorophenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(E)-(4-ethoxyphenyl)methylidene]pyridine-3-carbohydrazide
-
N'-[(E)-(4-ethoxyphenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(E)-(4-hydroxyphenyl)methylidene]pyridine-3-carbohydrazide
-
N'-[(E)-phenylmethylidene]pyridine-3-carbohydrazide
-
N-(1-(3-bromophenyl)-3-(naphthalen-2-yl)-3-oxopropyl)acetamide
-
n-dodecyl gallate
50% inhibition of urate formation at 0.049 mM, 50% inhibition of superoxide anion generation at 0.0036 mM
N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-D-tyrosine
-
N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-L-tyrosine
-
N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-D-tryptophan
-
N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-L-alanine
-
N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-L-phenylalanine
-
N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-L-tyrosine
-
N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-D-tyrosine
-
N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-L-tyrosine
-
N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-L-alanine
-
N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-L-phenylalanine
-
N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-L-tyrosine
-
naringin
about 15% inhibition at 0.045 mM
naringin decanoate
about 24% inhibition at 0.045 mM
naringin hexanoate
about 15% inhibition at 0.045 mM
naringin laurate
below 10% inhibition at 0.045 mM
naringin octanoate
about 26% inhibition at 0.045 mM
naringin oleate
below 10% inhibition at 0.045 mM
octyl gallate
50% inhibition of urate formation at 0.262 mM, 50% inhibition of superoxide anion generation at 0.0045 mM
octyl protocatechuate
competitive inhibition of urate and superoxide anion formation
p-aminobenzamidine
-
pentyl caffeate
competitive inhibition of urate and superoxide anion formation
propyl caffeate
competitive inhibition of urate and superoxide anion formation
propyl gallate
50% inhibition of urate formation above 0.2 mM, 50% inhibition of superoxide anion generation at 0.0064 mM
propyl protocatechuate
sigmoidal inhibition of superoxide anion formation
protocatechuic acid
competitive inhibition of urate and superoxide anion formation
quercetin
salvianolic acid A
-
(E)-9-nitro-octadec-9-en-1-ol
-
slight inhibition
(E)-9-nitro-octadec-9-enoic acid
-
strong inhibition
1,2-Dihydroxybenzene 3,5-disulfonic acid
-
inhibits reaction with cytochrome c
1,3,6,7-tetrahydroxy-9H-xanthen-9-one
-
-
1-(9-ethyl-9H-carbazol-3-yl)-3,4-diphenylazetidin-2-one
-
-
1-(9-ethyl-9H-carbazol-3-yl)-3-phenyl-4-m-totylazetidin-2-one
-
-
1-(9-ethyl-9H-carbazol-3-yl)-3-phenyl-4-p-tolylazetidin-2-one
-
-
1-(9-ethyl-9H-carbazol-3-yl)-4-(2-nitrophenyl)-3-phenylazetidin-2-one
-
-
1-(9-ethyl-9H-carbazol-3-yl)-4-(3-methoxyphenyl)-3-phenylazetidin-2-one
-
-
1-(9-ethyl-9H-carbazol-3-yl)-4-(3-nitrophenyl)-3-phenylazetidin-2-one
-
-
1-(9-ethyl-9H-carbazol-3-yl)-4-(4-fluorophenyl)-3-phenylazetidin-2-one
-
-
1-(9-ethyl-9H-carbazol-3-yl)-4-(4-methoxyphenyl)-3-phenylazetidin-2-one
-
-
1-(9-ethyl-9H-carbazol-3-yl)-4-(4-nitrophenyl)-3-phenylazetidin-2-one
-
-
1-O-(4''-O-caffeoyl)-beta-glucopyranosyl-1,4-dihydroxy-2-(3',3'-dimethylallyl)benzene
-
-
1-[(2,4-dichlorobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
-
-
1-[(2,6-dichlorobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
-
-
1-[(2-bromobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
-
-
1-[(2-chlorobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
-
-
1-[(2-fluorobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
-
-
1-[(3-bromobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
-
-
1-[(3-chlorobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
-
-
1-[(3-fluorobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
-
-
1-[(4-bromobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
-
-
1-[(4-chlorobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
-
-
1-[(4-fluorobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
-
-
1-[3-cyano-4-(2,2-dimethylpropoxy)phenyl]-1H-pyrazole-4-carboxylic acid
-
-
10-nitro-octadec-9,12-dienoic acid
-
-
10-nitro-octadec-9-enoic acid
-
-
12-nitro-octadec-9,12-dienoic acid
-
-
13-nitro-octadec-9,12-dienoic acid
-
-
2,4-Diamino-6-hydroxy-s-triazine
-
-
2,4-dinitrofluorobenzene
-
-
2-(3,4-dihydroxy-5-methoxyphenyl)-5,7-dihydroxy-4H-chromen-4-one
-
competitive, 50% inhibition at 0.00022 mM
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one
-
competitive, 50% inhibition at 0.00124 mM
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-6-methoxy-4H-chromen-4-one
2-Amino-4-hydroxypterine-6-aldehyde
-
-
2-amino-6-hydroxy-8-mercaptopurine
-
mixed-type inhibition, the inhibitor specifically blocks the enzyme activity with the drug 6-mercaptopurine, but does affect activity with xanthine and hypoxanthine to a lesser extent, overview
2-amino-6-purine thiol
-
competitive inhibitor, the inhibitor specifically blocks the enzyme activity with the drug 6-mercaptopurine, but does affect activity with xanthine and hypoxanthine to a lesser extent, overview
2-chloroadenine
-
substrate analogue
2-[(2,3-dimethylphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(2,4-dimethylphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(2-bromophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(2-chlorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(2-fluorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(3-bromophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(3-chlorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(3-fluorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(4-bromophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(4-chloro-3-methylphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(4-chlorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(4-fluorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(4-methoxyphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[3-cyano-4-(2-methylpropoxy)phenyl]-4-methylthiazole-5-carboxylic acid
-
i.e. febuxostat, TEI-6720, or TMX-67, mixed-type inhibition of both the oxidized and reduced form of xanthine oxidase
2-[[(3,6,7-trihydroxy-9-oxo-9H-xanthen-1-yl)oxy]methyl]benzonitrile
-
-
3,3',4,4'-Tetrahydroxychalcone
-
-
3,4-di-O-caffeoylquinic acid methyl ester
-
reversible inhibition, IC50: 0.0036 mM
3,4-Dihydroxybenzaldehyde
-
mixed type inhibition, 50% inhibition at 0.0568 mM
3,5-di-O-caffeoylquinic acid
-
-
3,6,7-trihydroxy-1-[(2-methylbenzyl)oxy]-9H-xanthen-9-one
-
-
3,6,7-trihydroxy-1-[(2-nitrobenzyl)oxy]-9H-xanthen-9-one
-
-
3,6,7-trihydroxy-1-[(3-methylbenzyl)oxy]-9H-xanthen-9-one
-
-
3,6,7-trihydroxy-1-[(3-nitrobenzyl)oxy]-9H-xanthen-9-one
-
-
3,6,7-trihydroxy-1-[(4-methylbenzyl)oxy]-9H-xanthen-9-one
-
-
3,6,7-trihydroxy-1-[(4-nitrobenzyl)oxy]-9H-xanthen-9-one
-
-
3-[[(3,6,7-trihydroxy-9-oxo-9H-xanthen-1-yl)oxy]methyl]benzonitrile
-
-
4,5-di-O-caffeoylquinic acid
-
-
4,5-di-O-caffeoylquinic acid methyl ester
-
reversible inhibition
4-(2-bromophenyl)-1-(9-ethyl-9H-carbazol-3-yl)-3-phenylazetidin-2-one
-
-
4-(3-chlorophenyl)-1-(9-ethyl-9H-carbazol-3-yl)-3-phenylazetidin-2-one
