Information on EC 1.17.1.4 - xanthine dehydrogenase

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

EC NUMBER
COMMENTARY
1.17.1.4
-
RECOMMENDED NAME
GeneOntology No.
xanthine dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
xanthine + NAD+ + H2O = urate + NADH + H+
show the reaction diagram
Acts on a variety of purines and aldehydes. The animal enzyme can be interconverted to EC 1.1.3.22 xanthine oxidase, the oxidase form. That from liver exists in vivo mainly in the dehydrogenase form, but can be converted into EC 1.1.3.22 by storage at -20C, by treatment with proteolytic agents or organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate. The effect of thiol reagents can be reversed by thiols such as 1,4-dithioerythritol. EC 1.1.1.204 can also be converted into EC 1.1.3.22 by EC 1.8.4.7 enzyme-thiol transhydrogenase (oxidized-glutathione) in the presence of the oxidized glutathione. 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. Formerly EC 1.2.1.37
-
-
-
xanthine + NAD+ + H2O = urate + NADH + H+
show the reaction diagram
mechanism of conversion of dehydrogenase form to oxidase form
-
xanthine + NAD+ + H2O = urate + NADH + H+
show the reaction diagram
catalytically labile Mo-OH oxygen forms a bond with a carbon atom of substrate, the Mo=S group of the oxidized enzyme becomes protonated to afford Mo-SH on reduction of the molybdenum center
-
xanthine + NAD+ + H2O = urate + NADH + H+
show the reaction diagram
the catalytic sequence of Rhodobacter capsulatus XDH is initiated by abstraction of a proton from the Mo-OH group by the highly conserved active site subunit B residue Glu730, followed by nucleophilic attack of the resulting Mo-O on the carbon center of the substrate (C-2 in hypoxanthine and C-8 in xanthine) and concomitant hydride transfer to the Mo-S of the molybdenum center, reaction and substrate binding mechanisms, overview
O54050
xanthine + NAD+ + H2O = urate + NADH + H+
show the reaction diagram
reaction mechanism with substrate all-trans-retinol, overview
-
xanthine + NAD+ + H2O = urate + NADH + H+
show the reaction diagram
reaction mechanism, The reaction is initiated by proton abstraction from the Mo-OH group by Glu730, 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. Arg310 is involved in stablizing the transition state in the course of nucleophilic attack, overview
-
xanthine + NAD+ + H2O = urate + NADH + H+
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 + NAD+ + H2O = urate + NADH + H+
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
P22985
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
adenosine nucleotides degradation I
-
adenosine nucleotides degradation II
-
caffeine degradation III (bacteria, via demethylation)
-
guanosine nucleotides degradation I
-
guanosine nucleotides degradation II
-
guanosine nucleotides degradation III
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Purine metabolism
-
purine nucleobases degradation I (anaerobic)
-
purine nucleobases degradation II (anaerobic)
-
theophylline degradation
-
urate biosynthesis/inosine 5'-phosphate degradation
-
SYSTEMATIC NAME
IUBMB Comments
xanthine:NAD+ oxidoreductase
Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein [14]. The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [2,6,8,15] [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 [2,7,15].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AtXDH1
Q8GUQ8
-
EC 1.1.1.204
-
-
formerly
-
NAD-xanthine dehydrogenase
-
-
-
-
Retinol dehydrogenase
-
-
Rosy locus protein
-
-
-
-
xanthine oxidoreductase
-
-
-
-
xanthine oxidoreductase
Q8GUQ8
-
xanthine oxidoreductase
-
-
xanthine oxidoreductase
-
-
xanthine oxidoreductase
-
-
xanthine oxidoreductase
-
-
xanthine oxidoreductase
-
-
xanthine-NAD oxidoreductase
-
-
-
-
xanthine/NAD+ oxidoreductase
-
-
-
-
xanthine:NAD+ oxidoreductase
-
-
XDH
Pseudomonas putida 86
-
-
-
XDH
P22985
-
XDH/XO
-
-
-
-
XOR
-
-
-
-
XOR
-, Q8GUQ8
-
XOR
P22985
-
EC 1.2.1.37
-
-
formerly
-
additional information
-
mammalian XOR exists in two interconvertible forms, the xanthine dehydrogenase, XDH, form and the xanthine oxidase, XO, form. The primary gene product is XDH, which can be converted into XO
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
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
9054-84-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
induction by application of abscisic acid and in water-stressed leaves and roots
-
-
Manually annotated by BRENDA team
isozyme XDH1, expression in Pichia pastoris
Swissprot
Manually annotated by BRENDA team
increase in activity upon growth on selenite or molybdate, xanthine or uric acid
-
-
Manually annotated by BRENDA team
expression in Pseudomonas aeruginosa, for maximal level of functional expression, co-expression of xdhC gene is required which increases level of molybdenum incorporation. Iron and FAD content of expressed enzymes are independent of xdhC expression
-
-
Manually annotated by BRENDA team
large subunit; expression of genes xdhAB encoding the two subunits of enzyme, in Escherichia coli, produces active enzyme. Coexpression of xdhAB genes with Pseudomonas aeruginosa xdhC gene results in high levels of functional protein
Swissprot
Manually annotated by BRENDA team
small subunit; expression of genes xdhAB encoding the two subunits of enzyme, in Escherichia coli, produces active enzyme. Coexpression of xdhAB genes with Pseudomonas aeruginosa xdhC gene results in high levels of functional protein
Swissprot
Manually annotated by BRENDA team
Escherichia sp.
-
-
-
Manually annotated by BRENDA team
domesticus, male chicken
-
-
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
dehydrogenase activity predominant form
-
-
Manually annotated by BRENDA team
hyperuricemic mice induced by potassium oxonate
-
-
Manually annotated by BRENDA team
with ventilator-induced lung injury
-
-
Manually annotated by BRENDA team
no activity in Columba livia
-
-
-
Manually annotated by BRENDA team
no activity in Klebsiella sp.
-
-
-
Manually annotated by BRENDA team
Peptococcus sp.
-
-
-
Manually annotated by BRENDA team
Mill cv. Hass
-
-
Manually annotated by BRENDA team
ATCC strain 15692
-
-
Manually annotated by BRENDA team
strain 40
-
-
Manually annotated by BRENDA team
strain 86
-
-
Manually annotated by BRENDA team
Pseudomonas putida 40
strain 40
-
-
Manually annotated by BRENDA team
Pseudomonas putida 86
strain 86
-
-
Manually annotated by BRENDA team
cf. EC 1.17.3.2
UniProt
Manually annotated by BRENDA team
conversion of oxidoreductatse to oxidase
UniProt
Manually annotated by BRENDA team
expression of enzyme in baculovirus-insect cell system, yields a mixture of native dimeric, demolydbo-dimeric and monomeric forms. All forms contain flavin, the monomeric forms lack molybdopterin and the iron-sulfur centers. Monomeric forms require only three electrons for complete reduction
-
-
Manually annotated by BRENDA team
male and female Crj:CD(SD)IGS rats and male Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
male Sprague-Dawley rats, potassium oxonate-induced hyperuricemic rats
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
treated for 7 days with cocaine, or cocaine with a NADPH oxidase inhibitor apocynin, or cocaine with a xanthine oxidoreductase inhibitor allopurinol
-
-
Manually annotated by BRENDA team
Wistar rats
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
induction by application of abscisic acid and in water-stressed leaves and roots
-
-
Manually annotated by BRENDA team
formerly Micrococcus lactilyticus or Veillonella alcalescens
-
-
Manually annotated by BRENDA team
Veillonella sp.
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
the retinoic acid deficiency in breast tumour epithelial cells has been ascribed to an insufficient expression of either the enzyme(s) involved in its biosynthesis or the cellular retinol binding protein or both, overview
malfunction
-
potassium oxonate-induced hyperuricemia can be reduced by oral application of onions reducing serum uric acid levels in hyperuricemic rats. The compound probably does not act via simple enzyme inhibition mechanism
metabolism
-
xanthine dehydrogenase is an enzyme form of the xanthine dehydrogenase/oxidase enzyme, XDH, complex, that catalyzes the end step in the purine catabolic pathway and is directly involved in depletion of the adenylate pool in the cell
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
-, Q8GUQ8
AtXDH1 is a key enzyme in purine degradation where it oxidizes hypoxanthine to xanthine and xanthine to uric acid; 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 dehydrogenase is necessary for extracellular superoxide and hydrogen peroxide production by the organism. The selenium-dependent xanthine dehydrogenase triggers biofilm proliferation in Enterococcus faecalis through oxidant production
metabolism
-
xanthine dehydrogenase activity correlates with the presence of this labile selenoprotein complex and is absent in a selD, encoding selenophosphate synthetase, or an xdh mutant, overview. Peroxide levels are not increased in either the selD or the xdh mutant upon addition of selenite
additional information
-, Q8GUQ8
mammalian XOR exists in two interconvertible forms, the xanthine dehydrogenase, XDH, form and the xanthine oxidase, XO, form. The primary gene product is XDH, which can be converted into XO
additional information
-
active site structure, overview
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
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
additional information
-
biofilm formation is stimulated in the presence of uric acid, Se, and Mo and inhibited by auranofin or tungstate
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-methylhypoxanthine + NAD+ + H2O
1-methylxanthine + NADH
show the reaction diagram
-
10% of the activity compared to hypoxanthine
-
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
show the reaction diagram
-
-
-
-
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
show the reaction diagram
Peptococcus sp., Pseudomonas putida 40
-
-
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
show the reaction diagram
-
-
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
show the reaction diagram
-
10% of the activity compared to hypoxanthine
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
show the reaction diagram
Pseudomonas putida 40
-
-
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH + H+
show the reaction diagram
-
10fold reduced kred-value compared to xanthine, rather less effective than xanthine as a substrate
-
-
?
1-naphthaldehyde + NAD+ + ?
? + NADH
show the reaction diagram
-, Q8GUQ8
27.5% of the activity with xanthine
-
-
?
2 2-hydroxypurine + 2 NAD+ + 2 H2O
xanthine + 2,8-dihydroxypurine + 2 NADH + 2 H+
show the reaction diagram
-
considerable activity
84% xanthine, 8% 2,8-dihydroxypurine formed
?
2 hypoxanthine + 2 NAD+ + 2 H2O
xanthine + 6,8-dihydroxypurine + 2 NADH + 2 H+
show the reaction diagram
-
preferred substrate
100% xanthine, 51% 6,8-dihydroxypurine formed
?
2,6-diaminopurine + NAD+ + H2O
? + NADH + H+
show the reaction diagram
-
poor substrate
-
-
?
2,6-dithiopurine + NAD+ + H2O
? + NADH
show the reaction diagram
-
26% of the activity compared to hypoxanthine
-
?
2-amino-4-hydroxy-pterin + methylene blue + H2O
isoxanthopterin + reduced methylene blue
show the reaction diagram
-
-
-
?
2-amino-4-hydroxy-pterin + methylene blue + H2O
isoxanthopterin + reduced methylene blue
show the reaction diagram
-
-
-
?
2-amino-4-hydroxy-pterin + methylene blue + H2O
isoxanthopterin + reduced methylene blue
show the reaction diagram
-
-
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
r
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
precursor of the eye pigment drosopterin
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
conversion of xanthine dehydrogenase to xanthine oxidase is strongly influenced by in vitro cell culture of alveolar epithelial cells
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
11% of the activity compared to xanthine
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
r
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
precursor of the eye pigment drosopterin
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
conversion of xanthine dehydrogenase to xanthine oxidase is strongly influenced by in vitro cell culture of alveolar epithelial cells
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
11% of the activity compared to xanthine
-
?
2-amino-4-hydroxypterin + nitroblue tetrazolium + H2O
isoxanthopterin + reduced nitroblue tetrazolium
show the reaction diagram
-
very low activity, i.e. pterin
-
?
2-hydroxy-6-methylpurine + NAD+ + H2O
? + NADH + H+
show the reaction diagram
-
poor substrate
-
-
?
2-hydroxypurine + NAD+ + H2O
? + NADH
show the reaction diagram
-
35% of the activity compared to hypoxanthine, purine not oxidized
-
?
2-OH-purine + ferricyanide + H2O
? + ferrocyanide
show the reaction diagram
-
-
-
?
2-thioxanthine + NAD+ + H2O
2-thiourate + NADH
show the reaction diagram
-
57% of the activity compared to hypoxanthine
-
?
2-thioxanthine + NAD+ + H2O
2-thiourate + NADH + H+
show the reaction diagram
-
good substrate, effective substrate
-
-
?
3 purine + 3 NAD+ + 3 H2O
hypoxanthine + 8-hydroxypurine + 2-hydroxypurine + 3 NADH + 3 H+
show the reaction diagram
-
poor substrate
2.3% hypoxanthine, 2.3% 8-hydroxypurine and traces of 2-hydroxypurine formed
?
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + H+
show the reaction diagram
Pseudomonas putida, Pseudomonas putida 86
-
1.2% activity compared to xanthine
-
-
?
3-methylxanthine + ferricyanide + H2O
3-methylurate + ferrocyanide
show the reaction diagram
-
-
-
?
4-aminoimidazole-5-carboxamide + NADP+ + H2O
? + NADPH
show the reaction diagram
-
38% of the activity compared to hypoxanthine-NADP+
-
?
4-dimethylaminobenzaldehyde + NAD+ + H2O
4-dimethylaminobenzoate + NADH
show the reaction diagram
-
0.3% activity compared to xanthine
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
show the reaction diagram
Pseudomonas putida, Pseudomonas putida 86
-
0.7% activity compared to xanthine
-
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + ferricyanide + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + ferrocyanide
show the reaction diagram
-
i.e. allopurinol
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + methyl viologen + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced methyl viologen
show the reaction diagram
-
i.e. allopurinol, 8% of the activity compared to xanthine
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + NAD+ + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + NADH
show the reaction diagram
-
best substrate tested
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + NAD+ + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + NADH
show the reaction diagram
-
i.e. allopurinol
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + NAD+ + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + NADH
show the reaction diagram
-
i.e. allopurinol
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + nitroblue tetrazolium + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced nitroblue tetrazolium
show the reaction diagram
-
very low activity, i.e. allopurinol
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + nitroblue tetrazolium + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced nitroblue tetrazolium
show the reaction diagram
-
i.e. allopurinol
-
?
5-aminoimidazol-4-carboxamide + methyl viologen + H2O
? + reduced methyl viologen
show the reaction diagram
-
1.1% of the activity compared to xanthine
-
?
6,8-dihydropurine + NAD+ + H2O
? + NADH
show the reaction diagram
-
50% of the activity compared to hypoxanthine
-
?
6,8-dihydroxypurine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
18% urate formed
?
6,8-dihydroxypurine + O2
? + H2O2
show the reaction diagram
-
-
-
?
6,8-dihydroxypurine + O2 + H2O
? + H2O2
show the reaction diagram
-
-
-
?
6-mercaptopurine + methyl viologen + H2O
? + reduced methyl viologen
show the reaction diagram
-
9.5% of the activity compared to xanthine
-
?
6-thioxanthine + NAD+ + H2O
6-thiourate + NADH
show the reaction diagram
-
63% of the activity compared to hypoxanthine
-
?
6-thioxanthine + NAD+ + H2O
? + NADH + H+
show the reaction diagram
-
good substrate
-
-
?
6-thioxanthine + NAD+ + H2O
6-thiourate + NADH + H+
show the reaction diagram
-
effective substrate
-
-
?
8-azahypoxanthine + NAD+ + H2O
8-azaxanthine + NADH
show the reaction diagram
-
39% 0f the activity compared to hypoxanthine
-
?
8-azahypoxanthine + NAD+ + H2O
8-azaxanthine + NADH
show the reaction diagram
-
42% of the activity compared to hypoxanthine
-
?
8-azaxanthine + NAD+ + H2O
8-aza-urate + NADH
show the reaction diagram
-
very low activity
-
?
9-methylhypoxanthine + O2
9-methylxanthine + H2O2
show the reaction diagram
-
-
-
?
abscisic aldehyde + NAD+ + ?
