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(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages + H2O + O2
?
-
-
-
-
r
1,3-dimethylxanthine + H2O + O2
1,3-dimethylurate + H2O2
-
-
-
-
?
1,7-dimethylxanthine + H2O + O2
1,7-dimethylurate + H2o2
-
-
-
-
?
1-methyl-2-hydroxypurine + H2O + O2
1-methyl-2-hydroxy-7,9-dihydropurin-8-one + H2O2
-
-
-
?
1-methylxanthine + H2O + O2
1-methylurate + H2O2
2,3-dihydroxybenzaldehyde + H2O + O2
2,3-dihydroxybenzoate + H2O2
-
-
-
?
2,5-dihydroxybenzaldehyde + H2O + O2
?
-
-
-
-
?
2,6-diaminopurine + H2O + O2
2,6-diamino-7,9-dihydro-8H-purin-8-one
-
-
-
-
?
2-amino-4-hydroxypteridine + H2O + O2
?
2-amino-4-hydroxypterin + H2O + O2
? + H2O2
-
substrate inhibition kinetic pattern
-
-
?
2-amino-6-chloro-purine + H2O + O2
2-amino-6-chloro-7,9-dihydro-purin-8-one + H2O2
-
-
-
-
?
2-hydroxybenzaldehyde + H2O + O2
2-hydroxybenzoate + H2O2
-
-
-
-
?
2-mercaptopurine + H2O + O2
8-hydroxy-2-mercaptopurine + H2O2
-
no conversion to 2-thioxanthine
-
-
?
2-methoxybenzaldehyde + H2O + O2
2-methoxybenzoate + H2O2
-
-
-
-
?
2-methylbenzaldehyde + H2O + O2
2-methylbenzoate + H2O2
-
-
-
-
?
2-nitrobenzaldehyde + H2O + O2
2-nitrobenzoate + H2O2
-
-
-
-
?
2-oxo-6-methylpurine + H2O + O2
? + H2O2
-
low activity
-
-
?
2-thioxanthine + H2O + O2
2-thiourate + H2O2
-
-
-
-
?
2-thioxanthine + H2O + O2
2-thiouric acid + H2O2
-
-
-
-
?
3,4-dihydroxybenzaldehyde + H2O + O2
3,4-dihydroxybenzoate + H2O2
-
-
-
-
?
3,4-dimethoxybenzaldehyde + H2O + O2
3,4-dimethoxybenzoate + H2O2
-
-
-
-
?
3-hydroxy-4-methoxybenzaldehyde + H2O + O2
3-hydroxy-4-methoxybenzoate + H2O2
-
-
-
-
?
3-hydroxybenzaldehyde + H2O + O2
3-hydroxybenzoate + H2O2
-
-
-
-
?
3-methoxybenzaldehyde + H2O + O2
3-methoxybenzoate + H2O2
-
-
-
-
?
3-methylbenzaldehyde + H2O + O2
3-methylbenzoate + H2O2
-
-
-
-
?
3-methylhypoxanthine + H2O + O2
3-methylxanthine + H2O2
-
-
-
?
3-methylxanthine + H2O + O2
3-methylurate + H2O2
-
-
-
-
?
3-nitrobenzaldehyde + H2O + O2
3-nitrobenzoate + H2O2
-
-
-
-
?
4-hydroxy-3-methoxybenzaldehyde + H2O + O2
4-hydroxy-3-methoxybenzoate + H2O2
-
-
-
-
?
4-hydroxybenzaldehyde + H2O + O2
4-hydroxybenzoate + H2O2
-
-
-
-
?
4-hydroxyphenylglycoaldehyde + H2O + O2
?
-
-
-
-
?
4-methoxybenzaldehyde + H2O + O2
4-methoxybenzoate + H2O2
-
-
-
-
?
4-methylbenzaldehyde + H2O + O2
4-methylbenzoate + H2O2
-
-
-
-
?
4-nitrobenzaldehyde + H2O + O2
4-nitrobenzoate + H2O2
-
-
-
-
?
5-chloro-6-[(2-iminopyrrolidin-1-yl)methyl]-3H-pyrimidin-4-one + H2O + O2
?
-
-
-
-
?
6'-deoxyacyclovir + H2O + O2
acyclovir + H2O2
-
prodrug of the antiviral agent acyclovir
-
?
6,8-dihydroxypurine + H2O + O2
?
-
-
-
-
?
6,8-dihydroxypurine + H2O + O2
? + H2O2
6,8-dihydroxypurine binding structure, overview
-
-
?
6-amino-5-bromo-1H-pyrimidin-2-one + H2O + O2
?
-
-
-
-
?
6-amino-5-bromo-3H-pyrimidin-4-one + H2O + O2
?
-
-
-
-
?
6-amino-5-bromopyrimidine + H2O + O2
?
-
-
-
-
?
6-cyanopurine + H2O + O2
6-cyano-7,9-dihydropurine-8-one
-
-
-
?
6-formylpterin + H2O + O2
?
-
-
-
-
?
6-formylpterin + H2O + O2
? + H2O2
-
-
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
6-mercaptopurine + H2O + O2
6-mercapto-7,9-dihydropurin-8-one + H2O2
-
4.4% of activity with xanthin
-
?
6-mercaptopurine + H2O + O2
?
-
an anticancer drug
-
-
?
6-thioxanthine + H2O + O2
6-thiourate + H2O2
6-thioxanthine + H2O + O2
6-thiouric acid + H2O2
-
-
-
-
?
7-alkylpteridin-4-one + H2O + O2
7-alkyllumazine + H2O2
-
-
-
?
7-methylxanthine + H2O + O2
7-methylurate + H2O2
-
-
-
-
?
7-phenylpteridin-4-one + H2O + O2
7-phenyllumazine + H2O2
-
-
-
?
7H-pyrrolo[2,3-d]pyrimidin-2(1H)-one + H2O + O2
?
-
-
-
-
?
7H-pyrrolo[2,3-d]pyrimidin-4(3H)-one + H2O + O2
?
-
-
-
-
?
7H-pyrrolo[2,3-d]pyrimidine + H2O + O2
?
-
-
-
-
?
acetaldehyde + H2O + O2
acetic acid + H2O2
adenine + H2O + O2
6-amino-7,9-dihydropurin-8-one + H2O2
adenine + H2O + O2
? + H2O2
-
substrate inhibition kinetic pattern
-
-
?
aldehyde + indophenol
?
-
-
-
-
r
allopurinol + H2O + O2
oxypurinol + H2O2
benzaldehyde + H2O + O2
benzoate + H2O2
butanal + H2O + O2
butanoate + H2O2
-
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
dibromoacetonitrile + H2O + O2
?
-
-
-
-
r
formaldehyde + H2O + O2
?
-
-
-
-
r
formycin B + H2O + O2
?
-
-
-
-
?
FYX-051 + O2 + H2O
?
-
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
?
-
-
-
-
?
glyceryl trinitrate + 2,3-dihydroxybenzaldehyde
?
-
-
-
-
?
glyceryl trinitrate + NADH
? + NAD+ + H2O
-
-
further reaction of organic nitrite with thiols or ascorbate leads to generation of NO or nitrosothiols
-
?
glyceryl trinitrate + xanthine
urate + ?
-
-
-
-
?
guanine + H2O + O2
2-amino-7,9-dihydro-1H-purine-6,8-dione + H2O2
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
hypoxanthine + H2O + O2
urate + H2O2
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
indole-3-acetaldehyde + H2O + O2
?
-
-
-
-
?
indole-3-aldehyde + H2O + O2
?
-
-
-
-
?
isosorbide dinitrate + 2,3-dihydroxybenzaldehyde
?
-
-
-
-
?
isosorbide dinitrate + NADH
? + NAD+ + H2O
-
-
further reaction of organic nitrite with thiols or ascorbate leads to generation of NO or nitrosothiols
-
?
isosorbide dinitrate + xanthine
urate + ?
-
-
-
-
?
lumazine + H2O + O2
? + H2O2
-
classical Michaelis-Menten hyperbolic saturation kinetic pattern
-
-
?
N-methylnicotinamide + H2O + O2
?
-
poor oxidation reaction
-
-
r
N1-methylnicotinamide + H2O + O2
?
NADH + H2O + O2
NAD+ + H2O2
NADPH + indophenol
?
-
-
-
-
r
nitrate + 2,3-dihydroxybenzaldehyde
nitrite + ?
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
nitrate + xanthine
nitrite + urate + ?
-
-
-
-
?
nitrite + 2,3-dihydroxybenzaldehyde
NO + ?
-
NO generation occurs under aerobic conditions and is regulated by O2 tension, pH, nitrite, and reducing substrate concentrations
-
-
?
nitrite + NADH
NO + NAD+ + H2O
nitrite + O2 + hypoxanthine
peroxynitrite + ?
-
-
-
-
?
nitrite + O2 + pterin
peroxynitrite + ?
-
-
-
-
?
nitrite + xanthine
NO + ?
o-hydroxybenzaldehyde + H2O + O2
o-hydroxybenzoate + H2O2
-
-
-
?
organic nitrate + NADH
organic nitrite + NAD+ + H2O
-
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
-
-
-
?
pterin + H2O + O2
?
-
fluorometric assay method
-
-
?
pterin + H2O + O2
isoxanthopterin + H2O2
-
-
-
?
pterine + NAD+
? + H2O + NADH
-
-
-
?
purine + H2O + O2
7,9-dihydropurin-8-one + H2O2
purine + NAD+
? + H2O + NADH
-
-
-
?
pyridine 3-aldehyde + H2O + O2
?
-
-
-
-
r
pyridine-2-aldehyde + H2O + O2
?
-
-
-
-
?
pyridine-3-aldehyde + H2O + O2
?
-
-
-
-
?
pyridine-4-aldehyde + H2O + O2
?
-
-
-
-
?
pyrimidine derivatives + H2O + O2
?
salicylaldehyde + H2O + O2
salicylic acid + H2O2
-
-
-
?
succinate semialdehyde + H2O + O2
succinate + H2O2
-
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
-
-
-
-
?
xanthine + H2O + O2
?
-
-
-
-
?
xanthine + H2O + O2
superoxide + urate + ?
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
xanthine + H2O + O2
uric acid + H2O2
xanthine + methylene blue + O2
urate + reduced methylene blue
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NO2-
uric acid + NO
xanthine + O2 + H2O
urate + H2O2
xanthine + thionine + O2
urate + reduced thionine
-
-
-
-
?
xanthopterin + H2O + O2
?
-
-
-
-
?
xanthopterin + H2O + O2
? + H2O2
-
substrate activation kinetic pattern
-
-
?
additional information
?
