1.17.1.4: xanthine dehydrogenase
This is an abbreviated version!
For detailed information about xanthine dehydrogenase, go to the full flat file.
Word Map on EC 1.17.1.4
-
1.17.1.4
-
uric
-
1.2.1.37
-
1.1.1.204
-
allopurinol
-
environmental protection
-
ureide
-
1.1.3.22
-
medicine
-
1.2.3.1
-
xanthinuria
-
oxypurines
-
butyrophilins
-
synthesis
-
hypouricemic
-
agriculture
-
biotechnology
-
analysis
-
nutrition
-
molecular biology
- 1.17.1.4
-
uric
-
1.2.1.37
-
1.1.1.204
- allopurinol
- environmental protection
-
ureide
-
1.1.3.22
- medicine
-
1.2.3.1
-
xanthinuria
-
oxypurines
-
butyrophilins
- synthesis
-
hypouricemic
- agriculture
- biotechnology
- analysis
- nutrition
- molecular biology
Reaction
Synonyms
AtXDH1, EC 1.1.1.204, EC 1.2.1.37, IAO1, More, NAD-xanthine dehydrogenase, PaoABC, Retinol dehydrogenase, Rosy locus protein, VvXDH, xanthine dehydrogenase, xanthine dehydrogenase-1, xanthine dehydrogenase-2, xanthine dehydrogenase/oxidase, xanthine oxidoreductase, xanthine-NAD oxidoreductase, xanthine/NAD+ oxidoreductase, xanthine:NAD+ oxidoreductase, XDH, XDH/XO, XDH1, XDH2, XdhC, XOR, YagR, YagS, YagT
ECTree
1.17.1.4 xanthine dehydrogenaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.17.1.4 - xanthine dehydrogenase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-methylhypoxanthine + NAD+ + H2O
1-methylxanthine + NADH
-
10% of the activity compared to hypoxanthine
-
?
1-naphthaldehyde + NAD+ + ?
? + NADH
27.5% of the activity with xanthine
-
-
?
2 2-hydroxypurine + 2 NAD+ + 2 H2O
xanthine + 2,8-dihydroxypurine + 2 NADH + 2 H+
-
considerable activity
84% xanthine, 8% 2,8-dihydroxypurine formed
?
2 hypoxanthine + 2 NAD+ + 2 H2O
xanthine + 6,8-dihydroxypurine + 2 NADH + 2 H+
-
preferred substrate
100% xanthine, 51% 6,8-dihydroxypurine formed
?
2,6-dithiopurine + NAD+ + H2O
? + NADH
-
26% of the activity compared to hypoxanthine
-
?
2-amino-4-hydroxypterin + nitroblue tetrazolium + H2O
isoxanthopterin + reduced nitroblue tetrazolium
2-hydroxy-6-methylpurine + NAD+ + H2O
? + NADH + H+
-
poor substrate
-
-
?
2-hydroxypurine + NAD+ + H2O
? + NADH
-
35% of the activity compared to hypoxanthine, purine not oxidized
-
?
2-thioxanthine + NAD+ + H2O
2-thiourate + NADH
-
57% of the activity compared to hypoxanthine
-
?
3 purine + 3 NAD+ + 3 H2O
hypoxanthine + 8-hydroxypurine + 2-hydroxypurine + 3 NADH + 3 H+
-
poor substrate
2.3% hypoxanthine, 2.3% 8-hydroxypurine and traces of 2-hydroxypurine formed
?
4-aminoimidazole-5-carboxamide + NADP+ + H2O
? + NADPH
-
38% of the activity compared to hypoxanthine-NADP+
-
?
4-dimethylaminobenzaldehyde + NAD+ + H2O
4-dimethylaminobenzoate + NADH
-
0.3% activity compared to xanthine
-
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + ferricyanide + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + ferrocyanide
-
i.e. allopurinol
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + methyl viologen + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced methyl viologen
4-hydroxypyrazolo(3,4-d)pyrimidine + NAD+ + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + NADH
4-hydroxypyrazolo(3,4-d)pyrimidine + nitroblue tetrazolium + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced nitroblue tetrazolium
5-aminoimidazol-4-carboxamide + methyl viologen + H2O
? + reduced methyl viologen
-
1.1% of the activity compared to xanthine
-
?