? + NADH
show the reaction diagram
-, Q8GUQ8
28.9% of the activity with xanthine
-
-
?
acetaldehyde + 2,6-dichloroindophenol + H2O
?
show the reaction diagram
-
0.1% of activity with xanthine
-
-
?
acetaldehyde + 2,6-dichloroindophenol + H2O
?
show the reaction diagram
-
1.2% of activity with xanthine
-
-
?
acetaldehyde + ferricyanide + H2O
acetic acid + ferrocyanide
show the reaction diagram
-
5% of the activity compared to xanthine
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
very low activity
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
very low activity
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
very low activity
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
considerable activity for the recombinant enzyme
-
?
acetaldehyde + nitroblue tetrazolium + H2O
acetic acid + reduced nitroblue tetrazolium
show the reaction diagram
-
very low activity
-
?
adenine + ferricyanide + H2O
urate + ferrocyanide
show the reaction diagram
-
12% of the activity compared to xanthine
-
?
adenine + NAD+ + H2O
? + NADH
show the reaction diagram
-
low activity
-
?
adenine + NAD+ + H2O
? + NADH
show the reaction diagram
-
low activity
-
?
adenine-N1-oxide + NAD+ + H2O
? + NADH
show the reaction diagram
-
3.4% of the activity compared to hypoxanthine
-
?
benzaldehyde + ferricyanide + H2O
benzoate + ferrocyanide
show the reaction diagram
-
4% of the activity compared to xanthine
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
Pseudomonas putida, Pseudomonas putida 86
-
1.3% activity compared to xanthine
-
-
?
benzaldehyde + nitroblue tetrazolium + H2O
benzoate + reduced nitroblue tetrazolium
show the reaction diagram
-
very low activity
-
?
benzaldehyde + O2
benzoate + H2O2
show the reaction diagram
-
-
-
?
glyceraldehyde + 2,6-dichloroindophenol + H2O
?
show the reaction diagram
-
0.3% of activity with xanthine
-
-
?
glyceraldehyde + 2,6-dichloroindophenol + H2O
?
show the reaction diagram
-
12.1% of activity with xanthine
-
-
?
guanine + NAD+ + H2O
? + NADH
show the reaction diagram
-
81.3% of the activity compared to hypoxanthine
-
?
heptaldehyde + NAD+ + ?
? + NADH
show the reaction diagram
-, Q8GUQ8
12.5% of the activity with xanthine
-
-
?
hypoxanthine + 2 NAD+ + 2 H2O
urate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
hypoxanthine + 2 NAD+ + 2 H2O
urate + 2 NADH + 2 H+
show the reaction diagram
P22985
-
-
-
?
hypoxanthine + 2,6-dichorophenolindophenol + H2O
xanthine + ?
show the reaction diagram
-
considerable activity
-
?
hypoxanthine + 2,6-dichorophenolindophenol + H2O
xanthine + ?
show the reaction diagram
-
12.2% of the activity compared to NAD+
-
?
hypoxanthine + cytochrome c + H2O
xanthine + reduced cytochrome c
show the reaction diagram
-
2.1% of the activity compared to NAD+
-
?
hypoxanthine + ferricyanide
xanthine + ferrocyanide
show the reaction diagram
-
-
-
?
hypoxanthine + ferricyanide + H2O
xanthine + ferrocyanide
show the reaction diagram
-
-
-
-
?
hypoxanthine + ferricyanide + H2O
xanthine + ferrocyanide
show the reaction diagram
-
17.2% of the activity compared to NAD+
-
?
hypoxanthine + ferricyanide + H2O
xanthine + ferrocyanide
show the reaction diagram
-
98% of the activity compared to xanthine
-
?
hypoxanthine + ferricyanide + H2O
xanthine + ferrocyanide
show the reaction diagram
Pseudomonas putida 86
-
-
-
-
?
hypoxanthine + methyl viologen + H2O
xanthine + reduced methyl viologen
show the reaction diagram
-
-
-
?
hypoxanthine + methyl viologen + H2O
xanthine + reduced methyl viologen
show the reaction diagram
-
7% of the activity compared to xanthine
-
?
hypoxanthine + methylene blue + H2O
xanthine + reduced methylene blue
show the reaction diagram
-
39% of the activity compared to NAD+ as electron acceptor
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
r
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
preferred substrate
-
ir
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
subtilisin treatment leads to an active component I of 120000 kDa
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
NAD+-O2- dependent xanthine oxidase activity
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
NAD+-O2- dependent xanthine oxidase activity
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
predominant reaction
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
more rapidly oxidized than xanthine
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
12.4% of activity with xanthine
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
19% of activity with xanthine
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-, Q8GUQ8
94.7% of the activity with xanthine
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
preferred substrate
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
44% of the activity with xanthine
-
-
?
hypoxanthine + NAD+ + H2O
urate + ? + NADH
show the reaction diagram
-
149% activity compared to xanthine
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
-, Q8GUQ8
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
O54050
-, mechanism of substrate binding at the active site, importance of beta subunit residue Glu232 for substrate positioning, overview. The oxygen atom at the C-6 position of both substrates is oriented toward ArgB-310 in the active site
-
-
?
hypoxanthine + NADH
? + NO2- + NAD+
show the reaction diagram
-
0.1% of the xanthine oxidation rate
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
show the reaction diagram
-
-
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
show the reaction diagram
-
2.4% of the activity compared to NAD+
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
show the reaction diagram
-
40% of the activity compared to NAD+
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
show the reaction diagram
-
strict specificity for NADP+
-
?
hypoxanthine + nitroblue tetrazolium
xanthine + ?
show the reaction diagram
-
-
-
?
hypoxanthine + nitroblue tetrazolium
xanthine + ?
show the reaction diagram
-
18% of the activity compared to NAD+
-
?
hypoxanthine + O2
xanthine + H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + O2
xanthine + H2O2
show the reaction diagram
-
very low activity
-
?
hypoxanthine + O2 + H2O
xanthine + O2-
show the reaction diagram
-
-
no production of H2O2
-
?
hypoxanthine + phenazine methosulfate + H2O
urate + ?
show the reaction diagram
-
low activity
-
?
hypoxanthine + phenazine methosulfate + H2O
urate + ?
show the reaction diagram
-
effective electron acceptor
-
?
hypoxanthine + thio-NAD+ + H2O
xanthine + thio-NADH
show the reaction diagram
-
-
-
?
hypoxanthine + urate
xanthine + 6,8-dihydroxypurine
show the reaction diagram
-
oxygen-free assay
-
r
indole-3-acetaldehyde + NAD+ + H2O
indole-3-acetate + NADH + H+
show the reaction diagram
-
and similar aldehydes, 2-3% of the activity with xanthine
-
-
?
indole-3-carboxaldehyde + NAD+ + ?
? + NADH
show the reaction diagram
-, Q8GUQ8
31.3% of the activity with xanthine
-
-
?
inosine + NAD+ + H2O
? + NADH
show the reaction diagram
-
low activity
-
?
N-methylnicontinamide + NADP+ + H2O
? + NADPH
show the reaction diagram
-
low activity, only a substrate at pH values above 8.0
-
?
NAD(P)H + 2,6-dichlorophenolindophenol + H2O
NAD(P)+ + ?
show the reaction diagram
-
-
-
r
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
show the reaction diagram
-
-
-
-
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
show the reaction diagram
-
conversion to the oxidase type O by trypsinization leads to 80-100% decrease in the oxidation rate of NADH, conversion to the oxidase type O by heat-treatment leads to a diminution of NADH oxidation
-
-
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
show the reaction diagram
-
extremely slow reoxidation rate
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
show the reaction diagram
-
electron acceptor: nitroblue tetrazolium
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
show the reaction diagram
-
electron acceptor: nitroblue tetrazolium
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
show the reaction diagram
-
subtilisin treatment leads to an active component of 120000 kDa with enhanced activity
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
show the reaction diagram
-
only dehydrogenase type D shows considerable activities, not oxidase type O
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
show the reaction diagram
-
NADH diaphorase activity with several acceptors
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
show the reaction diagram
-
NADH diaphorase activity with several acceptors
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
show the reaction diagram
-
NADH diaphorase activity with several acceptors
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
show the reaction diagram
-
2,6-dichloroindophenol as electron acceptor
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
show the reaction diagram
-
2,6-dichloroindophenol, 3-acetylpyridine-adenine dinucleotide, methylene blue, phenazine methosulfate or trinitrobenzene sulfonate
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
show the reaction diagram
-
electron acceptors: 2,6-dichlorphenolindophenol or methyl viologen
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
show the reaction diagram
-
electron acceptor: 2,6-dichlorophenolindophenol, no activity for mutant E89K
-
?
NADH + O2 + H+
NAD+ + O2- + H2O2
show the reaction diagram
-
xanthine dehydrogenase catalyzes NADH oxidation leading to the formation of one O2- radical and half a H2O2 molecule, at rates three times those observed for xanthine oxidase. NADH efficiently oxidizes xanthine dehydrogenase, but only a great excess of NADH reduces xanthine oxidase
-
-
?
NADH + reduced phenazine methosulfate + cytochrome c
NAD+ + ?
show the reaction diagram
-
no activity for the mutant E89K
-
?
NADPH + electron acceptor + H2O
NADP+ + reduced electron acceptor
show the reaction diagram
-
electron acceptors: 2,6-dichlorophenolindophenol, methyl viologen, benzyl viologen, methylene blue
-
?
NADPH + nitroblue tetrazolium + H2O
NADP+ + reduced nitroblue tetrazolium
show the reaction diagram
-
diaphorase activity
-
?
NADPH + nitroblue tetrazolium + H2O
NADP+ + reduced nitroblue tetrazolium
show the reaction diagram
-
diaphorase activity
-
?
NADPH + O2
NADP+ + O2- + H+
show the reaction diagram
-
high NADPH oxidase activity
-
?
NADPH + phenazine methosulfate + cytochrome c
NADP+ + ?
show the reaction diagram
-
-
-
?
phthalazine + NAD+ + H2O
1-(2H)-phthalazinone + NADH
show the reaction diagram
-
0.4% activity compared to xanthine
-
-
?
propionaldehyde + NAD+ + H2O
propionic acid + NADH
show the reaction diagram
-
low activity
-
?
pterin + 2,6-dichloroindophenol + H2O
?
show the reaction diagram
-
22.7% of activity with xanthine
-
-
?
pterin + 2,6-dichloroindophenol + H2O
?
show the reaction diagram
-
9.7% of activity with xanthine
-
-
?
pterin + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
-
?
purine + 2,6-dichloroindophenol + H2O
?
show the reaction diagram
-
18.7% of activity with xanthine
-
-
?
purine + 2,6-dichloroindophenol + H2O
?
show the reaction diagram
-
8.5% of activity with xanthine
-
-
?
purine + ferricyanide + H2O
urate + ferrocyanide
show the reaction diagram
-
108% of the activity compared to xanthine
-
?
purine + methyl viologen + H2O
? + reduced methyl viologen
show the reaction diagram
-
2% of the activity compared to xanthine
-
?
purine + NAD+ + ?
? + NADH
show the reaction diagram
-, Q8GUQ8
10.3% of the activity with xanthine
-
-
?
purine + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
?
purine + NAD+ + H2O
? + NADH
show the reaction diagram
-
poor substrate
-
?
purine + NAD+ + H2O
? + NADH
show the reaction diagram
-
poor substrate
-
?
purine + NAD+ + H2O
? + NADH
show the reaction diagram
-
poor substrate
-
?
purine + NAD+ + H2O
? + NADH
show the reaction diagram
-
poor substrate
-
?
purine + NADP+ + H2O
? + NADPH
show the reaction diagram
-
60% of the activity compared to hypoxanthine
-
?
purine + nitroblue tetrazolium
?
show the reaction diagram
-
low activity
-
-
?
purine + O2 + H2O
8-hydroxypurine + H2O2
show the reaction diagram
-
-
-
?
purine + O2 + H2O
8-hydroxypurine + H2O2
show the reaction diagram
-
5% activity compared to xanthine
-
-
?
quinazoline + NAD+ + H2O
4-(3H)-quinazolinone + NADH
show the reaction diagram
-
2% activity compared to xanthine
-
-
?
salicylaldehyde + ferricyanide + H2O
salicylate + ferrocyanide
show the reaction diagram
-
2% of the activity compared to xanthine
-
?
salicylaldehyde + O2
salicylate + H2O2
show the reaction diagram
-
-
-
r
theobromine + NAD+ + H2O
? + NADH
show the reaction diagram
-
very low activity
-
?
theophylline + NAD+ + H2O
? + NADH
show the reaction diagram
-
low activity
-
?
urate + NADH
xanthine + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
subtilisin treatment leads to an active component of 120000 kDa
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
2.5% of the activity compared to methyl viologen as electron acceptor
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
13% of the activity compared to methylene blue as electron acceptor
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
very low activity for the mutant E89K
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
greatly enhanced activity for dehydrogenase type D and trypsin- or heat-treated oxidase types O
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
same activity compared to NAD+ as electron acceptor
-
r
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
show the reaction diagram
-
11% of the activity compared to ferricyanide as electron acceptor
-
?
xanthine + 3-acetylpyridine-adenine dinucleotide+ + H2O
urate + 3-acetylpyridine-adenine dinucleotide(H)
show the reaction diagram
-
same activity compared to NAD+
-
r
xanthine + 3-acetylpyridine-adenine dinucleotide+ + H2O
urate + 3-acetylpyridine-adenine dinucleotide(H)
show the reaction diagram
-
same activity compared to NAD+
-
r
xanthine + 3-acetylpyridine-adenine dinucleotide+ + H2O
urate + 3-acetylpyridine-adenine dinucleotide(H)
show the reaction diagram
-
low reverse activity
-
r
xanthine + benzyl viologen + H2O
urate + reduced benzyl viologen
show the reaction diagram
-
52% of the activity compared to methyl viologen as electron acceptor
-
?
xanthine + benzyl viologen + H2O
urate + reduced benzyl viologen
show the reaction diagram
-
18% of the activity compared to methylene blue as electron acceptor
-
?
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
show the reaction diagram
-
-
-
?
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
show the reaction diagram
-
low activity
-
?
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
show the reaction diagram
-
enhanced activity for heat- and trypsin-treated oxidase types O
-
?
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
show the reaction diagram
-
presence of ferredoxin enhances cytochrom c reduction
-
?
xanthine + DCIP + H2O
urate + reduced DCIP
show the reaction diagram
-
-
-
-
?
xanthine + FAD + H2O
urate + FADH
show the reaction diagram
-
35% of the activity compared to methylene blue as electron acceptor
-
?
xanthine + ferredoxin + H2O
urate + reduced ferredoxin
show the reaction diagram
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
show the reaction diagram
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
show the reaction diagram
Streptomyces sp., Clostridium sp., Veillonella sp., Penicillium sp., Escherichia sp.
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
show the reaction diagram
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
show the reaction diagram
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
show the reaction diagram
Peptococcus sp.
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
show the reaction diagram
-
99% of the activity compared to methyl viologen as electron acceptor
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
show the reaction diagram
-
specific ferricyanide-dependent activity, no activity with NAD+, NADP+, oxygen, cytochrome c, FAD or FMN
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
show the reaction diagram
-
58% of the activity compared to xanthine-NAD+
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
show the reaction diagram
-
preferred substrates, does not act with NAD+ or NADP+
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
show the reaction diagram
-
low activity for both dehydrogenase type D and oxidase type O
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
show the reaction diagram
-
low activity for both dehydrogenase type D and oxidase type O
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
show the reaction diagram
Pseudomonas putida 40
-
-
-
?
xanthine + FMN + H2O
urate + FMNH2
show the reaction diagram
-
44% of the activity compared to methylene blue as electron acceptor
-
?
xanthine + iodonitrotetrazolium + H2O
urate + reduced iodonitrotetrazolium
show the reaction diagram
-
-
-
?
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
show the reaction diagram
-
-
-
?
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
show the reaction diagram
-
-
-
?
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
show the reaction diagram
-
low activity
-
?