-
1-methylxanthine + H2O + O2
1-methylurate + H2O2
-
-
-
?
1-methylxanthine + H2O + O2
1-methylurate + H2O2
-
-
-
?
1-methylxanthine + H2O + O2
1-methylurate + H2O2
-
-
-
-
?
1-methylxanthine + H2O + O2
1-methylurate + H2O2
-
-
-
-
?
2-amino-4-hydroxypteridine + H2O + O2
?
-
-
-
-
r
2-amino-4-hydroxypteridine + H2O + O2
?
-
-
-
-
r
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
-
-
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
-
production of superoxide radicals
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
-
a two-step reaction with 6-thioxanthine as intermediate
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
-
-
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
-
an anticancer prodrug, no activation by xanthine oxidase but conversion to the inactive metabolite 6-thiouric acid, catabolism, overview
-
-
?
6-thioxanthine + H2O + O2
6-thiourate + H2O2
-
-
-
?
6-thioxanthine + H2O + O2
6-thiourate + H2O2
-
-
-
-
?
acetaldehyde + H2O + O2
acetic acid + H2O2
-
-
-
?
acetaldehyde + H2O + O2
acetic acid + H2O2
-
-
-
?
adenine + H2O + O2
6-amino-7,9-dihydropurin-8-one + H2O2
-
-
-
?
adenine + H2O + O2
6-amino-7,9-dihydropurin-8-one + H2O2
-
no activity with adenine
-
-
?
adenine + H2O + O2
6-amino-7,9-dihydropurin-8-one + H2O2
-
-
-
?
allopurinol + H2O + O2
?
-
-
-
-
?
allopurinol + H2O + O2
?
-
-
-
-
?
allopurinol + H2O + O2
oxypurinol + H2O2
-
-
allopurinol is a conventional substrate that generates superoxide radicals during its oxidation
-
?
allopurinol + H2O + O2
oxypurinol + H2O2
-
allopurinol is a substrate and a competitive inhibitor for xanthine oxidase, it binds irreversibly at the active site reducing molybdenum VI to IV
-
-
?
allopurinol + H2O + O2
oxypurinol + H2O2
-
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
-
-
-
-
?
benzaldehyde + H2O + O2
benzoate + H2O2
-
-
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
guanine + H2O + O2
2-amino-7,9-dihydro-1H-purine-6,8-dione + H2O2
-
-
-
-
?
guanine + H2O + O2
2-amino-7,9-dihydro-1H-purine-6,8-dione + H2O2
-
53.3% of activity with xanthin
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
a two-step reaction with xanthine as intermediate, production of superoxide radicals
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
via intermediate xanthine formation, production of superoxide radicals
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
hypoxanthine binding structure, overview
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
92.3% of activity with xanthin
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
92.3% of activity with xanthin
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
Megalodesulfovibrio gigas
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
production of superoxide radicals
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
N1-methylnicotinamide + H2O + O2
?
-
-
-
-
?
N1-methylnicotinamide + H2O + O2
?
-
-
-
-
?
NADH + H2O + O2
NAD+ + H2O2
-
-
-
?
NADH + H2O + O2
NAD+ + H2O2
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
reaction can be an important source of NO production in ischemic tissues
-
-
?
nitrite + NADH
NO + NAD+ + H2O
-
-
-
-
?
nitrite + NADH
NO + NAD+ + H2O
-
reaction can be an important source of NO production in ischemic tissues
-
-
?
nitrite + NADH
NO + NAD+ + H2O
-
NO generation occurs under aerobic conditions and is regulated by O2 tension, pH, nitrite, and reducing substrate concentrations
-
-
?
nitrite + xanthine
NO + ?
-
-
-
-
?
nitrite + xanthine
NO + ?
-
NO generation occurs under aerobic conditions and is regulated by O2 tension, pH, nitrite, and reducing substrate concentrations
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
and derivatives, e.g.: 4-amino-7-hydroxy pteridine, 4-hydroxy-7-azapteridine
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
7,9-dihydropurin-8-one + H2O2
-
purine and derivatives
-
?
purine + H2O + O2
7,9-dihydropurin-8-one + H2O2
-
purine and derivatives
-
?
purine + H2O + O2
7,9-dihydropurin-8-one + H2O2
-
23.3% of activity with xanthine
-
?
purine + H2O + O2
7,9-dihydropurin-8-one + H2O2
-
purine and derivatives
-
?
purine + H2O + O2
7,9-dihydropurin-8-one + H2O2
-
purine and derivatives
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
pyrimidine derivatives + H2O + O2
?
-
e.g. 2-hydroxypyrimidine
-
-
?
pyrimidine derivatives + H2O + O2
?
-
6-hydroxy-6-aminepyrimidine
-
-
?
pyrimidine derivatives + H2O + O2
?
-
7-hydroxy-(1,2,5)-thiadiazolo(3,4-d)-pyrimidine
-
-
?
pyrimidine derivatives + H2O + O2
?
-
7-hydroxy-(1,2,5)-thiadiazolo(3,4-d)-pyrimidine
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
658734, 660329, 673434, 675050, 684878, 685300, 686525, 689276, 714464, 714785, 715264, 716010 -
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
from dead cancer cells
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
-
active site structure, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
orientation of xanthine in the active site of xanthine oxidoreductase,structure, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals, determination of a reactive intermediate oxygen species relevant to superoxide and hydroxyl radicals, method optimization using electron transfer via H2O2, luminol, and aminophthallate, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
catalytically relevant binding mode of the substrate xanthine, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
effects of variations in the cofactor, the substrate, and the active site residue Glu802 on the reaction mechanism, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
substrate inhibition kinetic pattern
-
-
?
xanthine + H2O + O2
urate + H2O2
substrate orientation and catalytic specificity, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
-
the enzyme is involved in development of ischemia and equine laminitis, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
-
the enzyme plays a role in the development of distant organ dysfunction after abdominal surgery, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
old persons show higher enzyme expression and activity than young persons which promotes a worse prognosis for patients with chronic heart failure due to the increased contents of risk factor urate, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of reactive oxygen species via superoxide radicals involved in endothelial dysfunction
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
-
roles of active site residues E308 and R881 in binding and activation of purine substrate, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
the enzyme plays a role in the development of distant organ dysfunction after abdominal surgery, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
urate is involved in development of endothelial dysfunction, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
xanthine oxidase-derived extracellular superoxide anions stimulate activator protein 1 activity and hypertrophy in vascular smooth muscle via c-Jun N-terminal kinase and p38 mitogen-activated protein kinases, xanthine and xanthine oxidase treatment of smooth muscle cells lead to increased cell growth and size, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals, mechanism of stepwise enzyme reduction during catalysis, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
-
xanthine oxidase inhibition, meaning a decrease in myocardial oxidative stress, improves left ventricular dysfunction in dilated cardiomyopathic hamsters, modelling, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals, treatment with an enzyme inhibitor largely prevents the development of endothelial dysfunction and atherosclerosis in mice
-
-
?
xanthine + H2O + O2
urate + H2O2
-
the enzyme plays a role in the development of distant organ dysfunction after abdominal surgery, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
xanthine oxidoreductase, XOR, can exist in a dehydrogenase form, XD, and an oxidase form, XO. Part of total XOR activity in peroxisomes is XO activity. The major function of XOR activity in the cytoplasm of rat liver parenchymal cells and in sinusoidal cells is not the production of O2 radicals, but rather the production of uric acid which can act as a potent antioxidant
-
-
?
xanthine + H2O + O2
urate + H2O2
-
old animals show higher enzyme expression and activity than young rats which promotes a worse prognosis for patients with chronic heart failure due to the increased contents of risk factor urate, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals can be induced by gama-irradiation and contributes to oxidative stress and endothelial nitroredox imbalance with resultant endothelial dysfunction and altered vascular mechanics, mechanism and regulation, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
the enzyme is involved in regulation of reactive oxygen species in the functional response of veins and arteries to angiotensin II, norepinephrine, and acetylcholine
-
-
?
xanthine + H2O + O2
urate + H2O2
-
the enzyme plays a role in the development of distant organ dysfunction after abdominal surgery, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
urate is involved in development of endothelial dysfunction, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
xanthine oxidase inhibition by febuxostat lowers uric acid and alleviates systemic and glomerular hypertension in hyperuricaemia, experimentally-induced by inhibition of uricase with oxonic acid, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
xanthine oxidase is an important source of reactive oxygen species that contributes to neurovascular dysfunction in experimental diabetes, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals, mechanism of stepwise enzyme reduction during catalysis, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
catalytically relevant binding mode of the substrate xanthine, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
uric acid + H2O2
-
-
-
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
Arthrobacter S-2 enzyme: relatively specific
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor ferricyanide
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor 2,6-dichlorophenolindophenol
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
Arthrobacter S-2 enzyme: relatively specific
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor ferricyanide
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor 2,6-dichlorophenolindophenol
-
?
xanthine + H2O + O2
uric acid + H2O2
-
-
-
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor methylene blue
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor methylene blue
under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 H+ + 2 O2-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor NAD+
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor NAD+
under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 H+ + 2 O2-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 H+ + 2 O2-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor quinones
under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 H+ + 2 O2-
?
xanthine + H2O + O2
uric acid + H2O2
-
specificity for electron acceptor is low
-
?
xanthine + H2O + O2
uric acid + H2O2
-
specificity for electron acceptor is low
under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 H+ + 2 O2-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor triphenyltetrazolium chloride, phenazine methosulfate, nitrate, cytochrome c, ferritin
-
?
xanthine + H2O + O2
uric acid + H2O2
-
enzyme also oxidizes hypoxanthine, some other purines, pterines and aldehydes, i.e. possesses the activity of EC 1.2.3.1, probably acts on the hydrated derivatives of these substrates
under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 H+ + 2 O2-
?
xanthine + H2O + O2
uric acid + H2O2
-
low specificity to substrate
-
?
xanthine + H2O + O2
uric acid + H2O2
-
low specificity to substrate
under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 H+ + 2 O2-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor ferricyanide
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor ferricyanide
under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 H+ + 2 O2-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor 2,6-dichlorophenolindophenol
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor 2,6-dichlorophenolindophenol
under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 H+ + 2 O2-
?
xanthine + H2O + O2
uric acid + H2O2
-
the enzyme accelerates reaction rate via base-catalyzed chemistry in which a Mo-OH group undertakes nucleophilic attack on the carbon center to be hydroxylated, with concomitant hydride transfer to a catalytically essential Mo=S group in the molybdenum coordination sphere. This chemistry appears to proceed via obligate two-electron chemistry rather than in individual steps to yield a reduced enzyme product complex with product coordinmated to the active site molybdenum by means of the newly introduced hydroxyl group in a sinple end-on fashion. Product displacement by hydroxide and electron transfer to other redox-active centers in the enzyme complete the catalytic sequence
-
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor ferricyanide
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor 2,6-dichlorophenolindophenol
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor ferricyanide
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor 2,6-dichlorophenolindophenol
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
enzyme contributes to the oxidant stress component of ischemia-reperfusion injury to intestine and liver, O2- production decreases with increasing substrate concentrations
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
Megalodesulfovibrio gigas
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
-
electron acceptor O2
-
?
xanthine + NO2-
uric acid + NO
-
-
-
?
xanthine + NO2-
uric acid + NO
-
oxidation of the enzyme by NO2- or reduction by xanthine take place at the molybdenum site
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
xanthine oxidoreductase exists in two forms. The protein normally exists as xanthine dehydrogenase, XDH, EC 1.17.1.4, and utilizes NAD+ as its final electron acceptor in catalysis. Under certain conditions, most notably schemia and/or hypoxia, XDH can be converted to an oxidase form, XO, which can no longer reduce NAD+ and instead utilizes O2 exclusively as the terminal electron acceptor in the course of turnover. This conversion may occur either by oxidation of sulfhydryl groups and/or by limited proteolysis
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
binding modes of the substrate xanthine and mechanism of its hydroxylation, overview
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
conversion of xanthine to uric acid at the molybdenum-containing active site
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
binding modes of the substrate xanthine and mechanism of its hydroxylation, overview
-
-
?
additional information
?
