Information on EC 1.17.3.2 - xanthine oxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.17.3.2
-
RECOMMENDED NAME
GeneOntology No.
xanthine oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
xanthine + H2O + O2 = urate + H2O2
show the reaction diagram
mechanism
-
xanthine + H2O + O2 = urate + H2O2
show the reaction diagram
hydrogen-bonding arrangement of the substrate-bound complex at the active site, and proposed mechanism of the purine oxidation reaction by XOR
-
xanthine + H2O + O2 = urate + H2O2
show the reaction diagram
catalytic mechanism of xanthine oxidoreductase, overview
-
xanthine + H2O + O2 = urate + H2O2
show the reaction diagram
reaction mechanism, detailed overview. The reaction is initiated by proton abstraction from the Mo-OH group by Glu1261, the active-site base, followed by nucleophilic attack on the carbon to be hydroxylated, and hydride transfer to the Mo-S double bond. Suitable substrate orientation, overview. Arg880 is involved in stablizing the transition state in the course of nucleophilic attack, overview
-
xanthine + H2O + O2 = urate + H2O2
show the reaction diagram
reaction mechanism of XOR and binding modes of the substrate xanthine, overview. The oxidative hydroxylation of purine substrates takes place at the molybdenum center. Reducing equivalents introduced there are then transferred via two [2Fe-2S] centers to the FAD cofactor where reduction of the physiological electron acceptors occurs, NAD+ in the case of the dehydrogenase form, XDH, or O2 in the oxidase form, XO, of the enzyme occur
-
xanthine + H2O + O2 = urate + H2O2
show the reaction diagram
reaction mechanism for xanthine oxidase, overview. Catalysis is initiated by base-assisted nucleophilic attack of the equatorial Mo-OH on the C-8 carbon of xanthine with concomitant hydride transfer from C-8 to Mo=S, which simultaneously results in reduction of Mo(VI) to Mo(IV). Reoxidation of the molybdenum center occurs by electron transfer to the other redox-active centers of the enzyme, accompanied by deprotonation of the Mo-SH bond and displacement of bound product by hydroxide from solvent to regenerate the Mo-OH group
-
xanthine + H2O + O2 = urate + H2O2
show the reaction diagram
favored mechanism for the reaction with xanthine, overview
-
xanthine + H2O + O2 = urate + H2O2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
caffeine degradation III (bacteria, via demethylation)
-
Caffeine metabolism
-
Drug metabolism - other enzymes
-
Metabolic pathways
-
Purine metabolism
-
theophylline degradation
-
SYSTEMATIC NAME
IUBMB Comments
xanthine:oxygen oxidoreductase
An iron-molybdenum flavoprotein (FAD) containing [2Fe-2S] centres. Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1, aldehyde oxidase. Under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 O2.- + 2 H+. The mammalian enzyme predominantly exists as an NAD-dependent dehydrogenase (EC 1.17.1.4, xanthine dehydrogenase). During purification the enzyme is largely converted to the O2-dependent xanthine oxidase form (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [4,5,7,10] [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo [4,6,10].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
EC 1.1.3.2
-
formerly
EC 1.1.3.22
-
-
-
-
EC 1.2.3.2.
-
-
formerly
-
hypoxanthine oxidase
-
-
-
-
hypoxanthine-xanthine oxidase
-
-
-
-
oxidase, xanthine
-
-
-
-
Schardinger enzyme
-
-
-
-
xanthine oxidase
-
one of two conformational stages of the enzyme with different activities, the second is xanthine dehydrogenase
xanthine oxidoreductase
-
-
-
-
xanthine oxidoreductase
-
-
xanthine oxidoreductase
-
-
xanthine oxidoreductase
-
-
xanthine oxidoreductase
-
-
xanthine oxidoreductase
-
-
xanthine oxidoreductase
-
-
xanthine oxidoreductase
-
xanthine oxidoreductase can exists in a dehydrogenase form, XD, and an oxidase form, XO
xanthine oxidoreductase
P22985
-
xanthine oxidoreductase
Rattus norvegicus Sprague-Dawley
-
-
-
xanthine: oxygen oxidoreductase
-
-
xanthine:O2 oxidoreductase
-
-
-
-
xanthine:oxygen oxidoreductase
-
-
xanthine:xanthine oxidase
-
-
-
-
XnOx
-
-
XOR
-
xanthine oxidoreductase can exists in a dehydrogenase form, XD, and an oxidase form, XO
XOR
P22985
-
XOR
Rattus norvegicus Sprague-Dawley
-
-
-
hypoxanthine:oxygen oxidoreductase
-
-
-
-
additional information
-
XOR can adopt its XOR xanthone oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4
additional information
-
formerly EC 1.1.3.22
additional information
-
formerly EC 1.1.3.22
additional information
P22985
XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4
CAS REGISTRY NUMBER
COMMENTARY
9002-17-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Arthrobacter sp. S-2
S-2
-
-
Manually annotated by BRENDA team
commercial preapration
UniProt
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
Israeli-Holstein cows
-
-
Manually annotated by BRENDA team
Enterobacter cloacae KY 3074
KY 3074
-
-
Manually annotated by BRENDA team
Patas monkey
-
-
Manually annotated by BRENDA team
Erythrocebus patas Patas monkey
Patas monkey
-
-
Manually annotated by BRENDA team
f. catus
-
-
Manually annotated by BRENDA team
domesticus, male chicken
-
-
Manually annotated by BRENDA team
female and male
-
-
Manually annotated by BRENDA team
gastric mucosa of Helicobacter pylori positive and negative pediatric patients
-
-
Manually annotated by BRENDA team
gene XO
-
-
Manually annotated by BRENDA team
Greek population
-
-
Manually annotated by BRENDA team
lentil
-
-
Manually annotated by BRENDA team
male TO-2 cardiomyopathic Syrian hamsters
-
-
Manually annotated by BRENDA team
C57/BL6, C57/10Scn, and C57/10J mice
-
-
Manually annotated by BRENDA team
hyperuricemic mice induced by potassium oxonate
-
-
Manually annotated by BRENDA team
infected with Salmonella typhimurium and Pseudomonas aeruginosa
-
-
Manually annotated by BRENDA team
male ICR mice
-
-
Manually annotated by BRENDA team
male mice
-
-
Manually annotated by BRENDA team
mouse embryo cell lines: 3T3, 3T6, B-3T3, 3T12
-
-
Manually annotated by BRENDA team
white, mongrel, 3-months-old, female mice
-
-
Manually annotated by BRENDA team
Mus musculus BALB/c
male mice
-
-
Manually annotated by BRENDA team
male New Zealand White rabbits
-
-
Manually annotated by BRENDA team
conversion of xanthine oxidoreductase to oxidase
UniProt
Manually annotated by BRENDA team
male sprague-dawley rats
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
the xanthine dehydrogenase form can be obtained through incubation of xanthine oxidase with sulphydryl reducing reagents
-
-
Manually annotated by BRENDA team
xanthine oxidoreductase can exists in a dehydrogenase form, XD, and in an oxidase form, XO
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
male
-
-
Manually annotated by BRENDA team
a cultivar resistant to Russian wheat aphid, biotype SA1, Diuraphis noxia; cv. Tugela, a cultivar sensitive to Russian wheat aphid, biotype SA1, Diuraphis noxia
-
-
Manually annotated by BRENDA team
Triticum aestivum Tugela DN
a cultivar resistant to Russian wheat aphid, biotype SA1, Diuraphis noxia; cv. Tugela, a cultivar sensitive to Russian wheat aphid, biotype SA1, Diuraphis noxia
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
the enzyme is a key enzyme in th epathogenesis of hyperuricemia
metabolism
-
xanthine oxidase, a key enzyme in purine metabolism, produces reactive oxygen species causing vascular injuries and chronic heart failure
metabolism
-
the enzyme plays an important role in the metabolism of many xenobiotics and drugs, such as purines and pyrimidines, mercaptopurine and azathioprine, thiazides, pyrazinamide, and acyclovir
metabolism
-
xanthine oxidase is a key enzyme in the purine metabolic pathway, catalysing the oxidation of hypoxanthine to uric acid
metabolism
-
xanthine oxidase is the key enzyme that catalyzes the oxidation of hypoxanthine to xanthine and then to uric acid
metabolism
-
effects of enzyme inhibition in inflammatory macrophages, overview
physiological function
-
xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation
physiological function
-
xanthine oxidase is a key enzyme that can catalyze the conversion of xanthine to uric acid, causing various diseases in humans
physiological function
-
xanthine oxidoreductase is a ubiquitous molybdenum-iron-flavo enzyme with a central role in purine catabolism where it catalyzes the oxidation of hypoxanthine to xanthine and of xanthine to uric acid
physiological function
-
xanthine oxidase functions not only to hydroxylate xanthine at C-8 to give uric acid, but also hypoxanthine at C-2 to give xanthine in the immediate preceding step of purine catabolism
metabolism
Rattus norvegicus Sprague-Dawley
-
effects of enzyme inhibition in inflammatory macrophages, overview
-
additional information
-
the enzyme also serves as an important biological source of reactive oxygen species that are involved in many pathological processes, such as inflammation, atherosclerosis, cancer, and aging
additional information
-
elevated level of blood uric acid, hyperuricemia, is the underlying cause of gout, development of enzyme inhibitors more efficacious, than allopurinol, to treat gout and possibly against cardiovascular diseases, overview
additional information
-
the enzyme is regulated by substrates at active sites via cooperative interactions between catalytic subunits. A substrate can regulate the activity of xanthine oxidase via binding at the active sites, or a xanthine oxidase catalytic subunit can simultaneously serve as a regulatory unit
additional information
-
serum xanthine oxidase activity is correlated with serum uric acid levels, while no correlation is observed for liver xanthine oxidase activity. The serum uric acid levels in mice treated with the flavonoids genistein, apigenin, quercetin, rutin and astilbin are higher than control levels. No statistically significant difference in serum and liver xanthine oxidase activities between normal control mice and hyperuricemic mice
additional information
-
active site structure, overview
additional information
-
XOR can adopt its XOR xanthone oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4
additional information
-
XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4
additional information
-
xanthine oxidoreductase is implicated in many inflammatory diseases. Inhibition of XOR within the inflammatory mononuclear phagocytes, i.e. MNP, prevents neutrophil recruitment during adoptive transfer demonstrating the role of XOR in MNP-mediated neutrophil recruitment, role of XOR in the inflammatory state of MNP, overview. XOR activity is specifically increased by inflammatory mononuclear phagocyte differentiation. Inhibition of XOR reduces levels of CINC-1 secreted by inflammatory mononuclear phagocytes, and increases levels of SUMO-PPARgamma in the cell lines
additional information
Mus musculus BALB/c
-
serum xanthine oxidase activity is correlated with serum uric acid levels, while no correlation is observed for liver xanthine oxidase activity. The serum uric acid levels in mice treated with the flavonoids genistein, apigenin, quercetin, rutin and astilbin are higher than control levels. No statistically significant difference in serum and liver xanthine oxidase activities between normal control mice and hyperuricemic mice
-
additional information
Rattus norvegicus Sprague-Dawley
-
xanthine oxidoreductase is implicated in many inflammatory diseases. Inhibition of XOR within the inflammatory mononuclear phagocytes, i.e. MNP, prevents neutrophil recruitment during adoptive transfer demonstrating the role of XOR in MNP-mediated neutrophil recruitment, role of XOR in the inflammatory state of MNP, overview. XOR activity is specifically increased by inflammatory mononuclear phagocyte differentiation. Inhibition of XOR reduces levels of CINC-1 secreted by inflammatory mononuclear phagocytes, and increases levels of SUMO-PPARgamma in the cell lines
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-dimethylxanthine + H2O + O2
1,3-dimethylurate + H2O2
show the reaction diagram
-
-
-
-
?
1,7-dimethylxanthine + H2O + O2
1,7-dimethylurate + H2o2
show the reaction diagram
-
-
-
-
?
1-methyl-2-hydroxypurine + H2O + O2
1-methyl-2-hydroxy-7,9-dihydropurin-8-one + H2O2
show the reaction diagram
-
-
-
?
1-methylxanthine + H2O + O2
1-methylurate + H2O2
show the reaction diagram
-
-
-
-
?
1-methylxanthine + H2O + O2
1-methylurate + H2O2
show the reaction diagram
-
-
-
?
1-methylxanthine + H2O + O2
1-methylurate + H2O2
show the reaction diagram
-
-
-
-
?