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
show the reaction diagram
-
best substrates tested, no activity with NAD+ or NADP+, 40% of the activity in the reverse reaction
-
r
xanthine + methylene blue + H2O
urate + reduced methylene blue
show the reaction diagram
-
-
-
r
xanthine + methylene blue + H2O
urate + reduced methylene blue
show the reaction diagram
-
-
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
show the reaction diagram
-
-
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
show the reaction diagram
-
-
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
show the reaction diagram
-
-
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
show the reaction diagram
-
subtilisin treatment leads to an active component of 120000 kDa
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
show the reaction diagram
-
same activity for dehydrogenase type D and oxidase type O
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
show the reaction diagram
-
enhanced oxidation of xanthine for dehydrogenase type D and trypsin- or heat-treated oxidase type O
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
show the reaction diagram
-
3fold higher activity compared to NAD+ as electron acceptor
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
show the reaction diagram
-
87% of the activity compared to methyl viologen as electron acceptor
-
?
xanthine + myoglobin + H2O
urate + reduced myoglobin
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-, Q8GUQ8
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
Q8RLC0, Q8RLC1
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
100% activity
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
xanthine dehydrogenase form has distinct xanthine/oxygen activity, 35-42% of electrons transferred to O2 to form O2-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
conversion of dehydrogenase to oxidase type due to oxidation of sulfhydryl groups by molecular oxygen, dehydrogenase activity recovered by treatment with dithiothreitol
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
strict dehydrogenase activity, no utilization of O2
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
61% of the activity compared to hypoxanthine
91% urate formed
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
only dehydrogenase type D present
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
ping-pong reaction mechanism
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
NAD+-dependent form is postulated to play a regulatory role in purine metabolism
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
NAD+-linked activity, very low activity towards molecular oxygen
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
75% of the activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
degradative pathway of conversion of purines to ammonia
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
only present as stable dehydrogenase from, no conversion to the oxidase form
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
xanthine oxidase form is the principle major form in fresh mouse milk, dehydrogenase form is the major form in mammary gland, conversion to the dehydrogenase form by thiol active compounds
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
involved in pteridine metabolism, 40% of activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
conversion of xanthine dehydrogenase to the oxidase type by thiol-disulfide oxidoreductase, thiol reagents or oxidized glutathione
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
67% of the activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
regulation of xanthine dehydrogenase expression is subjected to nitrogen catabolite repression mediated through the GlnA-dependent signaling pathway
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
trypsin treatment leads to a complete conversion of xanthine dehydrogenase to xanthine oxidase activity
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
minimum degree of 1 : 1 for xanthine, 2 : 2 for NAD, 1 : 1 for urate and 1 : 2 for NADH in the xanthine/NAD+ oxidoreductase reaction required
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
xanthine dehydrogenase can be partially reduced in a triphasic reaction by either xanthine or NADH, oxidation of fully, 6-electron-reduced xanthine dehydrogenase by either urate or NAD+ is monophasic and depends on the oxidant concentration
NADH-binding to the 2-electron reduced enzyme is implicated in fixing end-point position in reactions involving pyridine nucleotides, urate-binding is involved in fixing end-point reactions involving xanthine and urate
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
subtilisin treatment leads to an active component I of 120000 kDa
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
Pseudomonas putida 40
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
P22985
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-, Q8GUQ8
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
O54050
-, mechanism of substrate binding at the active site, importance of beta subunit residue Glu232 for substrate positioning, overview. The oxygen atom at the C-6 position of both substrates is oriented toward ArgB-310 in the active site
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
catalytically relevant binding mode of the substrate xanthine, overview
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
P22985
catalytically relevant binding mode of the substrate xanthine, overview
-
-
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
show the reaction diagram
-
-
-
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
show the reaction diagram
-
heat-treated intermediate dehydrogenase/oxidase type O
-
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
show the reaction diagram
-
intermediate form of dehydrogenase/oxidase type D/O
-
?
xanthine + NADP+ + H2O
urate + NADPH
show the reaction diagram
-
strict specificity for NADP+
-
?
xanthine + NADP+ + H2O
urate + NADPH
show the reaction diagram
-
11% of the activity compared to NAD+
-
?
xanthine + nitroblue tetrazolium + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + nitroblue tetrazolium + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + nitroblue tetrazolium + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + nitroblue tetrazolium + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + nitroblue tetrazolium + H2O
urate + ?
show the reaction diagram
-
32% of the activity compared to methyl viologen as electron acceptor
-
-
xanthine + O2
hypoxanthine + ?
show the reaction diagram
-
dismutation reaction
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
-
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
Escherichia sp.
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
no production of H2O2
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
very low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
very low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
very low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
low activity
-
r
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
subtilisin treatment leads to an active component I of 120000 kDa
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
4% of the activity compared to xanthine-NAD+
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
presence of ferredoxin enhances rate of oxygen reduction
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
toxic reactions of xanthine oxidase-derived radicals are critical factors in several mechanisms of tissue pathology
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
NAD+-independent trypsin-treated oxidase type O
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
NAD+-independent xanthine oxidase activity, low activity present in the enzyme preparation, conversion of the NAD+-dependent to NAD+-independent activity by some thiol reagents
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
xanthine oxidase form transfers 22% electrons to oxygen to form superoxide
-
?
xanthine + p-benzoquinone + H2O
p-benzosemiquinone + urate
show the reaction diagram
-
electron acceptor p-benzoquinone for both dehydrogenase and oxidase types
-
?
xanthine + p-benzoquinone + H2O
hypoxanthine + hydroquinone
show the reaction diagram
-
electron donor only for oxidase type
-
?
xanthine + phenazine methosulfate + cytochrome c + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + phenazine methosulfate + cytochrome c + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + phenazine methosulfate + cytochrome c + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + phenazine methosulfate + cytochrome c + H2O
urate + ?
show the reaction diagram
-
very low activity for the mutant E89K
-
?
xanthine + phenazine methosulfate + H2O
urate + ?
show the reaction diagram
-
-
-
r
xanthine + phenazine methosulfate + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + phenazine methosulfate + H2O
urate + ?
show the reaction diagram
-
-
-
?
xanthine + phenazine methosulfate + H2O
urate + ?
show the reaction diagram
-
5fold higher activity compared to NAD+ as electron acceptor
-
?
xanthine + pyridinealdehyde-NAD+ + H2O
urate + pyridinealdehyde-NADH
show the reaction diagram
-
53% of the activity compared to NAD+, low reverse activity
-
r
xanthine + riboflavin + H2O
urate + reduced riboflavin
show the reaction diagram
-
41% of the activity compared to methylene blue as electron acceptor
-
?
xanthine + thio-NAD+ + H2O
urate + thio-NADH
show the reaction diagram
-
-
-
?
xanthine + thio-NAD+ + H2O
urate + thio-NADH
show the reaction diagram
-
same activity compared to NAD+
-
r
xanthine + trinitrobenzenesulfonate + H2O
urate + ?
show the reaction diagram
-
-
-
r
xanthine + trinitrobenzenesulfonate + H2O
urate + ?
show the reaction diagram
-
subtilisin treatment leads to an active component of 120000 kDa
-
?
xanthopterin + NAD+ + H2O
leucopterin + NADH
show the reaction diagram
-
regulation of the pteridine pathway by competitive inhibition of reaction products and the precursor of xanthopterin, 7,8-dihydroxyxanthopterin, regulation of the pteridine pathway by competitive inhibition of reaction products and the precursor of xanthopterin, 7,8-dihydroxanthopterin
-
?
xanthosine + NAD+ + H2O
? + NADH
show the reaction diagram
-
15.1% of the activity compared to hypoxanthine
-
?
isoguanine + NAD+ + H2O
? + NADH
show the reaction diagram
-
7.3% of the activity compared to hypoxanthine
-
?
additional information
?
-
-
major function of enzyme in liver parenchymal and sinusoidal cells is production of uric acid as a antioxidant
-
-
-
additional information
?
-
-
NADH oxidation by xanthine oxidoreductase may constitute an important pathway for reactive oxygen species-mediated tissue injuries. Xanthine oxidoreductase and xanthine oxidase catalyze the NADH oxidation, generating O2- radicals and inducing the peroxidation of liposomes, in a NADH and enzyme dependent manner
-
-
-
additional information
?
-
P47989
xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
-
-
-
additional information
?
-
-
xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
-
-
-
additional information
?
-
-
the dehydrogenase form of enzyme reacts significantly faster than the oxidase form
-
-
-
additional information
?
-
-
NAD+ is the most effcient electron acceptor, followed by 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyl-2H-tetrazolium chloride and ferricyanide
-
-
-
additional information
?
-
-
xanthine oxidoreductase is a regulator of adipogenesis and of nuclear recptor PPARgamma activityand is essential for the regulation of fat accretion
-
-
-
additional information
?
-
-
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant
-
-
-
additional information
?
-
-
model in which good substrates are bound correctly in the active site in an orientation that allows Arg310 to stabilize the transition state for the first step of the overall reaction via an electrostatic interaction at the C-6 position, thereby accelerating the reaction rate. Poor substrates bind upside down relative to this correct orientation and are unable to avail themselves of the additional catalytic power provided by Arg310 in wild-type enzyme but are significantly less affected by mutations at this position. Analysis of rapid reaction kinetic parameters
-
-
-
additional information
?
-
-
enzyme inhibition by orange juice and hesperetin participates in preventing oxidative stress by enhancing total antioxidant capacity and decreasing lipid peroxidation, overview
-
-
-
additional information
?
-
-
the enzyme is responsible for the synthesis of uric acid, the major end product of the metabolism of nitrogen compounds in birds, uric acid functions as an antioxidant to reduce oxidative stress
-
-
-
additional information
?
-
-
with the supply of molecular oxygen upon reperfusion of ischemic tissues, xanthine oxidoreductase metabolizes xanthine and hypoxanthine to uric acid, free radicals are generated, overview. Decrease in xanthine oxidoreductase expression is one of the beneficial mechanisms of trimetazidine on ischemia/reperfusion injury, preventing the degradation of purine nucleotides during the oxidation of hypoxanthine to xanthine and uric acid and formation of free radicals
-
-
-
additional information
?
-
-
xanthine dehydrogenase is the native form of xanthine oxidase, EC 1.17.3.2, conversion causes a loss of the NAD+ binding activity and of the retinol oxidation activity, the conversion with conformational changes is reversible, except for alteration due to proteolytic cleavage
-
-
-
additional information
?
-
-
xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. The difference in three-dimensional structures is centered on Ala535. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms
-
-
-
additional information
?
-
-
xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms
-
-
-
additional information
?
-
-, Q8GUQ8
XDH can be converted into XO, EC 1.17.3.2, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20%
-
-
-
additional information
?
-
-, Q8GUQ8
AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher than the activity with xanthine accompanied by a doubling in superoxide production and is dependent on sulfurated molybdenum cofactor, overview. FAD is crucial for NADH-based superoxide formation of AtXDH1, whereas the molybdenum cofactor has only little or no influence on the activity, residues E831, R909, E1297, W364, and Y421 are involved
-
-
-
additional information
?
-
-, Q8GUQ8
by an alternative activity, AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide. In comparison to the specific activity with xanthine as substrate, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher. Each sub-activity is determined by specific conditions such as the availability of substrates and co-substrates, which allows regulation of superoxide production by AtXDH1
-
-
-
additional information
?
-
-
xanthine and 2-hydroxy-6-methylpurine are substrates. Substrate binding structures, overview
-
-
-
additional information
?
-
Pseudomonas putida 86
-
NAD+ is the most effcient electron acceptor, followed by 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyl-2H-tetrazolium chloride and ferricyanide
-
-
-
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
2 2-hydroxypurine + 2 NAD+ + 2 H2O
xanthine + 2,8-dihydroxypurine + 2 NADH + 2 H+
show the reaction diagram
-
considerable activity
84% xanthine, 8% 2,8-dihydroxypurine formed
?
2 hypoxanthine + 2 NAD+ + 2 H2O
xanthine + 6,8-dihydroxypurine + 2 NADH + 2 H+
show the reaction diagram
-
preferred substrate
100% xanthine, 51% 6,8-dihydroxypurine formed
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
r
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
i.e. pterin
precursor of the eye pigment drosopterin
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
conversion of xanthine dehydrogenase to xanthine oxidase is strongly influenced by in vitro cell culture of alveolar epithelial cells
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
show the reaction diagram
-
11% of the activity compared to xanthine
-
?
3 purine + 3 NAD+ + 3 H2O
hypoxanthine + 8-hydroxypurine + 2-hydroxypurine + 3 NADH + 3 H+
show the reaction diagram
-
poor substrate
2.3% hypoxanthine, 2.3% 8-hydroxypurine and traces of 2-hydroxypurine formed
?
6,8-dihydroxypurine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
18% urate formed
?
6,8-dihydroxypurine + O2
? + H2O2
show the reaction diagram
-
-
-
?
guanine + NAD+ + H2O
? + NADH
show the reaction diagram
-
81.3% of the activity compared to hypoxanthine
-
?
hypoxanthine + 2 NAD+ + 2 H2O
urate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
hypoxanthine + 2 NAD+ + 2 H2O
urate + 2 NADH + 2 H+
show the reaction diagram
P22985
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
r
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
preferred substrate
-
ir
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
subtilisin treatment leads to an active component I of 120000 kDa
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
NAD+-O2- dependent xanthine oxidase activity
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
NAD+-O2- dependent xanthine oxidase activity
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
predominant reaction
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
more rapidly oxidized than xanthine
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH
show the reaction diagram
-
preferred substrate
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
-, Q8GUQ8
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
O54050
-
-
-
?
hypoxanthine + NADH
? + NO2- + NAD+
show the reaction diagram
-
0.1% of the xanthine oxidation rate
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
show the reaction diagram
-
-
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
show the reaction diagram
-
2.4% of the activity compared to NAD+
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
show the reaction diagram
-
40% of the activity compared to NAD+
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
show the reaction diagram
-
strict specificity for NADP+
-
?
hypoxanthine + O2
xanthine + H2O2
show the reaction diagram
-
-
-
?
hypoxanthine + O2
xanthine + H2O2
show the reaction diagram
-
very low activity
-
?
NADPH + O2
NADP+ + O2- + H+
show the reaction diagram
-
high NADPH oxidase activity
-
?
purine + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
?
purine + NAD+ + H2O
? + NADH
show the reaction diagram
-
poor substrate
-
?
purine + NAD+ + H2O
? + NADH
show the reaction diagram
-
poor substrate
-
?
purine + NAD+ + H2O
? + NADH
show the reaction diagram
-
poor substrate
-
?
purine + NAD+ + H2O
? + NADH
show the reaction diagram
-
poor substrate
-
?
purine + NADP+ + H2O
? + NADPH
show the reaction diagram
-
60% of the activity compared to hypoxanthine
-
?
purine + O2 + H2O
8-hydroxypurine + H2O2
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
xanthine dehydrogenase form has distinct xanthine/oxygen activity, 35-42% of electrons transferred to O2 to form O2-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
conversion of dehydrogenase to oxidase type due to oxidation of sulfhydryl groups by molecular oxygen, dehydrogenase activity recovered by treatment with dithiothreitol
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
strict dehydrogenase activity, no utilization of O2
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
61% of the activity compared to hypoxanthine
91% urate formed
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
only dehydrogenase type D present
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
ping-pong reaction mechanism
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
NAD+-dependent form is postulated to play a regulatory role in purine metabolism
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
NAD+-linked activity, very low activity towards molecular oxygen
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
75% of the activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
degradative pathway of conversion of purines to ammonia
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
only present as stable dehydrogenase from, no conversion to the oxidase form
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
xanthine oxidase form is the principle major form in fresh mouse milk, dehydrogenase form is the major form in mammary gland, conversion to the dehydrogenase form by thiol active compounds
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
involved in pteridine metabolism, 40% of activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
conversion of xanthine dehydrogenase to the oxidase type by thiol-disulfide oxidoreductase, thiol reagents or oxidized glutathione
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
67% of the activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
regulation of xanthine dehydrogenase expression is subjected to nitrogen catabolite repression mediated through the GlnA-dependent signaling pathway
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
trypsin treatment leads to a complete conversion of xanthine dehydrogenase to xanthine oxidase activity
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
minimum degree of 1 : 1 for xanthine, 2 : 2 for NAD, 1 : 1 for urate and 1 : 2 for NADH in the xanthine/NAD+ oxidoreductase reaction required
-
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
xanthine dehydrogenase can be partially reduced in a triphasic reaction by either xanthine or NADH, oxidation of fully, 6-electron-reduced xanthine dehydrogenase by either urate or NAD+ is monophasic and depends on the oxidant concentration
NADH-binding to the 2-electron reduced enzyme is implicated in fixing end-point position in reactions involving pyridine nucleotides, urate-binding is involved in fixing end-point reactions involving xanthine and urate
r
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
subtilisin treatment leads to an active component I of 120000 kDa
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-, Q8GUQ8
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
O54050
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
catalytically relevant binding mode of the substrate xanthine, overview
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
P22985
catalytically relevant binding mode of the substrate xanthine, overview
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
Pseudomonas putida 40
-
-
-
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
show the reaction diagram
-
-
-
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
show the reaction diagram
-
heat-treated intermediate dehydrogenase/oxidase type O
-
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
show the reaction diagram
-
intermediate form of dehydrogenase/oxidase type D/O
-
?
xanthine + NADP+ + H2O
urate + NADPH
show the reaction diagram
-
strict specificity for NADP+
-
?
xanthine + NADP+ + H2O
urate + NADPH
show the reaction diagram
-
11% of the activity compared to NAD+
-
?
xanthine + O2
hypoxanthine + ?
show the reaction diagram
-
dismutation reaction
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
-
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
Escherichia sp.
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
very low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
very low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
very low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
low activity
-
r
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
subtilisin treatment leads to an active component I of 120000 kDa
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
4% of the activity compared to xanthine-NAD+
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
presence of ferredoxin enhances rate of oxygen reduction
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
toxic reactions of xanthine oxidase-derived radicals are critical factors in several mechanisms of tissue pathology
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
NAD+-independent trypsin-treated oxidase type O
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
NAD+-independent xanthine oxidase activity, low activity present in the enzyme preparation, conversion of the NAD+-dependent to NAD+-independent activity by some thiol reagents
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
xanthine oxidase form transfers 22% electrons to oxygen to form superoxide
-
?
xanthopterin + NAD+ + H2O
leucopterin + NADH
show the reaction diagram
-
regulation of the pteridine pathway by competitive inhibition of reaction products and the precursor of xanthopterin, 7,8-dihydroxanthopterin
-
?
hypoxanthine + urate
xanthine + 6,8-dihydroxypurine
show the reaction diagram
-
oxygen-free assay
-
r
additional information
?