6,8-dihydropurine + NAD+ + H2O
? + NADH
-
50% of the activity compared to hypoxanthine
-
?
6,8-dihydroxypurine + NAD+ + H2O
urate + NADH
-
-
18% urate formed
?
6-mercaptopurine + methyl viologen + H2O
? + reduced methyl viologen
-
9.5% of the activity compared to xanthine
-
?
6-thioxanthine + NAD+ + H2O
6-thiourate + NADH
-
63% of the activity compared to hypoxanthine
-
?
6-thioxanthine + NAD+ + H2O
6-thiourate + NADH + H+
-
effective substrate
-
-
?
8-azaxanthine + NAD+ + H2O
8-aza-urate + NADH
-
very low activity
-
?
abscisic aldehyde + NAD+ + ?
? + NADH
28.9% of the activity with xanthine
-
-
?
acetaldehyde + ferricyanide + H2O
acetic acid + ferrocyanide
-
5% of the activity compared to xanthine
-
?
acetaldehyde + nitroblue tetrazolium + H2O
acetic acid + reduced nitroblue tetrazolium
-
very low activity
-
?
adenine + ferricyanide + H2O
urate + ferrocyanide
-
12% of the activity compared to xanthine
-
?
adenine-N1-oxide + NAD+ + H2O
? + NADH
-
3.4% of the activity compared to hypoxanthine
-
?
benzaldehyde + 2 ferricyanide + H2O
benzoate + 2 ferrocyanide + 2 H+
-
4% of the activity compared to xanthine
-
?
benzaldehyde + ferricyanide + H2O
benzoate + 2 ferrocyanide + 2 H+
-
-
-
?
benzaldehyde + nitroblue tetrazolium + H2O
benzoate + reduced nitroblue tetrazolium
-
very low activity
-
?
cinnamaldehyde + H2O + acceptor
cinnamic acid + reduced acceptor
-
-
-
?
guanine + NAD+ + H2O
? + NADH
-
81.3% of the activity compared to hypoxanthine
-
?
heptaldehyde + NAD+ + ?
? + NADH
12.5% of the activity with xanthine
-
-
?
hypoxanthine + cytochrome c + H2O
xanthine + reduced cytochrome c
-
2.1% of the activity compared to NAD+
-
?
hypoxanthine + methylene blue + H2O
xanthine + reduced methylene blue
-
39% of the activity compared to NAD+ as electron acceptor
-
?
hypoxanthine + NAD+ + H2O
urate + ? + NADH
-
149% activity compared to xanthine
-
-
?
hypoxanthine + NADH
? + NO2- + NAD+
-
0.1% of the xanthine oxidation rate
-
?
hypoxanthine + urate
xanthine + 6,8-dihydroxypurine
-
oxygen-free assay
-
r
hypoxanthine + uric acid imine
?
-
uric acid in its 2-electron oxidized form is able to act as an artificial electron acceptor from XDH in an electrochemically driven catalytic system
-
-
?
indole-3-acetaldehyde + NAD+ + H2O
indole-3-acetate + NADH + H+
-
and similar aldehydes, 2-3% of the activity with xanthine
-
-
?
indole-3-carboxaldehyde + NAD+ + ?
? + NADH
31.3% of the activity with xanthine
-
-
?
isoguanine + NAD+ + H2O
? + NADH
-
7.3% of the activity compared to hypoxanthine
-
?
N-methylnicontinamide + NADP+ + H2O
? + NADPH
-
low activity, only a substrate at pH values above 8.0
-
?
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
-
-
-
r
NADH + O2 + H+
NAD+ + O2- + H2O2
-
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+ + ?