1-methylxanthine + H2O + O2
1-methylurate + H2O2
show the reaction diagram
-
-
-
?
2,3-dihydroxybenzaldehyde + H2O + O2
2,3-dihydroxybenzoate + H2O2
show the reaction diagram
-
-
-
?
2,5-dihydroxybenzaldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
?
2,6-diaminopurine + H2O + O2
2,6-diamino-7,9-dihydro-8H-purin-8-one
show the reaction diagram
-
-
-
-
?
2-amino-4-hydroxypterin + H2O + O2
? + H2O2
show the reaction diagram
-
substrate inhibition kinetic pattern
-
-
?
2-amino-6-chloro-purine + H2O + O2
2-amino-6-chloro-7,9-dihydro-purin-8-one + H2O2
show the reaction diagram
-
-
-
-
?
2-hydroxybenzaldehyde + H2O + O2
2-hydroxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
2-mercaptopurine + H2O + O2
8-hydroxy-2-mercaptopurine + H2O2
show the reaction diagram
-
no conversion to 2-thioxanthine
-
-
?
2-methoxybenzaldehyde + H2O + O2
2-methoxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
2-methylbenzaldehyde + H2O + O2
2-methylbenzoate + H2O2
show the reaction diagram
-
-
-
-
?
2-nitrobenzaldehyde + H2O + O2
2-nitrobenzoate + H2O2
show the reaction diagram
-
-
-
-
?
2-oxo-6-methylpurine + H2O + O2
? + H2O2
show the reaction diagram
-
low activity
-
-
?
2-thioxanthine + H2O + O2
2-thiourate + H2O2
show the reaction diagram
-
-
-
-
?
2-thioxanthine + H2O + O2
2-thiouric acid + H2O2
show the reaction diagram
-
-
-
-
?
3,4-dihydroxybenzaldehyde + H2O + O2
3,4-dihydroxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
3,4-dimethoxybenzaldehyde + H2O + O2
3,4-dimethoxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
3-hydroxy-4-methoxybenzaldehyde + H2O + O2
3-hydroxy-4-methoxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
3-hydroxybenzaldehyde + H2O + O2
3-hydroxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
3-methoxybenzaldehyde + H2O + O2
3-methoxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
3-methylbenzaldehyde + H2O + O2
3-methylbenzoate + H2O2
show the reaction diagram
-
-
-
-
?
3-methylhypoxanthine + H2O + O2
3-methylxanthine + H2O2
show the reaction diagram
-
-
-
?
3-methylxanthine + H2O + O2
3-methylurate + H2O2
show the reaction diagram
-
-
-
-
?
3-nitrobenzaldehyde + H2O + O2
3-nitrobenzoate + H2O2
show the reaction diagram
-
-
-
-
?
4-hydroxy-3-methoxybenzaldehyde + H2O + O2
4-hydroxy-3-methoxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
4-hydroxybenzaldehyde + H2O + O2
4-hydroxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
4-hydroxyphenylglycoaldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
?
4-methoxybenzaldehyde + H2O + O2
4-methoxybenzoate + H2O2
show the reaction diagram
-
-
-
-
?
4-methylbenzaldehyde + H2O + O2
4-methylbenzoate + H2O2
show the reaction diagram
-
-
-
-
?
4-nitrobenzaldehyde + H2O + O2
4-nitrobenzoate + H2O2
show the reaction diagram
-
-
-
-
?
5-chloro-6-[(2-iminopyrrolidin-1-yl)methyl]-3H-pyrimidin-4-one + H2O + O2
?
show the reaction diagram
-
-
-
-
?
6'-deoxyacyclovir + H2O + O2
acyclovir + H2O2
show the reaction diagram
-
prodrug of the antiviral agent acyclovir
-
?
6,8-dihydroxypurine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
6,8-dihydroxypurine + H2O + O2
? + H2O2
show the reaction diagram
-
6,8-dihydroxypurine binding structure, overview
-
-
?
6-amino-5-bromo-1H-pyrimidin-2-one + H2O + O2
?
show the reaction diagram
-
-
-
-
?
6-amino-5-bromo-3H-pyrimidin-4-one + H2O + O2
?
show the reaction diagram
-
-
-
-
?
6-amino-5-bromopyrimidine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
6-cyanopurine + H2O + O2
6-cyano-7,9-dihydropurine-8-one
show the reaction diagram
-
-
-
?
6-formylpterin + H2O + O2
?
show the reaction diagram
-
-
-
-
?
6-formylpterin + H2O + O2
? + H2O2
show the reaction diagram
-
-
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
show the reaction diagram
-
-
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
show the reaction diagram
-
an anticancer prodrug, no activation by xanthine oxidase but conversion to the inactive metabolite 6-thiouric acid, catabolism, overview
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
show the reaction diagram
-
a two-step reaction with 6-thioxanthine as intermediate
-
-
?
6-mercaptopurine + H2O + O2
6-mercapto-7,9-dihydropurin-8-one + H2O2
show the reaction diagram
-
4.4% of activity with xanthin
-
?
6-mercaptopurine + H2O + O2
?
show the reaction diagram
-
an anticancer drug
-
-
?
6-thioxanthine + H2O + O2
6-thiourate + H2O2
show the reaction diagram
-
-
-
?
6-thioxanthine + H2O + O2
6-thiourate + H2O2
show the reaction diagram
-
-
-
-
?
6-thioxanthine + H2O + O2
6-thiouric acid + H2O2
show the reaction diagram
-
-
-
-
?
7-alkylpteridin-4-one + H2O + O2
7-alkyllumazine + H2O2
show the reaction diagram
-
-
-
?
7-methylxanthine + H2O + O2
7-methylurate + H2O2
show the reaction diagram
-
-
-
-
?
7-phenylpteridin-4-one + H2O + O2
7-phenyllumazine + H2O2
show the reaction diagram
-
-
-
?
7H-pyrrolo[2,3-d]pyrimidin-2(1H)-one + H2O + O2
?
show the reaction diagram
-
-
-
-
?
7H-pyrrolo[2,3-d]pyrimidin-4(3H)-one + H2O + O2
?
show the reaction diagram
-
-
-
-
?
7H-pyrrolo[2,3-d]pyrimidine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
acetaldehyde + H2O + O2
acetic acid + H2O2
show the reaction diagram
-
-
-
?
acetaldehyde + H2O + O2
acetic acid + H2O2
show the reaction diagram
-
-
-
?
adenine + H2O + O2
6-amino-7,9-dihydropurin-8-one + H2O2
show the reaction diagram
-
-
-
?
adenine + H2O + O2
6-amino-7,9-dihydropurin-8-one + H2O2
show the reaction diagram
-
-
-
?
adenine + H2O + O2
6-amino-7,9-dihydropurin-8-one + H2O2
show the reaction diagram
-
no activity with adenine
-
-
-
adenine + H2O + O2
? + H2O2
show the reaction diagram
-
substrate inhibition kinetic pattern
-
-
?
allopurinol + H2O + O2
?
show the reaction diagram
-
-
-
-
?
allopurinol + H2O + O2
?
show the reaction diagram
-
-
-
-
?
allopurinol + H2O + O2
oxypurinol + H2O2
show the reaction diagram
-
-
allopurinol is a conventional substrate that generates superoxide radicals during its oxidation
-
?
allopurinol + H2O + O2
oxypurinol + H2O2
show the reaction diagram
-
allopurinol is a substrate and a competitive inhibitor for xanthine oxidase, it binds irreversibly at the active site reducing molybdenum VI to IV
-
-
?
benzaldehyde + H2O + O2
benzoate + H2O2
show the reaction diagram
-
-
-
-
-
benzaldehyde + H2O + O2
benzoate + H2O2
show the reaction diagram
-
-
-
-
?
butanal + H2O + O2
butanoate + H2O2
show the reaction diagram
-
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
Equus caballus, Equus asinus, Erythrocebus patas, Erythrocebus patas Patas monkey
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
-
?
formycin B + H2O + O2
?
show the reaction diagram
-
-
-
-
?
FYX-051 + O2 + H2O
?
show the reaction diagram
-
the structure of bovine XOR exposed to the slow-reacting substrate FYX-051 shows a covalent intermediate of the hydroxylation reaction, in which the hydroxyl oxygen bridged the molybdenumatom and the acceptor carbon atom of the aromatic ring of the substrate
-
-
?
glyceraldehyde-3-phosphate + H2O + O2
?
show the reaction diagram
-
-
-
-
?
glyceryl trinitrate + 2,3-dihydroxybenzaldehyde
?
show the reaction diagram
-
-
-
-
?
glyceryl trinitrate + NADH
? + NAD+ + H2O
show the reaction diagram
-
-
further reaction of organic nitrite with thiols or ascorbate leads to generation of NO or nitrosothiols
-
?
glyceryl trinitrate + xanthine
urate + ?
show the reaction diagram
-
-
-
-
?
guanine + H2O + O2
2-amino-1,7,8-trihydro-6H-purin-8-one + H2O2
show the reaction diagram
-
-
-
-
?
guanine + H2O + O2
2-amino-1,7,8-trihydro-6H-purin-8-one + H2O2
show the reaction diagram
-
53.3% of activity with xanthin
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
92.3% of activity with xanthin
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
a two-step reaction with xanthine as intermediate, production of superoxide radicals
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
via intermediate xanthine formation, production of superoxide radicals
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
hypoxanthine binding structure, overview
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
Erythrocebus patas Patas monkey
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
Triticum aestivum Tugela DN
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
Arthrobacter sp. S-2
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
Enterobacter cloacae KY 3074
-
92.3% of activity with xanthin
-
?
indole-3-acetaldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
?
indole-3-aldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
?
isosorbide dinitrate + 2,3-dihydroxybenzaldehyde
?
show the reaction diagram
-
-
-
-
?
isosorbide dinitrate + NADH
? + NAD+ + H2O
show the reaction diagram
-
-
further reaction of organic nitrite with thiols or ascorbate leads to generation of NO or nitrosothiols
-
?
isosorbide dinitrate + xanthine
urate + ?
show the reaction diagram
-
-
-
-
?
N1-methylnicotinamide + H2O + O2
?
show the reaction diagram
-
-
-
-
-
N1-methylnicotinamide + H2O + O2
?
show the reaction diagram
-
-
-
-
-
NADH + H2O + O2
NAD+ + H2O2
show the reaction diagram
-
-
-
-
-
NADH + H2O + O2
NAD+ + H2O2
show the reaction diagram
-
-
-
?
nitrate + 2,3-dihydroxybenzaldehyde
nitrite + ?
show the reaction diagram
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
show the reaction diagram
-
-, reaction can be an important source of NO production in ischemic tissues
-
-
?
nitrate + xanthine
nitrite + urate + ?
show the reaction diagram
-
-
-
-
?
nitrite + 2,3-dihydroxybenzaldehyde
NO + ?
show the reaction diagram
-
NO generation occurs under aerobic conditions and is regulated by O2 tension, pH, nitrite, and reducing substrate concentrations
-
-
?
nitrite + NADH
NO + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
nitrite + NADH
NO + NAD+ + H2O
show the reaction diagram
-
reaction can be an important source of NO production in ischemic tissues
-
-
?
nitrite + NADH
NO + NAD+ + H2O
show the reaction diagram
-
NO generation occurs under aerobic conditions and is regulated by O2 tension, pH, nitrite, and reducing substrate concentrations
-
-
?
nitrite + O2 + hypoxanthine
peroxynitrite + ?
show the reaction diagram
-
-
-
-
?
nitrite + O2 + pterin
peroxynitrite + ?
show the reaction diagram
-
-
-
-
?
nitrite + xanthine
NO + ?
show the reaction diagram
-
-
-
-
?
nitrite + xanthine
NO + ?
show the reaction diagram
-
NO generation occurs under aerobic conditions and is regulated by O2 tension, pH, nitrite, and reducing substrate concentrations
-
-
?
o-hydroxybenzaldehyde + H2O + O2
o-hydroxybenzoate + H2O2
show the reaction diagram
-
-
-
?
organic nitrate + NADH
organic nitrite + NAD+ + H2O
show the reaction diagram
-
organic nitrite is the initial product in the process of xanthine oxidase mediated organic nitrate biotransformation and is the precursor of NO and nitrosothiols, serving as the link between organic nitrate and soluble guanylyl cyclase
-
-
?
propanal + H2O + O2
propanoate + H2O2
show the reaction diagram
-
-
-
?
pteridine + H2O + O2
?
show the reaction diagram
-
and derivatives, e.g.: 4-amino-7-hydroxy pteridine, 4-hydroxy-7-azapteridine
-
-
?