-
-
4-(4-chlorophenyl)-1-(9-ethyl-9H-carbazol-3-yl)-3-phenylazetidin-2-one
-
-
4-iminocyclohexa-2,5-dien-1-one
-
-
4-[[(3,6,7-trihydroxy-9-oxo-9H-xanthen-1-yl)oxy]methyl]benzonitrile
-
-
5,7-dihydroxy-2-(3,4,5-trimethoxyphenyl)-4H-chromen-4-one
-
competitive, 50% inhibition at 0.00051 mM
5,7-dihydroxy-2-(3-hydroxy-4,5-dimethoxyphenyl)-6-methoxy-4H-chromen-4-one
-
competitive, 50% inhibition at 0.00133 mM
5,7-dihydroxy-2-(3-hydroxy-4-methoxyphenyl)-4H-chromen-4-one
-
competitive, 50% inhibition at 0.00013 mM
5,7-dihydroxy-2-(4-hydroxy-3-methoxyphenyl)-3,6-dimethoxy-4H-chromen-4-one
-
competitive, 50% inhibition at 0.00115 mM
5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
-
competitive, 50% inhibition at 0.00036 mM
5,7-dihydroxy-2-(4-methoxyphenyl)-4H-chromen-4-one
-
competitive, 50% inhibition at 0.080016mM
5-(3-cyano-4-isobutoxyphenyl)isoxazole-3-carboxylic acid
-
-
5-(4-benzyloxy-3-cyanophenyl)isoxazole-3-carboxylic acid
-
-
5-(4-benzyloxy-3-nitrophenyl)isoxazole-3-carboxylic acid
-
-
5-(4-isobutoxy-3-nitrophenyl)isoxazole-3-carboxylic acid
-
-
5-[3-cyano-4-(4-methylbenzyloxy)phenyl]-isoxazole-3-carboxylic acid
-
-
5-[4-(4-chlorobenzyloxy)-3-cyanophenyl]isoxazole-3-carboxylic acid
-
-
5-[4-(4-chlorobenzyloxy)-3-nitrophenyl]isoxazole-3-carboxylic acid
-
-
5-[4-(4-methylbenzyloxy)-3-nitrophenyl]isoxazole-3-carboxylic acid
-
-
5-[4-(4-tert-butylbenzyloxy)-3-cyanophenyl]isoxazole-3-carboxylic acid
-
-
5-[4-(4-tert-butylbenzyloxy)-3-nitrophenyl]isoxazole-3-carboxylic acid
-
-
6-(N-benzoylamino)purine
-
competitive, 50% inhibition at 0.00045 mM. Hydrogen bonding interaction involves N7 of the purine ring and N-H of R880, the N-H of the purine ring and OH of T1010
6-formylpterin
-
-
7-methyl-2-(phenoxymethyl)-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
7-methyl-2-[(2-methylphenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
7-methyl-2-[(2-nitrophenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
7-methyl-2-[(3-methylphenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
7-methyl-2-[(3-nitrophenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
7-methyl-2-[(4-methylphenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
7-methyl-2-[(4-nitrophenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
8-bromoxanthine
-
-
9-nitro-octadec-9,12-dienoic acid
-
-
9-nitro-octadec-9-enoic acid
-
strong inhibition
acacetin 7-O-(3-O-acetyl-beta-D-glucopyranoside)
-
flavone glucoside from Chrysanthemum sinense, 50% inhibition at 0.080 mM
aldehydes
-
e.g. formaldehyde, 4-pyridinecarboxaldehyde, propionaldehyde, glycolaldehyde
allopurinol
alloxanthine
-
a mechanism-based inhibitor, binding structure, overview. Inhibition mechanism involves binding to molybdenum, overview
anacardic acid
-
inhibits generation of superoxide radicals by xanthine oxicasein a sigmoidal inhibition, binds to allosteric sites near the xanthine-binding domain in xanthine oxidase
apigenin
-
mixed type inhibition of xanthine, strong inhibitor of xanthine oxidase, weak inhibition of monoamine oxidase
arsenite
-
-
chicoric acid
-
i.e. dicaffeoyltartaric acid
chlorogenic acid
-
i.e. 5-O-caffeoylquinic acid
Cichorium intybus extract
-
leaves from var. silvestre, hydroxycinnamic acids and flavonoids show antioxidant activity, activity and contents of hydroxycinnamic acids and flavonoids decrease by less than 20% during storage of the minimally processed red chicory products, inhibitory compound overview
-
copper
-
-
cyanide
-
-
cyanidin 3-O-(6-O-malonyl-beta-D-glucoside)
-
-
cyanidin-3-O-beta-D-glucoside
-
-
desferrioxamine
-
significant decrease in CN- formation from dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
dimethylthiourea
-
significant decrease in rate of oxidation of dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
diphenylene iodonium
-
inhibits peroxynitrite generation
diphenylene iodonium chloride
dopamine
-
23% inhibition at 1 mM and at 0.1 mM
febuxostat
-
-
folic acid
-
uncompetitive inhibition of oxidation of dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
formaldehyde
genkwanin
-
-
guanine
-
-
hesperetin
-
50% inhibition at 0.039 mM
hydroxychavicol
-
i.e. 4-allyl-1,3-hydroxybenzene, a potent xanthine oxidase inhibitor obtained from the leaves of betel, Piper betle. Structure-activity relationships, the dihydroxyl group is required for the xanthine oxidase inhibitory activity, overview
hydroxylamine
-
-
luteolin
luteolin 7-methyl ether
-
-
luteolin 7-O-beta-D-glucuronide
-
-
mannitol
-
significant decrease in rate of oxidation of dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
methanol
-
-
myoglobin
-
inhibits reaction with cytochrome c as acceptor
-
noradrenaline
-
15% inhibition at 0.1 mM, 30% inhibition at 1 mM
O2
-
competitive inhibitor of NO production
oxypurinol
p-chloromercuribenzoate
-
-
phenylhydrazine
-
-
Pterines
-
or other heterocyclic compounds, which are either not oxidized or oxidized rather slowly
-
Purine-6-aldehyde
-
-
Purines
-
-
-
quercetin
-
competitive inhibition
quercetin 3-O-beta-D-glucoside
-
-
quercetin 3-O-beta-D-glucuronide
-
-
salicylate
-
-
Semicarbazide
-
-
silibinin
-
a mixed-type, not-time-dependent inhibitor
Superoxide dismutase
-
inhibits peroxynitrite generation
-
theaflavin-3,3'-di-O-gallate
-
50% inhibition at 0.049 mM
Trolox
-
a radical scavenger compound
Urea
-
-
xanthine
-
at high concentrations
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetonitrile
-
-
ascorbate
-
in absence of thiols or ascorbate, no NO generation is detected from xanthine oxidase mediated organic nitrate reduction
dimethylformamide
-
highly stimulating
dioxane
-
-
diphenylene iodonium chloride
-
strongly inhibits xanthine oxidase mediated NO generation with NADH serving as reducing substrate, with xanthine or 2,3-dihydroxybenzaldehyde as reducing substrates, NO generation is increased more than six times
dithiothreitol
-
enhance oxidation of dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
ethanol
-
-
glutathione
-
enhances oxidation of dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
L-cysteine
-
in absence of thiols or ascorbate, no NO generation is detected from xanthine oxidase mediated organic nitrate reduction
methanol
-
slightly stimulating
N-acetyl-L-Cys
-
enhance oxidation of dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
Propanol
-
slightly stimulating
tetrahydrofuran
-
-
thiol
-
in absence of thiols or ascorbate, no NO generation is detected from xanthine oxidase mediated organic nitrate reduction
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
xanthine
pH 7.4, 37°C
0.17
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
-
-
0.0298
1H-pyrrolo[2,3-d]pyrimidin-2-ol
-
substrate and inhibitor compound
0.0253 - 0.035
2,3-Dihydroxybenzaldehyde
0.068
2,5-dihydroxybenzaldehyde
-
-
0.19
2-Hydroxybenzaldehyde
-
-
0.00088
2-mercaptopurine
-
25°C
0.19
2-Methoxybenzaldehyde
-
-
0.03
2-Methylbenzaldehyde
-
pH 7.0
0.01
2-nitrobenzaldehyde
-
pH 7.0
0.00047
2-Thioxanthine
-
25°C
0.039
3,4-Dihydroxybenzaldehyde
-
-
0.68
3,4-dimethoxybenzaldehyde
-
-