-
-
major function of enzyme in liver parenchymal and sinusoidal cells is production of uric acid as a antioxidant
-
-
-
additional information
?
-
-
NADH oxidation by xanthine oxidoreductase may constitute an important pathway for reactive oxygen species-mediated tissue injuries. Xanthine oxidoreductase and xanthine oxidase catalyze the NADH oxidation, generating O2- radicals and inducing the peroxidation of liposomes, in a NADH and enzyme dependent manner
-
-
-
additional information
?
-
P47989
xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
-
-
-
additional information
?
-
-
xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
-
-
-
additional information
?
-
-
xanthine oxidoreductase is a regulator of adipogenesis and of nuclear recptor PPARgamma activityand is essential for the regulation of fat accretion
-
-
-
additional information
?
-
-
enzyme inhibition by orange juice and hesperetin participates in preventing oxidative stress by enhancing total antioxidant capacity and decreasing lipid peroxidation, overview
-
-
-
additional information
?
-
-
the enzyme is responsible for the synthesis of uric acid, the major end product of the metabolism of nitrogen compounds in birds, uric acid functions as an antioxidant to reduce oxidative stress
-
-
-
additional information
?
-
-
with the supply of molecular oxygen upon reperfusion of ischemic tissues, xanthine oxidoreductase metabolizes xanthine and hypoxanthine to uric acid, free radicals are generated, overview. Decrease in xanthine oxidoreductase expression is one of the beneficial mechanisms of trimetazidine on ischemia/reperfusion injury, preventing the degradation of purine nucleotides during the oxidation of hypoxanthine to xanthine and uric acid and formation of free radicals
-
-
-
additional information
?
-
-
xanthine dehydrogenase is the native form of xanthine oxidase, EC 1.17.3.2, conversion causes a loss of the NAD+ binding activity and of the retinol oxidation activity, the conversion with conformational changes is reversible, except for alteration due to proteolytic cleavage
-
-
-
additional information
?
-
-
xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. The difference in three-dimensional structures is centered on Ala535. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms
-
-
-
additional information
?
-
-
xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms
-
-
-
additional information
?
-
-, Q8GUQ8
XDH can be converted into XO, EC 1.17.3.2, 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
-
one FAD per hemimolecule
FAD
-
one FAD per subunit, central 40 kDa FAD-domain
FAD
-
generally viewed as the site at which NADH reacts
FAD
-
substitutions G348E, G353D, S357F located within the flavin/NAD+/NADH-domain
FAD
-
two FAD per enzyme molecule
FAD
-
trypsin-treated oxidase type O shows absence of FAD, heat-treated oxidase type O shows small measurable FAD
FAD
-
deflavo-enzyme completely loses xanthine/NAD+ activity, no loss of xanthine/2,6-dichorophenolindophenol activity, xanthine dehydrogenase form stabilizes the neutral form of flavin, xanthine oxidase form does not
FAD
-
1.69 mol FAD per mol enzyme
FAD
-
2 mol per mol enzyme
FAD
-
0.9 mol per subunit
FAD
-
1.0-1.1 molecules per alphabeta protomer
FAD
-
1 mol per mol of subunit
FAD
P47989
1 mol per mol of subunit
FAD
-
the FAD cofactor is open to solvent in XO, but much less accessible in XDH, binding site structure, overview
FAD
-, Q8GUQ8
a molybdenum-iron-flavoenzyme; a molybdenum-iron-flavoenzyme, activity-to-flavin ratio of 8 with xanthine as substrate and NAD+ as final electron acceptor, recombinant enzyme
FAD
P22985
role of Asp428 in the FAD reactivity, overview
ferricyanide
-
does not act with NAD+ or NADP+
ferricyanide
-
specific xanthine oxidizing activity
FMN
-
primarily flavin cofactor
heme
-
ferricyanide-linked activity, no FAD
molybdenum cofactor
-
the enzyme contains molybdenum cofactor comprising only molybdopterin and molybdenum
molybdenum cofactor
-
structure-function analysis, mechanism, overview
molybdenum cofactor
-
binding involves residues GluB730, GlnA102, CysA103, CysA106, CysA134, and CysA13 of the alpha and beta subunits
molybdenum cofactor
-
molybdenum-containing enzyme
molybdenum cofactor
-, Q8GUQ8
C-terminal
molybdenum cofactor
-
cofactor geometry, overview
molybdopterin
-
enzyme contains molybdopterin
molybdopterin
-
0.62 molecules per subunit
molybdopterin
P47989
0.09 molecules per subunit
molybdopterin
-
protein XdhC binds molybdenum cofactor in stoichiometric amounts, which subsequently can be inserted into molybdenum-free apoxanthine dehydrogenase. Protein XdhC is required for the stabilization of the sulfurated form of molybdenum cofactor
molybdopterin
-
in the crystal structure of reduced enzyme in complex with oxipurinol at 2.0 A resolution, electron density is observed between the N2 nitrogen atom of oxipurinol and the molybdenum atom of the molybdopterin cofactor
NAD+
-
cannot be replaced by NADP+
NAD+
-
cannot be replaced by NADP+
NAD+
-
cannot be replaced by NADP+
NAD+
-
physiological cofactor
NAD+
-
cannot be replaced by NADP+
NAD+
-
activity different from ferricyanide-linked activity
NAD+
-
cannot be replaced by NADP+
NAD+
-
cannot be replaced by NADP+
NAD+
-
cannot be replaced by NADP+
NAD+
-
cannot be replaced by NADP+
NAD+
-, Q8GUQ8
; NAD+ inhibits NADH oxidase activity of AtXDH1
NADH
-
reduces xanthine oxidase to reductase activity
NADH
-, Q8GUQ8
suppresses NAD+-dependent xanthine oxidation
NADP+
-
11% of the activity compared to NAD+
NADP+
-
40% of the activity compared to NAD+
[2Fe-2S] cluster
-
-
-
[2Fe-2S] cluster
-, Q8GUQ8
two N-terminal non-identical iron-sulfur clusters of the [2Fe-2S]-type
-
molybdopterin
P22985
cofactor geometry, overview
additional information
-
one molybdopterin-cofactor, two Fe2-S2-cluster, one FAD per subunit
-
additional information
-
cofactor compostion similar to eukaryotic enzymes
-
additional information
-
molybdoironflavoprotein: 17.5 mol iron, 18.4 mol acid-labile sulfur, 2.3 mol molybdenum, 1.1 mol tungsten, 0.95 mol selenium
-
additional information
-
-
-
additional information
-
molybdoironflavoprotein: molar ratio of molybdenum to iron to acid-labile-sulfur to FAD is 1 : 2 : 1.9 : 0.8
-
additional information
-
iron-containing flavoprotein
-
additional information
-
-
-
additional information
-
molybdoironflavoprotein: 1 : 1 : 4 ratio of molybdenum to FAD to iron
-
additional information
-
molybdoironflavoprotein: ratio of 2 : 1.4 : 7.6 of FAD to molybdenum to Fe-S
-
additional information
-
molybdoironflavoprotein: ratio of iron to FAD to molybdenum is 4 : 1 : 1
-
additional information
-
-
-
additional information
-
molybdoironflavoprotein: ratio of non-heme iron to acid-labile sulfur to FAD to molybdenum to tungsten to selenium is 7.7 : 7.5 : 1.7 : 1.8 : 0.12 : 0.13
-
additional information
-
molybdoironflavoprotein: 8 : 8 : 2 : 1.5 ratio of iron to sulfide to flavin to molybdenum
-
additional information
-
-
-
additional information
-
-
-
additional information
-
non-heme flavoprotein
-
additional information
-
-
-
additional information
-
iron-containing flavoprotein; molar ratio of FAD to iron to labile sulfide per mol enzyme is 2 : 14 : 2
-
additional information
-, Q8GUQ8
both NAD+ and NADH compete for the same binding site
-
additional information
-
cofactor conformation, binding structure analysis and mechanism, overview
-
additional information
P22985
cofactor conformation, binding structure analysis and mechanism, overview
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe
-
iron-sulfur groups
Fe
-
iron-sulfur groups
Fe
-
non-heme iron-sulfur groups, 7.7 g-atom Fe, 7.5 g- atom S2- per mol enzyme
Fe
-
8.2 mol iron per mol of enzyme
Fe
-
12.1 mol iron per mol enzyme
Fe
-
8 atoms iron per mol enzyme
Fe
-, Q8GUQ8
a molybdenum-iron-flavoenzyme
Fe2+
-
in a [Fe4-S4] domain
Iron
-
contains FeSI and FeSII clusters
Iron
-
FeS center
Iron
-
FeS center, EPR spectra, wild type 3.7 mol per subunit, active form of mutant R135C 2.8 mol per subunit, inactive form of mutant R135C 1.2 mol per subunit
Iron
-
3.7-3.9 atoms per alphabeta protomer
Iron
P47989
enzyme is about 30% deficient in iron-sulfur centers on basis of UV/vis and CD spectra
Iron
-
the enzyme is a molybdo-flavoprotein, the enzyme tetramer contains two [2Fe-2S] clusters
Iron
-, Q8GUQ8
a molybdenum-iron-flavoenzyme, contains [2Fe-2S] centers
Iron
-
two [2Fe-2S] centers
Iron
P22985
two [2Fe-2S] centers
Iron-sulfur-center
-
-
Iron-sulfur-center
-
2 Fe2-S2-clusters, located at the N-terminal 20 kDa domain
Iron-sulfur-center
-
2 Fe2-S2-clusters
Iron-sulfur-center
-
1 Fe2-S2-cluster
Iron-sulfur-center
-
-
Iron-sulfur-center
-
substitutions G42E, E89K, L127F located within the iron-sulfur domain
Iron-sulfur-center
-
-
Iron-sulfur-center
-
2 Fe2-S2-clusters
Iron-sulfur-center
-
2 Fe2-S2-clusters
Iron-sulfur-center
-
2 Fe2-S2-clusters
Iron-sulfur-center
-
-
Mo
-
1.7 mol molybdenum per mol enzyme
Mo
-
1 mol molybdenum per mol enzyme
Mo
-
2 molybdenum per mol enzyme
Mo
-
XOR is a molybdenum-containing enzyme
Mo
-, Q8GUQ8
a molybdenum-iron-flavoenzyme
Molybdenum
-
contains molybdenum-molybdopterin
Molybdenum
-
active form of mutant R135C Moco content 97%, inactive form of mutant R135C Moco content 3.8%
Molybdenum
-
0.18 atoms per subunit
Molybdenum
-
superoxide production depends on sulfuration of molybdenum cofactor
Molybdenum
-
1.1 atoms per alphabeta protomer in wild-type, 0.89 atoms per alphabeta protomer after expression of xdhABC genes, 0.24 atoms per alphabeta protomer after expression of xdhAB genes
Molybdenum
-
the enzyme contains molybdenum cofactor comprising only molybdopterin and molybdenum
Molybdenum
-
0.61 atoms per subunit
Molybdenum
P47989
0.04 atoms per subunit
Molybdenum
-
in milk, more than 90% of enzyme exists in the inactive demolybdo form
Molybdenum
-
protein XdhC binds molybdenum cofactor in stoichiometric amounts, which subsequently can be inserted into molybdenum-free apoxanthine dehydrogenase. Protein XdhC is required for the stabilization of the sulfurated form of molybdenum cofactor
Molybdenum
-
-
Molybdenum
-
the enzyme is molybdo-flavoprotein, one cofactor molecule per enzyme tetramer
Molybdenum
-, Q8GUQ8
a molybdenum-iron-flavo enzyme, which contains a C-terminal molybdenum cofactor-binding domain of 85 kDa
Molybdenum
-
XOR is a molybdenum-containing enzyme, cofactor geometry, overview
Molybdenum
P22985
XOR is a molybdenum-containing enzyme, cofactor geometry, overview
molybdenum-center
-
C-terminal 85 kDa molybdopterin-binding domain
molybdenum-center
-
-
molybdenum-center
-
-
molybdenum-center
-
molybdopterin cytosine dinucleotide cofactor
molybdenum-center
-
urate, xanthine and 8-bromoxanthine interact with the molybdenum-site of fully reduced xanthine oxidase
molybdenum-center
-
substitutions G800E, G1011E, G1164R, G1266D, S1275F located within the pterin molybdenum cofactor domain
molybdenum-center
-
contains molybdopterin mononucleotide rather than molybdopterin dinucleotide
molybdenum-center
-
-
molybdenum-center
-
1.8 g-atom molybdenum per native molecule
molybdenum-center
-
-
molybdenum-center
-
-
molybdopterin
-
enzyme contains molybdopterin
Se
-
3.4 g-atom per mol enzyme
Se
-
0.13 g-atom selenium per native enzyme molecule
selenium
-
dependent on, selenium is required in a labile form
Tungsten
-
3.4 g-atom per mol of enzyme
Tungsten
-
0.12 g-atom tungsten per native enzyme molecule
Zn
-
1.54 mol Zn per mol enzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-methylhypoxanthine
-
17% inhibition of xanthine dehydrogenase at 0.25 mM
17beta-estradiol
-
inhibition of enzyme activity in malignant and non-malignant mammary epithelial cells
2,6-dihydroxanthopterin
-
competitive inhibition of pterin oxidation, Ki: 0.0084 mM
-
2-(3-cyano-4-isobutoxyphenyl)-4-methyl-5-thiazolecarboxylic acid
-
i.e. TEI-6720, mixed type inhibitor, binds very tightly to active and inactive desulfo-form of enzyme
2-amino-4-hydroxypteridine-6-carboxyaldehyde
-
competitive inhibition of 2-amino-4-hydoxy-pterine oxidation, Ki: 0.000016 mM
2-amino-4-hydroxypteridine-6-carboxyaldehyde
-
competitive inhibition of 2-amino-4-hydroxy-pterine oxidation, Ki: 0.00025 mM, non-competitive inhibition of xanthine oxidation, Ki: 0.00051 mM
2-amino-4-hydroxypterin
-
substrate inhibition above 0.01 mM
2-Iodosobenzoic acid
-
50% inhibition at 0.0025 mM of NAD+-dependent activity by enzyme inactivation, not by conversion to the O2-dependent activity
2-Iodosobenzoic acid
-
effective inhibition of xanthine and pterine oxidation
4-(5-pyridin-4-yl-1H-1,2,4-triazol-3-yl)pyridine-2-carbonitrile
-
i.e. FYX-051, strong, in absence of xanthine slow hydroxylation of inhibitor
4-(5-pyridin-4-yl-1H-[1,2,4]triazol-3-yl) pyridine-2-carbonitrile
-
i.e. FYX-051, inhibition of xanthine oxidoreductase. In vivo, the inhibitor is modified by N1- and N2-glucuronidation, mainly catalyzed by UDP-glucuronosyltransferase UGT1A9
4-Amino-2,6-dihydroxypyrimidine
-
competitive inhibition of xanthine oxidation, Ki: 0.106 mM
4-chloromercuribenzoate
-
decreases NAD+-dependent activity from 0.01 up to 0.05 mM with simultaneous inactivation of the enzyme
4-chloromercuribenzoate
-
89.2% inhibition of hypoxanthine oxidation at 1 mM
4-chloromercuriphenyl sulfonic acid
-
98% inhibition at 0.001 mM
4-hydroxymercuribenzoate
-
76% inhibition of xanthine-NAD+-activity at 0.002 mM
4-hydroxymercuribenzoate
-
effective inhibition of xanthine and pterine oxidation
4-hydroxypyrazolo(3,4-d)pyrimidine
-
95% inhibition of hypoxanthine-NADP+-activity at 1 mM; i.e. allopurinol
4-hydroxypyrazolo(3,4-d)pyrimidine
-
i.e. allopurinol; rapid inactivation under anaerobic conditions at 0.1 mM
4-hydroxypyrazolo(3,4-d)pyrimidine
-
51% inhibition of hypoxanthine oxidation at 0.0001 mM
4-hydroxypyrazolo(3,4-d)pyrimidine
-
i.e. allopurinol; inhibition by direct coordination of the reaction product alloxanthine, to the molybdenum via a nitrogen atom
4-hydroxypyrazolo(3,4-d)pyrimidine
-
i.e. allopurinol; inhibition of pterine oxidation at 0.0003 mM
5,5-dithiobis-(2-nitrobenzoate)
-
conversion of dehydrogenase type D to oxidase type O, can be prevented and reversed by dithioerythritol
5,5-dithiobis-(2-nitrobenzoate)
-
conversion of dehydrogenase type D to oxidase type O due to modification of a limited number of critical sulfhydryl groups
5,5-dithiobis-(2-nitrobenzoate)
-
conversion from of NAD+-dependent to O2-dependent activity without any effect on the total activity
5,5-dithiobis-(2-nitrobenzoate)
-
30% inhibition at 1 mM, presence of NAD+, no conversion from dehydrogenase to oxidase activity detectable
5,5-dithiobis-(2-nitrobenzoate)
-
45.4% inhibition of hypoxanthine oxidation at 1 mM
6-chloro-2-[3-(4-hydroxyphenyl)-1-phenyl-1-H-pyrazol-4-yl]-chromen-4-one
-
broad spectrum antifungal activity against Trichoderma viridae, Penicillium chrysogenum, Fusarium moniliformae, Microsporum cannis, Serratia marcescens, Staphylococcus aureus
6-chloro-2-[3-(4-hydroxyphenyl)-1-phenyl-1-H-pyrazol-4-yl]-chromen-4-one
-