-
no activity for the mutant E89K
-
?
NADPH + electron acceptor + H2O
NADP+ + reduced electron acceptor
-
electron acceptors: 2,6-dichlorophenolindophenol, methyl viologen, benzyl viologen, methylene blue
-
?
NADPH + phenazine methosulfate + cytochrome c
NADP+ + ?
-
-
-
?
phthalazine + NAD+ + H2O
1-(2H)-phthalazinone + NADH
-
0.4% activity compared to xanthine
-
-
?
propionaldehyde + NAD+ + H2O
propionic acid + NADH
-
low activity
-
?
purine + ferricyanide + H2O
urate + ferrocyanide
-
108% of the activity compared to xanthine
-
?
purine + methyl viologen + H2O
? + reduced methyl viologen
-
2% of the activity compared to xanthine
-
?
purine + NAD+ + ?
? + NADH
10.3% of the activity with xanthine
-
-
?
purine + NADP+ + H2O
? + NADPH
-
60% of the activity compared to hypoxanthine
-
?
quinazoline + NAD+ + H2O
4-(3H)-quinazolinone + NADH
-
2% activity compared to xanthine
-
-
?
salicylaldehyde + ferricyanide + H2O
salicylate + ferrocyanide
-
2% of the activity compared to xanthine
-
?
xanthine + 3-acetylpyridine-adenine dinucleotide+ + H2O
urate + 3-acetylpyridine-adenine dinucleotide(H)
xanthine + FAD + H2O
urate + FADH2
-
35% of the activity compared to methylene blue as electron acceptor
-
?
xanthine + FMN + H2O
urate + FMNH2
-
44% of the activity compared to methylene blue as electron acceptor
-
?
xanthine + iodonitrotetrazolium + H2O
urate + reduced iodonitrotetrazolium
-
-
-
?
xanthine + p-benzoquinone + H2O
hypoxanthine + hydroquinone + ?
-
electron donor only for oxidase type
-
?
xanthine + p-benzoquinone + H2O
p-benzosemiquinone + urate
-
electron acceptor p-benzoquinone for both dehydrogenase and oxidase types
-
?
xanthine + pyridinealdehyde-NAD+ + H2O
urate + pyridinealdehyde-NADH
-
53% of the activity compared to NAD+, low reverse activity
-
r
xanthine + riboflavin + H2O
urate + reduced riboflavin
-
41% of the activity compared to methylene blue as electron acceptor
-
?
xanthine + ureic acid imine
?
-
uric acid in its 2-electron oxidized form is able to act as an artificial electron acceptor from XDH in an electrochemically driven catalytic system
-
-
?
xanthosine + NAD+ + H2O
? + NADH
-
15.1% of the activity compared to hypoxanthine
-
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
-
-
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
-
-
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
-
-
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
-
-
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
-
-
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
-
-
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
-
-
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
-
-
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
-
-
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
-
-
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
-
-
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
-
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
-
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
10% of the activity compared to hypoxanthine
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH + H+
-
10fold reduced kred-value compared to xanthine
-
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH + H+
-
rather less effective than xanthine as a substrate
-
-
?
2,6-dichloroindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
-
r
2,6-dichloroindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
-
r
2-amino-4-hydroxy-pterin + methylene blue + H2O
isoxanthopterin + reduced methylene blue
-
-
-
?
2-amino-4-hydroxy-pterin + methylene blue + H2O
isoxanthopterin + reduced methylene blue
-
-
-
?
2-amino-4-hydroxy-pterin + methylene blue + H2O
isoxanthopterin + reduced methylene blue
-
-
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
precursor of the eye pigment drosopterin
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
r
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
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
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
11% of the activity compared to xanthine
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
precursor of the eye pigment drosopterin
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
r
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
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
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
11% of the activity compared to xanthine
-
?
2-amino-4-hydroxypterin + nitroblue tetrazolium + H2O
isoxanthopterin + reduced nitroblue tetrazolium
-
very low activity
-
?