0.0451
3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
substrate and inhibitor compound
0.18
3-Hydroxy-4-methoxybenzaldehyde
-
-
0.18
3-Hydroxybenzaldehyde
-
-
0.024
3-methylbenzaldehyde
-
pH 7.0
0.001
3-Nitrobenzaldehyde
-
pH 7.0
0.12
4-hydroxy-3-methoxybenzaldehyde
-
-
0.17
4-hydroxybenzaldehyde
-
-
0.56
4-Hydroxyphenylglycolaldehyde
-
-
0.17
4-methoxybenzaldehyde
-
-
0.04
4-methylbenzaldehyde
-
pH 7.0
0.011
4-nitrobenzaldehyde
-
pH 7.0
0.0649
5-chloro-6-[(2-iminopyrrolidin-1-yl)methyl]-3H-pyrimidin-4-one
-
substrate and inhibitor compound
0.0325
6-amino-5-bromo-1H-pyrimidin-2-one
-
-
0.0238
6-amino-5-bromo-3H-pyrimidin-4-one
-
-
0.0444
6-amino-5-bromopyrimidine
-
-
0.002
6-Mercaptopurine
-
25°C
0.00046
6-Thioxanthine
-
25°C
0.0672
7H-pyrrolo[2,3-d]pyrimidine
-
substrate and inhibitor compound
130
acetaldehyde
-
-
20
aldehyde
-
cofactor 2,6-dichlorophenolindophenol
0.3
benzaldehyde
-
-
142
Butyraldehyde
-
-
97
dibromoacetonitrile
-
-
161.5
formaldehyde
-
-
2
glyceraldehyde 3-phosphate
-
-
0.49
glyceryl trinitrate
-
xanthine as cosubstrate
0.022 - 0.0475
hypoxanthine
0.3
Indole-3-acetaldehyde
-
-
0.085
Indole-3-aldehyde
-
-
1.64
isosorbide dinitrate
-
xanthine as cosubstrate
0.000077
methylene blue
-
pH 6.5
0.86 - 0.878
NADH
0.0005
NADPH
-
cofactor 2,6-dichlorophenolindophenol
0.04 - 1.2
nitrite
2.25
NO2-
-
-
1.03
o-hydroxybenzaldehyde
-
-
0.026 - 0.1
O2
430
propionaldehyde
-
-
0.0015 - 0.036
pterin
0.046
pyridine 3-aldehyde
-
-
0.36
Pyridine-2-aldehyde
-
-
1.7
Pyridine-4-aldehyde
-
-
1
succinate semialdehyde
-
-
0.000325
thionine
-
pH 6.5
0.00146 - 6.8
xanthine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.98
2-mercaptopurine
-
25°C
3.32
2-Thioxanthine
-
25°C
0.13
6-Mercaptopurine
-
25°C
2.76
6-Thioxanthine
-
25°C
4.35
hypoxanthine
-
cofactor 2,6-dichlorophenolindophenol
1.28 - 2.57
NADPH
1.16 - 108
xanthine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00015
2-(3,4-dihydroxy-5-methoxyphenyl)-5,7-dihydroxy-4H-chromen-4-one
-
pH 7.5, 25°C
0.0009
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one
-
pH 7.5, 25°C
0.00011 - 0.00015
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-6-methoxy-4H-chromen-4-one
0.00096 - 0.00624
2-amino-6-hydroxy-8-mercaptopurine
0.0013 - 0.0066
2-amino-6-purine thiol
0.0000006 - 0.0000031
2-[3-cyano-4-(2-methylpropoxy)phenyl]-4-methylthiazole-5-carboxylic acid
0.0031
3,4-di-O-caffeoylquinic acid methyl ester
-
25°C
0.0399
3,4-Dihydroxybenzaldehyde
-
pH 7.5, 25°C
0.00024
4,5-di-O-caffeoylquinic acid methyl ester
-
25°C
0.00037
5,7-dihydroxy-2-(3,4,5-trimethoxyphenyl)-4H-chromen-4-one
-
pH 7.5, 25°C
0.00102
5,7-dihydroxy-2-(3-hydroxy-4,5-dimethoxyphenyl)-6-methoxy-4H-chromen-4-one
-
pH 7.5, 25°C
0.00012
5,7-dihydroxy-2-(3-hydroxy-4-methoxyphenyl)-4H-chromen-4-one
-
pH 7.5, 25°C
0.00079
5,7-dihydroxy-2-(4-hydroxy-3-methoxyphenyl)-3,6-dimethoxy-4H-chromen-4-one
-
pH 7.5, 25°C
0.00028
5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
-
pH 7.5, 25°C
0.00011
5,7-dihydroxy-2-(4-methoxyphenyl)-4H-chromen-4-one
-
pH 7.5, 25°C
0.0000475
6-(N-benzoylamino)purine
-
25°C, pH 7.5
0.000094
6-formylpterin
-
-
0.4
8-bromoxanthine
-
25°C, pH 7.5
0.0538
acacetin 7-O-(3-O-acetyl-beta-D-glucopyranoside)
-
pH 7.5, 25°C
0.0018
allopurinol
-
pH 7.5, 25°C
0.0019
luteolin
-
pH 7.4, 25°C
0.0012
quercetin
-
pH 7.4, 25°C
0.08
xanthine
-
-
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011
2,4-dichloro-6-(2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazolin-5-yl)phenol
Bos taurus
pH 7.5, 22°C
0.0417
2-(3-phenyl-1H-pyrazol-5-yl)aniline
Bos taurus
pH 7.5, 22°C
0.2 - 92.5
3,4-dihydroxyphenyl dodecanoate
0.2
3,4-dihydroxyphenyl octanoate
Bos taurus
above, pH 10.0, 25°C, inhibition of urate formation
0.0437
5-(3,4-dimethoxyphenyl)-2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazoline
Bos taurus
pH 7.5, 22°C
0.021
5-(3-nitrophenyl)-2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazoline
Bos taurus
pH 7.5, 22°C
0.00293 - 0.0316
allopurinol
0.00357
apigenin
Bos taurus
pH 7.4, 37°C
0.026 - 110
butyl caffeate
0.0115 - 0.2
caffeic acid
0.00126
chrysin
Bos taurus
pH 7.4, 37°C
0.01 - 0.0164
decyl caffeate
0.0076 - 0.0125
heptyl caffeate
0.0108 - 0.019
hexyl caffeate
0.012 - 0.143
methyl caffeate
0.004
methyl N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-D-tyrosinate
Bos taurus
pH not specified in the publication, 37°C
0.0099
methyl N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-L-tyrosinate
Bos taurus
pH not specified in the publication, 37°C
0.0317
methyl N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-D-tryptophanate
Bos taurus
pH not specified in the publication, 37°C
0.0108
methyl N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-L-alaninate
Bos taurus
pH not specified in the publication, 37°C
0.0149
methyl N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-L-phenylalaninate
Bos taurus
pH not specified in the publication, 37°C
0.0135
methyl N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-L-tyrosinate
Bos taurus
pH not specified in the publication, 37°C
0.06
methyl N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-3-(1H-inden-3-yl)-D-alaninate
Bos taurus
above, pH not specified in the publication, 37°C
0.06
methyl N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-D-tyrosinate
Bos taurus
above, pH not specified in the publication, 37°C
0.06
methyl N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-L-tyrosinate
Bos taurus
above, pH not specified in the publication, 37°C
0.06
methyl N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-L-alaninate
Bos taurus
above, pH not specified in the publication, 37°C
0.06
methyl N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-L-phenylalaninate
Bos taurus
above, pH not specified in the publication, 37°C
0.06
methyl N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-L-tyrosinate
Bos taurus
above, pH not specified in the publication, 37°C
0.0009
N'-[(E)-(2,4,6-trihydroxyphenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.198
N'-[(E)-(2-bromophenyl)methylidene]pyridine-3-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.174
N'-[(E)-(2-fluorophenyl)methylidene]pyridine-3-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.1755
N'-[(E)-(2-hydroxy-3-methoxyphenyl)methylidene]pyridine-3-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.021
N'-[(E)-(2-hydroxy-3-methoxyphenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.18
N'-[(E)-(2-methylphenyl)methylidene]pyridine-3-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.01
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]pyridine-3-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.0124
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.161
N'-[(E)-(3,5-dihydroxyphenyl)methylidene]pyridine-3-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.205
N'-[(E)-(3-chlorophenyl)methylidene]pyridine-3-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.206
N'-[(E)-(3-chlorophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.264
N'-[(E)-(3-ethoxy-2-hydroxyphenyl)methylidene]pyridine-3-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.055