pteridine + H2O + O2
?
show the reaction diagram
Erythrocebus patas Patas monkey
-
-
-
-
?
pterin + H2O + O2
isoxanthopterin + H2O2
show the reaction diagram
-
-
-
?
pterin + H2O + O2
?
show the reaction diagram
-
fluorometric assay method
-
-
?
purine + H2O + O2
7,9-dihydropurin-8-one + H2O2
show the reaction diagram
-
purine and derivatives
-
?
purine + H2O + O2
7,9-dihydropurin-8-one + H2O2
show the reaction diagram
-
purine and derivatives
-
?
purine + H2O + O2
7,9-dihydropurin-8-one + H2O2
show the reaction diagram
-
purine and derivatives, 23.3% of activity with xanthine
-
?
purine + H2O + O2
7,9-dihydropurin-8-one + H2O2
show the reaction diagram
Enterobacter cloacae KY 3074
-
purine and derivatives
-
?
pyridine-2-aldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
?
pyridine-4-aldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
?
pyrimidine derivatives + H2O + O2
?
show the reaction diagram
-
e.g. 2-hydroxypyrimidine, 6-hydroxy-6-aminepyrimidine
-
-
?
pyrimidine derivatives + H2O + O2
?
show the reaction diagram
-
7-hydroxy-(1,2,5)-thiadiazolo(3,4-d)-pyrimidine
-
-
?
pyrimidine-3-aldehyde + H2O + O2
?
show the reaction diagram
-
-
-
-
?
salicylaldehyde + H2O + O2
salicylic acid + H2O2
show the reaction diagram
-
-
-
?
succinate semialdehyde + H2O + O2
succinate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor methylene blue
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
electron acceptor NAD+
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
specificity for electron acceptor is low
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
electron acceptor triphenyltetrazolium chloride, phenazine methosulfate, nitrate, cytochrome c, ferritin
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
Arthrobacter S-2 enzyme: relatively specific
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
low specificity to substrate
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
electron acceptor ferricyanide
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor ferricyanide
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor ferricyanide
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
electron acceptor 2,6-dichlorophenolindophenol
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor 2,6-dichlorophenolindophenol
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
electron acceptor 2,6-dichlorophenolindophenol
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Erythrocebus patas Patas monkey
-
electron acceptor O2
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
Arthrobacter sp. S-2
-
electron acceptor O2, Arthrobacter S-2 enzyme: relatively specific, electron acceptor ferricyanide, electron acceptor 2,6-dichlorophenolindophenol
-
?
xanthine + H2O + O2
uric acid + H2O2
show the reaction diagram
Enterobacter cloacae KY 3074
-
electron acceptor O2, electron acceptor ferricyanide, electron acceptor 2,6-dichlorophenolindophenol
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
P22985
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
P80457
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
from dead cancer cells
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
production of reactive oxygen species via superoxide radicals involved in endothelial dysfunction
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
roles of active site residues E308 and R881 in binding and activation of purine substrate, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
the enzyme is involved in development of ischemia and equine laminitis, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
P22985
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
show the reaction diagram
-
the enzyme plays a role in the development of distant organ dysfunction after abdominal surgery, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
urate is involved in development of endothelial dysfunction, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
xanthine oxidase is an important source of reactive oxygen species that contributes to neurovascular dysfunction in experimental diabetes, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
active site structure, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
P80457
orientation of xanthine in the active site of xanthine oxidoreductase,structure, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
production of superoxide radicals, mechanism of stepwise enzyme reduction during catalysis, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
catalytically relevant binding mode of the substrate xanthine, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
effects of variations in the cofactor, the substrate, and the active site residue Glu802 on the reaction mechanism, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
substrate inhibition kinetic pattern
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
substrate orientation and catalytic specificity, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
Triticum aestivum Tugela DN
-
-
-
-
?
xanthine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
superoxide + urate + ?
show the reaction diagram
-
-
-
-
?
xanthine + methylene blue + O2
urate + reduced methylene blue
show the reaction diagram
-
-
-
-
?
xanthine + NO2-
uric acid + NO
show the reaction diagram
-
-
-
?
xanthine + NO2-
uric acid + NO
show the reaction diagram
-
oxidation of the enzyme by NO2- or reduction by xanthine take place at the molybdenum site
-
-
-
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
binding modes of the substrate xanthine and mechanism of its hydroxylation, overview
-
-
?
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
conversion of xanthine to uric acid at the molybdenum-containing active site
-
-
?
xanthine + thionine + O2
urate + reduced thionine
show the reaction diagram
-
-
-
-
?
xanthopterin + H2O + O2
?
show the reaction diagram
-
-
-
-
?
xanthopterin + H2O + O2
? + H2O2
show the reaction diagram
-
substrate activation kinetic pattern
-
-
?
lumazine + H2O + O2
? + H2O2
show the reaction diagram
-
classical Michaelis-Menten hyperbolic saturation kinetic pattern
-
-
?
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
?
-
-
xanthine oxidase is necessary during the physiological involution of tissues
-
-
-
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
?
-
-
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 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 30C to 45C and by photosensitization of tumor cells with a hematoporphyrin derivative, overview
-
-
-
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, 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
?
-
-
xanthine oxidase inhibition in small intestine ischemia-reperfusion injury leads to reduction in neutrophil infiltration
-
-
-
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
?
-
-
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
?
-
-
single nucleotide polymorphisms alter the substrate specificity of the enzyme, overview
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
enzyme inhibition by orange juice and hesperetin participates in preventing oxidative stress by enhancing total antioxidant capacity and decreasing lipid peroxidation, 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%, 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%, 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, 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 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
?
-
-
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
?
-
-
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, xanthine and lumazine are good substrates, while 2-hydroxy-6-methylpurine is a slow and poor substrate
-
-
-
additional information
?
-
Triticum aestivum, Triticum aestivum Tugela DN
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-methylxanthine + H2O + O2
1-methylurate + H2O2
show the reaction diagram
-
-
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
show the reaction diagram
-
-
-
-
?
6-mercaptopurine + 2 H2O + 2 O2
6-thiouric acid + 2 H2O2
show the reaction diagram
-
an anticancer prodrug, no activation by xanthine oxidase but conversion to the inactive metabolite 6-thiouric acid, catabolism, overview
-
-
?
6-mercaptopurine + H2O + O2
?
show the reaction diagram
-
an anticancer drug
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
?
carboxylic aldehyde + H2O + O2
carboxylic acid + H2O2
show the reaction diagram
Equus caballus, Equus asinus, Erythrocebus patas, Erythrocebus patas Patas monkey
-
enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
-
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
show the reaction diagram
-
reaction can be an important source of NO production in ischemic tissues
-
-
?
nitrite + NADH
NO + NAD+ + H2O
show the reaction diagram
-
reaction can be an important source of NO production in ischemic tissues
-
-
?
organic nitrate + NADH
organic nitrite + NAD+ + H2O
show the reaction diagram
-
organic nitrite is the initial product in the process of xanthine oxidase mediated organic nitrate biotransformation and is the precursor of NO and nitrosothiols, serving as the link between organic nitrate and soluble guanylyl cyclase
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
P80457
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
from dead cancer cells
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
production of reactive oxygen species via superoxide radicals involved in endothelial dysfunction
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
production of superoxide radicals
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
roles of active site residues E308 and R881 in binding and activation of purine substrate, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
the enzyme is involved in development of ischemia and equine laminitis, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
P22985
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
show the reaction diagram
-
the enzyme plays a role in the development of distant organ dysfunction after abdominal surgery, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
urate is involved in development of endothelial dysfunction, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
xanthine oxidase is an important source of reactive oxygen species that contributes to neurovascular dysfunction in experimental diabetes, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
catalytically relevant binding mode of the substrate xanthine, overview
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
?
xanthine + H2O + O2
urate + H2O2
show the reaction diagram
Triticum aestivum Tugela DN
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
-
-
-
?
xanthine + O2 + H2O
urate + H2O2
show the reaction diagram
-
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
-
-
?
hypoxanthine + 2 H2O + 2 O2
urate + 2 H2O2
show the reaction diagram
Triticum aestivum Tugela DN
-
-
-
-
?
additional information
?
-
-
xanthine oxidase is necessary during the physiological involution of tissues
-
-
-
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
?
-
-
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 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 30C to 45C and by photosensitization of tumor cells with a hematoporphyrin derivative, overview
-
-
-
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, 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
?
-
-
xanthine oxidase inhibition in small intestine ischemia-reperfusion injury leads to reduction in neutrophil infiltration
-
-
-
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
?
-
-
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
?
-
-
enzyme inhibition by orange juice and hesperetin participates in preventing oxidative stress by enhancing total antioxidant capacity and decreasing lipid peroxidation, 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%, 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%
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
flavoprotein
FAD
-
flavoprotein
FAD
-
flavoprotein
FAD
-
flavoprotein
FAD
-
contains FAD, molybdenum and iron in the ratio 1 : 4 : 4; flavoprotein
FAD
-
flavoprotein
FAD
-
contains FAD, molybdenum and iron in the ratio 1 : 4 : 4; flavoprotein
FAD
-
flavoprotein
FAD
-
bovine liver: 1 FAD per subunit (2 per molecule); flavoprotein
FAD
-
required for reoxidation of the enzyme, contains two non-identical [2Fe-2S] centers
FAD
-
the FAD cofactor is open to solvent in XO, but much less accessible in XDH, binding site structure, overview
FAD
-
XOR is a molybdoflavin protein, is not affected by inhibitor nitro-oleic acid