noncompetitive, Ki-value 0.0011 mg/ml
6-chloro-2-[3-(4-hydroxyphenyl)-1-phenyl-1-H-pyrazol-4-yl]-chromen-4-one
-
broad spectrum antifungal activity against Trichoderma viridae, Penicillium chrysogenum, Fusarium moniliformae, Microsporum cannis, Serratia marcescens, Staphylococcus aureus
6-chloro-2-[3-(4-hydroxyphenyl)-1-phenyl-1-H-pyrazol-4-yl]-chromen-4-one
-
broad spectrum antifungal activity against Trichoderma viridae, Penicillium chrysogenum, Fusarium moniliformae, Micrnosporum cannis, Serratia marcescens, Staphylococcus aureus
6-chloro-2-[3-(4-hydroxyphenyl)-1-phenyl-1-H-pyrazol-4-yl]-chromen-4-one
-
broad spectrum antifungal activity against Trichoderma viridae, Penicillium chrysogenum, Fusarium moniliformae, Microsporum cannis, Serratia marcescens, Staphylococcus aureus
6-chloro-7-methyl-2-[3-(4-chlorophenyl)-1-phenyl-1-H-pyrazol-4-yl]-chromen-4-one
-
broad spectrum antifungal activity against Trichoderma viridae, Penicillium chrysogenum, Fusarium moniliformae, Microsporum cannis, Serratia marcescens, Staphylococcus aureus
6-chloro-7-methyl-2-[3-(4-chlorophenyl)-1-phenyl-1-H-pyrazol-4-yl]-chromen-4-one
-
competitive, Ki-value 0.00022 mg/ml
6-chloro-7-methyl-2-[3-(4-chlorophenyl)-1-phenyl-1-H-pyrazol-4-yl]-chromen-4-one
-
broad spectrum antifungal activity against Trichoderma viridae, Penicillium chrysogenum, Fusarium moniliformae, Microsporum cannis, Serratia marcescens, Staphylococcus aureus
6-Mercaptopurine
-
90% inhibition of hypoxanthine-NADP+-activity at 1 mM
8-Azaadenine
-
competitive inhibition of xanthine oxidation, Ki: 0.25 mM
8-Azaadenine
-
complete inhibition of xanthine dehydrogenase at 0.2 mM
8-Azaguanine
-
competitive inhibition of 2-amino-4-hydroxypterine oxidation, Ki: 0.0012 mM
8-Azaguanine
-
competitive inhibition of xanthine oxidation, Ki: 0.037 mM, non-competitive inhibition of 2-amino-4-hydroxy-pterine oxidation, Ki: 0.071 mM
8-Azaguanine
-
complete inhibition of xanthine dehydrogenase at 0.2 mM
8-Azaxanthine
-
50% inhibition of ferricyanide reduction in xanthine oxidation assay at 5 mM
8-azohypoxanthine
-
40% inhibition of xanthine dehydrogenase at 0.25 mM
acetaldehyde
-
inactivation
adenine
-
96% inhibition of hypoxanthine-NADP+-activity at 1 mM
adenine
-
some non-competitive inhibition
adenine
-
competitive inhibition of xanthine oxidation, Ki: 0.13 mM
adenine
-
effective inhibition of xanthine oxidation at 0.001 mM
adenine
-
competitive inhibition, Ki: 0.05 mM
adenine
-
62.8% inhibition of hypoxanthine oxidation at 0.5 mM
adenine
-
treatment of normal fruit in linear phase of growth arrests fruit growth
adenine
-
0.1 mM, 21% residual activity
adenine
-
presence of adenine in liver extracts causes a 45-60% decrease in xanthine oxidase and in xanthine oxidase plus xanthine dehydrogenase activities, removal by dialysis results in recovery of both activities to almost pre-treatment levels
Ag2+
-
complete inhibition of hypoxanthine oxidation at 0.01 mM
allopurinol
-
treatment of normal fruit in linear phase of growth arrests fruit growth
allopurinol
-, Q8GUQ8
strong
allopurinol
-
0.1 mM, complete inhibition
allopurinol
-
blocks xanthine dehydrogenase activity, without influencing xanthine oxidase activity
allopurinol
-
inhibition of xanthine oxidoreductase also suppresses high tidal volume mechanical ventilation-induced alveolar apoptosis
allopurinol
-
mechanism-based inhibitor. Allopurinol is oxidized by xanthine oxidoreductase itself to oxypurinol which forms a covalent bond with the reduced molybdenium atom
allopurinol
-
inhibits xanthine and hypoxanthine oxidation in vivo in intestine and pancreas, but enhances the activity in liver, tissue-dependent effects, overview
allopurinol
O54050
i.e. 1-H-pyrazolo [3,4-d] pyrimidine-4-one
allopurinol
-
shows strong enzyme inhibition and hypouricemic effect
allopurinol
-, Q8GUQ8
-
alloxanthine
-
a mechanism-based inhibitor, binding structure, overview. Inhibition mechanism involves binding to molybdenum, overview
amflutizole
-
blocks xanthine dehydrogenase activity, without influencing xanthine oxidase activity
Ammeline
-
competitive inhibition of xanthine oxidation Ki: 0.083 mM, uncompetitive inhibition of NADH oxidation Ki: 0.063 mM
Ammeline
-
competitive inhibition of 2-amino-4-hydroxy-pterine oxidation, Ki: 0.016 mM
Ammeline
-
competitive inhibition of xanthine oxidation, Ki: 0.021 mM, non-competitive inhibition of 2-amino-4-hydoxypterine oxidation, Ki: 0.045 mM
ammonium acetate
-
inhibits the enzyme in vivo after injection into the brain, blocked by MK-801, which alone does not affect the enzyme activity itself
arsenite
-
50% inhibition of hypoxanthine-NADP+-activity at 1 mM
arsenite
-
gradual inhibition of xanthine-2,6-dichloroindophenol-activity, paralleled by a corresponding increase of NADH-2,6-dichloroindophenol-activity
arsenite
-
90% loss of the ferricyanide-linked activity in the presence of 1.78 mM
arsenite
-
inhibition of xanthine or pterine oxidation at 0.3 mM, diaphorase activity unaffected
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
Cu2+
-
14% inhibition of hypoxanthine oxidation at 0.1 mM
CuSO4
-
conversion of the dehydrogenase type D to oxidase type O, prolonged incubation leads to complete inactivation, conversion can be reversed and prevented by dithioerythritol
diethyl dicarbonate
-
90% loss of NAD+ dependent activity at 1 mM, retains more than 90% of oxygen-dependent and 3-acetylpyridine adenine dinucleotide+-dependent NADH oxidation activity
diethyldithiocarbamate
-
72% inhibition of xanthine-NAD+-activity at 10 mM
diphenylene iodonium
-
powerful inhibition of NADH oxidation
EDTA
-
19.8% inhibition of hypoxanthine oxidation at 10 mM
febuxostat
-
structure-based inhibitor, forms numerous hydrogen bonds, slat bridges, and hydrophobic interactions with amino acids in the active site and nearly completely fills the narrow channel leading to the molydbenum center of the enzyme
FYX-051
-
inhibitor has features of both a mechanism-based and a structure-based inhibitor. It is a slow substrate and forms a stable reaction intermediate with the molybdenum atom in the enzyme
FYX-051
-
i.e. 4-(5-pyridin-4-yl-1H-[1, 2, 4]triazol-3-yl)pyridine-2-carbonitrile, a xanthine oxidoreductase inhibitor, that causes xanthine-mediated nephropathy inrats, but not in monkeys, toxicity study, overview
GSH
-
45% of the oxidase activity converted to dehydrogenase activity at 10 mM
GSSG
-
75% of the dehydrogenase activity converted to oxidase activity at 0.5 mM
Guanidine-HCl
-
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant. Above 3 M gunandine-HCl, even xanthine oxidase activity decreases drastically, but the xanthine oxidase form treated with 1.5 M can be completely reconverted into xanthine dehydrogenase by dialysis
Guanidine-HCl
-
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant
Guanine
-
some inhibition
Guanine
-
effective inhibition of xanthine oxidation at 0.001 mM
hesperetin
-
i.e. 3',5,7-trihydroxy-4'-methoxyflavanone, major flavanone component of orange juice, inhibits hepatic XDH activity and decreases serum uric acid levels, exhibits antioxidative and antihyperuricemic properties
Hg2+
-
complete inhibition of hypoxanthine oxidation at 0.1 mM
hypoxanthine
-
inactivation of xanthine oxidase activity, not in the presence of NAD+
iodoacetic acid
-
21% inhibition at 1 mM
KCN
-
addition of selenide in the presence of dithionite reactivates the inhibited enzyme
KCN
-
cyanolyzable selenium, 75% inhibition at 15 mM
KCN
-
complete inhibition of xanthine dehydrogenase activity, 70% reduction of diaphorase activity
KCN
-
irreversible inactivation
KCN
-
63% inhibition at 1 mM
KCN
-
complete inactivation of oxygen-linked activity in 15 min, decline of NAD+-linked activity in 75 min, ferricyanide-linked activity completely stable
KCN
-
10-50% inhibition of xanthine oxidation only in the presence of Tris or phosphate buffers from 0.01 to 0.1 M inhibitor concentration
KCN
-
35% inhibition of pterine oxidation, 60% inhibition of diaphorase activity at 5 mM
KCN
-
complete inhibition of hypoxanthine oxidation at 1 mM
KCN
-
37% inhibition at 1 mM
Leucopterin
-
competitive inhibition of xanthopterin oxidation, Ki: 0.0109 mM
methanol
-
slight inhibition of NAD+ reduction at 1.5 M, rapid inactivation if NAD+ is replaced by 2,6-dichloroindophenol, enhanced NADH diaphorase activity
methanol
-
50% inhibition in 3 min at 1.5 M
N-ethylmaleimide
-
conversion of dehydrogenase type D to oxidase type O, prevented by dithioerythritol but no reversible conversion
N6-furfuryladenine
-
0.1 mM, 59% residual activity
NaCN
-
69% inhibition of xanthine-NAD+-activity at 3.3 mM
NAD+
-
competitive inhibition of NADH oxidation, Ki: 0.0143 mM
NADH
-
partial reduction of dehydrogenase activity under anaeroboic conditions, oxidase activity more slowly reduced
NADH
-
inactivation closely related to associated diaphorase activity
NADH
-
accumulation of produced NADH inhibits activity to 50%
NADH
-
product inhibition
NADH
-
varied substrate: xanthine, product inhibition, Ki 0.05 mM, varied substrate: NAD+, dead-end inhibition type, Ki 0.022 mM
NADH
-, Q8GUQ8
suppresses NAD+-dependent xanthine oxidation
NADPH
-
inactivation closely related to diaphorase activity
NaN3
-
slight inhibition of dehydrogenase activity
NO
-
dose-dependent inhibition of xanthine dehydrogenase and oxidase activity, reaction with an essential sulfur in the molybdenum center, that damages the molybdopterin
o-phenanthroline
-
12% inhibition of xanthine-NAD+-activity at 7.5 mM
o-phenanthroline
-
50% inhibition at 5-15 mM
o-phenanthroline
-
19.5% inhibition of hypoxanthine oxidation at 10 mM
Oxipurinol
-
crystal structure of reduced enzyme in complex with oxipurinol at 2.0 A resolution. Electron density is observed between the N2 nitrogen atom of oxipurinol and the molybdenum atom of the molybdopterin cofactor. Oxipurinol forms hydrogen bonds with residues E802, R880, and E1261
oxypurinol
-
blocks xanthine dehydrogenase activity, without influencing xanthine oxidase activity
oxypurinol
O54050
-
oxypurinol
-
complete inhibition at 0.004 mM
p-hydroxymercuribenzoate
-, Q8GUQ8
strong
potassium cyanide
-, Q8GUQ8
strong
pterin-6-aldehyde
O54050
competitive inhibition pattern, mechanism of inhibitor binding at the active site, overview
purine
-
some inhibition
pyridoxal
-
Ki for 2-amino-4-hydroxypterine oxidation: 0.08 mM at 30 and 50C, competitive; Ki for xanthine oxidation: 0.05 mM at 30C, 0.11 mM at 50C, competitive
Quinacrine
-
29.7% inhibition of hypoxanthine oxidation at 1 mM
Salicylhydroxamic acid
-
71% inhibition of xanthine-NAD+-activity at 5 mM
Salicylhydroxamic acid
-
82% inhibition of hypoxanthine oxidation at 2.5 mM
Sodium dithionite
-
reduction of enzyme
Sodium dithionite
-
reduction of enzyme
Sodium dithionite
-
irreversible inactivation by reduction of xanthine dehydrogenase, no recovery after dithionite elimination
Superoxide dismutase
-
complete inhibition of the xanthine-cytochrome c activity for oxidase type O, lesser inhibition for dehydrogenase type D
-
tetraethyldithiodicarbonic diamide
-
i.e. disulfiram; transformation of the NAD+- to the O2-dependent activity up to 0.025 mM, up to 80% loss of NAD+-dependent activity, modification of one thiol group in the active centre, NAD+ protects against modification due to a single thiol group involved in NAD+-binding within the active centre
Tetraethylthiuram disulfide
-
conversion of dehydrogenase type D to oxidase type O, can be prevented and reversed by dithioerythritol
Thiourea
-
65% inhibition of xanthine dehydrogenase activity at 20 mM
Tiron
-
36.8% inhibition of hypoxanthine oxidation at 10 mM
Urate
-
15% inhibition of xanthine-NAD+-activity
Urate
-
50% inhibition of xanthine oxidation at 0.5 mM
Urate
-
inhibition of xanthine oxidation at 0.06 mM
Urate
-
competitive inhibition of xanthine oxidation, Ki: 0.064 mM
Urate
-
competitive inhibition of xanthine dehydrogenase, Ki: 0.144 mM
Urate
-
varied substrate: xanthine, dead-end inhibition type, Ki 0.18 mM, varied substrate: NAD+, product inhibition, Ki 0.45 mM
Urate
-
36.6% inhibition of hypoxanthine oxidation at 0.5 mM
Urea
-
competitive inhibition of xanthine oxidation Ki: 0.28 M, uncompetitive inhibition of NADH oxidation Ki: 1 M
Urea
-
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant
xanthine
-
reduction of enzyme
xanthine
-
irreversible inactivation by reduction of xanthine dehydrogenase; irreversible inhibition of xanthine oxidase activity, adenine and 8-azaadenine protects against inactivation, ferricyanide partially protects against inactivation, no inactivation in the presence of NAD+
xanthine
-
substrate inhibition above 0.05 mM, but in the presence of NAD+
xanthine
-
substrate inhibition above 0.13 mM
xanthine
-
40% inhibition of xanthine dehydrogenase at 0.25 mM
methanol
-
develops inhibition during course of catalysis, enhanced inhibition in the presence of ferricyanide in the oxygen-dependent oxidation of xanthine
additional information
-
no substrate inhibition
-
additional information
-
orange juice inhibits hepatic XDH activity and decreases serum uric acid levels and exhibits antioxidative and antihyperuricemic properties
-
additional information
-
hypouricemic effects of fresh onion juice and of allopurinol on serum uric acid levels in healthy and hypeuricemic rats, overview
-
additional information
-, Q8GUQ8
NAD+ inhibits NADH-dependent superoxide formation of AtXDH1
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4,4'-dithiodipyridine
-
reverses conversion of dehydrogenase to oxidase form
4-chloromercuribenzoate
-
increases total activity up to 0.005 mM
allopurinol
-
inhibits xanthine and hypoxanthine oxidation in vivo in intestine and pancreas, but enhances the activity in liver, tissue-dependent effects, overview
cellular retinol binding protein
-
CRBP and CRABP, strictly dependent on
-
dithioerythritol
-
recovery from oxidase to dehydrogenase type
DTT
-
recovery from oxidase to dehydrogenase type
DTT
-
recovery from oxidase to dehydrogenase type
Ferredoxin
-
26fold increase of cytochrome c reduction, 2fold increase of oxygen reduction
-
KCl
-
strong activation at 50 mM
NaCl
-
nearly 2fold activation at 100 mM
NAD+
-
6fold stimulation of aerobic rate of oxidation of xanthine
NH4Cl
-
2.5fold activation at 100 mM
PD98059
-
inhibitor used to block MEK-1/2 kinase, activates the promoter of xanthine oxidoreductase and significantly enhances expression of enzyme induced by insulin, acute phase cytokines, or growth factors
sodium nitroprusside
-
i.e. SNP, a NO donor, activates at concentrations of up to 3 mM, preventable by hemoglobin, overview
sulfide/dithionite
-, Q8GUQ8
treatment increases the specific activity of AtXDH1
-
thiol active compounds
-
reversible conversion of xanthine dehydrogenase to xanthine oxidase by modification of C535 and C992 and formation of a disulfide bond, that induces a conformational change
-
thiol active compounds
-
conversion of oxidase to dehydrogenase form
-
Urate
-
30% activation of hypoxanthine-NAD+ activity
methylene blue
-