-
-
XDH, EC 1.17.1.4, can be converted into xanthine oxidase, XO, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20%
-
-
?
additional information
?
-
-
XDH, EC 1.17.1.4, can be converted into xanthine oxidoreductase, XO, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20%
-
-
?
additional information
?
-
-
AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher than the activity with xanthine accompanied by a doubling in superoxide production and is dependent on sulfurated molybdenum cofactor, overview. FAD is crucial for NADH-based superoxide formation of AtXDH1, whereas the molybdenum cofactor has only little or no influence on the activity, residues E831, R909, E1297, W364, and Y421 are involved
-
-
?
additional information
?
-
-
AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher than the activity with xanthine accompanied by a doubling in superoxide production, overview. FAD is crucial for NADH-based superoxide formation of AtXDH1, whereas the molybdenum cofactor has only little or no influence on the activity, residues E831, R909, E1297, W364, and Y421 are involved
-
-
?
additional information
?
-
-
the catalytic reaction of xanthine oxidase is initiated by abstraction of a proton from the Mo-OH group by a conserved active site glutamate residue. The oxidative hydroxylation of xanthine to uric acid takes place at the molybdenum center and results in the two-electron reduction of the metal from Mo(VI) to Mo(IV). The enzyme is subsequently re-oxidized by NAD+ or molecular oxygen in a reaction that occurs at the FAD cofactor
-
-
?
additional information
?
-
-
the catalytic reaction of xanthine oxidase is initiated by abstraction of a proton from the Mo-OH group by a conserved active site glutamate residue. The oxidative hydroxylation of xanthine to uric acid takes place at the molybdenum center and results in the two-electron reduction of the metal from Mo(VI) to Mo(IV). The enzyme is subsequently re-oxidized by NAD+ or molecular oxygen in a reaction that occurs at the FAD cofactor
-
-
?
additional information
?
-
-
addition of xanthine oxidase to a solution of acetaldehyde and ascorbate increases the rate of ascorbate oxidation, due to the action of superoxide radicals generated in the process
-
-
?
additional information
?
-
-
hydroxyl free radicals generated by the hypoxanthine/xanthine oxidase/Fe system are implicated in oxidation of dibromoacetonitrile to CN-
-
-
?
additional information
?
-
-
5-chloro-6-methyl-3H-pyrimidin-4-one is no substrate
-
-
?
additional information
?
-
-
evaluation of a HPLC detection method for enzyme reaction products, overview
-
-
?
additional information
?
-
-
nature and position of functional group on thiopurine substrates influence activity of xanthine oxidase
-
-
?
additional information
?
-
-
the enzyme also catalyzes the oxidation of hypoxanthine to xanthine as xanthine dehydrogenase, EC 1.17.1.4, using NAD+ a oxidant substrate, XDH, mechanism of transition between XOR and XDH, after conversion reversibly via disulfide formation or irreversibly via proteolytic cleavage involving residues R335, R427, W336, and F549, overview
-
-
?
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
-
-
?
additional information
?
-
-
the oxidation of xanthine takes place at the molybdenum center, and the electrons thus introduced are rapidly transferred to FAD via the Fe-SI and Fe-SII centers. Glu1261, located near the Mo-OH in the salicylate bound-form of XOR, initiates catalysis by deprotonating the Mo-OH group
-
-
?
additional information
?
-
-
quantum mechanical/molecular mechanical study of the reductive half-reaction of wild-type xanthine oxidase, overview
-
-
?
additional information
?
-
-
role of Glu802 is facilitating the tautomerization of hypoxanthine in the course of hydroxylation by the enzyme, substrate binding structures, overview
-
-
?
additional information
?
-
-
xanthine and lumazine are good substrates, while 2-hydroxy-6-methylpurine is a slow and poor substrate
-
-
?
additional information
?
-
scavenging activities of 1,1-diphenyl-2-picryhydrazyl (DPPH) radical and O2 generated with phenazine methosulfate (PMS) and NADH,overview
-
-
?
additional information
?
-
-
the enzyme shows two conformational stages with different activities: one is the xanthine oxidase, the second is xanthine dehydrogenase, EC 1.17.1.4
-
-
?
additional information
?
-
-
xanthine oxidase inhibition in small intestine ischemia-reperfusion injury leads to reduction in neutrophil infiltration
-
-
?
additional information
?
-
-
enzyme inhibitors exert beneficial effect on endothelial dysfunction, mechanisms, overview, mechanism of action in cardiovascular disease, overview
-
-
?
additional information
?
-
-
phosphatidylinositol 3-kinase and xanthine oxidase regulate nitric oxide and reactive oxygen species productions by apoptotic lymphocyte microparticles in endothelial cells, overview
-
-
?
additional information
?
-
-
the enzyme activity, but not oxidative damage parameters, at the time of sepsis diagnosis is significantly higher in non-survival septic patients than in survival patients, overview
-
-
?
additional information
?
-
-
the enzyme and its superoxide producing activity are involved in endothelial dysfunction in atherosclerosis, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the oxidation of endogenous and exogenous purines and pyrimidines
-
-
?
additional information
?
-
-
the enzyme is induced by heat shock, the reactive oxygen species produced by heat shock may play an important role in the heat shock-induced activation of MAPKs, which can induce MMP-1 and-9 expressions, overview
-
-
?
additional information
?
-
-
evaluation of a HPLC detection method for enzyme reaction products, overview
-
-
?
additional information
?
-
-
single nucleotide polymorphisms alter the substrate specificity of the enzyme, overview
-
-
?
additional information
?
-
-
the enzyme interacts with the Toll-like receptor-4, TLR-4, inducing proinflammatory cytokine production, extracellular superoxide production by the enzyme leads to nuclear translocation of nuclear factor-kappaB and increased neutrophil production of the NFkappaB-dependent cytokines tumor necrosis factor-alpha and macrophage inhibitory protein-2 mediated by TLR-4, overview
-
-
?
additional information
?
-
-
the enzyme is capable to generate superoxide radicals and H2O2 derived from it, the synthesis of the radicals is increased upon a temperature shift from 30°C to 45°C and by photosensitization of tumor cells with a hematoporphyrin derivative, overview
-
-
?
additional information
?
-
-
the enzyme, together with mitochondrial complex III, is responsible for reactive oygen species production in ischemic muscle, they act in tissue damage after ischemic-reperfusion, regulation, overview
-
-
?
additional information
?
-
-
xanthine oxidase inhibition in small intestine ischemia-reperfusion injury leads to prevention of intestine necrosis
-
-
?
additional information
?
-
-
chronic enzyme inhibition by allopurinol or febuxostat cannot prevent or treat the progression of congestive heart failure induced by coronary artery ligation in rabbits, overview
-
-
?
additional information
?
-
-
xanthine oxidase is necessary during the physiological involution of tissues
-
-
?
additional information
?
-
-
enzyme inhibitors exert beneficial effect on endothelial dysfunction, mechanisms, overview, mechanism of action in cardiovascular disease, overview
-
-
?
additional information
?
-
-
xanthine oxidase inhibition in small intestine ischemia-reperfusion injury leads to reduction in villar necrosis, reduced intestinal MPO levels, reduced circulating neutrophil priming and reduction in pulmonary damage, prevention of permeability changes in intestinal mucosa, reduction in length of necrotic small bowel by 60%, reduction in intestinal apoptosis and tissue MDA levels; reduction in plasma MDA levels and improvement in renal function, and improved small intestine anastomotic healing and animal survival, overview
-
-
?
additional information
?
-
-
xanthine oxidase-derived reactive oxygen species contribute to the development of D-galactosamine-induced liver injury in rats, overview
-
-
?
additional information
?
-
-
enzyme inhibition by orange juice and hesperetin participates in preventing oxidative stress by enhancing total antioxidant capacity and decreasing lipid peroxidation, overview
-
-
?
additional information
?
-
-
the oxidation of xanthine takes place at the molybdenum cofactor, and the electrons thus introduced are rapidly transferred to FAD via the Fe-SI and Fe-SII centers. Glu1261, located near the Mo-OH in the salicylate bound-form of XOR, initiates catalysis by deprotonating the Mo-OH group
-
-
?
additional information
?
-
purified recombinant wild-type and DELTAC mutant enzymes both exhibit mostly xanthine oxidase activity
-
-
?
additional information
?
-
ionized Glu232 of wild-type enzyme plays an important role in catalysis by discriminating against the monoanionic form of xanthine. Proposed orientations of xanthine binding in the active site of xanthine oxidoreductase, using the predominant tautomers of the neutral and monoanionic forms of xanthine, overview
-
-
?
additional information
?
-
-
xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine to uric acid, and oxygen radicals that are formed as a by-product at both of these oxidation steps may participate in plant defense reactions
-
-
?
additional information
?
-
-
xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine to uric acid, and oxygen radicals that are formed as a by-product at both of these oxidation steps may participate in plant defense reactions
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-methylxanthine + H2O + O2
1-methylurate + H2O2
-
-
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
6-mercaptopurine + H2O + O2
?