2-amino-4-hydroxypterin + nitroblue tetrazolium + H2O
isoxanthopterin + reduced nitroblue tetrazolium
-
i.e. pterin
-
?
2-thioxanthine + NAD+ + H2O
2-thiourate + NADH + H+
-
good substrate
-
-
?
2-thioxanthine + NAD+ + H2O
2-thiourate + NADH + H+
-
effective substrate
-
-
?
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + H+
-
1.2% activity compared to xanthine
-
-
?
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + H+
-
1.2% activity compared to xanthine
-
-
?
3-methylxanthine + ferricyanide + H2O
3-methylurate + ferrocyanide
-
-
-
?
3-methylxanthine + ferricyanide + H2O
3-methylurate + ferrocyanide
-
-
-
?
3-methylxanthine + ferricyanide + H2O
3-methylurate + ferrocyanide
-
-
-
?
3-methylxanthine + ferricyanide + H2O
3-methylurate + ferrocyanide
-
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
-
0.7% activity compared to xanthine
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
-
0.7% activity compared to xanthine
-
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + methyl viologen + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced methyl viologen
-
i.e. allopurinol
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + methyl viologen + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced methyl viologen
-
8% of the activity compared to xanthine
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + NAD+ + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + NADH
-
best substrate tested
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + NAD+ + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + NADH
-
i.e. allopurinol
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + NAD+ + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + NADH
-
i.e. allopurinol
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + nitroblue tetrazolium + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced nitroblue tetrazolium
-
i.e. allopurinol
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + nitroblue tetrazolium + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced nitroblue tetrazolium
-
very low activity
-
?
4-hydroxypyrazolo(3,4-d)pyrimidine + nitroblue tetrazolium + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced nitroblue tetrazolium
-
i.e. allopurinol
-
?
8-azahypoxanthine + NAD+ + H2O
8-azaxanthine + NADH
-
42% of the activity compared to hypoxanthine
-
?
8-azahypoxanthine + NAD+ + H2O
8-azaxanthine + NADH
-
39% 0f the activity compared to hypoxanthine
-
?
acetaldehyde + 2,6-dichloroindophenol + H2O
?
-
1.2% of activity with xanthine
-
-
?
acetaldehyde + 2,6-dichloroindophenol + H2O
?
-
0.1% of activity with xanthine
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
very low activity
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
considerable activity for the recombinant enzyme
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
very low activity
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
very low activity
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
1.3% activity compared to xanthine
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
1.3% activity compared to xanthine
-
-
?
glyceraldehyde + 2,6-dichloroindophenol + H2O
?
-
12.1% of activity with xanthine
-
-
?
glyceraldehyde + 2,6-dichloroindophenol + H2O
?
-
0.3% of activity with xanthine
-
-
?
hypoxanthine + 2,6-dichlorophenolindophenol + H2O
xanthine + ?
-
considerable activity
-
?
hypoxanthine + 2,6-dichlorophenolindophenol + H2O
xanthine + ?
-
12.2% of the activity compared to NAD+
-
?
hypoxanthine + ferricyanide + H2O
xanthine + ferrocyanide
-
17.2% of the activity compared to NAD+
-
?
hypoxanthine + ferricyanide + H2O
xanthine + ferrocyanide
-
98% of the activity compared to xanthine
-
?
hypoxanthine + methyl viologen + H2O
xanthine + reduced methyl viologen
-
-
-
?
hypoxanthine + methyl viologen + H2O
xanthine + reduced methyl viologen
-
-
-
?
hypoxanthine + methyl viologen + H2O
xanthine + reduced methyl viologen
-
7% of the activity compared to xanthine
-
?
hypoxanthine + NAD+ + 2 H2O
urate + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
94.7% of the activity with xanthine
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
12.4% of activity with xanthine
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
NAD+-O2- dependent xanthine oxidase activity
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
NAD+-O2- dependent xanthine oxidase activity
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
predominant reaction
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
subtilisin treatment leads to an active component I of 120000 kDa
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
more rapidly oxidized than xanthine
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
preferred substrate
-
ir
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
19% of activity with xanthine
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
44% of the activity with xanthine
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
preferred substrate
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
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 + NADP+ + H2O
xanthine + NADPH
-
strict specificity for NADP+
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
-
40% of the activity compared to NAD+
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
-
2.4% of the activity compared to NAD+
-
?
hypoxanthine + nitroblue tetrazolium
xanthine + ?