FAD
-
a molybdenum-iron-flavoenzyme
FAD
-
the Mo(VI) ion at the active site is reduced to Mo(IV), which then transfers two electrons, via the 2Fe-2S clusters, to the FAD cofactor
FAD
-
role of Asp428 in the FAD reactivity, overview
molybdenum cofactor
-
structure-function analysis, mechanism, overview
molybdenum cofactor
-
XOR is a molybdoflavin protein
molybdenum cofactor
-
molybdenum-containing enzyme
molybdenum cofactor
-
C-terminal
molybdenum cofactor
-
cofactor geometry, overview
molybdenum cofactor
-
[Mo(S2C2H2)(dO) (ORunfixed)(sSH)]2- moiety
[2Fe-2S] cluster
-
two N-terminal non-identical iron-sulfur clusters of the [2Fe-2S]-type
-
molybdopterin
-
one cofactor per subunit, oxidation of xanthine takes place at this center, electrons are rapidly distributed to the other centers by intramolecular electron transfer
additional information
-
negligible reactivity toward NAD+
-
additional information
-
the enzyme contains two 2Fe-2S clusters
-
additional information
-
the molybdenum center is located in a separate subunit from the Fe/S- and flavin-containing parts of the enzyme
-
additional information
-
cofactor conformation, binding structure analysis and mechanism, overview
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CoCl2
-
increased activity of xanthine oxidase in cells exposed to CoCl2 and subsequent increase in reactive oxygen species derived from enzyme activity, which results in accumulation of hypoxia-inducible factor 1alpha. Blockade of enzyme activity by allopurinol, N-acetyl-L-cysteine or siRNA significantly attenuates expression of hypoxia-inducible factor 1alpha and thus the induction of genes such as erythropoietin and vascular endothelial growth factor
Cu2+
-
Cu2+ either stimulates or inhibits xanthine oxidase activity, depending on metal concentration (inhibition above 0.7 mM) and pre-incubation length, the latter also determining the inhibition type. Cu2+-enzyme complex formation is characterized by modifications in xanthine oxidase electronic absorption bands, intrinsic fluorescence, and alpha-helical and beta-sheet content. Apparent dissociation constant values imply high- and low-affinity Cu2+ binding sites in the vicinity of the enzyme's reactive centers, Cu2+ binding to high-affinity sites causes alterations around xanthine oxidase molybdenum and flavin adenine dinucleotide centers, changes in secondary structure, and moderate activity inhibition, binding to low affinity sites causes alterations around all xanthine oxidase reactive centers including FeS, changes in tertiary structure as reflected by alterations in spectral properties, and drastic activity inhibition. Stimulation is attributed to transient stabilization of xanthine oxidase optimal conformation. Potential role of copper in the regulation of xanthine oxidase activity, binding kinetics, detailed overview
Fe
-
a molybdenum-iron-flavoenzyme
Fe2+
-
xanthine oxidase dependent oxidation of ascorbate is markedly increased in presence of iron
Fe2+
-
in [2Fe-2S] centers of FAD cofactor
Fe2+
-
two 2Fe-2S clusters. The Mo(VI) ion at the active site is reduced to Mo(IV), which then transfers two electrons, via the 2Fe-2S clusters, to the FAD cofactor
Fe2+
-
in a [Fe2-S2] domain
Fe2+
-
Fe2S2 cluster
Iron
-
iron-molybdenum protein
Iron
-
iron-molybdenum protein
Iron
-
iron-molybdenum protein
Iron
-
iron-molybdenum protein
Iron
-
contains FAD, iron and molybdenum in the ratio 1/4/4; iron-molybdenum protein
Iron
-
iron-molybdenum protein
Iron
-
iron-molybdenum protein
Iron
-
iron-molybdenum protein
Iron
-
contains FAD, iron and molybdenum in the ratio 1/4/4; iron-molybdenum protein
Iron
-
iron-molybdenum protein
Iron
-
iron-molybdenum protein
Iron
-
iron-molybdenum protein
Iron
-
bovine liver: 2 Fe-S centres per subunit, 4 per molecule; iron-molybdenum protein
Iron
-
iron-molybdenum protein
Iron
-
two [2Fe-2S] centers
Mo
-
XOR is a molybdenum-containing enzyme
Mo
-
a molybdenum-iron-flavoenzyme
Mo4+
-
the Mo(VI) ion at the active site is reduced to Mo(IV), which then transfers two electrons, via the 2Fe-2S clusters, to the FAD cofactor
Molybdenum
-
an iron-molybdenum protein; molybdenum cofactor is a complex between molybdenum and molybdopterin (a 6-alkylpterin with 4-carbon side chain which has an enedithiol at carbon 1' and 2', a hydroxyl at carbon 3', and a terminal phosphate group)
Molybdenum
-
an iron-molybdenum protein
Molybdenum
-
an iron-molybdenum protein
Molybdenum
-
an iron-molybdenum protein
Molybdenum
-
an iron-molybdenum protein
Molybdenum
-
an iron-molybdenum protein; contains FAD, molybdenum and iron in the ratio 1/4/4
Molybdenum
-
an iron-molybdenum protein
Molybdenum
-
an iron-molybdenum protein
Molybdenum
-
an iron-molybdenum protein
Molybdenum
-
an iron-molybdenum protein; contains FAD, molybdenum and iron in the ratio 1/4/4
Molybdenum
-
an iron-molybdenum protein
Molybdenum
-
an iron-molybdenum protein
Molybdenum
-
an iron-molybdenum protein
Molybdenum
-
an iron-molybdenum protein; purification of the molybdenum cofactor from milk xanthine oxidase
Molybdenum
-
an iron-molybdenum protein; liver enzyme: 1 molybdenum atom per subunit, 2 per molecule
Molybdenum
-
an iron-molybdenum protein
Molybdenum
-
nitrate reduction to nitrite as well as nitrite reduction to NO occurs at the molybdenum site
Molybdenum
-
the enzyme accelerates reaction rate via base-catalyzed chemistry in which a Mo-OH group undertakes nucleophilic attack on the carbon center to be hydroxylated, with concomitant hydride transfer to a catalytically essential Mo=S group in the molybdenum coordination sphere. This chemistry appears to proceed via obligate two-electron chemistry rather than in individual steps to yield a reduced enzyme product complex with product coordinmated to the active site molybdenum by means of the newly introduced hydroxyl group in a sinple end-on fashion
Molybdenum
-
molybdopterin domain structure of enzyme mutant E308V, overview
Molybdenum
-
active site molybdenum center structure, overview
Molybdenum
-
XOR is a molybdoflavin protein
Molybdenum
-
a molybdenum-containing enzyme
Molybdenum
-
the molybdenum center is a pyranopterin-MoVI-OS-OH. The pyranopterin cofactor is coordinated to the metall via an enedithiolate side chain, coordination geometry, overview
Molybdenum
-
direct Mo-C bond in the active site
Molybdenum
-
XOR is a molybdenum-containing enzyme. In the oxidized form of XORs, the Mo(VI) ion is in the center of a square-pyramidal geometry, coordinated by an oxo-ligand at the apical position and one hydroxo and one sulfido ligand at equatorial positions,3a in addition to the two vicinal sulfur ligands contributed by the pterin group, cofactor geometry, overview
Molybdenum
-
XOR is a molybdenum-containing enzyme. In the oxidized form of XORs, the Mo(VI) ion is in the center of a square-pyramidal geometry, coordinated by an oxo-ligand at the apical position and one hydroxo and one sulfido ligand at equatorial positions, in addition to the two vicinal sulfur ligands contributed by the pterin group, cofactor geometry, overview
Molybdenum
-
molybdopterin cofactor
additional information
-
the molybdenum center is located in a separate subunit from the Fe/S- and flavin-containing parts of the enzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(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-(4'-nitrophenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
-
-
1-(4'-trifluoromethylphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
-
-
1-4-tolyl-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
-
-
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
-
-
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-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-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 nezyme dimer, binding structure, overview
2-hydroxy-6-[(E)-2-(4-hydroxyphenyl)ethenyl]-4-methoxybenzaldehyde
-
a resveratrol derivative
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-[(2,3-dimethylphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(2,4-dimethylphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(2-bromophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(2-chlorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(2-fluorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(3-bromophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(3-chlorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(3-fluorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(4-bromophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(4-chloro-3-methylphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(4-chlorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(4-fluorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[(4-methoxyphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
-
2-[3-cyano-4-(2-methylpropoxy)phenyl]-4-methylthiazole-5-carboxylic acid
-
i.e. febuxostat, TEI-6720, or TMX-67, mixed-type inhibition of both the oxidized and reduced form of xanthine oxidase
2-[[(3,6,7-trihydroxy-9-oxo-9H-xanthen-1-yl)oxy]methyl]benzonitrile
-
-
3,3',4,4'-Tetrahydroxychalcone
-
-
3,4-di-O-caffeoylquinic acid methyl ester
-
reversible inhibition, IC50: 0.0036 mM
3,4-Dihydroxybenzaldehyde
-
mixed type inhibition, 50% inhibition at 0.0568 mM
3,5-di-O-caffeoylquinic acid
-
-
3,6,7-trihydroxy-1-[(2-methylbenzyl)oxy]-9H-xanthen-9-one
-
-
3,6,7-trihydroxy-1-[(2-nitrobenzyl)oxy]-9H-xanthen-9-one
-
-
3,6,7-trihydroxy-1-[(3-methylbenzyl)oxy]-9H-xanthen-9-one
-
-
3,6,7-trihydroxy-1-[(3-nitrobenzyl)oxy]-9H-xanthen-9-one
-
-
3,6,7-trihydroxy-1-[(4-methylbenzyl)oxy]-9H-xanthen-9-one
-
-
3,6,7-trihydroxy-1-[(4-nitrobenzyl)oxy]-9H-xanthen-9-one
-
-
3-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-(4'-aminopyrazolo[3,4-d]pyrimidin-1-yl)-benzonitrile
-
-
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-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-[[(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-(3-cyano-4-isobutoxyphenyl)isoxazole-3-carboxylic acid
-
-
5-(4-benzyloxy-3-cyanophenyl)isoxazole-3-carboxylic acid
-
-
5-(4-benzyloxy-3-nitrophenyl)isoxazole-3-carboxylic acid
-
-
5-(4-isobutoxy-3-nitrophenyl)isoxazole-3-carboxylic acid
-
-
5-amino-1-(4'-carboxyphenyl)-1H-pyrazole-4-carbonitrile
-
-
5-methylbenzimidazole
-
poor inhibitor
5-nitrobenzimidazole
-
-
-
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-aminopurine
-
-
6-formylpterin
-
-
6-O-methylguanine
-
poor inhibitor
6-Thioguanine
-
-
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-bromoxanthine
-
-
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
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
-
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
-
competitive, 50% inhibition at 0.0025 mM
allopurinol
-
enzyme inhibition with allopurinol does not improve endothelium-dependent vasodilation before
allopurinol
-
strong competitive inhibition
allopurinol
-
a suicide inhibitor of XOD, a pyrazolopyrimidine derivative, and an analogue of hypoxanthine
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
-
36.6% inhibition at 0.04 mM
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
-
40% inhibition at 0.0285 g per kg body weight
allopurinol
-
-
allopurinol
-
inhibits xanthine and hypoxanthine oxidation in vivo in intestine and pancreas, but enhances the activity in liver, tissue-dependent effects, overview
allopurinol
-
shows strong enzyme inhibition and hypouricemic effect
allopurinol
-
a time-dependent inhibitor
allopurinol
-
decreasesserum xanthine oxidase activity but increases liver xanthine oxidase activity significantly
allopurinol
-
i.e. 4-hydroxypyrazolo(3,4-d)pyrimidine, a purine analogue and a competitive inhibitor
alloxanthine
-
-
alloxanthine
-
a mechanism-based inhibitor, binding structure, overview. Inhibition mechanism involves binding to molybdenum, overview
amentoflavone
-
a flavone compound from Selaginellaceae with antiviral activity
Aminoglutethimide
-
-
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
apigenin
-
mixed type inhibition of xanthine, strong inhibitor of xanthine oxidase, weak inhibition of monoamine oxidase
ascorbate
-
43.5% inhibition at 0.04 mM
ascorbic acid
-
-
asperuloside
-
from Paederia scandens extract
Azaguanine
-
-
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
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
chicoric acid
-
i.e. dicaffeoyltartaric acid
chlorogenic acid
-
i.e. 5-O-caffeoylquinic acid
Cichorium intybus extract
-
leaves from var. silvestre, hydroxycinnamic acids and flavonoids show antioxidant activity, activity and contents of hydroxycinnamic acids and flavonoids decrease by less than 20% during storage of the minimally processed red chicory products, inhibitory compound overview