-
an anticancer drug
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
nitrate + NADH
nitrite + NAD+ + H2O
-
reaction can be an important source of NO production in ischemic tissues
-
-
?
nitrite + NADH
NO + NAD+ + H2O
-
reaction can be an important source of NO production in ischemic tissues
-
-
?
organic nitrate + NADH
organic nitrite + NAD+ + H2O
-
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
-
-
?
xanthine + H2O + O2
urate + H2O2
xanthine + O2 + H2O
urate + H2O2
additional information
?
-
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
-
-
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
-
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
-
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
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
-
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
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
production of superoxide radicals
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
pteridine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
purine + H2O + O2
?
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
from dead cancer cells
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
-
catalytically relevant binding mode of the substrate xanthine, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
the enzyme is involved in development of ischemia and equine laminitis, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
the enzyme plays a role in the development of distant organ dysfunction after abdominal surgery, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
old persons show higher enzyme expression and activity than young persons which promotes a worse prognosis for patients with chronic heart failure due to the increased contents of risk factor urate, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of reactive oxygen species via superoxide radicals involved in endothelial dysfunction
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
-
roles of active site residues E308 and R881 in binding and activation of purine substrate, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
the enzyme plays a role in the development of distant organ dysfunction after abdominal surgery, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
urate is involved in development of endothelial dysfunction, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
xanthine oxidase-derived extracellular superoxide anions stimulate activator protein 1 activity and hypertrophy in vascular smooth muscle via c-Jun N-terminal kinase and p38 mitogen-activated protein kinases, xanthine and xanthine oxidase treatment of smooth muscle cells lead to increased cell growth and size, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
xanthine oxidase inhibition, meaning a decrease in myocardial oxidative stress, improves left ventricular dysfunction in dilated cardiomyopathic hamsters, modelling, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals, treatment with an enzyme inhibitor largely prevents the development of endothelial dysfunction and atherosclerosis in mice
-
-
?
xanthine + H2O + O2
urate + H2O2
-
the enzyme plays a role in the development of distant organ dysfunction after abdominal surgery, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
xanthine oxidoreductase, XOR, can exist in a dehydrogenase form, XD, and an oxidase form, XO. Part of total XOR activity in peroxisomes is XO activity. The major function of XOR activity in the cytoplasm of rat liver parenchymal cells and in sinusoidal cells is not the production of O2 radicals, but rather the production of uric acid which can act as a potent antioxidant
-
-
?
xanthine + H2O + O2
urate + H2O2
-
old animals show higher enzyme expression and activity than young rats which promotes a worse prognosis for patients with chronic heart failure due to the increased contents of risk factor urate, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
-
production of superoxide radicals can be induced by gama-irradiation and contributes to oxidative stress and endothelial nitroredox imbalance with resultant endothelial dysfunction and altered vascular mechanics, mechanism and regulation, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
the enzyme is involved in regulation of reactive oxygen species in the functional response of veins and arteries to angiotensin II, norepinephrine, and acetylcholine
-
-
?
xanthine + H2O + O2
urate + H2O2
-
the enzyme plays a role in the development of distant organ dysfunction after abdominal surgery, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
urate is involved in development of endothelial dysfunction, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
xanthine oxidase inhibition by febuxostat lowers uric acid and alleviates systemic and glomerular hypertension in hyperuricaemia, experimentally-induced by inhibition of uricase with oxonic acid, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
xanthine oxidase is an important source of reactive oxygen species that contributes to neurovascular dysfunction in experimental diabetes, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
catalytically relevant binding mode of the substrate xanthine, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
xanthine oxidoreductase exists in two forms. The protein normally exists as xanthine dehydrogenase, XDH, EC 1.17.1.4, and utilizes NAD+ as its final electron acceptor in catalysis. Under certain conditions, most notably schemia and/or hypoxia, XDH can be converted to an oxidase form, XO, which can no longer reduce NAD+ and instead utilizes O2 exclusively as the terminal electron acceptor in the course of turnover. This conversion may occur either by oxidation of sulfhydryl groups and/or by limited proteolysis
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
-
-
-
-
?
additional information
?
-
-
XDH, EC 1.17.1.4, can be converted into xanthine oxidase, XO, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20%
-
-
?
additional information
?
-
-
XDH, EC 1.17.1.4, can be converted into xanthine oxidoreductase, XO, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20%
-
-
?
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
-
-
?
additional information
?
-
-
xanthine oxidase inhibition in small intestine ischemia-reperfusion injury leads to reduction in neutrophil infiltration
-
-
?
additional information
?
-
-
enzyme inhibitors exert beneficial effect on endothelial dysfunction, mechanisms, overview, mechanism of action in cardiovascular disease, overview
-
-
?
additional information
?
-
-
phosphatidylinositol 3-kinase and xanthine oxidase regulate nitric oxide and reactive oxygen species productions by apoptotic lymphocyte microparticles in endothelial cells, overview
-
-
?
additional information
?
-
-
the enzyme activity, but not oxidative damage parameters, at the time of sepsis diagnosis is significantly higher in non-survival septic patients than in survival patients, overview
-
-
?
additional information
?
-
-
the enzyme and its superoxide producing activity are involved in endothelial dysfunction in atherosclerosis, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the oxidation of endogenous and exogenous purines and pyrimidines
-
-
?
additional information
?
-
-
the enzyme is induced by heat shock, the reactive oxygen species produced by heat shock may play an important role in the heat shock-induced activation of MAPKs, which can induce MMP-1 and-9 expressions, overview
-
-
?
additional information
?
-
-
the enzyme interacts with the Toll-like receptor-4, TLR-4, inducing proinflammatory cytokine production, extracellular superoxide production by the enzyme leads to nuclear translocation of nuclear factor-kappaB and increased neutrophil production of the NFkappaB-dependent cytokines tumor necrosis factor-alpha and macrophage inhibitory protein-2 mediated by TLR-4, overview
-
-
?
additional information
?
-
-
the enzyme is capable to generate superoxide radicals and H2O2 derived from it, the synthesis of the radicals is increased upon a temperature shift from 30°C to 45°C and by photosensitization of tumor cells with a hematoporphyrin derivative, overview
-
-
?
additional information
?
-
-
the enzyme, together with mitochondrial complex III, is responsible for reactive oygen species production in ischemic muscle, they act in tissue damage after ischemic-reperfusion, regulation, overview
-
-
?
additional information
?
-
-
xanthine oxidase inhibition in small intestine ischemia-reperfusion injury leads to prevention of intestine necrosis
-
-
?
additional information
?
-
-
chronic enzyme inhibition by allopurinol or febuxostat cannot prevent or treat the progression of congestive heart failure induced by coronary artery ligation in rabbits, overview
-
-
?
additional information
?
-
-
xanthine oxidase is necessary during the physiological involution of tissues
-
-
?
additional information
?
-
-
enzyme inhibitors exert beneficial effect on endothelial dysfunction, mechanisms, overview, mechanism of action in cardiovascular disease, overview
-
-
?
additional information
?
-
-
xanthine oxidase inhibition in small intestine ischemia-reperfusion injury leads to reduction in villar necrosis, reduced intestinal MPO levels, reduced circulating neutrophil priming and reduction in pulmonary damage, prevention of permeability changes in intestinal mucosa, reduction in length of necrotic small bowel by 60%, reduction in intestinal apoptosis and tissue MDA levels; reduction in plasma MDA levels and improvement in renal function, and improved small intestine anastomotic healing and animal survival, overview
-
-
?
additional information
?
-
-
xanthine oxidase-derived reactive oxygen species contribute to the development of D-galactosamine-induced liver injury in rats, overview
-
-
?
additional information
?
-
-
enzyme inhibition by orange juice and hesperetin participates in preventing oxidative stress by enhancing total antioxidant capacity and decreasing lipid peroxidation, overview
-
-
?