N'-[(E)-(3-ethoxy-2-hydroxyphenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.184
N'-[(E)-(3-nitrophenyl)methylidene]pyridine-3-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.174
N'-[(E)-(3-nitrophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.195
N'-[(E)-(4-chlorophenyl)methylidene]pyridine-3-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.179
N'-[(E)-(4-chlorophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.242
N'-[(E)-(4-ethoxyphenyl)methylidene]pyridine-3-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.33
N'-[(E)-(4-ethoxyphenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.184
N'-[(E)-(4-hydroxyphenyl)methylidene]pyridine-3-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.0211
N'-[(E)-phenylmethylidene]pyridine-3-carbohydrazide
Bos taurus
pH 7.4, 30°C
0.0121
N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-D-tyrosine
Bos taurus
pH not specified in the publication, 37°C
0.0048
N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-L-tyrosine
Bos taurus
pH not specified in the publication, 37°C
0.005
N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-D-tryptophan
Bos taurus
pH not specified in the publication, 37°C
0.0064
N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-L-alanine
Bos taurus
pH not specified in the publication, 37°C
0.00604
N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-L-phenylalanine
Bos taurus
pH not specified in the publication, 37°C
0.0045
N-[(2E)-3-[2-(3,4-dihydroxyphenyl)-7-hydroxy-1-benzofuran-4-yl]prop-2-enoyl]-L-tyrosine
Bos taurus
pH not specified in the publication, 37°C
0.06
N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-D-tyrosine
Bos taurus
above, pH not specified in the publication, 37°C
0.06
N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-3-hydroxy-L-tyrosine
Bos taurus
above, pH not specified in the publication, 37°C
0.06
N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-L-alanine
Bos taurus
above, pH not specified in the publication, 37°C
0.06
N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-L-phenylalanine
Bos taurus
above, pH not specified in the publication, 37°C
0.06
N-[(2E)-3-[2-(3,4-dimethoxyphenyl)-7-methoxy-1-benzofuran-4-yl]prop-2-enoyl]-L-tyrosine
Bos taurus
above, pH not specified in the publication, 37°C
0.11751
naringin decanoate
Bos taurus
pH 7.4, 37°C
0.11035
naringin octanoate
Bos taurus
pH 7.4, 37°C
0.082 - 0.125
octyl protocatechuate
0.01 - 0.018
pentyl caffeate
0.0115 - 0.03
propyl caffeate
0.0627 - 0.125
propyl protocatechuate
0.022 - 0.125
protocatechuic acid
0.0083
salvianolic acid A
Bos taurus
above, pH not specified in the publication, 37°C
0.02173
1,3,6,7-tetrahydroxy-9H-xanthen-9-one
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.03477
1-(9-ethyl-9H-carbazol-3-yl)-3,4-diphenylazetidin-2-one
Bos taurus
-
pH 7.6, 37°C
0.0367
1-(9-ethyl-9H-carbazol-3-yl)-3-phenyl-4-m-totylazetidin-2-one
Bos taurus
-
pH 7.6, 37°C
0.04742
1-(9-ethyl-9H-carbazol-3-yl)-3-phenyl-4-p-tolylazetidin-2-one
Bos taurus
-
pH 7.6, 37°C
0.03037
1-(9-ethyl-9H-carbazol-3-yl)-4-(2-nitrophenyl)-3-phenylazetidin-2-one
Bos taurus
-
pH 7.6, 37°C
0.03808
1-(9-ethyl-9H-carbazol-3-yl)-4-(3-methoxyphenyl)-3-phenylazetidin-2-one
Bos taurus
-
pH 7.6, 37°C
0.0244
1-(9-ethyl-9H-carbazol-3-yl)-4-(3-nitrophenyl)-3-phenylazetidin-2-one
Bos taurus
-
pH 7.6, 37°C
0.04124
1-(9-ethyl-9H-carbazol-3-yl)-4-(4-fluorophenyl)-3-phenylazetidin-2-one
Bos taurus
-
pH 7.6, 37°C
0.0316
1-(9-ethyl-9H-carbazol-3-yl)-4-(4-methoxyphenyl)-3-phenylazetidin-2-one
Bos taurus
-
pH 7.6, 37°C
0.0327
1-(9-ethyl-9H-carbazol-3-yl)-4-(4-nitrophenyl)-3-phenylazetidin-2-one
Bos taurus
-
pH 7.6, 37°C
0.00641
1-[(2-chlorobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.02006
1-[(4-bromobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.0047
1-[(4-chlorobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.00054 - 0.0177
2-amino-6-hydroxy-8-mercaptopurine
0.0026 - 0.0164
2-amino-6-purine thiol
0.0018
2-[(2,4-dimethylphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Bos taurus
-
pH 7.5, temperature not specified in the publication
0.000603
2-[(2-bromophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Bos taurus
-
pH 7.5, temperature not specified in the publication
0.00165
2-[(2-chlorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Bos taurus
-
pH 7.5, temperature not specified in the publication
0.000634
2-[(4-chloro-3-methylphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Bos taurus
-
pH 7.5, temperature not specified in the publication
0.000461
2-[(4-chlorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Bos taurus
-
pH 7.5, temperature not specified in the publication
0.000269
2-[(4-methoxyphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Bos taurus
-
pH 7.5, temperature not specified in the publication
0.0036
3,4-di-O-caffeoylquinic acid methyl ester
Bos taurus
-
reversible inhibition, IC50: 0.0036 mM
0.00708
3,6,7-trihydroxy-1-[(2-methylbenzyl)oxy]-9H-xanthen-9-one
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.01356
3,6,7-trihydroxy-1-[(3-methylbenzyl)oxy]-9H-xanthen-9-one
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.00573
3,6,7-trihydroxy-1-[(4-methylbenzyl)oxy]-9H-xanthen-9-one
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.05804
4-(2-bromophenyl)-1-(9-ethyl-9H-carbazol-3-yl)-3-phenylazetidin-2-one
Bos taurus
-
pH 7.6, 37°C
0.0386
4-(3-chlorophenyl)-1-(9-ethyl-9H-carbazol-3-yl)-3-phenylazetidin-2-one
Bos taurus
-
pH 7.6, 37°C
0.0216
4-(4-chlorophenyl)-1-(9-ethyl-9H-carbazol-3-yl)-3-phenylazetidin-2-one
Bos taurus
-
pH 7.6, 37°C
0.00467
4-[[(3,6,7-trihydroxy-9-oxo-9H-xanthen-1-yl)oxy]methyl]benzonitrile
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.00036
5-(3-cyano-4-isobutoxyphenyl)isoxazole-3-carboxylic acid
Bos taurus
-
pH 7.5, 25°C
0.00059
5-(4-benzyloxy-3-cyanophenyl)isoxazole-3-carboxylic acid
Bos taurus
-
pH 7.5, 25°C
0.00097
5-(4-benzyloxy-3-nitrophenyl)isoxazole-3-carboxylic acid
Bos taurus
-
pH 7.5, 25°C
0.001
5-(4-isobutoxy-3-nitrophenyl)isoxazole-3-carboxylic acid
Bos taurus
-
pH 7.5, 25°C
0.00063
5-[4-(4-chlorobenzyloxy)-3-cyanophenyl]isoxazole-3-carboxylic acid
Bos taurus
-
pH 7.5, 25°C
0.00283
5-[4-(4-chlorobenzyloxy)-3-nitrophenyl]isoxazole-3-carboxylic acid
Bos taurus
-
pH 7.5, 25°C
0.00101
5-[4-(4-tert-butylbenzyloxy)-3-cyanophenyl]isoxazole-3-carboxylic acid
Bos taurus
-
pH 7.5, 25°C
0.01275
5-[4-(4-tert-butylbenzyloxy)-3-nitrophenyl]isoxazole-3-carboxylic acid
Bos taurus
-
pH 7.5, 25°C
0.000326
7-methyl-2-[(2-methylphenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Bos taurus
-
pH 7.5, temperature not specified in the publication
0.00103
7-methyl-2-[(3-methylphenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Bos taurus
-
pH 7.5, temperature not specified in the publication
0.002501
7-methyl-2-[(4-nitrophenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Bos taurus
-
pH 7.5, temperature not specified in the publication
0.00073 - 0.0307
allopurinol
0.00074
apigenin
Bos taurus
-
pH 7.5, 25°C
0.0167
hydroxychavicol
Bos taurus
-
-
0.00059