-
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
-
-
cyclosporin A
-
-
decyl gallate
P80457
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
Dinitrophenol quinimine
-
-
-
diphenylene iodonium
-
inhibits peroxynitrite generation
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
dithranol
-
-
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
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
-
a potent non-purine, selective inhibitor of the enzyme
febuxostat
-
the inhibitor lowers uric acid and alleviates systemic and glomerular hypertension in experimental hyperuricaemia
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
-
-
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
formaldehyde
-
-
formaldehyde
-
determination and analysis of the structure of the formaldehyde-inhibited Mo(V) state of xanthine oxidase, overview
FYX-051
-
-
Gallic acid
P80457
50% inhibition of urate formation above 0.2 mM, 50% inhibition of superoxide anion generation at 0.0026 mM
genkwanin
-
-
green tea extract
-
-
-
Guanine
-
-
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
hexyl gallate
P80457
50% inhibition of urate formation above 0.2 mM, 50% inhibition of superoxide anion generation at 0.0052 mM
hydroxychavicol
-
i.e. 4-allyl-1,3-hydroxybenzene, a potent xanthine oxidase inhibitor obtained from the leaves of betel, Piper betle. Structure-activity relationships, the dihydroxyl group is required for the xanthine oxidase inhibitory activity, overview
hydroxylamine
-
-
Imidazotriazines
-
-
-
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
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
-
mixed type inhibition of xanthine, strong inhibitor of xanthine oxidase, weak inhibition of monoamine oxidase
luteolin
-
competitive inhibition
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
P80457
50% inhibition of urate formation above 0.2 mM, 50% inhibition of superoxide anion generation at 0.0049 mM
Myoglobin
-
inhibits reaction with cytochrome c as acceptor
-
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
P80457
50% inhibition of urate formation at 0.049 mM, 50% inhibition of superoxide anion generation at 0.0036 mM
Naringenin
-
-
noradrenaline
-
15% inhibition at 0.1 mM, 30% inhibition at 1 mM
O2
-
competitive inhibitor of NO production
octyl gallate
P80457
50% inhibition of urate formation at 0.262 mM, 50% inhibition of superoxide anion generation at 0.0045 mM
orange juice
-
inhibits hepatic XOR activity and decreases serum uric acid levels and exhibits antioxidative and antihyperuricemic properties
-
oxypurinol
-
-
oxypurinol
-
inhibits NO generation triggered by xanthine, NADH or 2,3-dihydroxybenzaldehyde
oxypurinol
-
enzyme inhibition with oxypurinol improves endothelium-dependent vasodilation before
oxypurinol
-
active metabolite of allopurinol
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
p-Aminophenol quinimine
-
-
-
p-chloromercuribenzoate
-
-
paederoside
-
from Paederia scandens extract
phenylhydrazine
-
-
propyl gallate
P80457
50% inhibition of urate formation above 0.2 mM, 50% inhibition of superoxide anion generation at 0.0064 mM
Pterines
-
or other heterocyclic compounds, which are either not oxidized or oxidized rather slowly
-
Purine-6-aldehyde
-
-
Purines
-
-
-
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
-
competitive inhibition
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
Semicarbazide
-
-
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
xanthine
-
substrate inhibition at high concentration
xanthine
-
no substrate inhibition
xanthine
-
at high concentrations
Y-700
-
-
-
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]
-
-
-
[Mn(C17H16N2O2)N3]
-
-
-
[Zn(C9H10N2)(Cl)2]
-
-
-
Mn[Mn(CH3COO)(C25H20N2O2)]2
-
-
-
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
-
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
-
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
-
substrate-dependent inhibitory potencies, 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
-
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
-
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
-
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
-
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
-
eugenol, methyleugenol, and dihydromethyleugenol are poor inhibitors
-
additional information
-
no inhibition by curcumin in vitro
-
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
-
NAD+ and diphenylene iodonium inhibit NADH-dependent superoxide formation of AtXDH1; NAD+ inhibits NADH-dependent superoxide formation of AtXDH1
-
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
-
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
-
inhibition of xanthine oxidase by thiosemicarbazones, hydrazones and dithiocarbazates derived from hydroxy-substituted benzaldehydes, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetonitrile
-
-
allopurinol
-
inhibits xanthine and hypoxanthine oxidation in vivo in intestine and pancreas, but enhances the activity in liver, tissue-dependent effects, overview
angiotensin II
-
Ang II substantially increases endothelial enzyme protein levels and enzyme-dependent superoxide production in cultured endothelial cells
apigenin
-
increases liver xanthine oxidase activities significantly, but has no effect on serum xanthine oxidase activities
apoptotic lymphocyte microparticles
-
microparticles are membrane vesicles released during cell activation and apoptosis, they activate reactive oxygen species production by xanthine oxidase in endothelial cells and aorta, inhibition of phosphoinositol 3-kinase enhances the activating effect, xanthine oxidase inhibitors reduce it, overview
-
ascorbate
-
in absence of thiols or ascorbate, no NO generation is detected from xanthine oxidase mediated organic nitrate reduction
astilbin
-
significantly increases serum xanthine oxidase activities, and decreases liver xanthine oxidase activities significantly
-
Dimethylformamide
-
highly stimulating
Dioxane
-
-
diphenylene iodonium chloride
-
strongly inhibits xanthine oxidase mediated NO generation with NADH serving as reducing substrate, with xanthine or 2,3-dihydroxybenzaldehyde as reducing substrates, NO generation is increased more than six times
dithiothreitol
-
enhance oxidation of dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
ethanol
-
-
glutathione
-
enhances oxidation of dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
L-cysteine
-
in absence of thiols or ascorbate, no NO generation is detected from xanthine oxidase mediated organic nitrate reduction
N-acetyl-L-Cys
-
enhance oxidation of dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
potassium oxonate
-
slight activation in vivo
-
Propanol
-
slightly stimulating
quercetin
-
significantly increases serum xanthine oxidase activities, and decreases liver xanthine oxidase activities significantly
rutin
-
significantly increases serum xanthine oxidase activities
sulfide/dithionite
-
treatment increases the specific activity of AtXDH1
-
tetrahydrofuran
-
-
Th-1 cytokine
-
increases XOR activity in inflammatory mononuclear phagocytes in vivo
-
thiol
-
in absence of thiols or ascorbate, no NO generation is detected from xanthine oxidase mediated organic nitrate reduction
methanol
-
slightly stimulating
additional information
-
study on the effect of food extracts on enzyme activity in vitro. Orange juice and pink grapefruit juice are activating
-
additional information
-
bacterial infection of mammary gland induces the enzyme in milk, while enzyme activity in milk is not affected by bacteria, overview
-
additional information
-
heat shock, e.g. by infrared light, induces the enzyme and reactive oxygen species production in keratinocytes and skin, overview
-
additional information
-
liver injury due to treatment with D-galactosamine imduces the hepatic enzyme expression
-
additional information
-
experimental sepsis induces the enzyme in the intestine
-
additional information
-
heat stress at 44C induces the enzyme
-
additional information
-
colon obstruction induces a hyperdynamic circulatory reaction, significantly elevated the motility index and increased mucosal leucocyte accumulation and XOR activity, the increase in activity is counteracted by kynurenic acid
-
additional information
-
gama-irradiation induces enzyme expression
-
additional information
-
the enzyme activity is stimulated by organic solvents, but the effect is reduced with increasing temperature, from 27C to 37C, the inhibitory effects of all organic solvents on the enzyme activity are increased at higher temperature
-
additional information
-
XOR activity is specifically increased by inflammatory mononuclear phagocyte differentiation
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.13
-
1-Methylxanthine
-
-
0.0298
-
1H-pyrrolo[2,3-d]pyrimidin-2-ol
-
substrate and inhibitor compound
0.0253
-
2,3-Dihydroxybenzaldehyde
-
in presence of 1.0 mM nitrate
0.035
-
2,3-Dihydroxybenzaldehyde
-
-
0.068
-
2,5-dihydroxybenzaldehyde
-
-
0.00143
-
2-Amino-4-hydroxypteridine
-
+ methylene blue
0.0067
-
2-Amino-4-hydroxypteridine
-
+ methylene blue
0.19
-
2-Hydroxybenzaldehyde
-
-
0.00088
-
2-mercaptopurine
-
25C
0.19
-
2-Methoxybenzaldehyde
-
-
0.03
-
2-Methylbenzaldehyde
-
pH 7.0
0.01
-
2-nitrobenzaldehyde
-
pH 7.0
0.00047
-
2-Thioxanthine
-
25C
0.039
-
3,4-Dihydroxybenzaldehyde
-
-
0.68
-
3,4-dimethoxybenzaldehyde
-
-
0.0451
-
3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
substrate and inhibitor compound
0.18
-
3-Hydroxy-4-methoxybenzaldehyde
-
-
0.18
-
3-Hydroxybenzaldehyde
-
-
0.024
-
3-methylbenzaldehyde
-
pH 7.0
0.001
-
3-Nitrobenzaldehyde
-
pH 7.0
0.12
-
4-Hydroxy-3-methoxybenzaldehyde
-
-
0.17
-
4-hydroxybenzaldehyde
-
-
0.56
-
4-Hydroxyphenylglycolaldehyde
-
-
0.17
-
4-Methoxybenzaldehyde
-
-
0.04
-
4-methylbenzaldehyde
-
pH 7.0
0.011
-
4-Nitrobenzaldehyde
-
pH 7.0
0.0649
-
5-chloro-6-[(2-iminopyrrolidin-1-yl)methyl]-3H-pyrimidin-4-one
-
substrate and inhibitor compound
0.0325
-
6-amino-5-bromo-1H-pyrimidin-2-one
-
-
0.0238
-
6-amino-5-bromo-3H-pyrimidin-4-one
-
-
0.0444
-
6-amino-5-bromopyrimidine
-
-
0.002
-
6-Mercaptopurine
-
25C
0.00046
-
6-Thioxanthine
-
25C
0.0672
-
7H-pyrrolo[2,3-d]pyrimidine
-
substrate and inhibitor compound
130
-
acetaldehyde
-
-
20
-
aldehyde
-
cofactor 2,6-dichlorophenolindophenol
0.004
-
allopurinol
-
-
0.3
-
benzaldehyde
-
-
0.93
-
benzaldehyde
-
-
142
-
Butyraldehyde
-
-
97
-
dibromoacetonitrile
-
-
161.5
-
formaldehyde
-
-
0.55
-
formycin B
-
-
2
-
glyceraldehyde 3-phosphate
-
-
0.49
-
glyceryl trinitrate
-
xanthine as cosubstrate
0.0017
-
hypoxanthine
-
pH 8.5, 25C, recombinant wild-type enzyme
0.00924
-
hypoxanthine
-
membrane-bound enzyme
0.0134
-
hypoxanthine
-
free enzyme
0.021
-
hypoxanthine
-
pH 8.5, 25C, recombinant mutant R881M
0.022
-
hypoxanthine
-
-
0.0475
-
hypoxanthine
-
cofactor 2,6-dichlorophenolindophenol
0.3
-
Indole-3-acetaldehyde
-
-
0.085
-
Indole-3-aldehyde
-
-
1.64
-
isosorbide dinitrate
-
xanthine as cosubstrate
48
-
N-methylnicotinamide
-
-
0.86
-
NADH
-
in presence of 1.0 mM nitrate
0.878
-
NADH
-
-
0.0005
-
NADPH
-
cofactor 2,6-dichlorophenolindophenol
0.04
-
nitrite
-
pterin as cosubstrate
0.07
-
nitrite
-
hypoxanthine as cosubstrate
1
-
nitrite
-
with xanthine as cosubstrate
1.2
-
nitrite
-
with NADH as cosubstrate
2.25
-
NO2-
-
-
1.03
-
o-hydroxybenzaldehyde
-
-
0.026
-
O2
-
with xanthine as cosubstrate
0.05
-
O2
-
cosubstrate xanthine, pH 8.5
0.08
-
O2
-
cosubstrate xanthine, pH 10.0
0.1
-
O2
-
with NADH as cosubstrate
0.129
-
O2
P22985
xanthine oxidoreductase mutant W335A/F336L, pH 7.8, 25C; xanthine oxidoreductase mutant W335A/F336L treated with dithiothreitol, pH 7.8, 25C
430
-
propionaldehyde
-
-
0.0015
-
pterin
-
cell-associated enzyme, determined in intact cell monolayers
0.0016
-
pterin
-
-
0.036
-
pterin
-
-
0.36
-
Pyridine-2-aldehyde
-
-
0.046
-
Pyridine-3-aldehyde
-
-
1.7
-
Pyridine-4-aldehyde
-
-
1
-
Succinate semialdehyde
-
-
0.000325
-
thionine
-
pH 6.5
0.00146
-
xanthine
-
-
0.0017
-
xanthine
-
pH 8.1, 37C, average value, wild-type enzyme
0.0018
-
xanthine
-
-
0.002
-
xanthine
-
-
0.003
-
xanthine
-
-
0.0034
-
xanthine
-
cell-associated enzyme, determined in intact cell monolayers
0.0036
-
xanthine
-
-
0.0065
-
xanthine
-
-
0.0072
-
xanthine
-
-
0.0088
-
xanthine
-
pH 8.5, 25C, recombinant wild-type enzyme
0.015
-
xanthine
-
heparin-Sepharose 6B-bound enzyme
0.024
-
xanthine
-
kidney enzyme
0.025
-
xanthine
-
-
0.0264
-
xanthine
-
membrane-bound enzyme
0.0279
-
xanthine