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(2S)-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-2,3-dihydro-4H-chromen-4-one
-
a flavone compound from Selaginellaceae with antiviral activity
(4'-methoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
-
-
(E)-9-nitro-octadec-9-en-1-ol
-
slight inhibition
(E)-9-nitro-octadec-9-enoic acid
-
strong inhibition
1,2,4-triazolo[1,5-a]pyrimidine
-
poor inhibitor
1,2-Dihydroxybenzene 3,5-disulfonic acid
-
inhibits reaction with cytochrome c
1,3,6,7-tetrahydroxy-9H-xanthen-9-one
-
-
1-(3-(furan-2-yl)-4,5-dihydro-5-(pyridin-4-yl)pyrazol-1-yl)ethanone
-
1-(4'-nitrophenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
-
-
1-(4'-trifluoromethylphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
-
-
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
-
-
1-4-tolyl-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
-
-
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-dichloro-6-(2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazolin-5-yl)phenol
-
2,4-dihydroxy-6-[(E)-2-(4-hydroxyphenyl)ethenyl]benzaldehyde
-
-
2,4-dinitrofluorobenzene
-
-
2,6-diaminopurine
-
poor inhibitor
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
-
competitive, 50% inhibition at 0.00019 mM; competitive, 50% inhibition at 0.00020 mM
2-(3-phenyl-1H-pyrazol-5-yl)aniline
-
2-(4-chlorophenyl)-5-(3,4-dimethoxyphenyl)-5,6-dihydropyrazolo[1,5-c]quinazoline
-
2-Amino-4-hydroxy-6-formylpterine
2-Amino-4-hydroxypterine-6-aldehyde
-
-
2-amino-6-chloropurine
-
poor inhibitor
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-Aminopurine
-
poor inhibitor
2-chloro-6(methylamino)purine
-
competitive
2-chloroadenine
-
substrate analogue
2-coumaric acid
-
competitively inhibits the enzyme by binding to the active site, have a protective effect against reactive oxygen species in cells, structure-function relationship, computational molecular docking, overview
2-hydroxy-4-methoxy-6-[(E)-2-(4-methoxyphenyl)ethenyl]benzaldehyde
-
a resveratrol derivative
2-hydroxy-6-methylpurine
interacts with Arg880 in both active sites of the enzyme dimer, binding structure, overview
2-hydroxy-6-[(E)-2-(4-hydroxyphenyl)ethenyl]-4-methoxybenzaldehyde
-
a resveratrol derivative
2-methoxy-4-(2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazolin-5-yl)phenol
-
2-methoxycinnamic acid
-
competitively inhibits the enzyme by binding to the active site, have a protective effect against reactive oxygen species in cells, structure-function relationship, computational molecular docking, overview
2-phenylpyrazolo[1,5-c]quinazoline
-
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-(4-chlorophenyl)-1H-pyrazol-5-yl]aniline
-
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
3,4-dihydroxyphenyl dodecanoate
sigmoidal inhibition of superoxide anion formation
3,4-dihydroxyphenyl octanoate
-
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-coumaric acid
-
competitively inhibits the enzyme by binding to the active site, have a protective effect against reactive oxygen species in cells, structure-function relationship, computational molecular docking, overview
3-methoxycinnamic acid
-
competitively inhibits the enzyme by binding to the active site, have a protective effect against reactive oxygen species in cells, structure-function relationship, computational molecular docking, overview
3-[[(3,6,7-trihydroxy-9-oxo-9H-xanthen-1-yl)oxy]methyl]benzonitrile
-
-
4'-methylether robustaflavone
-
a flavone compound from Selaginellaceae with antiviral activity
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-(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-(3-chlorophenyl)-1-(9-ethyl-9H-carbazol-3-yl)-3-phenylazetidin-2-one
-
-
4-(4'-aminopyrazolo[3,4-d]pyrimidin-1-yl)-benzonitrile
-
-
4-(4-chlorophenyl)-1-(9-ethyl-9H-carbazol-3-yl)-3-phenylazetidin-2-one
-
-
4-Aminopyrazolo[3,4-d]pyrimidine
-
competitive
4-coumaric acid
-
competitively inhibits the enzyme by binding to the active site, have a protective effect against reactive oxygen species in cells, structure-function relationship, computational molecular docking, overview
4-Hydroxycoumarin
-
competitive inhibition and interaction with the molybdopterin region of the enzyme, structure-function relationship of coumarin derivatives in inhibition of the enzyme, structure-based computer-aided molecular modeling, overview
4-iminocyclohexa-2,5-dien-1-one
-
-
4-methoxycinnamic acid
-
competitively inhibits the enzyme by binding to the active site, have a protective effect against reactive oxygen species in cells, structure-function relationship, computational molecular docking, overview
4-methylesculetin
-
competitive inhibition and interaction with the molybdopterin region of the enzyme, structure-function relationship of coumarin derivatives in inhibition of the enzyme, structure-based computer-aided molecular modeling, overview
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
-
4-[[(3,6,7-trihydroxy-9-oxo-9H-xanthen-1-yl)oxy]methyl]benzonitrile
-
-
5,6-Dimethylbenzimidazole
-
poor inhibitor
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-(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-cyano-4-isobutoxyphenyl)isoxazole-3-carboxylic acid
-
-
5-(3-nitrophenyl)-2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazoline
-
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-amino-1-(4'-carboxyphenyl)-1H-pyrazole-4-carbonitrile
-
-
5-methylbenzimidazole
-
poor inhibitor
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-O-methylguanine
-
poor inhibitor
7-hydroxy-4-methylcoumarin
-
low competitive inhibition and interaction with the molybdopterin region of the enzyme, structure-function relationship of coumarin derivatives in inhibition of the enzyme, structure-based computer-aided molecular modeling, overview
7-hydroxycoumarin
-
low competitive inhibition and interaction with the molybdopterin region of the enzyme, structure-function relationship of coumarin derivatives in inhibition of the enzyme, structure-based computer-aided molecular modeling, overview
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-Hydroxyquinoline-7-sulfonic acid
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
amentoflavone
-
a flavone compound from Selaginellaceae with antiviral activity
aminoguanidine
-
78.6% inhibition at 0.04 mM
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
ascorbate
-
43.5% inhibition at 0.04 mM
asperuloside
-
from Paederia scandens extract
butyl caffeate
competitive inhibition of urate and superoxide anion formation
Ca2+
-
83% inhibition at 1 mM
caffeic acid phenethyl ester
-
55.0% inhibition at 0.004 mM, competitively inhibits the enzyme by binding to the active site, have a protective effect against reactive oxygen species in cells, structure-function relationship, computational molecular docking, overview
cassia oil
-
oral adminstration of cassia oil significantly reduces serum and hepatic urate levels in hyperuricemic mice. At 600 mg/kg, cassia oil is as potent as allopurinol. This hypouricemic effect is explained by inhibiting activities of liver xanthine oxidase and xanthine oxidoreductase
catechin
inhibits at lower concentration
chicoric acid
-
i.e. dicaffeoyltartaric acid
chlorogenic acid
-
i.e. 5-O-caffeoylquinic acid
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
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
-
Cinnamic acid
-
40.2% inhibition at 0.04 mM, competitively inhibits the enzyme by binding to the active site, have a protective effect against reactive oxygen species in cells, structure-function relationship, computational molecular docking, overview
Cu2(C16H24N2O)2ClO4
-
-
-
Cu[Cu(CH3COO)(C17H16N2O2)]2
-
-
-
cyanidin 3-O-(6-O-malonyl-beta-D-glucoside)
-
-
cyanidin-3-O-beta-D-glucoside
-
-
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
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
esculetin
-
strong, competitive inhibition and interaction with the molybdopterin region of the enzyme, structure-function relationship of coumarin derivatives in inhibition of the enzyme, structure-based computer-aided molecular modeling, overview
ferulic acid
-
competitively inhibits the enzyme by binding to the active site, have a protective effect against reactive oxygen species in cells, structure-function relationship, computational molecular docking, overview
folic acid
-
uncompetitive inhibition of oxidation of dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
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
Hg2+
-
95% inhibition at 1 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
ioniceraflavone
-
i.e. 5,5'',7,7''-tetrahydroxy-2,2''-di(p-hydroxyphenyl)-2'',3''-dihydro[3,6'']bichromenyl-4,4''-dione, from ethanolic leaf extracts of Lonicera hypoglauca
isoferulic acid
-
competitively inhibits the enzyme by binding to the active site, have a protective effect against reactive oxygen species in cells, structure-function relationship, computational molecular docking, overview
kaempferol
inhibits at lower concentration
lithospermic acid
-
isolated from roots of medicinal herb Salvia mitiorrhiza, the compound shows competitive enzyme inhibition activity and in vivo hypouricemic and anti-inflammatory effects in rats pretreated with uricase inhibitor potassium oxonate, overview
losartan
-
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 7-methyl ether
-
-
luteolin 7-O-beta-D-glucuronide
-
-
magnesium lithospermate B
-
from Salvia miltiorrhiza, an eastern medical plant, i.e. Danshen or Dansham, competitive inhibition, the compound shows hypouricemic activity in vivo against potassium oxonate-induced hyperuricaemia in mice
mannitol
-
significant decrease in rate of oxidation of dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
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
-
Mn[Mn(CH3COO)(C25H20N2O2)]2
-
-
-
myoglobin
-
inhibits reaction with cytochrome c as acceptor
-
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-(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
-
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
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
noradrenaline
-
15% inhibition at 0.1 mM, 30% inhibition at 1 mM
O2
-
competitive inhibitor of NO production
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
orange juice
-
inhibits hepatic XOR activity and decreases serum uric acid levels and exhibits antioxidative and antihyperuricemic properties
-
paederoside
-
from Paederia scandens extract
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
Pterines
-
or other heterocyclic compounds, which are either not oxidized or oxidized rather slowly
-
pycnogenol
-
extract from french maritime pine bark, contains 75% (w/w) procyanidins formed by catechin and epicatechin but also taxifolin and phenolcarbonic acids and their glycosides, uncompetitive inhibitor, 0.01 mg/ml, 35% inhibition, 0.1 mg/ml, 80% inhibition, enzyme recovers activity upon dissociation of pycnogenol from enzyme
-
Pyridine
-
highly reduced activity of xanthine oxidase in the presence of pyridine, overview
quercetin 3-O-beta-D-glucoside
-
-
quercetin 3-O-beta-D-glucuronide
-
-
renierol
-
a natural enzyme inhibitor from the marine sponge Haliclona sp.