luteolin
Bos taurus
-
pH 7.5, 25°C
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51082.2
purified native enzyme, pH 7.6, 37°C
1.67
-
-
10.16
-
-
2.4 - 5.1
-
-
2.963
-
-
7.8
-
milk
additional information
-
20 mU/ml of milk irrespective of infections of mammary gland with bacteria
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
assay at, superoxide anion generation by xanthine oxidase
7
assay at
7.5
assay at
9.8
assay at
7
-
assay at
7.5
-
assay at
7.6
-
assay at
7.8
-
assay at
8
-
assay at
8.3
-
-
8.5
-
conversion of dibromoacetonitrile to CN-
additional information
-
the rate of xanthine oxidation is pH dependent, and the neutral form of xanthine binds stronger to the enzyme than the monoanion
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.6
-
under aerobic conditions, NO generation increases more than three times as the pH value decreases from pH 7.4 to 6.0
6 - 9
-
-
6.5 - 9.5
-
pH 6.5: about 40% of maximal activity, pH 9.5: about 65% of maximal activity, conversion of dibromoacetonitrile to CN-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
30
assay at
23
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27 - 50
-
-
30 - 45
-
30°C: about 60% of maximal activity, 45°C: about 75% of maximal activity, conversion of dibromoacetonitrile to CN-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
xanthine oxidase mediated nitrite reduction can be a source of NO in heart tissue under conditions of tissue normoxia, and it is further increased with mild hypoxia
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
enzyme from milk and mammary gland
-
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
XDH_BOVIN
1332
0
146790
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
approximate value, bovine milk, ultrafiltration
131000
-
1 * 152000, 1 * 131000, SDS-PAGE
150000
-
2 * 150000, SDS-PAGE
152000
-
1 * 152000, 1 * 131000, SDS-PAGE
275000
-
gel filtration
290000
-
-
295000
-
-
303000
-
sedimentation equilibrium
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 150000, SDS-PAGE
dimer
homodimer
additional information
-
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
flavoprotein
-
-
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzme in complex with inhibitor quercetin, X-ray diffraction structure determintion and analysis at 2.0 A resolution
enzyme in complex with inhibitor 2-hydroxy-6-methylpurine, 10 mg/ml purified enzyme in 40 mM Tris-HCl, pH 7.8, 20 mM diphosphate, pH 8.5, 0.2 mM EDTA and 5 mM DTT, batch method mixing 0.02 ml of protein solution and 0.01 ml of precipitant solution, the latter containing of 12-14% PEG 8000, 0.1 M potassium phosphate, and 0.2 mM EDTA, pH 7.2, for 2-3 days at 25°C, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement
purified enzyme in complex with hypoxanthine or 6-mercaptopurine, mixing of 0.01 ml of 5 mg/ml protein solution with 0.005-0.006 ml of 12% polyethylene glycol 8000 solution, at pH 7.0, crystallization in the darkness at 25°C, ligand binding by soaking of crystals, X-ray diffraction structure determination and analysis at 1.8 and 2.6 A resolution, respectively
2.5 A resolution, each enzyme subunit is composed of an N-terminal 20000 Da domain containing two iron sulfur centers, a central 40000 Da FAD domain and a C-terminal 85000 molybdopterin binding domain, the four redox centers are aligned in a linear fashion
-
batch method most suitable for crystallization
-
crystal structure determination and analysis of the enzyme in complex with a variety of substrates and substrate analogues, e.g. with 2-hydroxy-6-methylpurine or hypoxanthine, X-ray diffraction structure analysis at 1.8-3.1 A resolution
-
crystal structures for bovine xanthine oxidase in complex with indole-3-acetaldehyde and guanine, both at 1.6 A resolution is reported. In the case of indole-3-acetaldehyde, a modest, sterically allowed rotation juxtaposes the aldehyde group with the molybdenum center that allows hydroxylation to take place. With guanine, the substrate must rotate approximately 180° to present its 8 position to the active site molybdenum center for hydroxylation, and this rotation is sterically prohibited
-
urate complexes of the reduced form of native milk enzyme reaction intermediate, X-ray diffraction structure determination and analysis at 2.1 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E1261X
-
mutation of Glu1261 leads to a complete loss of activity
E802Q
-
site-directed mutagenesis, altered kinetics of the mutant enzyme compared to the wild-type enzyme
additional information
-
immobilization of the enzyme to heparin sepharose
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
purified native enzyme, 70% activity is retained after 60 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
low operational stability by immobilization
-
phosphate stabilizes
-
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
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme activity is stimulated by organic solvents, but the effect is reduced with increasing temperature, from 27°C to 37°C, the inhibitory effects of all organic solvents on the enzyme activity are increased at higher temperature, dependent on pH, overview
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
photooxidation, protection by competitive inhibitors
-
644645
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 1645fold from milk to homogeneity by ammonium sulfate fracionation and affinity chromatography using a resin with diazotizated p-aminobenzamidine coupled to L-tyrosine, elution by benzamidine
native enzyme partially by gel filtration from fresh unpasteurized milk
ammonium sulfate precipitation and affinity chromatography
-
ammonium sulfate, DEAE-Sepaharose
-
native enzyme from fresh bovine cream
-
native enzyme from milk by ammonium sulfate fractionation, followed by affinity chromatography on heparin-agarose
-
purification of the molybdenum cofactor of milk xanthine oxidase
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme is a target for rational design of flavonoid-type inhibitors against xanthine oxidase useful for the treatment of hyperuricemia, gout, and inflammatory disease states
biotechnology
-
construction of amperometric biosensors based in xanthine oxidase which has been immobilized by covalent binding to gold electrodes modified with dithiobis-N-succinimidyl propionate. Redox dyes thionine and methylene blue work well as electron acceptors for reduced enzyme
synthesis
-
the enzyme can be used for production of superoxide, from oxidation of an aldehyde, which in a co-oxidation system reacts with the aldehyde and converts beta-carotene to beta-ionone, method optimization, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kramer, S.P.; Johnson, J.L.; Ribeiro, A.A.; Millington, D.S.; Rajagopalan, K.V.
The structure of the molybdenum cofactor. Characterization of di-(carboxamidomethyl)molybdopterin from sulfite oxidase and xanthine oxidase
J. Biol. Chem.
262
16357-16363
1987
Bos taurus
Manually annotated by BRENDA team
Johnson, J.L.; Hainline, B.E.; Rajagopalan, K.V.