-
18% of the activity compared to NAD+
-
?
hypoxanthine + phenazine methosulfate + H2O
urate + ?
-
effective electron acceptor
-
?
hypoxanthine + phenazine methosulfate + H2O
urate + ?
-
low activity
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
electron acceptor: nitroblue tetrazolium
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
extremely slow reoxidation rate
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
NADH diaphorase activity with several acceptors
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
-
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
electron acceptors: 2,6-dichlorphenolindophenol or methyl viologen
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
electron acceptor: 2,6-dichlorophenolindophenol, no activity for mutant E89K
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
NADH diaphorase activity with several acceptors
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
2,6-dichloroindophenol, 3-acetylpyridine-adenine dinucleotide, methylene blue, phenazine methosulfate or trinitrobenzene sulfonate
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
subtilisin treatment leads to an active component of 120000 kDa with enhanced activity
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
NADH diaphorase activity with several acceptors
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
2,6-dichloroindophenol as electron acceptor
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
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
-
only dehydrogenase type D shows considerable activities, not oxidase type O
-
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
electron acceptor: nitroblue tetrazolium
-
?
NADPH + nitroblue tetrazolium + H2O
NADP+ + reduced nitroblue tetrazolium
-
diaphorase activity
-
?
NADPH + nitroblue tetrazolium + H2O
NADP+ + reduced nitroblue tetrazolium
-
diaphorase activity
-
?
pterin + 2,6-dichloroindophenol + H2O
?
-
9.7% of activity with xanthine
-
-
?
purine + 2,6-dichloroindophenol + H2O
?
-
8.5% of activity with xanthine
-
-
?
purine + NAD+ + H2O
8-hydroxypurine + NADH + H+
-
5% activity compared to xanthine
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
very low activity for the mutant E89K
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
same activity compared to NAD+ as electron acceptor
-
r
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
2.5% of the activity compared to methyl viologen as electron acceptor
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
subtilisin treatment leads to an active component of 120000 kDa
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
11% of the activity compared to ferricyanide as electron acceptor
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
greatly enhanced activity for dehydrogenase type D and trypsin- or heat-treated oxidase types O
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
13% of the activity compared to methylene blue as electron acceptor
-
?
xanthine + 3-acetylpyridine-adenine dinucleotide+ + H2O
urate + 3-acetylpyridine-adenine dinucleotide(H)
-
same activity compared to NAD+
-
r
xanthine + 3-acetylpyridine-adenine dinucleotide+ + H2O
urate + 3-acetylpyridine-adenine dinucleotide(H)
-
low reverse activity
-
r
xanthine + 3-acetylpyridine-adenine dinucleotide+ + H2O
urate + 3-acetylpyridine-adenine dinucleotide(H)
-
same activity compared to NAD+
-
r
xanthine + benzyl viologen + H2O
urate + reduced benzyl viologen
-
52% of the activity compared to methyl viologen as electron acceptor
-
?
xanthine + benzyl viologen + H2O
urate + reduced benzyl viologen
-
18% of the activity compared to methylene blue as electron acceptor
-
?
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
-
enhanced activity for heat- and trypsin-treated oxidase types O
-
?
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
-
low activity
-
?