6fold activation of aerobic rate of oxidation of xanthine
additional information
-
activation mechanism based on the results of mutations at the positions of the second Glu and Arg residues, overview
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.021
-
2,6-dichloroindophenol
-
diaphorase activity
0.001
-
2-amino-4-hydroxypterin
-
-
0.0035
-
2-amino-4-hydroxypterin
-
-
0.004
-
2-amino-4-hydroxypterin
-
pH 7.0, electron acceptor: methylene blue
0.0061
-
2-amino-4-hydroxypterin
-
body preparation, cosubstrate: NAD+
0.0071
-
2-amino-4-hydroxypterin
-
pH 8.0, electron acceptor: methylene blue
0.0072
-
2-amino-4-hydroxypterin
-
wing preparation, co substrate: NAD+
0.011
-
2-amino-4-hydroxypterin
-
increased Km in the presence of pyridoxal
0.102
-
3-acetylpyridine adenine dinucleotide+
-
NADH oxidation
0.021
-
3-acetylpyridine-adenine dinucleotide
-
xanthine oxidation
0.0258
-
4-hydroxypyrazolo(3,4-d)pyrimidine
-
cosubstrate: NAD+
1
-
4-hydroxypyrazolo(3,4-d)pyrimidine
-
electron acceptor: 2,6-dichlorophenolindophenol; i.e. allopurinol
0.0071
-
adenine
-
cosubstrate: NAD+
0.0809
-
DCPIP
-
pH 7.8, 25C, mutants Q102A and Q102G
0.0823
-
DCPIP
-
pH 7.8, 25C, wild-type enzyme
0.0041
-
hypoxanthine
-
electron acceptor: NAD+
0.0075
-
hypoxanthine
-
electron acceptor: nitroblue tetrazolium
0.0088
-
hypoxanthine
-
wild-type, pH 8.5, 25C
0.018
-
hypoxanthine
-
pH 8.5
0.02
-
hypoxanthine
-
cosubstrate: NAD+
0.021
-
hypoxanthine
-
xanthine dehydrogenase activity
0.04
-
hypoxanthine
-
-
0.0451
-
hypoxanthine
-
co substrate: NAD+
0.047
0.079
hypoxanthine
-
measured in the pH range from 6 to 8.9, pH-independent Km
0.0525
-
hypoxanthine
-
-
0.055
-
hypoxanthine
-
-
0.072
-
hypoxanthine
-
mutant R881M, pH 8.5, 25C
0.21
-
hypoxanthine
-
electron acceptor: NADP+
0.29
-
hypoxanthine
-
cosubstrate: NAD+
0.5
-
hypoxanthine
-
electron acceptor: 2,6-dichlorophenolindophenol
0.44
-
methyl viologen
-
electron donor: xanthine
0.00219
-
NAD+
-
pH 7.2, 25C
0.0022
-
NAD+
-
oxidation of 2-amino-4-hydroxy-pterin
0.00252
-
NAD+
-
pH 7.2, 25C
0.00274
-
NAD+
-
pH 7.2, 25C
0.0033
-
NAD+
-
electron donor: 2-amino-4-hydroxypterine
0.00412
-
NAD+
-
pH 7.2, 25C
0.006
-
NAD+
-
electron donor: pterin
0.0067
-
NAD+
-
electron donor: xanthine
0.0125
-
NAD+
-
xanthine oxidation at pH 7.5
0.019
-
NAD+
-
pH 7.9, pH dependence, increasing Km with increasing pH
0.02
-
NAD+
-
at pH 7.5, hypoxanthine oxidation
0.025
-
NAD+
-
electron donor: xanthine
0.025
-
NAD+
-
cosubstrate: hypoxanthine
0.025
-
NAD+
-
pH 8.5
0.028
-
NAD+
-
xanthine dehydrogenase activity
0.0328
-
NAD+
-
pH 7.8, 25C, wild-type enzyme
0.033
-
NAD+
-
increased Km for mutant G353D, electron acceptor: pterin
0.0373
-
NAD+
-
pH 7.8, 25C, mutant Q102G
0.04
-
NAD+
-
ping-pong reaction mechanism
0.0402
-
NAD+
-
pH 7.8, 25C, mutant Q102A
0.054
-
NAD+
-
immobilized enzyme preparation, pH 7.9, pH dependence, minimum Km at pH 8.1, increasing values below and above
0.1
-
NAD+
Q8RLC0, Q8RLC1
coexpression of genes xdhABC, conditions of high aeration, pH 7.8, 25C; coexpression of genes xdhABC, conditions of high aeration, pH 7.8, 25C
0.103
-
NAD+
-
wild-type, pH 7.8, 25C
0.1065
-
NAD+
-
cosubstrate: hypoxanthine
0.113
-
NAD+
Q8RLC0, Q8RLC1
coexpression of genes xdhABC, conditions of low aeration, pH 7.8, 25C; coexpression of genes xdhABC, conditions of low aeration, pH 7.8, 25C
0.12
-
NAD+
-
cosubstrate: xanthine
0.124
-
NAD+
-
cosubstrate: xanthine
0.148
-
NAD+
Q8RLC0, Q8RLC1
coexpression of genes xdhAB, conditions of high aeration, pH 7.8, 25C; coexpression of genes xdhAB, conditions of high aeration, pH 7.8, 25C
0.156
-
NAD+
Q8RLC0, Q8RLC1
coexpression of genes xdhAB, conditions of low aeration, pH 7.8, 25C; coexpression of genes xdhAB, conditions of low aeration, pH 7.8, 25C
0.16
-
NAD+
-
cosubstrate: hypoxanthine
0.16
-
NAD+
-
electron donor: xanthine
0.171
-
NAD+
-
electron donor: xanthine
0.0057
-
NADH
-
electron acceptor: nitroblue tetrazolium
0.0063
-
NADH
-
at pH 7.0, Tris-maleate buffer
0.009
-
NADH
-
electron acceptor: 2,6-dichlorophenolindophenol
0.011
-
NADH
-
at pH 8.0, Tris-maleate buffer
0.048
-
NADH
-
increased Km for mutant G353D, electron acceptor: 2,6-dichlorophenolindophenol
6
-
NADH
-
diaphorase activity
0.038
-
NADP+
-
electron donor: hypoxanthine
0.0113
-
Nitroblue tetrazolium
-
electron donor: xanthine
0.0056
-
phenazine methosulfate
-
electron donor: xanthine
0.0182
-
purine
-
cosubstrate: NAD+
0.02
-
thio-NAD+
-
cosubstrate: hypoxanthine
0.0003
-
xanthine
-
electron acceptor: NAD+
0.0017
-
xanthine
-
dehydrogenase type D, absence of NAD+
0.002
-
xanthine
-
oxidase type O, absence of NAD+
0.00215
-
xanthine
-
pH 7.2, 25C
0.0026
-
xanthine
-
cosubstrate NAD+
0.0045
-
xanthine
-
electron acceptor: 2,6-dichlorophenolindophenol
0.005
-
xanthine
-
at pH 7.5, ping-pong-reaction mechanism, strongly pH-dependent
0.00633
-
xanthine
-
pH 7.2, 25C
0.00714
-
xanthine
-
pH 7.2, 25C
0.00774
-
xanthine
-
pH 7.2, 25C
0.0082
-
xanthine
-
electron acceptor: NAD+
0.0082
-
xanthine
-
xanthine dehydrogenase activity
0.0086
-
xanthine
-
electron acceptor: nitroblue tetrazolium
0.0088
-
xanthine
-
wild-type, pH 8.5, 25C
0.012
-
xanthine
-
electron acceptor: oxygen
0.017
-
xanthine
-
electron acceptor: ferricyanide
0.017
-
xanthine
-
pH 7.9, increasing Km with increasing pH
0.017
-
xanthine
-
pH 8.5
0.018
-
xanthine
-
electron acceptor: NAD+, 30C
0.0227
-
xanthine
-
pH 7.8, 25C, mutant Q102G, with NAD+
0.0236
-
xanthine
-
cosubstrate: NAD+
0.024
-
xanthine
-
ping-pong reaction mechanism
0.029
-
xanthine
-
electron acceptors: phenazine methosulfate/cytochrome c
0.0293
-
xanthine
-
pH 7.8, 25C, mutant Q102A, with NAD+
0.032
-
xanthine
-
electron acceptor: NAD+
0.0325
-
xanthine
-
-
0.035
-
xanthine
-
immobilized enzyme preparation, pH 7.9, pH dependence, minimum Km at pH 8.1, increasing values below and above
0.036
-
xanthine
-
increased Km in the presence of pyridoxal at 30C
0.04
-
xanthine
-
electron acceptor: NAD+, 50C
0.0442
-
xanthine
-
pH 7.8, 25C, wild-type enzyme, with NAD+
0.059
-
xanthine
-
increased Km in the presence of pyridoxal at 50C
0.061
-
xanthine
-
wing preparation, cosubstrate: NAD+
0.064
-
xanthine
-
-
0.064
-
xanthine
-
wild-type, pH 7.8, 25C
0.0647
-
xanthine
-
body preparation, cosubstrate: NAD+
0.066
-
xanthine
-
electron acceptor: NAD+
0.066
-
xanthine
Q8RLC0, Q8RLC1
coexpression of genes xdhAB, conditions of high aeration, pH 7.8, 25C; coexpression of genes xdhAB, conditions of high aeration, pH 7.8, 25C
0.067
-
xanthine
-
electron acceptor: NADP+
0.067
-
xanthine
Q8RLC0, Q8RLC1
coexpression of genes xdhAB, conditions of low aeration, pH 7.8, 25C; coexpression of genes xdhAB, conditions of low aeration, pH 7.8, 25C
0.07
-
xanthine
-
cosubstrate; NAD+
0.072
-
xanthine
-
mutant E803V, pH 8.5, 25C
0.085
-
xanthine
Q8RLC0, Q8RLC1
coexpression of genes xdhABC, conditions of high aeration, pH 7.8, 25C; coexpression of genes xdhABC, conditions of high aeration, pH 7.8, 25C
0.163
-
xanthine
-
mutant E232A, pH 7.8, 25C
1.35
-
xanthine
-
electron acceptor: methyl viologen
80.09
-
xanthine
Q8RLC0, Q8RLC1
coexpression of genes xdhABC, conditions of low aeration, pH 7.8, 25C; coexpression of genes xdhABC, conditions of low aeration, pH 7.8, 25C
0.0018
-
Xanthopterin
-
cosubstrate: NAD+
0.00083
-
methylene blue
-
electron donor: 2-amino-4-hydroxy-pterine
additional information
-
additional information
-
rapid reaction kinetic parameters for substrates xanthine, 2-thioxanthine, 6-thioxanthine, 1-methylxanthine, 2-hydroxy-6-methylpurine, and 2,6-diaminopurine, in wild-type and mutants R310K and R310M
-
additional information
-
additional information
-
Km-value is 0.0025 mg/ml xanthine
-
additional information
-
additional information
-
2-position hydroxylation is crucial for 8-position hydroxylation. Stopped-flow studies indicate that the rate-limiting step of the reductive half-reaction is not electron transfer from the xanthine substrate to the molybdenum center, but product release
-
additional information
-
additional information
-
kinetics in presence and absence of cellular retinol binding proteins, apo-CRBP and apo-CRABP, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.717
-
cytochrome c
-
cosubstrate xanthine
5.67
-
dichloroindophenol
-
cosubstrate xanthine
20.2
-
Ferredoxin
-
cosubstrate xanthine
-
18.2
-
ferricyanide
-
cosubstrate xanthine
0.33
-
hypoxanthine
-
mutant R881M, pH 8.5, 25C
0.75
-
hypoxanthine
-
electron acceptor: oxygen
30
-
hypoxanthine
-
wild-type, pH 8.5, 25C
17.1
-
NADH
-
activation of mutant G1011E activity after preincubation with phenazine methosulfate and cytochrome c, electron acceptor: methylene blue
29
-
NADH
-
activation of mutant G1011E activity after preincubation with ferricyanide, electron acceptor: methylene blue
9.55
-
Nitro blue tetrazolium
-
cosubstrate xanthine
0.8
-
oxygen
-
cosubstrate xanthine
0.7
-
purine
-
electron acceptor: oxygen
0.1
-
Salicylaldehyde
-
electron acceptor: oxygen
0.4
-
xanthine
Q8RLC0, Q8RLC1
coexpression of genes xdhAB, conditions of low aeration, pH 7.8, 25C; coexpression of genes xdhAB, conditions of low aeration, pH 7.8, 25C
0.99
-
xanthine
-
wild-type, pH 8.5, 25C
1.35
-
xanthine
-
mutant E803V, pH 8.5, 25C
2.5
-
xanthine
-
electron acceptor: oxygen
4.4
-
xanthine
-
mutant E232A, pH 7.8, 25C
6.33
-
xanthine
-
electron acceptor: NAD+
12.2
-
xanthine
-
electron acceptor: NAD+
15
-
xanthine
-
electron acceptor: oxygen
18.33
-
xanthine
-
wild-type, pH 8.5, 25C
22.8
-
xanthine
-
mutant E89K, electron acceptor: NAD+
24.9
-
xanthine
-
electron acceptor: NAD+
27
-
xanthine
Q8RLC0, Q8RLC1
coexpression of genes xdhAB, conditions of high aeration, pH 7.8, 25C; coexpression of genes xdhAB, conditions of high aeration, pH 7.8, 25C
31
-
xanthine
-
recombinant enzyme, electron acceptor: phenazine methosulfate-cytochrome c
31.6
-
xanthine
-
pH 7.8, 25C, mutant Q102G, with DCIP
34.3
-
xanthine
-
pH 7.8, 25C, mutant Q102A, with DCIP
39.5
-
xanthine
-
pH 7.8, 25C, mutant Q102A, with NAD+
40.6
-
xanthine
-
pH 7.8, 25C, mutant Q102G, with NAD+
66.1
-
xanthine
-
pH 7.8, 25C, wild-type enzyme, with DCIP
77.5
-
xanthine
-
pH 7.8, 25C, wild-type enzyme, with NAD+
86
-
xanthine
Q8RLC0, Q8RLC1
coexpression of genes xdhABC, conditions of low aeration, pH 7.8, 25C; coexpression of genes xdhABC, conditions of low aeration, pH 7.8, 25C
108
-
xanthine
-
wild-type, pH 7.8, 25C
118
-
xanthine
Q8RLC0, Q8RLC1
coexpression of genes xdhABC, conditions of high aeration, pH 7.8, 25C; coexpression of genes xdhABC, conditions of high aeration, pH 7.8, 25C
120
-
xanthine
-
electron acceptor: NAD+
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.001
-
oxypurinol
O54050
-
0.1036
-
pterin-6-aldehyde
O54050
pH 7.5, 25C
additional information
-
additional information
-
6-chloro-2-[3-(4-hydroxyphenyl)-1-phenyl-1-H-pyrazol-4-yl]-chromen-4-one, Ki-value 0.0011 mg/ml, 6-chloro-7-methyl-2-[3-(4-chlorophenyl)-1-phenyl-1-H-pyrazol-4-yl]-chromen-4-one, Ki-value 0.00022 mg/ml, respectively
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0011
-
-
substrate pterin, 22C, pH 8.3
0.013
-
-
substrate xanthine, 22C, pH 8.3
0.044
-
-, Q8GUQ8
purified recombinant enzyme, substrate xanthine, pH 8.0
0.06
-
-
substrate xanthine, pH 7.2, 25C
0.16
-
-
xanthine oxidase activity
0.21
-
-
substrate NAD+, pH 7.2, 25C
0.23
-
-
xanthine-NAD+ assay
0.25
-
-
substrate NAD+, pH 7.2, 25C
0.27
-
-
substrate NAD+, pH 7.2, 25C; substrate xanthine, pH 7.2, 25C
0.29
-
-
substrate NAD+, pH 7.2, 25C
0.65
-
-, Q8GUQ8
purified recombinant enzyme, pH 8.0, 25C
0.69
-
-
substrate xanthine, pH 7.2, 25C
0.702
-
-, Q8GUQ8
purified recombinant enzyme, substrate NADH, pH 6.6
0.9
-
-
crude extract
1.17
-
-
pH 8.5
1.56
-
-
xanthine dehydrogenase activity
1.712
-
-, Q8GUQ8
purified recombinant enzyme, in presence of sulfide/dithionite
1.83
-
-
substrate xanthine, pH 7.2, 25C
2.4
-
-
-
2.47
-
-
-
2.6
-
-
xanthine-2,6-dichlorophenolindophenol assay
2.8
-
-
highest activity if growth medium contains urate and is supplemented with 0.0001 mM selenite and 0.0001 mM tungstate
3.7
-
-
highest activity if growth medium contains urate and is supplemented with 0.0001 mM selenite and 0.0001 mM molybdate
6.58
-
-
pH 7.8, 25C, expression of xdhAB genes
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
26.7
-
-
hypoxanthine-NAD+ assay
29.5
-
-
kidney enzyme with allopurinol at 50 mg/kg body weight
35.2
-
-
after 39.1fold purification
49.9
-
-
kidney enzyme
72.56
-
-
xanthine-ferricyanide assay
80
-
-
pH 7.8, 25C, expression of xdhABC genes
163
-
-
ferricyanide-linked activity
164
-
-
hypoxanthine-NADP+-assay
additional information
-
-
enzymic activity is only detectable after resulfuration of purified enzyme
additional information
-
-
tissue-dependent enzyme activity, overview
additional information
-
-
serum uric acid levels in healthy and hypeuricemic rats, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
xanthine oxidation, presence of oxygen, two pH-optima
6.6
-
-, Q8GUQ8
substrate NADH
7
-
-
optimum value in the reverse reaction with urate and reduced methyl viologen
7.4
-
-
assay at
7.4
-
-
assay at
7.5
7.8
-
assay at
7.5
-
O54050
assay at
7.8
-
-
at 30C
7.8
-
-
assay at
8
8.6
-
xanthine-NAD+, NADH-nitroblue tetrazolium or xanthine-nitroblue tetrazolium assay
8
-
-, Q8GUQ8
assay at; substrate xanthine
8.2
-
-
-
8.5
-
-
optimum value for oxidation of xanthine and reduction of methyl viologen
8.5
-
-
-
9.5
-
-
xanthine oxidation, presence of oxygen, two pH-optima
9.8
-
-
second optimum for NADH-nitroblue tetrazolium assay
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9.2
-
trends to increasing activities at higher values
6.6
8
-, Q8GUQ8
-
7.2
8.7
-
-
8
8.5
-, Q8GUQ8
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
25
-
O54050
assay at
25
-
-, Q8GUQ8
assay at; assay at
37
-
-
highest activity, but unstable
37
-
-
assay at
37
-
-
assay at
41
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
41
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.3
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
mRNA expression increases 8-fold during the first 12 hr postinduction and subsequently declines to preinduction levels by day 3. Xanthine dehydrogenase activity is maximally induced at 24 hr postinduction, while xanthine oxidase activity remains relatively unchanged
Manually annotated by BRENDA team
-
xanthine oxidoreductase is activated in a p38 MAP kinase-dependent manner following high tidal volume mechanical ventilation and is involved in resulting increased alveolar cell apoptosis
Manually annotated by BRENDA team
-
low enzyme activity
Manually annotated by BRENDA team
-
inducible by hypoxanthine
Manually annotated by BRENDA team
-
inducible by xanthine, selenite and molybdate
Manually annotated by BRENDA team
-
inducible by xanthine, hypoxanthine or adenine
Manually annotated by BRENDA team
-
inducible by xanthine
Manually annotated by BRENDA team
-
alveolar type II cells
Manually annotated by BRENDA team
-
selenium is needed for xanthine dehydrogenase formation
Manually annotated by BRENDA team
-