Characterization of the molybdenum cofactor of sulfite oxidase, xanthine, oxidase, and nitrate reductase. Identification of a pteridine as a structural component
J. Biol. Chem.
255
1783-1786
1980
Bos taurus
Manually annotated by BRENDA team
Bray, R.C.
Molybdenum iron-sulfur flavin hydroxylases and related enzymes
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
12
299-419
1975
Bos taurus, Gallus gallus, Drosophila melanogaster
-
Manually annotated by BRENDA team
Eger, B.T.; Okamoto, K.; Enroth, C.; Sato, M.; Nishino, T.; Pai, E.F.; Nishino, T.
Purification, crystallization and preliminary X-ray diffraction studies of xanthine dehydrogenase and xanthine oxidase isolated from bovine milk
Acta Crystallogr. Sect. D
56
1656-1658
2000
Bos taurus
-
Manually annotated by BRENDA team
Enroth, C.; Eger, B.T.; Okamoto, K.; Nishino, T.; Nishino, T.; Pai, E.F.
Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion
Proc. Natl. Acad. Sci. USA
97
10723-10728
2000
Bos taurus
Manually annotated by BRENDA team
Nathans, G.R.; Hade, E.P.K.
Bovine milk xanthine oxidase: purification by ultrafiltration and conventional methods which omit addition of proteases: some criteria for homogeneity of native xanthine oxidase
Biochim. Biophys. Acta
526
328-344
1978
Bos taurus
Manually annotated by BRENDA team
Bruder, G.; Heid, H.; Jarasch, E.D.; Keenan, T.W.; Mather, I.H.
Characteristics of membrane-bound and soluble forms of xanthine oxidase from milk and endothelial cells of capillaries
Biochim. Biophys. Acta
701
357-369
1982
Bos taurus
Manually annotated by BRENDA team
Berglund, L.; Rasmussen, J.T.; Andersen, M.D.; Rasmussen, M.S.; Petersen, T.E.
Purification of the bovine xanthine oxidoreductase from milk fat globule membranes and cloning of complementary deoxyribonucleic acid
J. Dairy Sci.
79
198-204
1996
Bos taurus
Manually annotated by BRENDA team
zer, N.; Muftuoglu, M.; Ataman, D.; Ercan, A.; gus, I.H.
Simple, high-yield purification of xanthine oxidase from bovine milk
J. Biochem. Biophys. Methods
39
153-159
1999
Bos taurus
Manually annotated by BRENDA team
Houston, M.; Esteveze, A.; Chumley, P.; Aslan, M.; Marklund, S.; Parks, D.A.; Freeman, B.A.
Binding of xanthine oxidase to vascular endothelium
J. Biol. Chem.
274
4985-4994
1999
Bos taurus
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
Avis, P.G.; Bergel, F.; Bray, R.C.
Cellular constituents. The chemistry of xanthine oxidase. Part I. The preparation of a crystalline xanthine oxidase from cow's milk
J. Chem. Soc.
2
1100-1105
1955
Bos taurus
-
Manually annotated by BRENDA team
Coughlan, M.P.; Rajagopalan, K.V.; Handler, P.
The role of molybdenum in xanthine oxidase and related enzymes. Reactivity with cyanide, arsenite, and methanol
J. Biol. Chem.
244
2658-2663
1969
Bos taurus
Manually annotated by BRENDA team
Stirpe, F.; Della Corte, E.
The regulation of rat liver xanthine oxidase: conversion of type D (dehydrogenase) into type O (oxidase) by a thermolabile factor, and reversibility by dithioerythritol
Biochim. Biophys. Acta
212
195-197
1970
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Li, H.; Samouilov, A.; Liu, X.; Zweier, J.L.
characterization of the magnitude and kinetics of xanthine oxidase-catalyzed nitrite reduction
J. Biol. Chem.
276
24482-24489
2001
Bos taurus
Manually annotated by BRENDA team
Bray, R.C.
Xanthine oxidase
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
7
533-556
1963
Bos taurus
-
Manually annotated by BRENDA team
Batelli, M.G.; Lorenzoni, E.; Stirpe, F.
Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties
Biochem. J.
131
191-198
1973
Bos taurus
Manually annotated by BRENDA team
De Renzo, E.C.
Chemistry and biochemistry of xanthine oxidase
Adv. Enzymol. Relat. Subj. Biochem.
17
293-328
1956
Bos taurus, Gallus gallus, Rattus norvegicus
Manually annotated by BRENDA team
Tramper, J.
Preparation of immobilized milk xanthine oxidase and application in organic synthesis
Methods Enzymol.
136
254-262
1987
Bos taurus
-
Manually annotated by BRENDA team
Waud, W.R.; Brady, F.O.; Wiley, R.D.; Rajagopalan, K.V.
A new purification procedure for bovine milk xanthine oxidase: effect of proteolysis on the subunit structure
Arch. Biochem. Biophys.
169
695-701
1975
Bos taurus
Manually annotated by BRENDA team
Van Spanning, R.J.M.; Wansell-Bettenhaussen, C.W.; Oltmann, L.F.; Stouthamer, A.H.
Extraction and purification of molybdenum cofactor from milk xanthine oxidase
Eur. J. Biochem.
169
349-352
1987
Bos taurus
Manually annotated by BRENDA team
Cabre, F.; Canela, E.I.
Purification properties and functional groups of bovine liver xanthine oxidase
Biochem. Soc. Trans.
15
511-512
1987
Bos taurus
-
Manually annotated by BRENDA team
Morpeth, F.F.; Bray, R.C.
Mechanism-based inactivation of mitochondrial monoamine oxidase by N-(1-methylcyclopropyl)benzylamine
Biochemistry
23
1322-1338
1984
Bos taurus
Manually annotated by BRENDA team
Morpeth, F.F.
Studies on the specificity toward aldehyde substrates and steady-state kinetics of xanthine oxidase
Biochim. Biophys. Acta
744
328-334
1983
Bos taurus
Manually annotated by BRENDA team
Briley, M.S.; Eisenthal, R.
Association of xanthine oxidase with the bovine milk-fat-globule membrane. Nature of the enzyme-membrane association
Biochem. J.
147
417-423
1975
Bos taurus
Manually annotated by BRENDA team
Panoutsopoulos, G.I.; Beedham, C.
Kinetics and specificity of guinea pig liver aldehyde oxidase and bovine milk xanthine oxidase towards substituted benzaldehydes
Acta Biochim. Pol.
51
649-663
2004
Bos taurus
Manually annotated by BRENDA team
Mohamadin, A.M.; Abdel-Naim, A.B.
In vitro activation of dibromoacetonitrile to cyanide: role of xanthine oxidase
Arch. Toxicol.
77
86-93
2003
Bos taurus
Manually annotated by BRENDA team
Li, H.; Samouilov, A.; Liu, X.; Zweier, J.L.
Characterization of the magnitude and kinetics of xanthine oxidase-catalyzed nitrate reduction: evaluation of its role in nitrite and nitric oxide generation in anoxic tissues
Biochemistry
42
1150-1159
2003
Bos taurus
Manually annotated by BRENDA team
Tai, L.A.; Hwang, K.C.
Cooperative catalysis in the homodimer subunits of xanthine oxidase
Biochemistry
43
4869-4876
2004
Bos taurus
Manually annotated by BRENDA team
Masuoka, N.; Kubo, I.
Characterization of xanthine oxidase inhibition by anacardic acids
Biochim. Biophys. Acta
1688
245-249
2004
Bos taurus
Manually annotated by BRENDA team
Lovstad, R.A.
A kinetic study on iron stimulation of the xanthine oxidase dependent oxidation of ascorbate
BioMetals
16
435-439
2003
Bos taurus
Manually annotated by BRENDA team
Millar, T.M.
Peroxynitrite formation from the simultaneous reduction of nitrite and oxygen by xanthine oxidase
FEBS Lett.
562
129-133
2004
Bos taurus
Manually annotated by BRENDA team
Li, H.; Samouilov, A.; Liu, X.; Zweier, J.L.