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
robustaflavone
-
a flavone compound from Selaginellaceae with antiviral activity
scandoside
-
from Paederia scandens extract
scopoletin
-
low competitive inhibition and interaction with the molybdopterin region of the enzyme, structure-function relationship of coumarin derivatives in inhibition of the enzyme, structure-based computer-aided molecular modeling, overview
silibinin
-
a mixed-type, not-time-dependent inhibitor
Superoxide dismutase
-
inhibits peroxynitrite generation
-
Tetraethylthiuram disulfide
theaflavin-3,3'-di-O-gallate
-
50% inhibition at 0.049 mM
Trolox
-
a radical scavenger compound
Zn[(Zn(C3H4N2)(C17H18N2O2))2(NO3)](NO3)
-
-
Zn[{Zn(C3H4N2)(C17H18N2O2)}2(NO3)](NO3)
-
-
-
[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
-
-
[Cd(C12H16N2)(m-NCS)2]
-
-
-
[Co(C16H23N2O)2]ClO4
-
-
-
[Cu(C13H11N2O)(H2O)] x ClO4
-
-
-
[Cu(C13H11N2O)(H2O)](NO3) x H2O
-
-
-
[Cu2(C16H24N2O)2Cl4]
-
-
-
1-[3-cyano-4-(2,2-dimethylpropoxy)phenyl]-1H-pyrazole-4-carboxylic acid
-
-
1-[3-cyano-4-(2,2-dimethylpropoxy)phenyl]-1H-pyrazole-4-carboxylic acid
-
-
2-Amino-4-hydroxy-6-formylpterine
-
-
2-Amino-4-hydroxy-6-formylpterine
-
-
2-[(2,3-dimethylphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
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-[(2,4-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-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-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-[(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-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-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-[(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-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-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-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-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-[(4-methoxyphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
7-methyl-2-(phenoxymethyl)-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
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-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-[(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-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-[(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-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
-
-
7-methyl-2-[(4-nitrophenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
8-Hydroxyquinoline-7-sulfonic acid
-
-
8-Hydroxyquinoline-7-sulfonic acid
-
-
Ag+
-
85% inhibition at 1 mM
allopurinol
-
-
allopurinol
-
96% inhibition at 1 mM
allopurinol
-
used as anti-gout drug
allopurinol
-
inhibits substrate binding at the molybdenum site
allopurinol
-
competitive inhibition of oxidation of dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
allopurinol
-
inhibits peroxynitrite generation, IC50: 0.007 mM
allopurinol
-
IC50: 0.0026 mM
allopurinol
-
allopurinol is a conventional substrate that generates superoxide radicals during its oxidation to oxypurinol
allopurinol
-
competitive, 50% inhibition at 0.0025 mM
allopurinol
-
a suicide inhibitor of XOD, a pyrazolopyrimidine derivative, and an analogue of hypoxanthine
allopurinol
-
a time-dependent inhibitor
allopurinol
59.2% inhibition at 0.05 mM
allopurinol
90% inhibition at 0.045 mM
allopurinol
-
inhibits xanthine and hypoxanthine oxidation in vivo in intestine and pancreas, but enhances the activity in liver, tissue-dependent effects, overview
allopurinol
-
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
allopurinol
-
enzyme inhibition with allopurinol does not improve endothelium-dependent vasodilation before
allopurinol
-
i.e. 1, 5-dihydro-4H-pyrazolo [3, 4-d]pyrimidine-4-one, allopurinol is a substrate and a competitive inhibitor for xanthine oxidase, it binds irreversibly at the active site reducing molybdenum VI to IV, and it is used for treatment of hyperuricemia
allopurinol
-
treatment of TO-2 hamsters with allopurinol inhibits both the decrease in GSH/GSSG ratio and the increase in malondialdehyde levels in the heart
allopurinol
-
strong competitive inhibition
allopurinol
-
36.6% inhibition at 0.04 mM
allopurinol
-
decreasesserum xanthine oxidase activity but increases liver xanthine oxidase activity significantly
allopurinol
-
i.e. 1, 5-dihydro-4H-pyrazolo [3, 4-d]pyrimidine-4-one, allopurinol is a substrate and a competitive inhibitor for xanthine oxidase, it binds irreversibly at the active site reducing molybdenum VI to IV, and it is used for treatment of hyperuricemia
allopurinol
-
treatment with the inhibitor improves nerve and vascular function in diabetic rats, sciatic nerve and superior cervical ganglion blood flow is halved by diabetes and allopurinol corrects this by approximately 63%, Ngamma-nitro-L-arginine acts as an antagonist, effects on diabetic and non-diabetic rats, overview
allopurinol
-
40% inhibition at 0.0285 g per kg body weight
allopurinol
-
shows strong enzyme inhibition and hypouricemic effect
allopurinol
-
i.e. 4-hydroxypyrazolo(3,4-d)pyrimidine, a purine analogue and a competitive inhibitor
alloxan
-
-
alloxanthine
-
alloxanthine
-
a mechanism-based inhibitor, binding structure, overview. Inhibition mechanism involves binding to molybdenum, overview
apigenin
-
mixed type inhibition of xanthine, strong inhibitor of xanthine oxidase, weak inhibition of monoamine oxidase
apigenin
binding structure, thermodynamic, and kinetic analysis, computational docking
arsenite
-
-
ascorbic acid
-
-
Borate
-
-
caffeic acid
competitive inhibition of urate and superoxide anion formation
caffeic acid
-
42.8% inhibition at 0.04 mM, competitively inhibits the enzyme by binding to the active site, have a protective effect against reactive oxygen species in cells, structure-function relationship, computational molecular docking, overview
chalcones
-
-
Cu2+
-
76% inhibition at 1 mM
cyanide
-
-
diphenylene iodonium chloride
-
inhibits nitrate reduction only when NADH is used as reducing substrate and does not inhibit nitrite generation when xanthine is used
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
epicatechin
inhibits at lower concentration
febuxostat
-
-
febuxostat
-
i.e. 2-[3-cyano-4-(2-methylpropoxy)-phenyl]-4-methylthiazole-5-carboxylic acid, a nonpurine-selective inhibitor used for management of hyperuricemia in patients with gout, effects of age and gender on pharmacokinetics, pharmacodynamics, and safety, detailed overview
febuxostat
-
i.e. 2-[3-cyano-4-(2-methylpropoxy)phenyl]-4-methylthiazole-5-carboxylic acid, a non-purine selective inhibitor of xanthine oxidase, an anti-hyperuricaemia drug with low drug-drug interaction potential in clinical use, in vitro drug-drug interaction studies, using ibuprofen, verapamil, nitrendipine, captopril, bezafibrate, warfarin, and digoxin. Febuxostat does not influence the plasma protein binding, and the presence of ibuprofen or warfarin does not change the plasma protein binding of febuxostat of ibuprofen or warfarin, overview
febuxostat
-
a potent non-purine, selective inhibitor of the enzyme
febuxostat
-
the inhibitor lowers uric acid and alleviates systemic and glomerular hypertension in experimental hyperuricaemia
formaldehyde
-
-
formaldehyde
-
determination and analysis of the structure of the formaldehyde-inhibited Mo(V) state of xanthine oxidase, overview
green tea extract
-
-
-
hesperetin
-
50% inhibition at 0.039 mM
hesperetin
-
i.e. 3',5,7-trihydroxy-4'-methoxyflavanone, major flavanone component of orange juice, inhibits hepatic XOR activity and decreases serum uric acid levels, exhibits antioxidative and antihyperuricemic properties
hydroxylamine
-
-
Imidazotriazines
-
-
isatin
-
-
luteolin
-
mixed type inhibition of xanthine, strong inhibitor of xanthine oxidase, weak inhibition of monoamine oxidase
luteolin
-
competitive inhibition
methanol
-
-
ninhydrin
-
-
oxypurinol
-
-
oxypurinol
-
inhibits NO generation triggered by xanthine, NADH or 2,3-dihydroxybenzaldehyde
oxypurinol
-
the suicide inhibitor allopurinol is oxidized to oxypurinol by XOR at the molybdenum cofactor, where oxypurinol then noncompetitively inhibits enzyme activity. Complete inhibition of free enzyme at 0.1 mM, 50% inhibition of heparin resin-bound enzyme
oxypurinol
-
enzyme inhibition with oxypurinol improves endothelium-dependent vasodilation before
oxypurinol
-
active metabolite of allopurinol
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
quercetin
-
competitive inhibition
quercetin
inhibits at lower concentration
quercetin
structure analysis of quercetin in complex with the enzyme, overview. The inhibitor adopts a single orientation with its benzopyran moiety sandwiched between Phe 914 and Phe 1009 and ring B pointing toward the solvent channel leading to the molybdenum active center. The favorable steric complementarity of the conjugated three-ring structure of quercetin with the active site and specific hydrogen-bonding interactions of exocyclic hydroxy groups with catalytically relevant residues Arg 880 and Glu 802 correlate well with a previously reported structure-activity relationship of flavonoid inhibitors of xanthine oxidase
Tetraethylthiuram disulfide
-
-
Tetraethylthiuram disulfide
-
-
thiocyanate
-
-
xanthine
-
no substrate inhibition
xanthine
-
at high concentrations
xanthine
-
substrate inhibition at high concentration
additional information
-
NAD+ and diphenylene iodonium inhibit NADH-dependent superoxide formation of AtXDH1; NAD+ inhibits NADH-dependent superoxide formation of AtXDH1
-
additional information
-
study on the effect of food extracts on enzyme activity in vitro. Extract of black tea, extract of rooibus herbal tea, purple grape juice, extract of clove, and cranberry juice are inhibitory
-
additional information
-
substrate-dependent inhibitory potencies, overview
-
additional information
-
enzyme inhibition by aqueous extract from Pieris brassicae larvae reared on Brassica oleracea L. var. costata, phenolic profiles of plant and insect larvae, overview. The extract shows an effective concentration-dependent protective activity against superoxide and hydroxyl radicals, kinetics, overview
-
additional information
-
no inhibition by (9Z,11E)-13-(hydroxyimino)octadeca-9,11-dienoic acid, (9Z,11E)-13-oxooctadec-9,11-dienoic acid, (E)-12-nitrooctadec-12-enoic acid, (Z)-9-nitrooctadec-9-enoic acid, 9-nitrooctadecanoic acid, (E)-9-nitrooctadec-9-enamide, (E)-10-nitrooctadec-9-enamide, (E)-9-nitro-N'-biotinyl-octadec-9-enehydrazide, and (E)-10-nitro-N'-biotinyl-octadec-9-enehydrazide. Irreversible inhibition, e.g. by thiol reagents, including glutathione, 2-mercaptoethanol, and dithiothreitol, inhibits XOR activity in a concentration-dependent manner. Inhibition is specific to site of fatty acid nitration and conformation in vivo. Structure-function study, inhibition of electron transfer reactions at the molybdenum cofactor, overview
-
additional information
-
eugenol, methyleugenol, and dihydromethyleugenol are poor inhibitors
-
additional information