-
free enzymen
0.0552
-
xanthine
-
pH not specified in the publication, temperature not specified in the publication, mutant E802Q
0.0644
-
xanthine
-
pH not specified in the publication, temperature not specified in the publication, wild-type enzyme
0.072
-
xanthine
-
pH 8.5, 25C, recombinant mutant E308V
0.088
-
xanthine
-
cofactor 2,6-dichlorophenolindophenol
0.13
-
xanthine
-
-
0.13
-
xanthine
-
-
0.26
-
xanthine
-
liver enzyme
6.6
-
xanthine
-
in presence of 2 mM NADH
6.8
-
xanthine
-
in presence of 0.5 mM 2,3-dihydroxybenzaldehyde
7.7e-05
-
methylene blue
-
pH 6.5
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
steady-state kinetics analysis of wild-type and mutant enzymes with hypoxanthine of xanthine, and of mutant enzymes with benzaldehyde or 4-(dimethyamino)cinnamaldehyde as aldehyde oxidase substrates, overview
-
additional information
-
additional information
-
enzyme kinetics at all pH values studied is non-hyperbolic, and the use of the Michaelis-Menten equation is not adequate
-
additional information
-
additional information
-
detailed kinetics of wild-type in comparison to mutant enzymes, overview
-
additional information
-
additional information
-
steady-state kinetics study of enzyme activity in the presence of Cu2+ and with different pre-incubation times, KM values of 0.0096-0.020 mM, overview
-
additional information
-
additional information
-
in vitro steady-state kinetic studies, kinetics with cofactor cytochrome C, overview
-
additional information
-
additional information
-
thermodynamics and kinetics of xanthine oxidase in the presence of pyridine, Km for xanthine is increased 4.8fold and Vmax is reduced 1.8fold at 0.5% pyridine, overview
-
additional information
-
additional information
-
kinetic analysis, Michaelis-Menten model, detailed overview. Binding of a 6-formylpterin at one of the two xanthine oxidase active sites slows down the turnover rate of xanthine at the adjacent active site and converts the V-[S] plot from substrate inhibition kinetic pattern to a classical Michaelis-Menten hyperbolic saturation pattern. In contrast, binding of xanthine at an active site accelerates the turnover rate of 6-formylpterin at the neighboring active site
-
additional information
-
additional information
-
steady-state and reductive half-reaction rapid kinetics at pH 7.0 and pH 8.5, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.98
-
2-mercaptopurine
-
25C
3.32
-
2-Thioxanthine
-
25C
0.13
-
6-Mercaptopurine
-
25C
2.76
-
6-Thioxanthine
-
25C
0.33
-
hypoxanthine
-
pH 8.5, 25C, recombinant mutant R881M
4.35
-
hypoxanthine
-
cofactor 2,6-dichlorophenolindophenol
30
-
hypoxanthine
-
pH 8.5, 25C, recombinant wild-type enzyme
1.28
-
NADPH
-
cosubstrate cytochrome c
2.57
-
NADPH
-
cosubstrate indophenol
0.41
-
xanthine
P22985
xanthine oxidoreductase mutant W335A/F336L, pH 7.8, 25C
1.16
-
xanthine
-
pH not specified in the publication, temperature not specified in the publication, mutant E802Q
1.35
-
xanthine
-
pH 8.5, 25C, recombinant mutant E308V
4.92
-
xanthine
-
(+ O2)
5.25
-
xanthine
-
cofactor 2,6-dichlorophenolindophenol
9.73
-
xanthine
P22985
xanthine oxidoreductase mutant W335A/F336L treated with dithiothreitol, pH 7.8, 25C
12.47
-
xanthine
P22985
xanthine oxidoreductase mutant W335A/F336L, pH 7.8, 25C
16.2
-
xanthine
-
pH 8.2, 23.5C
18.3
-
xanthine
-
pH 8.5, 25C, recombinant wild-type enzyme
108
-
xanthine
-
pH not specified in the publication, temperature not specified in the publication, wild-type enzyme
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00015
-
2-(3,4-dihydroxy-5-methoxyphenyl)-5,7-dihydroxy-4H-chromen-4-one
-
pH 7.5, 25C
0.0009
-
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one
-
pH 7.5, 25C
0.00011
-
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-6-methoxy-4H-chromen-4-one
-
pH 7.5, 25C
0.00015
-
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-6-methoxy-4H-chromen-4-one
-
pH 7.5, 25C
0.00096
-
2-amino-6-hydroxy-8-mercaptopurine
-
pH 7.4, competitive versus substrate 6-mercaptopurine
0.00098
-
2-amino-6-hydroxy-8-mercaptopurine
-
pH 7.4, noncompetitive versus substrate 6-mercaptopurine
0.0057
-
2-amino-6-hydroxy-8-mercaptopurine
-
pH 7.4, competitive versus substrate xanthine
0.00624
-
2-amino-6-hydroxy-8-mercaptopurine
-
pH 7.4, noncompetitive versus substrate xanthine
0.0013
-
2-amino-6-purine thiol
-
pH 7.4, competitive versus substrate 6-mercaptopurine
0.0066
-
2-amino-6-purine thiol
-
pH 7.4, competitive versus substrate xanthine
6e-07
-
2-[3-cyano-4-(2-methylpropoxy)phenyl]-4-methylthiazole-5-carboxylic acid
-
25C, pH 7.4, oxidized form of enzyme
3.1e-06
-
2-[3-cyano-4-(2-methylpropoxy)phenyl]-4-methylthiazole-5-carboxylic acid
-
25C, pH 7.4, reduced form of enzyme
0.0031
-
3,4-di-O-caffeoylquinic acid methyl ester
-
25C
0.0399
-
3,4-Dihydroxybenzaldehyde
-
pH 7.5, 25C
0.00024
-
4,5-di-O-caffeoylquinic acid methyl ester
-
25C
0.00037
-
5,7-dihydroxy-2-(3,4,5-trimethoxyphenyl)-4H-chromen-4-one
-
pH 7.5, 25C
0.00102
-
5,7-dihydroxy-2-(3-hydroxy-4,5-dimethoxyphenyl)-6-methoxy-4H-chromen-4-one
-
pH 7.5, 25C
0.00012
-
5,7-dihydroxy-2-(3-hydroxy-4-methoxyphenyl)-4H-chromen-4-one
-
pH 7.5, 25C
0.00079
-
5,7-dihydroxy-2-(4-hydroxy-3-methoxyphenyl)-3,6-dimethoxy-4H-chromen-4-one
-
pH 7.5, 25C
0.00028
-
5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
-
pH 7.5, 25C
0.00011
-
5,7-dihydroxy-2-(4-methoxyphenyl)-4H-chromen-4-one
-
pH 7.5, 25C
4.75e-05
-
6-(N-benzoylamino)purine
-
25C, pH 7.5
9.4e-05
-
6-formylpterin
-
-
0.4
-
8-bromoxanthine
-
25C, pH 7.5
0.0538
-
acacetin 7-O-(3-O-acetyl-beta-D-glucopyranoside)
-
pH 7.5, 25C
0.0018
-
allopurinol
-
pH 7.5, 25C
0.0012
-
quercetin
-
pH 7.4, 25C
0.08
-
xanthine
-
-
0.0019
-
luteolin
-
pH 7.4, 25C
additional information
-
additional information
-
inhibition kinetics
-
additional information
-
additional information
-
inhibition kinetics
-
additional information
-
additional information
-
inhibition kinetics
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0196
-
(4'-methoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
-
-
0.02173
-
1,3,6,7-tetrahydroxy-9H-xanthen-9-one
-
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
-
-
0.00018
-
1-(4'-trifluoromethylphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
-
-
0.0174
-
1-4-tolyl-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine
-
-
0.00641
-
1-[(2-chlorobenzyl)oxy]-3,6,7-trihydroxy-9H-xanthen-9-one
-
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
-
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
-
pH not specified in the publication, temperature not specified in the publication
0.0025
-
2,4-dihydroxy-6-[(E)-2-(4-hydroxyphenyl)ethenyl]benzaldehyde
-
pH 7.8, 25C
0.00054
-
2-amino-6-hydroxy-8-mercaptopurine
-
pH 7.4, versus substrate 6-mercaptopurine
0.0051
-
2-amino-6-hydroxy-8-mercaptopurine
-
pH 7.4, versus substrate hypoxanthine
0.0177
-
2-amino-6-hydroxy-8-mercaptopurine
-
pH 7.4, versus substrate xanthine
0.0026
-
2-amino-6-purine thiol
-
pH 7.4, versus substrate 6-mercaptopurine
0.0073
-
2-amino-6-purine thiol
-
pH 7.4, versus substrate hypoxanthine
0.0164
-
2-amino-6-purine thiol
-
pH 7.4, versus substrate xanthine
0.0102
-
2-chloro-6(methylamino)purine
-
pH 7.5, 25C
0.0169
-
2-hydroxy-4-methoxy-6-[(E)-2-(4-methoxyphenyl)ethenyl]benzaldehyde
-
pH 7.8, 25C
0.0266
-
2-hydroxy-6-[(E)-2-(4-hydroxyphenyl)ethenyl]-4-methoxybenzaldehyde
-
pH 7.8, 25C
0.00176
-
2-[(2,4-dimethylphenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
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
-
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
-
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
-
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
-
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
-
pH 7.5, temperature not specified in the publication
0.00059
-
2-[(2-fluorophenoxy)methyl]-7-methyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
pH 7.5, temperature not specified in the publication
0.0036
-
3,4-di-O-caffeoylquinic acid methyl ester
-
reversible inhibition, IC50: 0.0036 mM
0.00708
-
3,6,7-trihydroxy-1-[(2-methylbenzyl)oxy]-9H-xanthen-9-one
-
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
-
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
-
pH not specified in the publication, temperature not specified in the publication
0.0004
-
4-(4'-aminopyrazolo[3,4-d]pyrimidin-1-yl)-benzonitrile
-
-
0.0303
-
4-Aminopyrazolo[3,4-d]pyrimidine
-
pH 7.5, 25C
0.0969
-
4-coumaric acid
-
pH 8.0, 37C, versus xanthine
0.0781
-
4-Hydroxycoumarin
-
pH 7.0, 37C, versus xanthine
0.184
-
4-methoxycinnamic acid
-
pH 8.0, 37C, versus xanthine
0.00467
-
4-[[(3,6,7-trihydroxy-9-oxo-9H-xanthen-1-yl)oxy]methyl]benzonitrile
-
pH not specified in the publication, temperature not specified in the publication
0.00036
-
5-(3-cyano-4-isobutoxyphenyl)isoxazole-3-carboxylic acid
-
pH 7.5, 25C
0.00059
-
5-(4-benzyloxy-3-cyanophenyl)isoxazole-3-carboxylic acid
-
pH 7.5, 25C
0.00097
-
5-(4-benzyloxy-3-nitrophenyl)isoxazole-3-carboxylic acid
-
pH 7.5, 25C
0.001
-
5-(4-isobutoxy-3-nitrophenyl)isoxazole-3-carboxylic acid
-
pH 7.5, 25C
0.0361
-
5-amino-1-(4'-carboxyphenyl)-1H-pyrazole-4-carbonitrile
-
-
0.0868
-
5-nitrobenzimidazole
-
pH 7.5, 25C
-
0.00063
-
5-[4-(4-chlorobenzyloxy)-3-cyanophenyl]isoxazole-3-carboxylic acid
-
pH 7.5, 25C
0.00283
-
5-[4-(4-chlorobenzyloxy)-3-nitrophenyl]isoxazole-3-carboxylic acid
-
pH 7.5, 25C
0.00101
-
5-[4-(4-tert-butylbenzyloxy)-3-cyanophenyl]isoxazole-3-carboxylic acid
-
pH 7.5, 25C
0.01275
-
5-[4-(4-tert-butylbenzyloxy)-3-nitrophenyl]isoxazole-3-carboxylic acid
-
pH 7.5, 25C
0.0109
-
6-aminopurine
-
pH 7.5, 25C
0.0924
-
6-Thioguanine
-
pH 7.5, 25C
0.000555
-
7-methyl-2-(phenoxymethyl)-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
pH 7.5, temperature not specified in the publication
0.000326
-
7-methyl-2-[(2-methylphenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
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
-
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
-
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
-
pH 7.5, temperature not specified in the publication
0.00102
-
7-methyl-2-[(4-methylphenoxy)methyl]-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-5-one
-
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
-
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
-
pH 7.5, temperature not specified in the publication
0.00073
-
allopurinol
-
pH 7.5, temperature not specified in the publication
0.000753
-
allopurinol
-
pH 7.5, temperature not specified in the publication
0.00091
-
allopurinol
-
pH 7.4, versus substrate hypoxanthine
0.0011
-
allopurinol
-
pH 7.0, 37C, versus xanthine
0.00143
-
allopurinol
-
pH 8.0, 37C, competitive versus xanthine
0.00192
-
allopurinol
-
pH 7.4, versus substrate 6-mercaptopurine
0.00236
-
allopurinol
-
pH 7.4, versus substrate xanthine
0.0026
-
allopurinol
-
IC50: 0.0026 mM
0.007
-
allopurinol
-
inhibits peroxynitrite generation, IC50: 0.007 mM
0.0078
-
allopurinol
-
pH 7.5, 25C
0.0103
-
allopurinol
-
pH 7.8
0.0134
-
allopurinol
-
pH 7.8, 25C
0.0307
-
allopurinol
-
-
0.00074
-
apigenin
-
pH 7.5, 25C
0.0654
-
caffeic acid
-
pH 8.0, 37C, competitive versus xanthine; pH 8.0, 37C, versus xanthine
0.00626
-
caffeic acid phenethyl ester
-
pH 8.0, 37C, competitive versus xanthine
0.1567
-
caffeic acid phenethyl ester
-
pH 8.0, 37C, inhibition of hydroxylradical formation in the dimethyl-1-pyrroline-N-oxide spin-trapping assay
0.00367
-
Cd2+
-
pH 7.8
0.0234
-
Cu2(C16H24N2O)2ClO4
-
pH 7.8
-
0.0014
-
Cu2+
-
pH 7.8
0.013
-
Cu[Cu(CH3COO)(C17H16N2O2)]2
-
pH 7.8
-
0.0939
-
ferulic acid
-
pH 8.0, 37C, versus xanthine
0.0167
-
hydroxychavicol
-
-
0.1432
-
isoferulic acid
-
pH 8.0, 37C, versus xanthine
0.00059
-
luteolin
-
pH 7.5, 25C
0.0184
-
N-(4''-carboxyphenyl)-N-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosyl)pyrazolo[3,4-d] pyrimidine
-
-
0.081
-
N-(4'-carboxyphenyl)-1H-4-aminopyrazolo[3,4-d]pyrimidine
-
-
1.36
1.85
renierol
-
pH 7.5, inhibition of superoxide and urate production, respectively
0.0139
-
resveratrol
-
pH 7.8, 25C
0.0461
-
Zn2+
-
pH 7.8
0.0232
-
Zn[(Zn(C3H4N2)(C17H18N2O2))2(NO3)](NO3)
-
pH 7.8
8e-05
-
[4'-(4''-aminopyrazolo[3,4-d]pyrimidin-1''-yl)-benzoylamino]-acetic acid methyl ester
-
-
0.0379
-
[4'-(5-amino-4-cyanopyrazol-1-yl)-benzoylamino]-acetic acid methyl ester
-
-
0.0022
-
[Cd(C12H16N2)(m-NCS)2]
-
pH 7.8
-
0.047
-
[Co(C16H23N2O)2]ClO4
-
pH 7.8
-
0.0962
-
[Cu(C13H11N2O)(H2O)] x ClO4
-
pH 7.8
-
0.08125
-
[Cu(C13H11N2O)(H2O)](NO3) x H2O
-
pH 7.8
-
0.0104
-
[Cu2(C16H24N2O)2Cl4]
-
pH 7.8
-
0.0539
-
[Mn(C17H16N2O2)N3]
-
pH 7.8
-
0.0195
-
[Zn(C9H10N2)(Cl)2]
-
pH 7.8