Characterization of the effects of oxygen on xanthine oxidase-mediated nitric oxide formation
J. Biol. Chem.
279
16939-16946
2004
Bos taurus
Manually annotated by BRENDA team
Li, H.; Cui, H.; Liu, X.; Zweier, J.L.
Xanthine oxidase catalyzes anaerobic transformation of organic nitrates to nitric oxide and nitrosothiols: characterization of this mechanism and the link between organic nitrate and guanylyl cyclase activation
J. Biol. Chem.
280
16594-16600
2005
Bos taurus
Manually annotated by BRENDA team
Choi, E.Y.; Stockert, A.L.; Leimkuhler, S.; Hille, R.
Studies on the mechanism of action of xanthine oxidase
J. Inorg. Biochem.
98
841-848
2004
Bos taurus
Manually annotated by BRENDA team
Gongora, L.; Manez, S.; Giner, R.M.; Recio, M.d.C.; Schinella, G.; Rios, J.L.
Inhibition of xanthine oxidase by phenolic conjugates of methylated quinic acid
Planta Med.
69
396-401
2003
Bos taurus
Manually annotated by BRENDA team
Casero, E.; de Quesada, A.M.; Jin, J.; Quintana, M.C.; Pariente, F.; Abruna, H.D.; Vazquez, L.; Lorenzo, E.
Comprehensive study of bioanalytical platforms: xanthine oxidase
Anal. Chem.
78
530-537
2006
Bos taurus
Manually annotated by BRENDA team
Galbusera, C.; Orth, P.; Fedida, D.; Spector, T.
Superoxide radical production by allopurinol and xanthine oxidase
Biochem. Pharmacol.
71
1747-1752
2006
Bos taurus
Manually annotated by BRENDA team
Noro, T.; Oda, Y.; Miyase, T.; Ueno, A.; Fukushima, S.
Inhibitors of xanthine oxidase from the flowers and buds of Daphne genkwa
Chem. Pharm. Bull.
31
3984-3987
1983
Bos taurus
Manually annotated by BRENDA team
Veskoukis, A.S.; Kouretas, D.; Panoutsopoulos, G.I.
Substrate specificity of guinea pig liver aldehyde oxidase and bovine milk xanthine oxidase for methyl- and nitrobenzaldehydes
Eur. J. Drug Metab. Pharmacokinet.
31
11-16
2005
Bos taurus
Manually annotated by BRENDA team
Dew, T.P.; Day, A.J.; Morgan, M.R.
Xanthine oxidase activity in vitro: effects of food extracts and components
J. Agric. Food Chem.
53
6510-6515
2005
Bos taurus
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
Tamta, H.; Thilagavathi, R.; Chakraborti, A.K.; Mukhopadhyay, A.K.
6-(N-benzoylamino)purine as a novel and potent inhibitor of xanthine oxidase: inhibition mechanism and molecular modeling studies
J. Enzyme Inhib. Med. Chem.
20
317-324
2005
Bos taurus
Manually annotated by BRENDA team
Takano, Y.; Hase-Aoki, K.; Horiuchi, H.; Zhao, L.; Kasahara, Y.; Kondo, S.; Becker, M.A.
Selectivity of febuxostat, a novel non-purine inhibitor of xanthine oxidase/xanthine dehydrogenase
Life Sci.
76
1835-1847
2005
Bos taurus
Manually annotated by BRENDA team
Masuoka, N.; Nihei, K.; Kubo, I.
Xanthine oxidase inhibitory activity of alkyl gallates
Mol. Nutr. Food Res.
50
725-731
2006
Bos taurus (P80457)
Manually annotated by BRENDA team
Banach, K.; Bojarska, E.; Kazimierczuk, Z.; Magnowska, L.; Bzowska, A.
Kinetic model of oxidation catalyzed by xanthine oxidase-the final enzyme in degradation of purine nucleosides and nucleotides
Nucleosides Nucleotides Nucleic Acids
24
465-469
2005
Bos taurus
Manually annotated by BRENDA team
Nguyen, M.T.; Awale, S.; Tezuka, Y.; Ueda, J.Y.; Tran, Q.; Kadota, S.
Xanthine oxidase inhibitors from the flowers of Chrysanthemum sinense
Planta Med.
72
46-51
2006
Bos taurus
Manually annotated by BRENDA team
Silanikove, N.; Shapiro, F.; Leitner, G.
Posttranslational ruling of xanthine oxidase activity in bovine milk by its substrates
Biochem. Biophys. Res. Commun.
363
561-565
2007
Bos taurus
Manually annotated by BRENDA team
Tamta, H.; Kalra, S.; Thilagavathi, R.; Chakraborti, A.K.; Mukhopadhyay, A.K.
Nature and position of functional group on thiopurine substrates influence activity of xanthine oxidase - enzymatic reaction pathways of 6-mercaptopurine and 2-mercaptopurine are different
Biochemistry (Moscow)
72
170-177
2007
Bos taurus
Manually annotated by BRENDA team
Ly, M.H.; Hoang, L.C.; Belin, J.M.; Wache, Y.
Improved co-oxidation of beta-carotene to beta-ionone using xanthine oxidase-generated reactive oxygen species in a multiphasic system
Biotechnol. J.
3
220-225
2008
Bos taurus
Manually annotated by BRENDA team
Kalra, S.; Jena, G.; Tikoo, K.; Mukhopadhyay, A.K.
Preferential inhibition of xanthine oxidase by 2-amino-6-hydroxy-8-mercaptopurine and 2-amino-6-purine thiol
BMC Biochem.
8
8
2007
Bos taurus
Manually annotated by BRENDA team
Sato, E.; Mokudai, T.; Niwano, Y.; Kamibayashi, M.; Kohno, M.
Existence of a new reactive intermediate oxygen species in hypoxanthine and xanthine oxidase reaction
Chem. Pharm. Bull.
56
1194-1197
2008
Bos taurus
Manually annotated by BRENDA team
Reigan, P.; Gbaj, A.; Stratford, I.J.; Bryce, R.A.; Freeman, S.
Xanthine oxidase-activated prodrugs of thymidine phosphorylase inhibitors
Eur. J. Med. Chem.
43
1248-1260
2008
Bos taurus
Manually annotated by BRENDA team
Lavelli, V.
Antioxidant activity of minimally processed red chicory (Cichorium intybus L.) evaluated in xanthine oxidase-, myeloperoxidase-, and diaphorase-catalyzed reactions
J. Agric. Food Chem.
56
7194-7200
2008
Bos taurus
Manually annotated by BRENDA team
Pauff, J.M.; Zhang, J.; Bell, C.E.; Hille, R.
Substrate orientation in xanthine oxidase: crystal structure of enzyme in reaction with 2-hydroxy-6-methylpurine
J. Biol. Chem.
283
4818-4824
2008
Bos taurus (P80457)
Manually annotated by BRENDA team
Tsujii, A.; Nishino, T.
Mechanism of transition from xanthine dehydrogenase to xanthine oxidase: Effect of guanidine-HCl or urea on the activity
Nucleosides Nucleotides Nucleic Acids
27
881-887
2008
Bos taurus
Manually annotated by BRENDA team
Hadizadeh, M.; Keyhani, E.; Keyhani, J.; Khodadadi, C.
Functional and structural alterations induced by copper in xanthine oxidase
Acta Biochim. Biophys. Sin.
41
603-617
2009
Bos taurus
Manually annotated by BRENDA team
Rashidi, M.R.; Soruraddin, M.H.; Taherzadeh, F.; Jouyban, A.
Catalytic activity and stability of xanthine oxidase in aqueous-organic mixtures
Biochemistry (Moscow)
74
97-101
2009
Bos taurus
Manually annotated by BRENDA team
Nishino, T.; Okamoto, K.; Eger, B.T.; Pai, E.F.; Nishino, T.
Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase
FEBS J.
275
3278-3289
2008
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Sousa, C.; Pereira, D.M.; Valentao, P.; Ferreres, F.; Pereira, J.A.; Seabra, R.M.; Andrade, P.B.