-
no inhibition by curcumin in vitro
-
additional information
-
inhibitory effects of Tamus communis root extracts, traditionally used in folk medicine in Algeria and containing polyphenols and flavonoids, on the enzyme, extracts with methanol, chloroform, or ethyl acetate and distilled water as solvents, overview
-
additional information
-
xanthone derivatives as xanthine oxidase inhibitors, synthesis of a series of xanthone derivatives, overview. No inhibition by 8d, 8e, 8f, 8h, 8j, 8k, 8m, 8n, 8o, 8p, 8q, 8s, and 8t
-
additional information
-
synthesis and inhibitory activity of 7-methyl-2-(phenoxymethyl)-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one derivatives, molecular modeling and docking studies, overview
-
additional information
-
synthesis of some 5-phenylisoxazole-3-carboxylic acid derivatives as potent xanthine oxidase inhibitors, molecular modeling using 5-(3-cyano-4-isobutoxyphenyl)isoxazole-3-carboxylic acid and febuxostat, overview. No inhibition by 5-[4-(4-methylbenzyloxy)-3-nitrophenyl]isoxazole-3-carboxylic acid and 5-[3-cyano-4-(4-methylbenzyloxy)phenyl]-isoxazole-3-carboxylic acid
-
additional information
rational design, synthesis, and xanthine oxidase inhibitory activity of 5,6-dihydropyrazolo/pyrazolo[1,5-c]quinazoline derivatives, molecular docking into the enzyme's active site, structure activity relationship, overview. Mode of binding and important interactions such as hydrogen bonding, Pi-Pi stacking with amino acid residues like Ser876, Thr1010, Phen914, Phe1009, and Phe649 with close proximity to dioxothiomolybdenum
-
additional information
xanthine oxidase inhibitory activity of nicotino/isonicotinohydrazides, in vitro, in silico, and in vivo studies, overview. No inhibition by N'-[(E)-(2-nitrophenyl)methylidene]pyridine-3-carbohydrazide, N'-[(E)-(4-nitrophenyl)methylidene]pyridine-3-carbohydrazide, N'-[(E)-(3-hydroxyphenyl)methylidene]pyridine-3-carbohydrazide, N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]pyridine-3-carbohydrazide, N'-[(E)-(2-ethoxyphenyl)methylidene]pyridine-3-carbohydrazide, N'-[(E)-(2-methoxyphenyl)methylidene]pyridine-3-carbohydrazide, N'-[(E)-(3,4-dimethoxyphenyl)methylidene]pyridine-3-carbohydrazide, N'-[(E)-(2,3,4-trimethoxyphenyl)methylidene]pyridine-3-carbohydrazide, N'-[(E)-(2-hydroxy-6-methoxyphenyl)methylidene]pyridine-3-carbohydrazide, N'-[(E)-(2-hydroxy-5-methoxyphenyl)methylidene]pyridine-3-carbohydrazide, N'-[(E)-(2,4-dichlorophenyl)methylidene]pyridine-3-carbohydrazide, N'-[(E)-(2-hydroxy-5-methylphenyl)methylidene]pyridine-3-carbohydrazide, N'-[(E)-[4-(methylsulfanyl)phenyl]methylidene]pyridine-3-carbohydrazide, N'-[(E)-[4-(dimethylamino)phenyl]methylidene]pyridine-3-carbohydrazide, N'-[(E)-phenylmethylidene]pyridine-4-carbohydrazide, N'-[(E)-(2-nitrophenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(4-nitrophenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(4-hydroxyphenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(3-hydroxyphenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(2,4-dihydroxyphenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(2-ethoxyphenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(3,4-diethoxyphenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(3,4-dimethoxyphenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(4-ethoxy-3-hydroxyphenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(3-hydroxy-4-methoxyphenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(2-hydroxy-5-methoxyphenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(2-chlorophenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(2-fluorophenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(2,4-dichlorophenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(2-chloro-5-nitrophenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-(2-hydroxyphenyl)methylidene]pyridine-4-carbohydrazide, N'-[(E)-[4-(methylsulfanyl)phenyl]methylidene]pyridine-4-carbohydrazide, and N'-[(E)-[4-(dimethylamino)phenyl]methylidene]pyridine-4-carbohydrazide
-
additional information
synthesis and evaluation of xanthine oxidase inhibitory and antioxidant activities of 2-arylbenzo[b]furan derivatives based on salvianolic acid C, mode of XO inhibition, molecular modeling, Structure-activity relationships, overview. Molecular docking simulations of compounds methyl-(E)-(3-(2-(3,4-dihydroxyphenyl)-7-hydroxybenzofuran-4-yl)acryloyl)-L-phenylalaninate, (E)-(3-(2-(3,4-dihydroxyphenyl)-7-hydroxybenzofuran-4-yl)acryloyl)-L-phenylalanine, and (E)-(3-(2-(3,4-dimethoxyphenyl)-7-methoxybenzofuran-4-yl)acryloyl)-L-phenylalanine into the binding pocket of the bovine milk XDH/Febuxostat complex, PDB ID 1N5X
-
additional information
chrysin and its structural analogue apigenin exhibit an additive effect on inhibition of the enzyme, computational docking, overview. Structurally, both chrysin and apigenin possess two-benzene rings, which is very important in the inhibition on the activity of xanthine oxidase, whereas apigenin possesses an extra C-4' hydroxy group which might be the main reason of causing different inhibition compared to chrysin
-
additional information
effects of quercetin, kaempferol, (+) catechin, and (-) epicatechin on superoxide radical production through the modulation of manganese superoxide dismutase and xanthine oxidase activities, structure-activity relationships, overview
-
additional information
alkyl caffeates are strong antioxidants and inhibitors of xanthine oxidase. Caffeic acid derivatives equally suppressed O2- generation, and the suppression is stronger than inhibition of xanthine oxidase. Suppression of O2- generation catalyzed by xanthine oxidase with caffeic acid derivatives is not due to enzyme inhibition or O2 - scavenging but due to the reduction of xanthine oxidase molecules. Alkyl caffeates are effective inhibitors of uric acid and O2- catalyzed by xanthine oxidase as well as antioxidants for edible oil
-
additional information
natural flavonoids are attractive leads for rational design of preventive and therapeutic xanthine oxidase inhibitors due to their beneficial antioxidant, anti-inflammatory, and antiproliferative activities in addition to their micromolar inhibitory activities toward xanthine oxidase
-
additional information
-
the enzyme activity is not affected by smoking or gender
-
additional information
-
screening and characterization of 6-aminopurine-based xanthine oxidase inhibitors isolated from Triticum aestivum leaves water extracts, structure determination by mass spectrometry and NMR spectrometry analysis, overview
-
additional information
-
inhibitory potencies and cytotoxicity of resveratrol derivatives, no inhibition of xanthine oxidase by 4,6-dihydroxy-2-[(E)-2-(4-hydroxyphenyl)ethenyl]benzene-1,3-dicarbaldehyde, 4-(3-bromopropoxy)-2-((E)-2-[4-(3-bromopropoxy)phenyl]ethenyl)-6-hydroxybenzaldehyde, 2,4-dimethoxy-6-[(E)-2-(4-methoxyphenyl)ethenyl]benzaldehyde, ethyl (4-formyl-3-hydroxy-5-[(E)-2-(4-hydroxyphenyl)ethenyl]phenoxy)acetate, ethyl (4-((E)-2-[5-(2-ethoxy-2-oxoethoxy)-2-formyl-3-hydroxyphenyl]ethenyl)phenoxy)acetate, ethyl (4-((E)-2-[3,5-bis(2-ethoxy-2-oxoethoxy)-2-formylphenyl]ethenyl)phenoxy)acetate, and 4-(3-bromopropoxy)-2-hydroxy-6-[(E)-2-(4-hydroxyphenyl)ethenyl]benzaldehyde, overview
-
additional information
-
synthesis of N-aryl-5-amino-4-cyanopyrazole derivatives as enzyme inhibitors, potencies of the compounds in enzyme inhibition and cell growth inhibition, overview
-
additional information
-
enzyme inhibition by flavonoids in stem and leaf extract of Sida rhombifolia or Sidaguri, a traditional Indonesian medicinal plant. Extract fraction analysis and inhibition kinetics, overview
-
additional information
-
development of a photodiode array chip-based xanthine assay for high-throughput screening of xanthiine oxidase inhibitors using a PDA microchip system, mechanism of drug action, enzyme-inhibitor interaction analysis, overview
-
additional information
-
inhibitory effects of Tamus communis root extracts, traditionally used in folk medicine in Algeria and containing polyphenols and flavonoids, on the enzyme, extracts with methanol, chloroform, or ethyl acetate and distilled water as solvents, overview
-
additional information
-
coumarin and dihydrocoumarin are poor inhibitors, measurement of combined reactive oxygen species-scavenging and xanthine oxidase-inhibition activities, 3D modeling of the docking of coumarin derivatives on xanthine oxidase, overview
-
additional information
-
inhibitory potency of Schiff base transition metal complexes, structures, overview
-
additional information
-
inhibitory effects of phenylpropanoids on DNA relaxation activities, 1,1-diphenyl-2-picrylhydrazyl, and 5,5-dimethyl-1-pyrroline-N-oxide, and on iron-induced hydroxyl radical formation, hydroxyl radical-scavenger properties of the compounds, overview, 3D modelling of docking
-
additional information
-
ethanol leaf extracts of Lonicera hypoglauca, an endemic rattan growing in Taiwan, inhibits xanthine oxidase and reduces serum uric acid in mice, overview
-
additional information
-
inhibition of xanthine oxidase by thiosemicarbazones, hydrazones and dithiocarbazates derived from hydroxy-substituted benzaldehydes, overview
-
additional information
-
inhibitory effects of Tamus communis root extracts, traditionally used in folk medicine in Algeria and containing polyphenols and flavonoids, on the enzyme, extracts with methanol, chloroform, or ethyl acetate and distilled water as solvents, overview
-
additional information
-
alcoholic extract of air-dried aerial parts of the plant Paederia scandens has inhibitory activity on the enzyme and in vivo antihypouricemic activity in hyperuricemic rats pretreated with potassium oxonate, overview, no inhibition by benzbromarone and potassium oxonate
-
additional information
-
synthesis and inhibitory activity of 7-methyl-2-(phenoxymethyl)-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one derivatives, molecular modeling and docking studies, overview
-
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0.0196
(4'-methoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
Homo sapiens
-
-
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
0.0022
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
-
-
0.03477
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
0.0174
1-4-tolyl-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
Homo sapiens
-
-
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
0.011
2,4-dichloro-6-(2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazolin-5-yl)phenol
Bos taurus
pH 7.5, 22°C
0.0025
2,4-dihydroxy-6-[(E)-2-(4-hydroxyphenyl)ethenyl]benzaldehyde
Homo sapiens
-
pH 7.8, 25°C
0.0417
2-(3-phenyl-1H-pyrazol-5-yl)aniline
Bos taurus
pH 7.5, 22°C
0.00054 - 0.0177
2-amino-6-hydroxy-8-mercaptopurine
0.0026 - 0.0164
2-amino-6-purine thiol
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
0.00176 - 0.0018
2-[(2,4-dimethylphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
0.000413 - 0.000603