-
0.0254
-
Mn[Mn(CH3COO)(C25H20N2O2)]2
-
pH 7.8
-
additional information
-
additional information
-
in vitro bi-substrate-inhibitor-enzyme simulation and kinetics, overview
-
additional information
-
additional information
-
IC50 of lithopsermic acid is 0.0052 mg/ml
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
IC50 values for Tamnus communis root extract on cytochrome C reduction by the enzyme, overview
-
additional information
-
additional information
-
IC50 of licewraflavone is 0.00085 mg/ml and for allopurinol is 0.00040 mg/ml
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0002
0.0022
-
enzyme activity in embryo cell lines
0.003
-
-
crude, cell-free liver enzyme extract
0.044
-
-
purified recombinant enzyme, substrate xanthine, pH 8.0
0.702
-
-
purified recombinant enzyme, substrate NADH, pH 6.6
1.67
-
-
-
1.712
-
-
purified recombinant enzyme, in presence of sulfide/dithionite
1.8
-
-
-
2.04
-
-
colostrum
2.4
5.1
-
-
2.963
-
-
-
5.2
-
-
-
7.8
-
-
milk
8.571
-
-
-
10.16
-
-
-
17.5
-
-
pancreas enzyme with allopurinol at 50 mg/kg body weight
17.8
-
-
pancreas enzyme
25.2
-
-
intestine enzyme with allopurinol at 50 mg/kg body weight
26.6
-
-
intestine enzyme
29.5
-
-
kidney enzyme with allopurinol at 50 mg/kg body weight
49.9
-
-
kidney enzyme
123
-
-
milk
189.6
-
-
electron acceptor O2
800
-
-
electron acceptors O2 and NAD+
additional information
-
-
rate of extracellular catabolism of 6-mercaptopurine by XOD
additional information
-
-
measurement of cytokine production and factor translocation, overview
additional information
-
-
20 mU/ml of milk irrespective of infections of mammary gland with bacteria
additional information
-
-
in vivo evaluation of xanthine oxidase activities in a Greek population sample by the RP-HPLC monitoring of caffeine metabolic ratios after caffeine feeding experiments after a methylxanthine-free diet, detection method optimization and evaluation, overview
additional information
-
-
measurement of reactive oxygen species production by human neutrophils
additional information
-
-
-
additional information
-
-
-
additional information
-
-
activities of wild-type in comparison to mutant enzymes, overview
additional information
-
-
tissue-dependent enzyme activity, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
generation of nitrite or NO
5
-
-
-
6.6
-
-
substrate NADH
7
-
-
assay at
7
-
-
assay at
7
-
-
assay at
7
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
-
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.6
-
-
assay at
7.8
-
-
assay at
7.8
-
-
assay at
7.8
-
-
assay at
7.8
-
-
assay at
7.8
-
-
assay at
8
-
-
assay at
8
-
-
assay at
8
-
-
substrate xanthine
8.1
-
-
assay at
8.2
-
-
-
8.3
-
-
-
8.35
-
-
-
8.5
-
-
conversion of dibromoacetonitrile to CN-
8.5
-
-
assay at
additional information
-
-
the rate of xanthine oxidation is pH dependent, and the neutral form of xanthine binds stronger to the enzyme than the monoanion
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
9
-
pH 5.0: about 10% of activity maximum, pH 9.0: about 25% of activity maximum
6
7.6
-
under aerobic conditions, NO generation increases more than three times as the pH value decreases from pH 7.4 to 6.0
6
9
-
pH 6.0: about 25% of activity maximum, pH 9.0: about 20% of activity maximum
6
9
-
-
6.5
9.5
-
pH 6.5: about 40% of maximal activity, pH 9.5: about 65% of maximal activity, conversion of dibromoacetonitrile to CN-
7.7
9.1
-
at pH 7.7 and 9.1: about 30% of activity maximum
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
-
22
-
-
assay at room temperature
22
-
-
assay at room temperature
22
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
37
-
-
assay at
37
-
-
conversion of dibromoacetonitrile to CN-
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
41
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
5C: about 10% of activity maximum, 60C: about 50% of activity maximum
27
50
-
-
30
45
-
30C: about 60% of maximal activity, 45C: about 75% of maximal activity, conversion of dibromoacetonitrile to CN-
additional information
-
-
increase of activity from 30C to 44C, inactivation at 60C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
lower enzyme activity compared to vena cava
Manually annotated by BRENDA team
-
smooth muscle cells
Manually annotated by BRENDA team
-
mouse embryo cell line: 3T12
Manually annotated by BRENDA team
-
positive correlation between plasma xanthine oxidase and age of the individual
Manually annotated by BRENDA team
-
a lymphoid cell line
Manually annotated by BRENDA team
Erythrocebus patas Patas monkey
-
-
-
Manually annotated by BRENDA team
-
xanthine oxidase mediated nitrite reduction can be a source of NO in heart tissue under conditions of tissue normoxia, and it is further increased with mild hypoxia
Manually annotated by BRENDA team
-
enzyme expression is increased in the failing heart
Manually annotated by BRENDA team
-
enzyme activity in intestinal tissues in experimental sepsis, overview
Manually annotated by BRENDA team
-
a nasopharyngeal epidermoid tumor cell line
Manually annotated by BRENDA team
Triticum aestivum Tugela DN
-
-
-
Manually annotated by BRENDA team
-
together with intestine highest enzyme activity of any tissue due to xanthine oxidase rich parenchyma cells of this tissues
Manually annotated by BRENDA team
-
xanthine oxidase activity falls for the first 11 days after infection with smooth type Salmonella typhimurium, coinciding with the period of bacterial growth in the liver. Mild infection with Pseudomonas aeruginosa stimulates xanthine oxidase
Manually annotated by BRENDA team
Erythrocebus patas Patas monkey, Mus musculus BALB/c
-
-
-
Manually annotated by BRENDA team
-
alveolar macrophages purified from the lung by lavage, and interstitial macrophages. Inflammatory cells express high levels of XOR activity, while in resident alveolar macrophage the enzyme content is extremely low prior to cytokine insufflation
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
alveolar macrophages purified from the lung by lavage, and interstitial macrophages. Inflammatory cells express high levels of XOR activity, while in resident alveolar macrophage the enzyme content is extremely low prior to cytokine insufflation
-
Manually annotated by BRENDA team
-
after weaning, during the involution of the mammary gland, enzyme activity increases and high mitochondrial H2O2 production takes place. Inhibition of xanthine oxidase slows down the involution of the mammary gland due to the decrease in the number of apoptotic cells and prevents the production of H2O2 that occurs during apoptosis
Manually annotated by BRENDA team
-
tumor cell line
Manually annotated by BRENDA team
-
unpasteurized milk
Manually annotated by BRENDA team
-
grade I from buttermilk
Manually annotated by BRENDA team
-
buttermilk
Manually annotated by BRENDA team
-
gastric mucosa of Helicobacter pylori positive and negative pediatric patients
Manually annotated by BRENDA team
-
cremaster muscle
Manually annotated by BRENDA team
-
tumor cell line
Manually annotated by BRENDA team
-
from bone marrow of different samples
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
positive correlation between plasma xanthine oxidase activity and expression and age of the animal
Manually annotated by BRENDA team
-
a mouse monocyte-macrophage cell line, ATCC TIB-71
Manually annotated by BRENDA team
Mus musculus BALB/c
-
-
-
Manually annotated by BRENDA team
-
tumor cell line
Manually annotated by BRENDA team
-
positive correlation between plasma xanthine oxidase activity and expression and age of the animal
Manually annotated by BRENDA team
-
higher enzyme activity compared to aorta
Manually annotated by BRENDA team
Erythrocebus patas Patas monkey
-
-
-
Manually annotated by BRENDA team
additional information
-
control of the enzyme under the circadian clock, activity is 15times higher in light than in darkness
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
co-localization of the enzyme with Toll-like receptor-4 on the cell surface membrane, inhibited by heparin
Manually annotated by BRENDA team
-
co-localization of the enzyme with Toll-like receptor-4 on the cell surface membrane, inhibited by heparin
-
Manually annotated by BRENDA team
-
secretion to milk
-
Manually annotated by BRENDA team
-
secreted enzyme
-
Manually annotated by BRENDA team
-
the enzyme is secreted to milk
-
Manually annotated by BRENDA team
Mus musculus BALB/c
-
-
-
-
Manually annotated by BRENDA team
Mus musculus BALB/c
-
-
-
Manually annotated by BRENDA team
-
milk lipid globule membrane possesses enzyme activity capable of catalyzing the conversion of xanthine dehydrogenase to xanthine oxidase, kinetic of this process is consistent with the rapid appearence of xanthine oxidase in milk
-
Manually annotated by BRENDA team
-
membrane-bound
-
Manually annotated by BRENDA team
-
enzyme is associated with bovine milk-fat-globule membrane
-
Manually annotated by BRENDA team
-
co-localization of the enzyme with Toll-like receptor-4 on the cell surface membrane, inhibited by heparin
Manually annotated by BRENDA team
-
enzyme from milk and mammary gland
-
Manually annotated by BRENDA team
-
matrix and core of peroxisomes of liver parenchymal cells, xanthine oxidoreductase and xanthine oxidase detected
Manually annotated by BRENDA team
additional information
-
distribution of enzyme in milk globules, mammary gland and liver
-
Manually annotated by BRENDA team
additional information
-
enzyme binds to endothelial cells in a partially heparin-reversible manner
-
Manually annotated by BRENDA team
additional information
-
enzyme binds specifically and with high affinity to bovine aortic endothelial cells, increasing cell xanthine oxidase activity up to 10fold, circulating xanthine oxidase may therefore bind to vascular cells, impairing cell function via oxidative mechanisms
-
Manually annotated by BRENDA team
additional information
-
liver enzyme: in supernatant fraction
-
Manually annotated by BRENDA team
additional information
-
only XOR activity is present in the cytoplasm of rat liver parenchymal cells. In Kupffer cells and sinusoidal endothelial cell xanthine oxidoreductase activity is demonstrated in vesicles and occasionally on granular endoplasmic reticulum. Xanthine oxidase activity is not found in Kupffer cells and sinusoidal cells
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
100000
-
-
approximate value, bovine milk, ultrafiltration
128000
-
-
gel filtration
146000
-
-
gel filtration
275000
-
-
gel filtration
280000
-
-
gel filtration
290000
-
-
-
295000
-
-
-
300000
-
-
gel filtration
300000
-
-
gel filtration
303000
-
-
sedimentation equilibrium
310000
-
-
gel filtration
additional information
-
-
-
additional information
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 80000, SDS-PAGE
dimer
-
2 * 69000, SDS-PAGE
dimer
-
2 * 150000, SDS-PAGE
dimer
-
1 * 152000, 1 * 131000, SDS-PAGE
dimer
-
2 * 130000-140000
dimer
-
2 * 120000
dimer
-
2 * 150000, SDS-PAGE
dimer
-
2 * 150000, SDS-PAGE
dimer
-
the two XOD subunits are strongly cooperative in both binding and catalysis
dimer
Arthrobacter sp. S-2
-
2 * 80000, SDS-PAGE
-
dimer
Enterobacter cloacae KY 3074
-
2 * 69000, SDS-PAGE
-
homodimer
-
composed of two identical subunits of about 145 kDa, each being subdivided into three domains: a N-terminal iron-sulfur-binding domain of 20 kDa, a 40 kDa domain harboring a FAD-binding site, and a C-terminal molybdenum cofactor-binding domain of 85 kDa
homodimer
-
-
oligomer
-
x * 52000 + x * 99000, SDS-PAGE
homodimer
-
alpha2, with four redox-active centers in each subunit laid out in discretely folding domains, structure, overview
additional information
-
on polyacrylamide gel electrophoresis in presence of SDS and 2-mercaptoethanol the purified xanthine oxidase is dissociated into one major band of approximately 150000 Da and three bands of 100000 Da, 60000 Da and 40000 Da
additional information
-
comparison of structural alterations of xanthine oxidase leading to xanthine dehydrogenase, EC 1.17.14, activity involving residues R335, R427, W336, and F549, mechanism of transition, overview
additional information
-
structural comparison of xanthine dehydrogenase, EC 1.17.1.4, and xanthine oxidase, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
Arthrobacter sp. S-2
-
-
-
flavoprotein
-
-
additional information
-
-
proteolytic modification
-
-
additional information
Arthrobacter sp. S-2
-
-
-
flavoprotein
-
-
additional information
-