0.0025 mg/ml sodium tungstate in the growth medium reduces level of ferricyanide-linked enzyme to 3%
Manually annotated by BRENDA team
-
inducible by urate, selenite and tungstate
Manually annotated by BRENDA team
-
inducible by urate, selenite and molybdate
Manually annotated by BRENDA team
Pseudomonas putida 40
-
-
-
Manually annotated by BRENDA team
Pseudomonas putida 86
-
inducible by hypoxanthine
-
Manually annotated by BRENDA team
-
high rate of dehydrogenase activity
Manually annotated by BRENDA team
-
high rate of dehydrogenase activity
Manually annotated by BRENDA team
-
lung epithelial cell
Manually annotated by BRENDA team
-
mammary epithelial cell line
Manually annotated by BRENDA team
-
enzyme activity is maximal in late linear phase of fruit growth
Manually annotated by BRENDA team
-
high rate of dehydrogenase activity
Manually annotated by BRENDA team
-
only oxidase type O form
Manually annotated by BRENDA team
-
low enzyme activity
Manually annotated by BRENDA team
-
exists preliminary as oxidase form, promotes oxidative incorporation of iron into mucosal transferrin, facilitates dietary iron absorption
Manually annotated by BRENDA team
-
only oxidase type O form, can be converted to dehydrogenase type D by dithioerythritol
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
only oxidase type O form
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
analysis of an aba1 gene deficient mutant
Manually annotated by BRENDA team
-, Q8GUQ8
cold stress causes decrease, desiccation and senesence cause strong increase in activity
Manually annotated by BRENDA team
B3FYT9
in leaf peroxisomes, the superoxide-generating form, xanthine oxidase XOD is predominant over the xanthine dehydrogenase form XDH, with a XDH/XOD ratio of 0.5. In crude extracts of pea leaves, the XDH form is more abundant, with a XDH/XOD ratio of 1.6
Manually annotated by BRENDA team
-
high oxidase and reductase activities at nearly the same rates
Manually annotated by BRENDA team
-
dehydrogenase and oxidase forms
Manually annotated by BRENDA team
-
exists preliminary as dehydrogenase form, participates in mobilization of iron from ferritin stores
Manually annotated by BRENDA team
-
isolated cells of liver
Manually annotated by BRENDA team
-
the dehydrogenase form of liver xanthine oxidoreduxtase is intrinsically more efficient at generating superoxide anion radicals than the oxidase form, independently of the reducing substrat
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
only oxidase type O form
Manually annotated by BRENDA team
-
lung xanthine oxidoreductase activity is significantly increased after 2 h of mechanical ventilation without changes in enzyme expression. Increase occurs via activation of p38 MAP kinase and ERK and plays a critical role in the pathogenesis of pulmonary edema associated with ventilator-induced lung injury
Manually annotated by BRENDA team
-
low enzyme activity
Manually annotated by BRENDA team
-
constitutive expression and high activity of XDH in non-malignant cells
Manually annotated by BRENDA team
-
high level of xanthine oxidoreductase
Manually annotated by BRENDA team
-
low XDH expression and activity
Manually annotated by BRENDA team
-
low XDH expression and activity
Manually annotated by BRENDA team
-
only oxidase type in stored milk, 94% NAD+-dependent dehydrogenase type in fresh milk
Manually annotated by BRENDA team
-
in milk, more than 90% of enzyme exists in the inactive demolybdo form
Manually annotated by BRENDA team
-
xanthine oxidoreductase associated with milk phospholipid membranes was found to be distributed among an intra-membranous pool in which it takes the form of a mixture of xanthine oxidase and xanthine dehydrogenase, with a clear predominance of xanthine dehydrogenase, and a free pool of xanthine oxidase, of which 33% is found in the outer surface of milk fat globule membrane, 20.5% in the outer surface of whey membrane particles, and the remaining 46.7% in apparent solution. The inner-membrane xanthine oxidoreductase may play a nonenzymatic role in fat secretion, whereas extramembranous xanthine oxidase is freely available for a role in the innate gland immune system and may affect milk quality
Manually annotated by BRENDA team
-
only oxidase type O form
Manually annotated by BRENDA team
-
identification of zinc-binding protein identical to xanthine oxidoreductase of 85 kDa
Manually annotated by BRENDA team
-
very low oxidase and dehydrogenase activities
Manually annotated by BRENDA team
-
high rate of dehydrogenase activity
Manually annotated by BRENDA team
-
low oxidase activity
Manually annotated by BRENDA team
-
only oxidase type O form
Manually annotated by BRENDA team
-
selection of 11 rosy mutant strain, corresponding to single amino acid substitutions for detailed studies on the activities
Manually annotated by BRENDA team
-
five different forms in electrophoretic mobility, but no differences in kinetic constants
Manually annotated by BRENDA team
-
analysis of a rosy mutant strain
Manually annotated by BRENDA team
additional information
-
enzyme tissue distribution, no age-dependent differences, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
parenchymal cells, dehydrogenase activity
Manually annotated by BRENDA team
-
100000 x g supernatant, cerebral cortex, liver
Manually annotated by BRENDA team
-
subcellular fractionation
Manually annotated by BRENDA team
-
subcellular fractionation
Manually annotated by BRENDA team
-
immunohistochemic determination
Manually annotated by BRENDA team
-
fat-globule, milk
-
Manually annotated by BRENDA team
-
milk phospholipid membrane, mixture of xanthine oxidase and xanthine dehydrogenase, with a clear predominance of xanthine dehydrogenase
Manually annotated by BRENDA team
-
matrix and core, of parenchymal cells, both oxidase and dehydrogenase activity
Manually annotated by BRENDA team
B3FYT9
in leaf peroxisomes, the superoxide-generating form, xanthine oxidase XOD is predominant over the xanthine dehydrogenase form XDH, with a XDH/XOD ratio of 0.5. Enzyme is localized to the matrix of peroxisome
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
125000
-
-
gel filtration, sedimentation equilibrium analysis
129000
-
-
native PAGE
224000
-
-
gel filtration
230000
300000
-
gel filtration
250000
-
-
sucrose density gradient centrifugation
255000
-
-
sucrose density gradient centrifugation, gel filtration
270000
300000
-, Q8GUQ8
gel filtration
275000
-
-
gel filtration
285000
-
-
native PAGE
287000
-
-
gel filtration
290000
-
-
-
290000
-
B3FYT9
PAGE
300000
-
-
non-denaturating disc gel electrophoresis
300000
-
-
native gel electrophoresis
300000
-
-
sedimentation equilibrium measurements
300000
-
-
gel filtration
300000
-
-
gel filtration
325000
-
-
gel filtration
345000
-
-
gel filtration
350000
-
-
gel filtration
350000
-
-
native PAGE
357000
-
-
sucrose density gradient centrifugation
529000
-
-
gel filtration
530000
-
-
gel filtration
540000
-
-
gel filtration
580000
-
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 140000, SDS-PAGE, trypsin-treated: x * 90000, SDS-PAGE, conversion of dehydrogenase to oxidase activity
?
-
x * 92000 + x * 46000, SDS-PAGE
?
-
x * 150000, SDS-PAGE
?
-
alpha1, x * 90000 + beta1, x * 60000, SDS-PAGE
?
-
x * 147782, calculation from sequence of cDNA
?
-
x * 150000, SDS-urea -PAGE
?
-
x * 72000, SDS-PAGE
?
-
x * 150000, SDS-phosphate gel electrophoresis
?
-
x * 54000 + x * 76000, SDS-PAGE
?
-
x * 145300, SDS-PAGE
?
-
x * 150000, SDS-PAGE
?
-
x * 148300, MALDI-TOF
?
P47989
x * 148000, MALDI-TOF
dimer
-
-
dimer
-
2 * 145000, data from crystallization
dimer
-
alpha1, 1 * 155000 + beta1, 1 * 135000, SDS-PAGE
dimer
-
1 * 130000 + 1 * 140000, SDS-PAGE
dimer
-
2 * 141000, SDS-PAGE
dimer
-
2 * 155000, SDS-PAGE
dimer
-
2 * 67000, SDS-PAGE
dimer
-, Q8GUQ8
2 * 150000, SDS-PAGE
dimer
-
2 * 150000, SDS-PAGE
dodecamer
-
tetramer of alpha/beta/gamma-protomers, alpha4, 4 * 81300 + beta4, 4 * 30000 + gamma4, 4 * 17500, SDS-PAGE
dodecamer
-
alpha4, 4 * 80000 + beta4, 4 * 35000 + gamma4, 4 * 16000, SDS-PAGE
heterooctamer
-
2 * 91041 + 2 * 46238, MALDI-TOF mass spectrometry; 2 * 94000 + 2 * 51000, SDS-PAGE
heterooctamer
Pseudomonas putida 86
-
2 * 91041 + 2 * 46238, MALDI-TOF mass spectrometry; 2 * 94000 + 2 * 51000, SDS-PAGE
-
heterotetramer
-
(alphabeta)2 structure, mechanism of assembly and cofactor insertion on two different polypeptides: dimerization of the (alphabeta) subunits has to precede molybdenum cofactor insertion, the two subunits act independently without cooperativity, incomplete assembly of FeSI impairs the formation of the XDH (alphabeta)2 heterotetramer and, thus, insertion of the molybdenum cofactor into the enzyme, overview
heterotetramer
-
alpha2beta2
oligomer
B3FYT9
x * 59000, SDS-PAGE
pentamer
-
1 * 110000 + 1 * 83000 + 1 * 56000 + 1 * 53000 + 1 * 26000, SDS-PAGE
tetramer
-
2 * 81000 + 2 * 63000, SDS-PAGE
tetramer
-
4 * 84200, SDS-PAGE
tetramer
O54050
(alphabeta)2 heterotetramer
trimer
-
1 * 82400 + 1 * 28500 + 1 * 18400, SDS-PAGE
homodimer
-, Q8GUQ8
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
additional information
-
structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
flavoprotein
-, Q8GUQ8
-
flavoprotein
-
-
phosphoprotein
-
3.6 mol per alpha/beta-protomer
additional information
-
conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2.1 A resolution for both xanthine oxidase and dehydrogenase forms, irreversible pancreatin cleaved xanthine oxidase form results in blocking access of substrate NAD+ to the FAD cofactor
-
batch method, 2.5 and 3.3 A resolution for irreversible proteolytically cleaved xanthine oxidase form, 2.1 A resolution for dehydrogenase form
-
highly active bovine XOR in its XDH form is soaked in a large excess of NADH under strictly anaerobic conditions in order to reduce both FAD cofactor and iron sulfur centers and to block any electron transfer from the Mo center. The Mo ions in the crystal are fully reduced by soaking in 4 mM titanium citrate solution followed by 0.25 mM urate, crystal structure determination and analysis, superimposition, modelling
-
in complex with inhibitor FYX051, which is slowly hydroxylated by the enzyme
-
in complex with inhibotrs allopurinol, febuxostat, and FYX-051
-
in complex with TEI-6720
-
reduced enzyme in complex with oxipurinol at 2.0 A resolution. Electron density is observed between the N2 nitrogen atom of oxipurinol and the molybdenum atom of the molybdopterin cofactor. Oxipurinol forms hydrogen bonds with residues E802, R880, and E1261
-
mutant E803V, decrease in activity towards purine substrates is not due to large conformational change in the mutant protein
-
C535A/C992R/C1324S triple mutant XDH crystal structure analysis
-
mutant C535A/C992R/C1324S
-
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
P22985
2.7 A resolution, direct coordination of alloxanthine to the molybdenum via a nitrogen atom
-
crystal structure determination of the free enzyme and the enzyme in complex with inhibitor alloxanthine
-
purified recombinant wild-type enzyme and subunit beta mutants E232A and E232Q with or without molybdenum cofactor, hanging drop vapor diffusion method, 15 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 1 mM EDTA, 200 mM NaCl,and 2.5 mM dithiothreitol are mixed 1 mM NAD+ and inhibitor pterin-6-aldehyde and with the reservoir solution containing 6-8 mM BaCl2, 6-8% polyethylene glycol 8000, 100 mM Tris-HCl, pH 8.3, 5-25mM dithiothreitol, and 3-4% isopropanol, whereas the EB232Q variant is mixed in a 1:2 ratio with the same reservoir solution, X-ray diffraction structure determination and analysis at 2.6-3.4 A resolution, overview
O54050
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
12
-
stable for 24 h if stored at 4C
7
8.5
-
stable within, loss of activity at more acidic pHs
7
-
-
unstable below, stabilized and activated at higher pH values
7.5
-
-
stable at 4C, one day, absence of DTT
8.5
-
-
4C, absence of DTT, marked decrease of activity within hours
9.2
-
-
recombinant enzyme, half-life: 10-15 h at 0-4C
11
-
-
no effect on activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-20
-
-
stable up to 10 days
-20
-
-
conversion of dehydrogenase type D to oxidase type O
-20
-
-
stable dehydrogenase form, no conversion to the oxidase form
2
-
-
dehydrogenase type stable under anaerobic conditions
4
-
-
liver extract: conversion of dehydrogenase to oxidase activity, some loss of activity after 7 days, extract from cerebrellum and cerebral cortex: stable for 7 days
4
-
-
free enzyme, half-life: 18 days, immobilized enzyme, half-life: 88 days
4
-
-
up to 150% activity when kept 24-120 h in a pH range of 9-11
30
-
-
enhanced stability of immobilized enzyme preparation if N2 and hemoglobin is included, reaction of oxygen products causes instability of the working enzyme, half-life: 250-560 min, compared to immobilized enzyme without additions of about 145 min
37
-
-
conversion to an intermediate dehydrogenase-oxidase type O form in 30 min
37
-
-
stable dehydrogenase activity, no conversion to the oxidase form
37
-
-
stable for 4 min
37
-
-
30 min, increase in activity of both xanthine oxidase and xanthine oxidase plus dehydrogenase. No increase in presence of adenine
38
-
-
dehydrogenase type unstable, change to oxidase type inhibited under anaerobic conditions
40
-
-
stable for 10 min, pH 8.5
55
-
-
stable below
60
-
-
conversion of dehydrogenase type D to oxidase type O
65
-
-
complete loss of activity in 10 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant
-
complete loss of activity when stored below 0C
-
crude and purified enzyme preparations form readily insoluble inactive aggregates, not stable to freezing and thawing
-
extremely labile
-
subunit alpha more sensitive to SDS-heat treatment
-
oxygen-linked activity rather unstable during storage at 4C, ferricyanide-linked activity stable to freezing and thawing
-
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant
-
treatment accelerating conversion of dehydrogenase type D to oxidase type O is lyophilization, storage at -20C, exposure to 20% ammonium sulfate, 0.5 mM NAD+ or 0.01 mM xanthine
-
enzyme from crude extract can be stabilized by addition of nicotinamide, cysteine and EDTA, purified enzyme more stable
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Methanol
-
sensitive to, half-life: 3 min at 1.5 M
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
conversion of dehydrogenase to oxidase type under aerobic conditions
-
644618
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, 0.1 M sodium diphosphate, 0.3 mM EDTA, pH 7.5, 1 mM salicylate, 2.5 mM DTT, 3 months
-
1C, 1 mM DTT in conjunction with 0.1 M ammonium sulfate, 60-70% retaining activity after 8-12 days
-
-80C, 6 months
-
4C, 1 week
-
-20C, 24 h, activity of both xanthine oxidase and xanthine oxidase plus dehydrogenase is lower in liver extracts with the combined presence of adenine and dithiotreitol/phenylmethylsulfonyl fluoride
-
-20C, pH 8.6, 3 days
-
4C, 25 mM Tris-boric acid, pH 8.5, 2.5 mM EDTA, 2 mM 2-mercaptoethanol, 0.2 mM sodium molybdate, one year