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
-
presence of ferredoxin enhances cytochrom c reduction
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
99% of the activity compared to methyl viologen as electron acceptor
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
preferred substrates, does not act with NAD+ or NADP+
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
specific ferricyanide-dependent activity, no activity with NAD+, NADP+, oxygen, cytochrome c, FAD or FMN
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
58% of the activity compared to xanthine-NAD+
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
low activity for both dehydrogenase type D and oxidase type O
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
low activity for both dehydrogenase type D and oxidase type O
-
?
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
-
-
-
?
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
-
-
-
?
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
-
best substrates tested, no activity with NAD+ or NADP+, 40% of the activity in the reverse reaction
-
r
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
-
-
-
?
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
-
low activity
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
-
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
87% of the activity compared to methyl viologen as electron acceptor
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
-
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
subtilisin treatment leads to an active component of 120000 kDa
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
same activity for dehydrogenase type D and oxidase type O
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
enhanced oxidation of xanthine for dehydrogenase type D and trypsin- or heat-treated oxidase type O
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
3fold higher activity compared to NAD+ as electron acceptor
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
-
-
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
regulation of xanthine dehydrogenase expression is subjected to nitrogen catabolite repression mediated through the GlnA-dependent signaling pathway
-
?
xanthine + NAD+ + H2O
urate + NADH
-
xanthine dehydrogenase form has distinct xanthine/oxygen activity, 35-42% of electrons transferred to O2 to form O2-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
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
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH
-
involved in pteridine metabolism, 40% of activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
-
only dehydrogenase type D present
-
?
xanthine + NAD+ + H2O
urate + NADH
-
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
-
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
-
subtilisin treatment leads to an active component I of 120000 kDa
-
?
xanthine + NAD+ + H2O
urate + NADH
-
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
-
degradative pathway of conversion of purines to ammonia
-
r
xanthine + NAD+ + H2O
urate + NADH
-
only present as stable dehydrogenase from, no conversion to the oxidase form
-
?
xanthine + NAD+ + H2O
urate + NADH
-
NAD+-linked activity, very low activity towards molecular oxygen
-
?
xanthine + NAD+ + H2O
urate + NADH
-
75% of the activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
-
NAD+-dependent form is postulated to play a regulatory role in purine metabolism
-
?
xanthine + NAD+ + H2O
urate + NADH
-
conversion of xanthine dehydrogenase to the oxidase type by thiol-disulfide oxidoreductase, thiol reagents or oxidized glutathione
-
?
xanthine + NAD+ + H2O
urate + NADH
-
trypsin treatment leads to a complete conversion of xanthine dehydrogenase to xanthine oxidase activity
-
r
xanthine + NAD+ + H2O
urate + NADH
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH
-
67% of the activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
-
61% of the activity compared to hypoxanthine
91% urate formed
?
xanthine + NAD+ + H2O
urate + NADH
-
strict dehydrogenase activity, no utilization of O2
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
catalytically relevant binding mode of the substrate xanthine, overview
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
catalytically relevant binding mode of the substrate xanthine, overview
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
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+
when catalyzing the sequential oxidation of hypoxanthine to xanthine to uric acid, XDH uses the NAD+ as final electron receptor to produce NADH
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
product release is principally rate-limiting in catalysis
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
Rhodobacter capsulatus CGMCC 1.3366
when catalyzing the sequential oxidation of hypoxanthine to xanthine to uric acid, XDH uses the NAD+ as final electron receptor to produce NADH
-
-
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
-
heat-treated intermediate dehydrogenase/oxidase type O
-
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
-
intermediate form of dehydrogenase/oxidase type D/O
-
?
xanthine + NADP+ + H2O
urate + NADPH
-
11% of the activity compared to NAD+
-
?
xanthine + NADP+ + H2O
urate + NADPH
-
strict specificity for NADP+
-
?
xanthine + nitroblue tetrazolium + H2O
urate + ?