Pieris brassicae inhibits xanthine oxidase
J. Agric. Food Chem.
57
2288-2294
2009
Bos taurus
Manually annotated by BRENDA team
Kelley, E.E.; Batthyany, C.I.; Hundley, N.J.; Woodcock, S.R.; Bonacci, G.; Del Rio, J.M.; Schopfer, F.J.; Lancaster, J.R.; Freeman, B.A.; Tarpey, M.M.
Nitro-oleic acid, a novel and irreversible inhibitor of xanthine oxidoreductase
J. Biol. Chem.
283
36176-36184
2008
Bos taurus
Manually annotated by BRENDA team
Murata, K.; Nakao, K.; Hirata, N.; Namba, K.; Nomi, T.; Kitamura, Y.; Moriyama, K.; Shintani, T.; Iinuma, M.; Matsuda, H.
Hydroxychavicol: a potent xanthine oxidase inhibitor obtained from the leaves of betel, Piper betle
J. Nat. Med.
63
355-359
2009
Bos taurus
Manually annotated by BRENDA team
Pauff, J.M.; Hille, R.
Inhibition studies of bovine xanthine oxidase by luteolin, silibinin, quercetin, and curcumin
J. Nat. Prod.
72
725-731
2009
Bos taurus
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
Hu, L.; Hu, H.; Wu, W.; Chai, X.; Luo, J.; Wu, Q.
Discovery of novel xanthone derivatives as xanthine oxidase inhibitors
Bioorg. Med. Chem. Lett.
21
4013-4015
2011
Bos taurus
Manually annotated by BRENDA team
Sathisha, K.R.; Khanum, S.A.; Chandra, J.N.; Ayisha, F.; Balaji, S.; Marathe, G.K.; Gopal, S.; Rangappa, K.S.
Synthesis and xanthine oxidase inhibitory activity of 7-methyl-2-(phenoxymethyl)-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one derivatives
Bioorg. Med. Chem.
19
211-220
2011
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Tai, L.A.; Hwang, K.C.
Regulation of xanthine oxidase activity by substrates at active sites via cooperative interactions between catalytic subunits: implication to drug pharmacokinetics
Curr. Med. Chem.
18
69-78
2011
Bos taurus
Manually annotated by BRENDA team
Wang, S.; Yan, J.; Wang, J.; Chen, J.; Zhang, T.; Zhao, Y.; Xue, M.
Synthesis of some 5-phenylisoxazole-3-carboxylic acid derivatives as potent xanthine oxidase inhibitors
Eur. J. Med. Chem.
45
2663-2670
2010
Bos taurus
Manually annotated by BRENDA team
Cao, H.; Pauff, J.; Hille, R.
Substrate orientation and the origin of catalytic power in xanthine oxidoreductase
Indian J. Chem.
50A
355-362
2011
Bos taurus
-
Manually annotated by BRENDA team
Shanmugam, M.; Zhang, B.; McNaughton, R.L.; Kinney, R.A.; Hille, R.; Hoffman, B.M.
The structure of formaldehyde-inhibited xanthine oxidase determined by 35 GHz 2H ENDOR spectroscopy
J. Am. Chem. Soc.
132
14015-14017
2010
Bos taurus
Manually annotated by BRENDA team
Okamoto, K.; Kawaguchi, Y.; Eger, B.; Pai, E.; Nishino, T.
Crystal structures of urate bound form of xanthine oxidoreductase: Substrate orientation and structure of the key reaction intermediate
J. Am. Chem. Soc.
132
17080-17083
2010
Bos taurus, Rattus norvegicus (P22985)
Manually annotated by BRENDA team
Cao, H.; Pauff, J.M.; Hille, R.
Substrate orientation and catalytic specificity in the action of xanthine oxidase: the sequential hydroxylation of hypoxanthine to uric acid
J. Biol. Chem.
285
28044-28053
2010
Bos taurus (P80457)
Manually annotated by BRENDA team
Metz, S.; Thiel, W.
QM/MM studies of xanthine oxidase: variations of cofactor, substrate, and active-site Glu802
J. Phys. Chem. B
114
1506-1517
2010
Bos taurus
Manually annotated by BRENDA team
Bytyqi-Damoni, A.; Genc, H.; Zengin, M.; Beyaztas, S.; Gencer, N.; Arslan, O.
In vitro effect of novel beta-lactam compounds on xanthine oxidase enzyme activity
Artif. Cells Blood Substit. Immobil. Biotechnol.
40
369-377
2012
Bos taurus
Manually annotated by BRENDA team
Cao, H.; Hall, J.; Hille, R.
Substrate Orientation and Specificity in Xanthine Oxidase: Crystal structures of the enzyme in complex with indole-3-acetaldehyde and guanine
Biochemistry
53
533-541
2014
Bos taurus
Manually annotated by BRENDA team
Kumar, D.; Kaur, G.; Negi, A.; Kumar, S.; Singh, S.; Kumar, R.
Synthesis and xanthine oxidase inhibitory activity of 5,6-dihydropyrazolo/pyrazolo[1,5-c]quinazoline derivatives
Bioorg. Chem.
57
57-64
2014
Bos taurus (P80457)
Manually annotated by BRENDA team
Zafar, H.; Hayat, M.; Saied, S.; Khan, M.; Salar, U.; Malik, R.; Choudhary, M.I.; Khan, K.M.
Xanthine oxidase inhibitory activity of nicotino/isonicotinohydrazides a systematic approach from in vitro, in silico to in vivo studies
Bioorg. Med. Chem.
25
2351-2371
2017
Bos taurus (P80457)
Manually annotated by BRENDA team
Tang, H.J.; Zhang, X.W.; Yang, L.; Li, W.; Li, J.H.; Wang, J.X.; Chen, J.
Synthesis and evaluation of xanthine oxidase inhibitory and antioxidant activities of 2-arylbenzo[b]furan derivatives based on salvianolic acid C
Eur. J. Med. Chem.
124
637-648
2016
Bos taurus (P80457)
Manually annotated by BRENDA team
Lin, S.; Zhang, G.; Liao, Y.; Pan, J.
Inhibition of chrysin on xanthine oxidase activity and its inhibition mechanism
Int. J. Biol. Macromol.
81
274-282
2015
Bos taurus (P80457)
Manually annotated by BRENDA team
Di Majo, D.; La Guardia, M.; Leto, G.; Crescimanno, M.; Flandina, C.; Giammanco, M.
Flavonols and flavan-3-ols as modulators of xanthine oxidase and manganese superoxide dismutase activity
Int. J. Food Sci. Nutr.
65
886-892
2014
Bos taurus (P80457)
Manually annotated by BRENDA team
Masuoka, N.; Kubo, I.
Suppression of superoxide anion generation catalyzed by xanthine oxidase with alkyl caffeates and the scavenging activity
Int. J. Food Sci. Nutr.
67
283-287
2016
Bos taurus (P80457)
Manually annotated by BRENDA team
Beyaztas, S.; Arslan, O.
Purification of xanthine oxidase from bovine milk by affinity chromatography with a novel gel
J. Enzyme Inhib. Med. Chem.
30
442-447
2015
Bos taurus (P80457), Bos taurus
Manually annotated by BRENDA team
de Araujo, M.E.M.B.; Franco, Y.E.M.; Alberto, T.G.; Messias, M.C.F.; Leme, C.W.; Sawaya, A.C.H.F.; Carvalho, P.O.
Kinetic study on the inhibition of xanthine oxidase by acylated derivatives of flavonoids synthesised enzymatically
J. Enzyme Inhib. Med. Chem.
32
978-985
2017
Bos taurus (P80457)
Manually annotated by BRENDA team
Cao, H.; Pauff, J.M.; Hille, R.
X-ray crystal structure of a xanthine oxidase complex with the flavonoid inhibitor quercetin
J. Nat. Prod.
77
1693-1699
2014
Bos taurus (P80457)
Manually annotated by BRENDA team