reversible conversion of xanthine dehydrogenase to xanthin oxidase can be achieved by modification of Cys535 and Cys992, tryptic proteolysis of xanthine dehydrogenase after Lys551 or pancreatin cleavage after Leu219 and Lys569 results in irreversible transformation to xanthine oxidase
additional information
-
the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
additional information
-
bovine milk enzyme: conversion from oxidase into dehydrogenase by treatment with dithioerythritol or dihydrolipoic acid; oxidase is converted into an irreversible oxidase form by pretreatment with chymotrypsin, papain or subtilisin, but only partially with trypsin
additional information
-
the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
proteolytic modification
-
-
additional information
-
the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
proteolytic modification
-
-
additional information
-
the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
proteolytic modification
-
-
additional information
-
-
proteolytic modification
-
-
additional information
-
-
proteolytic modification
-
-
additional information
-
-
proteolytic modification
-
-
additional information
Enterobacter cloacae KY 3074
-
-
-
proteolytic modification
Enterobacter cloacae KY 3074
-
-
-
additional information
-
the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
proteolytic modification
-
-
additional information
-
the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
proteolytic modification
-
-
additional information
-
the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
proteolytic modification
-
-
additional information
Erythrocebus patas Patas monkey
-
the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
-
proteolytic modification
Erythrocebus patas Patas monkey
-
-
-
additional information
-
the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
proteolytic modification
-
-
additional information
-
-
proteolytic modification
-
-
additional information
-
-
additional information
-
the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
proteolytic modification
-
-
additional information
-
-
proteolytic modification
-
-
additional information
-
-
proteolytic modification
-
-
additional information
-
the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
additional information
-
-
proteolytic modification
-
-
additional information
-
-
additional information
-
the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
proteolytic modification
-
-
additional information
-
the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
proteolytic modification
-
-
additional information
-
liver enzyme is unstable as dehydrogenase and is gradually converted to oxidase
additional information
-
the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
additional information
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2.5 A resolution, each enzyme subunit is composed of an N-terminal 20000 Da domain containing two iron sulfur centers, a central 40000 Da FAD domain and a C-terminal 85000 molybdopterin binding domain, the four redox centers are aligned in a linear fashion
-
batch method most suitable for crystallization
-
crystal structure determination and analysis of the enzyme in complex with a variety of substrates and substrate analogues, e.g. with 2-hydroxy-6-methylpurine or hypoxanthine, X-ray diffraction structure analysis at 1.8-3.1 A resolution
-
enzyme in complex with inhibitor 2-hydroxy-6-methylpurine, 10 mg/ml purified enzyme in 40 mM Tris-HCl, pH 7.8, 20 mM diphosphate, pH 8.5, 0.2 mM EDTA and 5 mM DTT, batch method mixing 0.02 ml of protein solution and 0.01 ml of precipitant solution, the latter containing of 12-14% PEG 8000, 0.1 M potassium phosphate, and 0.2 mM EDTA, pH 7.2, for 2-3 days at 25C, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement
-
purified enzyme in complex with hypoxanthine or 6-mercaptopurine, mixing of 0.01 ml of 5 mg/ml protein solution with 0.005-0.006 ml of 12% polyethylene glycol 8000 solution, at pH 7.0, crystallization in the darkness at 25C, ligand binding by soaking of crystals, X-ray diffraction structure determination and analysis at 1.8 and 2.6 A resolution, respectively
-
urate complexes of the reduced form of native milk enzyme reaction intermediate, X-ray diffraction structure determination and analysis at 2.1 A resolution
-
2.25 A resolution, enzyme contains a molybdoptererin cofactor and two different [2Fe-2S] centers, enzyme is folded into four domains, the first two bind the iron sulfur centers, the last two are involved in molybtopterin binding
-
purified recombinant mutant E308V, 15mg/ml protein in 5 mM Tris, pH 8.5, containing 1mM sodium salicylate and 0.1mM EDTA, incubation with 5 mM dithiothreitol for 1 h at room temperature, aliquots of 0.005 ml protein solution are mixed with 0.005 ml of 100 mM sodium citrate, pH 5.0, containing 8-11% polyethylene glycol 8000, 5 mM DTT, 1 mM sodium salicylate, 0.1 mM EDTA, and placed on siliconized glass plates, 7 days at 20C, X-ray diffraction structure determination and analysis at 2.6 A resolution
-
W335A/F336L double mutant enzyme crystal structure analysis
-
xanthine oxidoreductase mutant W335A/F336L, showing two similar, but not identical subunits. The cluster involved in conformation-switching is completely disrupted in one subunit, but remains partly associated in the other. Xanthine oxidase and oxidoreductase forms of the mutant are in equilibrium that greatly favors the oxidase form, but upon incubation with dithiothreitol equilibrium is partly shifted towards the oxidoreductase form
P22985
XOR complexed with the artificial substrate 4-[5-pyridine-4-yl-1H-[1,2,4]triazol-3-yl]pyridine-2-carbonitril, FYX-051, crystal structure analysis. Urate complexes of the purified recombinant demolybdo-form of mutant D428A, X-ray diffraction structure determination and analysis at 1.7 A resolution
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.2
6.8
-
60C, 30 min
7.8
-
-
5C or 10C, 6 months, no significant loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
-
-
pH 6.2-6.8, 30 min, stable
70
-
-
30 min, complete loss of activity
additional information
-
-
the thermostability of xanthine oxidase in the presence of pyridine is highly increased compared to the unbound enzyme, overview
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stable for more than 1 year with alternate freezing and thawing
-
low operational stability by immobilization
-
phosphate stabilizes
-
the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
-
the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
-
heparin-Sepharose 6B-bound enzyme, half-life: 120 h and 67 h at 4C and 20C respectively, free enzyme, 61 h and 45 h at 4C and 67C respectively
-
the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
-
rat liver enzyme is unstable as dehydrogenase and is gradually converted to oxidase
-
the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol
-
the xanthine dehydrogenase form can be obtained through incubation of xanthine oxidase with sulfhydryl reducing reagents
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
the enzyme activity is stimulated by organic solvents, but the effect is reduced with increasing temperature, from 27C to 37C, the inhibitory effects of all organic solvents on the enzyme activity are increased at higher temperature, dependent on pH, overview
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
photooxidation, protection by competitive inhibitors
-
644645
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-75C, more than 1 year with alternate freezing and thawing, stable
-
-20C, 27% loss of activity after 2 weeks, 51% loss of activity after 4 weeks, 89% loss of activity after 12 weeks, goat enzyme
-
4C, 31% loss of activity after 6 days, 54% loss of activity after 12 days, 72% loss of activity after 16 days, goat enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His-tagged XDH1 from Pichia pastoris by nickel affinity and anion exchange chromatography
-
ammonium sulfate, DEAE-Sepaharose
-
native enzyme from fresh bovine cream
-
native enzyme from milk by ammonium sulfate fractionation, followed by affinity chromatography on heparin-agarose
-
native enzyme partially by gel filtration from fresh unpasteurized milk
-
purification of the molybdenum cofactor of milk xanthine oxidase
-
native enzyme from milk by ammonium sulfate fractionation, followed by affinity chromatography on heparin-agarose
-
recombinant wild-type and mutant enzymes from Escherichia coli strain JM109 by anion exchange and hydroxyapatite chromatography, ultrafiltration, and gel filtration
-
60% ammonium sulfate, benzamidine-Sepharose
-
native enzyme from milk by ammonium sulfate fractionation, followed by affinity chromatography on heparin-agarose
-
ammonium sulfate, hydroxyapatite, DEAE-cellulose
-
from liver
-
simultaneous purification of xanthine oxidase and aldehyde oxidase
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of His-tagged XDH1 in Pichia pastoris
-
expression in Escherichia coli
-
expression of wild-type and mtant enzymes in Escherichia coli strain JM109
-
gene XO, DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes, genotyping, expression in COS-7 cells
-
ectopic overexpression of XOR cDNA and uric acid supplementation reducing SUMO-PPARgamma in inflammatory mononuclear phagocytes
-
expression of enzyme mutant D428A in Spodoptera frugiperda Sf9 cells via the baculovirus transfection system in mostly the demolybdo-form
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E1261X
-
mutation of Glu1261 leads to a complete loss of activity
C1318Y
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
D1109T
-
naturally occuring nonsynonymous single nucleotide polymorphism
E308V
-
site-directed mutagenesis, mutant molybdopterin domain structure, overview, the xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site, the E803V mutation almost completely abrogates the activity towards hypoxanthine as a substrate, but the decrease in activity towards purine substrate is not due to large conformational change in the mutant enzyme
G172R
-
naturally occuring nonsynonymous single nucleotide polymorphism
H1221R
-
naturally occuring nonsynonymous single nucleotide polymorphism, the mutant variant shows about twofold increased activity compared to the wild-type enzyme
N909K
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
P1150R
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
P555S
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
R149C
-
naturally occuring single nucleotide polymorphism, inactive mutant
R607Q
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
R881M
-
site-directed mutagenesis, the xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site, the R881M mutant lacks activity towards xanthine, but retaines slight activity towards hypoxanthine
T109K
-
naturally occuring single nucleotide polymorphism, inactive mutant
T623I
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
W335A/F336L
P22985
xanthine oxidoreductase mutant displaying xanthine oxidase activity
W335A/F336L
-
xanthine oxidase locked mutant
E802Q
-
site-directed mutagenesis, altered kinetics of the mutant enzyme compared to the wild-type enzyme
additional information
-
immobilization of the enzyme to heparin sepharose
I703V
-
naturally occuring single nucleotide polymorphism, the mutant variant shows abput twofold increased activity compared to the wild-type enzyme
additional information
-
enzyme mutantions can lead to xanthinuria
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
construction of amperometric biosensors based in xanthine oxidase which has been immobilized by covalent binding to gold electrodes modified with dithiobis-N-succinimidyl propionate. Redox dyes thionine and methylene blue work well as electron acceptors for reduced enzyme
synthesis
-
the enzyme can be used for production of superoxide, from oxidation of an aldehyde, which in a co-oxidation system reacts with the aldehyde and converts beta-carotene to beta-ionone, method optimization, overview
diagnostics
-
the enzyme activity detection in sepsis can be used for a negative prognosis in sepsis diagnosis, overview
medicine
-
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
medicine
-
in Helicobacter pylori positive and negative pediatric patients, the activities of xanthine oxidase, myeloperoxidase, and superoxide dismutase in gastric mucosa are not affected by presence/absence of Helicobacter pylori
pharmacology
-
the enzyme is a target in treatment of heart failure
medicine
-
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
pharmacology
-
inhibition of xanthine oxidase is a potential therapeutic approach to diabetic neuropathy and vasculopathy