2-[(2-bromophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
0.000183 - 0.00165
2-[(2-chlorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
0.00059
2-[(2-fluorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
pH 7.5, temperature not specified in the publication
0.00256
2-[(3-bromophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
pH 7.5, temperature not specified in the publication
0.00618
2-[(3-chlorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
pH 7.5, temperature not specified in the publication
0.00198
2-[(3-fluorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
pH 7.5, temperature not specified in the publication
0.000623 - 0.000634
2-[(4-chloro-3-methylphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
0.000449 - 0.000461
2-[(4-chlorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
0.000269 - 0.000289
2-[(4-methoxyphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
0.0036
3,4-di-O-caffeoylquinic acid methyl ester
Bos taurus
-
reversible inhibition, IC50: 0.0036 mM
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
0.00708
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
0.0004
4-(4'-aminopyrazolo[3,4-d]pyrimidin-1-yl)-benzonitrile
Homo sapiens
-
-
0.0216
4-(4-chlorophenyl)-1-(9-ethyl-9H-carbazol-3-yl)-3-phenylazetidin-2-one
Bos taurus
-
pH 7.6, 37°C
0.0303
4-Aminopyrazolo[3,4-d]pyrimidine
Homo sapiens
-
pH 7.5, 25°C
0.0969
4-coumaric acid
Mus musculus
-
pH 8.0, 37°C, versus xanthine
0.0781
4-Hydroxycoumarin
Mus musculus
-
pH 7.0, 37°C, versus xanthine
0.184
4-methoxycinnamic acid
Mus musculus
-
pH 8.0, 37°C, versus xanthine
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
0.0437
5-(3,4-dimethoxyphenyl)-2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazoline
Bos taurus
pH 7.5, 22°C
0.00036
5-(3-cyano-4-isobutoxyphenyl)isoxazole-3-carboxylic acid
Bos taurus
-
pH 7.5, 25°C
0.021
5-(3-nitrophenyl)-2-phenyl-5,6-dihydropyrazolo[1,5-c]quinazoline
Bos taurus
pH 7.5, 22°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
0.0361
5-amino-1-(4'-carboxyphenyl)-1H-pyrazole-4-carbonitrile
Homo sapiens
-
-
0.0868
5-nitrobenzimidazole
Homo sapiens
-
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
0.0109
6-aminopurine
Homo sapiens
-
pH 7.5, 25°C
0.0924
6-thioguanine
Homo sapiens
-
pH 7.5, 25°C
0.000555
7-methyl-2-(phenoxymethyl)-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
pH 7.5, temperature not specified in the publication
0.000326 - 0.000362
7-methyl-2-[(2-methylphenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
0.00103 - 0.00107
7-methyl-2-[(3-methylphenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
0.00102
7-methyl-2-[(4-methylphenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
pH 7.5, temperature not specified in the publication
0.00203 - 0.002501
7-methyl-2-[(4-nitrophenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
0.00073 - 0.0316
allopurinol
0.00074 - 0.00357
apigenin
0.026 - 110
butyl caffeate
0.0115 - 0.2
caffeic acid
0.00626 - 0.1567
caffeic acid phenethyl ester
0.00367
Cd2+
Mus musculus
-
pH 7.8
0.00126
chrysin
Bos taurus
pH 7.4, 37°C
0.0234
Cu2(C16H24N2O)2ClO4
Mus musculus
-
pH 7.8
-
0.0014
Cu2+
Mus musculus
-
pH 7.8
0.013
Cu[Cu(CH3COO)(C17H16N2O2)]2
Mus musculus
-
pH 7.8
-
0.01 - 0.0164
decyl caffeate
0.0939
ferulic acid
Mus musculus
-
pH 8.0, 37°C, versus xanthine
0.0076 - 0.0125
heptyl caffeate
0.0108 - 0.019
hexyl caffeate
0.0167
hydroxychavicol
Bos taurus
-
-
0.1432
isoferulic acid
Mus musculus
-
pH 8.0, 37°C, versus xanthine
0.00059
luteolin
Bos taurus
-
pH 7.5, 25°C
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
0.0254
Mn[Mn(CH3COO)(C25H20N2O2)]2
Mus musculus
-
pH 7.8
-
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
0.0184
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
-
-
0.0121
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
1.36 - 1.85
renierol
Mus musculus
-
pH 7.5, inhibition of superoxide and urate production, respectively
0.0139
resveratrol
Homo sapiens
-
pH 7.8, 25°C
0.0083
salvianolic acid A
Bos taurus
above, pH not specified in the publication, 37°C
0.0461
Zn2+
Mus musculus
-
pH 7.8
0.0232
Zn[(Zn(C3H4N2)(C17H18N2O2))2(NO3)](NO3)
Mus musculus
-
pH 7.8
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
-
-
0.0022
[Cd(C12H16N2)(m-NCS)2]
Mus musculus
-
pH 7.8
-
0.047
[Co(C16H23N2O)2]ClO4
Mus musculus
-
pH 7.8
-
0.0962
[Cu(C13H11N2O)(H2O)] x ClO4
Mus musculus
-
pH 7.8
-
0.08125
[Cu(C13H11N2O)(H2O)](NO3) x H2O
Mus musculus
-
pH 7.8
-
0.0104
[Cu2(C16H24N2O)2Cl4]
Mus musculus
-
pH 7.8
-
0.0539
[Mn(C17H16N2O2)N3]
Mus musculus
-
pH 7.8
-
0.0195
[Zn(C9H10N2)(Cl)2]
Mus musculus
-
pH 7.8
-
additional information
additional information
-
0.00054
2-amino-6-hydroxy-8-mercaptopurine
Bos taurus
-
pH 7.4, versus substrate 6-mercaptopurine
0.0051
2-amino-6-hydroxy-8-mercaptopurine
Bos taurus
-
pH 7.4, versus substrate hypoxanthine
0.0177
2-amino-6-hydroxy-8-mercaptopurine
Bos taurus
-
pH 7.4, versus substrate xanthine
0.0026
2-amino-6-purine thiol
Bos taurus
-
pH 7.4, versus substrate 6-mercaptopurine
0.0073
2-amino-6-purine thiol
Bos taurus
-
pH 7.4, versus substrate hypoxanthine
0.0164
2-amino-6-purine thiol
Bos taurus
-
pH 7.4, versus substrate xanthine
0.00176
2-[(2,4-dimethylphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
pH 7.5, temperature not specified in the publication
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
0.000413
2-[(2-bromophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
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
0.000183
2-[(2-chlorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
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
0.000623
2-[(4-chloro-3-methylphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
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
0.000449
2-[(4-chlorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
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
0.000289
2-[(4-methoxyphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
pH 7.5, temperature not specified in the publication
0.2
3,4-dihydroxyphenyl dodecanoate
Bos taurus
above, pH 10.0, 25°C, inhibition of urate formation
92.5
3,4-dihydroxyphenyl dodecanoate
Bos taurus
above, pH 10.0, 25°C, inhibition of urate formation
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
0.000362
7-methyl-2-[(2-methylphenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
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
0.00107
7-methyl-2-[(3-methylphenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
pH 7.5, temperature not specified in the publication
0.00203
7-methyl-2-[(4-nitrophenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
Rattus norvegicus
-
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
allopurinol
Bos taurus
-
pH 7.5, temperature not specified in the publication
0.000753
allopurinol
Rattus norvegicus
-
pH 7.5, temperature not specified in the publication
0.00091
allopurinol
Bos taurus
-
pH 7.4, versus substrate hypoxanthine
0.0011
allopurinol
Mus musculus
-
pH 7.0, 37°C, versus xanthine
0.00143
allopurinol
Mus musculus
-
pH 8.0, 37°C, competitive versus xanthine
0.00192
allopurinol
Bos taurus
-
pH 7.4, versus substrate 6-mercaptopurine
0.00236
allopurinol
Bos taurus
-
pH 7.4, versus substrate xanthine
0.0026
allopurinol
Bos taurus
-
IC50: 0.0026 mM
0.00293
allopurinol
Bos taurus
pH 7.4, 37°C
0.00361
allopurinol
Bos taurus
pH not specified in the publication, 37°C
0.007
allopurinol
Bos taurus
-
inhibits peroxynitrite generation, IC50: 0.007 mM
0.0078
allopurinol
Homo sapiens
-
pH 7.5, 25°C
0.0103
allopurinol
Mus musculus
-
pH 7.8
0.0134
allopurinol
Homo sapiens
-
pH 7.8, 25°C
0.01467
allopurinol
Bos taurus
pH 7.4, 37°C
0.0307
allopurinol
Bos taurus
-
-
0.0316
allopurinol
Bos taurus
pH 7.5, 22°C
0.00074
apigenin
Bos taurus
-
pH 7.5, 25°C
0.00357
apigenin
Bos taurus
pH 7.4, 37°C
0.026
butyl caffeate
Bos taurus
pH 10.0, 25°C, inhibition of urate formation
110
butyl caffeate
Bos taurus
pH 10.0, 25°C, inhibition of urate formation
0.0115
caffeic acid
Bos taurus
above, pH 10.0, 25°C, inhibition of urate formation
0.0654
caffeic acid
Mus musculus
-
pH 8.0, 37°C, competitive versus xanthine
0.0654
caffeic acid
Mus musculus
-
pH 8.0, 37°C, versus xanthine
0.2
caffeic acid
Bos taurus
above, pH 10.0, 25°C, inhibition of urate formation
0.00626
caffeic acid phenethyl ester
Mus musculus
-
pH 8.0, 37°C, competitive versus xanthine
0.1567
caffeic acid phenethyl ester
Mus musculus
-
pH 8.0, 37°C, inhibition of hydroxylradical formation in the dimethyl-1-pyrroline-N-oxide spin-trapping assay
0.01
decyl caffeate
Bos taurus
pH 10.0, 25°C, inhibition of urate formation
0.0164
decyl caffeate
Bos taurus
pH 10.0, 25°C, inhibition of urate formation
0.0076
heptyl caffeate
Bos taurus
pH 10.0, 25°C, inhibition of urate formation
0.0125
heptyl caffeate
Bos taurus
pH 10.0, 25°C, inhibition of urate formation
0.0108
hexyl caffeate
Bos taurus
pH 10.0, 25°C, inhibition of urate formation
0.019
hexyl caffeate
Bos taurus
pH 10.0, 25°C, inhibition of urate formation
0.012
methyl caffeate
Bos taurus
pH 10.0, 25°C, inhibition of urate formation
0.143
methyl caffeate
Bos taurus
pH 10.0, 25°C, inhibition of urate formation
0.082
octyl protocatechuate
Bos taurus
above, pH 10.0, 25°C, inhibition of urate formation
0.125
octyl protocatechuate
Bos taurus
above, pH 10.0, 25°C, inhibition of urate formation
0.01
pentyl caffeate
Bos taurus
pH 10.0, 25°C, inhibition of urate formation
0.018
pentyl caffeate
Bos taurus
pH 10.0, 25°C, inhibition of urate formation
0.0115
propyl caffeate
Bos taurus
pH 10.0, 25°C, inhibition of urate formation
0.03
propyl caffeate
Bos taurus
pH 10.0, 25°C, inhibition of urate formation
0.0627
propyl protocatechuate
Bos taurus
above, pH 10.0, 25°C, inhibition of urate formation
0.125
propyl protocatechuate
Bos taurus
above, pH 10.0, 25°C, inhibition of urate formation
0.022
protocatechuic acid
Bos taurus
above, pH 10.0, 25°C, inhibition of urate formation
0.125
protocatechuic acid
Bos taurus
above, pH 10.0, 25°C, inhibition of urate formation
additional information
additional information
Bos taurus
-
-
-
additional information
additional information
Selaginella labordei
-
-
-
additional information
additional information
Rattus norvegicus
-
IC50 of lithopsermic acid is 0.0052 mg/ml
-
additional information
additional information
Bos taurus
-
in vitro bi-substrate-inhibitor-enzyme simulation and kinetics, overview
-
additional information
additional information
Mus musculus
-
IC50 of licewraflavone is 0.00085 mg/ml and for allopurinol is 0.00040 mg/ml
-
additional information
additional information
Homo sapiens
-
IC50 values for Tamnus communis root extract on cytochrome C reduction by the enzyme, overview
-
additional information
additional information
Bos taurus
-
IC50 values for Tamnus communis root extract on cytochrome C reduction by the enzyme, overview
-
additional information
additional information
Ovis aries
-
IC50 values for Tamnus communis root extract on cytochrome C reduction by the enzyme, overview
-
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