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His-tagged wild-type and mutant XDH1 variants from Pichia pastoris strain KM71 by nickel affinity chromatography and anion exchange chromatography; recombinant His-tagged XDH1 from Pichia pastoris by nickel affinity and anion exchange chromatography
-, Q8GUQ8
highly active bovine XOR in its XDH form is prepared by folate affinity chromatography
-
to homogeneity, 2 types: dehydrogenase type, chromatography techniques, oxidase type: affinity chromatography
-
to homogeneity, presence of DTT required for purification of the dehydrogenase form
-
in presence of dithiothreitol
-
to homogeneity, chromatography, preparative gel electrophoresis
-
to homogeneity, chromatography techniques, preparative gel electrophoresis
-
to homogeneity, chromatography techniques
-
near homogeneity, chromatography techniques
-
to homogeneity, chromatography steps
-
529fold purification, several (NH4)2SO4 precipitation steps
-
near homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, immunoaffinity chromatography
-
to homogeneity, recombinant enzyme
-
to homogeneity, chromatography techniques
-
immobilized on n-octylamine-substituted Sepharose 4B; to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
after expression in Escherichia coli
-
native enzyme partially from mammary gland epithelial cells by gel filtration
-
to homogeneity, immobilized preparation
-
to homogeneity, affinity chromatography
-
to homogeneity, immunoabsorption chromatography
-
; ammonium sulfate precipitation, phenyl-Sepharose column chromatography, DEAE-10 Macro-Prep MP10 column chromatography, and Bio-Prep SE-1000/17 column chromatography
-
to homogeneity, chromatography techniques
-
to homogeneity, mainly ferricyanide- and NAD+-linked activities, chromatography steps
-
to crystalline state, chromatography techniques
-
adenine may play a role in preventing the dehydrogenase to oxidase conversion during extract preparation, storage, overnight dialysis and heat treatment
-
from liver
-
during purification conversion from dehydrogenase type D to oxidase type O, reversible by dithioerythritol
-
nearly homogenous, dehydrogenase type D, chromatography steps, oxidase type O purified by nearly the same procedure, but heated to 60C after homogenization
-
purified as antibody complex
-
to homogeneity, affinity chromatography
-
to homogeneity, chromatography techniques
-
to homogeneity, mainly NAD+-dependent activity
-
recombinant His-tagged wild-type and mutant XDHs from Escherichia coli strain TP1000 by nickel affinity and anion exchange chromatography, followed by ultrafiltration and gel filtration
-
recombinant wild-type and mutant enzymes with or without molybdenum cofactor by nickel affinity and anion exchange chromatography, followed by gel filtration
O54050
to homogeneity, affinity chromatography
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, precipitation and chromatography techniques
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of His-tagged wild-type and mutant XDH1 variants in Pichia pastoris strain KM71; expression of His-tagged XDH1 in Pichia pastoris
-, Q8GUQ8
expression in Aspergillus nidulans
-
expression analysis
-
expression of enzyme mutant D428A in Spodoptera frugiperda Sf9 cells via the baculovirus transfection system in mostly the demolybdo-form
P22985
C-terminally His6-tagged wild-type and mutant XDHs expression in Escherichia coli strain TP1000
-
expression of wild-type and mutant enzymes
O54050
recombinant expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
downregulation of enzyme expression in malignant and non-malignant mammary epithelial cells by 17beta-estradiol
-
trimetazidine causes no significant differences in XOR expression in kidneys without ischemia, whereas the XOR expression in ischemic kidneys is significantly decreased, overview
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E1297A
-, Q8GUQ8
site-directed mutagenis
R909A
-, Q8GUQ8
site-directed mutagenis
W364A
-, Q8GUQ8
site-directed mutagenis
Y421A
-, Q8GUQ8
site-directed mutagenis
E89K
-
natural mutant strain, lacking iron-sulfur centers, activity to xanthine/NAD+ or xanthine/pterin not affected, but xanthine/phenazine methosulfate activity abolished
G1011E
-
within the molybdenum domain, no activity without oxidative activation
G353D
-
modifications to the NAD+-NADH-binding sites
E803V
-
almost complete loss of activity with hypoxanthine, weak activity with xanthine, significant aldehyde oxidase activity
E803V
-
very low steady-state activity towards xanthine or hypoxanthine, loss of hydrogen bonding with one of these residues greatly influences the electron transfer process to the molybdenum center, changing the rate-limiting step in the reductive half-reaction
R881M
-
almost complete loss of activity with xanthine, weak activity with hypoxanthine, significant aldehyde oxidase activity
C535A
-
resistant to conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine
C535A/C992R
-
slow conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine, conversion is blocked by NADH
C535A/C992R/C1316S
-
completely resistant to conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine
C535A/C992R/C1316S
-
mutation in residues involved in conversion of xanthin dehydrogenase to xanthine oxidase by formation of disulfide bonds. Using guanidine-HCl, the mutant can be converted into the oxidase form
C535A/C992R/C1324S
-
completely resistant to conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine
C535A/C992R/C1324S
-
an XDH-locked enzyme mutant that cannot be induced by sulfhydryl reagents to adopt the XO form
C992R
-
resistant to conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine
W335A/F336L
P22985
mutant oxidoreductase displaying xanthine oxidase activity
C134A/C136A
-
site-directed mutagenesis, an inactive subunit A mutant
C44A/C47A
-
site-directed mutagenesis, an instable subunit A mutant that cannot be purified
E220R/D517R
-
site-directed mutagenesis, a subunit B mutant that is mainly dimeris incontrast to the tetrameric wild-type enzyme, inactive mutant
E232A
-
decrease in kcat value, increase in KM-value
E730A
-
no enzymic activity
E730D
-
no enzymic activity
E730Q
-
no enzymic activity
E730R
-
no enzymic activity
EB232Q
O54050
catalytically inactive active site mutant, inactive desulfo enzyme form
Q102A
-
site-directed mutagenesis, a subunit A mutant that shows altered metal content and reduced KM and Kcat with xanthine compared to the wild-type enzyme
Q102G
-
site-directed mutagenesis, a subunit A mutant that shows altered metal content and reduced KM and Kcat with xanthine compared to the wild-type enzyme
R135C
-
mutation corresponding to human protein variant of a patient suffering from xanthinuria I. Mutation results in an active (alphabeta)2 heterotetrameric form besides an inactive alphabeta heterodimeric form missing the FeSI center
R310K
-
absorption spectra similar to wild-type. 20fold decrease of kred-value; kred, the limiting rate of enzyme reduction by substrate at high substrate concentration is 20-fold decreased
R310M
-
absorption spectra similar to wild-type. 20000fold decrease of kred-value; kred, the limiting rate of enzyme reduction by substrate at high substrate concentration is 20000-fold decreased
R330M
-
the activity with substrate 2-hydroxy-6-methylpurine is only slightly affected
E831A
-, Q8GUQ8
site-directed mutagenis
additional information
-
T-DNA insertion mutant, loss of superoxide producing activity
S357F
-
modifications to the NAD+-NADH-binding sites
additional information
-
isolation of selD and xdh in-frame deletion mutants with null phenotype for biofilm formation. The wild-type strain produces significant levels of superoxide, whereas the selD and xdh mutants do not exhibit superoxide production, overview
R881M
-
very low steady-state activity towards xanthine or hypoxanthine, loss of hydrogen bonding with one of these residues greatly influences the electron transfer process to the molybdenum center, changing the rate-limiting step in the reductive half-reaction
additional information
-
enzyme null mutant mice demonstrate 50% reduction in adipose mass compared to control, while obese mice exhibit increased concentrations of xanthine oxidoreductase mRNA and urate in adipose tissues. In vitro, knockdown of xanthine oxidoreductase inhibits adipogenesis and nuclear receptor PPARgamma activity; xanthine oxidoreductase expression is elevated 2-fold in white adipose tissue of obese ob/ob mice relative to wild-type, and treatment of ob/ob mice with leptin reduces xanthine oxidoreductase mRNA to wild-type levels. Similarly, serum uric-acid levels are elevated in ob/ob mice relative to wild-type and normalized by leptin treatment. Adipose stores from 2-week-old mice lacking xanthine oxidoreductase activityshow a 12% reduction in body weight compared with wild-type, due to a 50% reduction in adipose content. Serum analysis in xanthine oxidoreductase -/- mice shows significantly decreased free fatty-acid concentrations, while no significant differences are evident for glucose and serum triglycerides
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant. Above 3 M guandine-HCl, even xanthine oxidase activity decreases drastically, but the xanthine oxidase form treated with 1.5 M can be completely reconverted into xanthine dehydrogenase by dialysis
-
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nutrition
-
xanthine oxidoreductase associated with milk phospholipid membranes is found to be distributed among an intra-membranous pool in which it takes the form of a mixture of xanthine oxidase and xanthine dehydrogenase, with a clear predominance of xanthine dehydrogenase, and a free pool of xanthine oxidase, of which 33% is found in the outer surface of milk fat globule membrane, 20.5% in the outer surface of whey membrane particles, and the remaining 46.7% in apparent solution. The inner-membrane xanthine oxidoreductase may play a nonenzymatic role in fat secretion, whereas extramembranous xanthine oxidase is freely available for a role in the innate gland immune system and may affect milk quality
synthesis
Q8RLC0, Q8RLC1
expression of genes xdhAB encoding the two subunits of enzyme, in Escherichia coli, produces active enzyme with moleybdenum content of 0.11-0.16 mol per alphabeta protomer and iron and FAD levels at stoichiometries similar to native enzyme. Coexpression of xdhAB genes with Pseudomonas aeruginosa xdhC gene increases level of molybdenum incorporated to a 1:1 stoichiometry and results in high levels of functional protein, up to 2284 units per mg and 8039 mg per l; expression of genes xdhAB encoding the two subunits of enzyme, in Escherichia coli, produces active enzyme with moleybdenum content of 0.11-0.16 mol per alphabeta protomer and iron and FAD levels at stoichiometries similar to native enzyme. Coexpression of xdhAB genes with Pseudomonas aeruginosa xdhC gene increases level of molybdenum incorporated to a 1:1 stoichiometry and results in high levels of functional protein, up to 2284 units per mg and 8039 mg per l
synthesis
-
for maximal level of functional expression, co-expression of xdhC gene is required which increases level of molybdenum incorporation. Iron and FAD content of expressed enzymes are independent of xdhC expression
analysis
-
use of rosy mutant strains to probe structure and function of xanthine dehydrogenase
synthesis
-
immobilized xanthine dehydrogenase for use in organic synthesis
medicine
-
the enzyme inhibitor 4-(5-pyridin-4-yl-1H-[1,2,4]triazol-3-yl) pyridine-2-carbonitrile, i.e. FYX-051, is modified in vivo by N1- and N2-glucuronidation, mainly catalyzed by UDP-glucuronosyltransferase UGT1A9
medicine
-
xanthine oxidoreductase is activated in a p38 MAP kinase-dependent manner following high tidal volume mechanical ventilation and is involved in resulting increased alveolar cell apoptosis
medicine
-
demonstration of a functional link between xanthine oxidoreductase expression and mammary epithelial cell migration, potential role in enzyme in suppressing breast cancer pathogenesis. Level of xanthine oxidoreductase is markedly reduced in highly invasive mammary tumor cells, and over-expression of enzyme cDNA in cell lines possessing weak expression and high migratory capacity inhibits their migration in vitro
medicine
-
lung xanthine oxidoreductase activity is significantly increased after 2 h of mechanical ventilation without changes in enzyme expression. Increase occurs via activation of p38 MAP kinase and ERK and plays a critical role in the pathogenesis of pulmonary edema associated with ventilator-induced lung injury
medicine
-
enzyme null mutant mice demonstrate 50% reduction in adipose mass compared to control, while obese mice exhibit increased concentrations of xanthine oxidoreductase mRNA and urate in adipose tissues. In vitro, knockdown of xanthine oxidoreductase inhibits adipogenesis and nuclear receptor PPARgamma activity. Xanthine oxidoreductase is a potential therapeutic target for metabolic abnormalities beyond hyperuricemia
medicine
-
oral adminstration of cassia oil significantly reduces serum and hepatic urate levels in hyperuricemic mice. At 600mg/kg, cassia oil is as potent as allopurinol. This hypouricemic effect is explained by inhibiting activities of liver xanthine oxidase and xanthine oxidoreductase
medicine
-
demonstration of a functional link between xanthine oxidoreductase expression and mammary epithelial cell migration, potential role in enzyme in suppressing breast cancer pathogenesis. Over-expression of enzyme cDNA in cell lines possessing weak expression and high migratory capacity inhibits their migration in vitro
agriculture
-
treatment of normal fruit in linear phase of growth with enzyme inhibitors allopurinol or adenine arrests fruit growth
medicine
-
cocaine-induced cardiac disfunction is associated with an increase in NADPH oxidase and xanthine oxidoreductase activities by 59% and 29%, respectively, and a decrease in catalase activity. Apocynin or allopurinol treatment prevents the cocaine-induced cardiac alteration by restoration of cardiac output, stroke volume and fractional shortening. This is associated with a reduction of the myocardial production of superoxide anions and an enhancement of catalase activity. Apocynin treatment prevents anthine oxidoreductase up-regulation supporting the hypothesis that NADPH oxidase-derived reactive oxygen species play a role in modulating reactive oxygen species production by xanthine oxidoreductase
synthesis
-
expression of enzyme in baculovirus-insect cell system, yields a mixture of native dimeric, demolydbo-dimeric and monomeric forms. All forms contain flavin, the monomeric forms lack molybdopterin and the iron-sulfur centers. Monomeric forms require only three electrons for complete reduction
medicine
-
modification of xanthine oxidoreductase by disulfiram that is used in the management of chronic alcolism