-
32% of the activity compared to methyl viologen as electron acceptor
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
xanthine oxidase form transfers 22% electrons to oxygen to form superoxide
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
subtilisin treatment leads to an active component I of 120000 kDa
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
4% of the activity compared to xanthine-NAD+
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
toxic reactions of xanthine oxidase-derived radicals are critical factors in several mechanisms of tissue pathology
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
NAD+-independent trypsin-treated oxidase type O
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
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+
-
presence of ferredoxin enhances rate of oxygen reduction
-
?
xanthine + phenazine methosulfate + cytochrome c + H2O
urate + ?
-
-
-
?
xanthine + phenazine methosulfate + cytochrome c + H2O
urate + ?
-
-
-
?
xanthine + phenazine methosulfate + cytochrome c + H2O
urate + ?
-
-
-
?
xanthine + phenazine methosulfate + cytochrome c + H2O
urate + ?
-
very low activity for the mutant E89K
-
?
xanthine + phenazine methosulfate + H2O
urate + ?
-
5fold higher activity compared to NAD+ as electron acceptor
-
?
xanthine + thio-NAD+ + H2O
urate + thio-NADH
-
same activity compared to NAD+
-
r
xanthine + trinitrobenzenesulfonate + H2O
urate + ?
-
subtilisin treatment leads to an active component of 120000 kDa
-
?
xanthopterin + NAD+ + H2O
leucopterin + NADH
-
regulation of the pteridine pathway by competitive inhibition of reaction products and the precursor of xanthopterin, 7,8-dihydroxyxanthopterin
-
?
xanthopterin + NAD+ + H2O
leucopterin + NADH
-
regulation of the pteridine pathway by competitive inhibition of reaction products and the precursor of xanthopterin, 7,8-dihydroxanthopterin
-
?
additional information
?
-
-
The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
-
-
?
additional information
?
-
-
The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
-
-
?
additional information
?
-
-
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
?
-
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
?
-
-
AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher than the activity with xanthine accompanied by a doubling in superoxide production and is dependent on sulfurated molybdenum cofactor, overview. FAD is crucial for NADH-based superoxide formation of AtXDH1, whereas the molybdenum cofactor has only little or no influence on the activity, residues E831, R909, E1297, W364, and Y421 are involved
-
-
?
additional information
?
-
AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher than the activity with xanthine accompanied by a doubling in superoxide production 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
?
-
-
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
?
-
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
?
-
autofluorescent objects (AFOs) formation within mesophyll cells of the mutant plants is a marker for xanthine accumulation with both spatial and temporal resolution, AFOs are highly enriched in xanthine
-
-
?
additional information
?
-
The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
-
-
?
additional information
?
-
autofluorescent objects (AFOs) formation within mesophyll cells of the mutant plants is a marker for xanthine accumulation with both spatial and temporal resolution, AFOs are highly enriched in xanthine
-
-
?
additional information
?
-
-
The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
-
-
?
additional information
?
-
IAO1 causes the nonenzymatic conversion of tryptophan to indole-3-acetaldehyde and the enzymatic conversion of indole-3-acetalaldehyde to indole-3-acetic acid, reaction of EC 1.2.3.1
-
-
-
additional information
?
-
-
xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
-
-
?
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
?
-
-
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
?
-
-
The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
-
-
?
additional information
?
-
-
the dehydrogenase form of enzyme reacts significantly faster than the oxidase form
-
-
?
additional information
?
-
-
The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
-
-
?
additional information
?
-
-
The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
-
-
?
additional information
?
-
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The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
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additional information
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The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
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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
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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
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additional information
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The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
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xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
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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
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additional information
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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
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additional information
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The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
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additional information
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The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
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xanthine oxidoreductase is a regulator of adipogenesis and of nuclear recptor PPARgamma activityand is essential for the regulation of fat accretion
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additional information
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The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
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NAD+ is the most effcient electron acceptor, followed by 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyl-2H-tetrazolium chloride and ferricyanide
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additional information
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The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
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additional information
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NAD+ is the most effcient electron acceptor, followed by 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyl-2H-tetrazolium chloride and ferricyanide
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major function of enzyme in liver parenchymal and sinusoidal cells is the production of uric acid as a antioxidant
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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
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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
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enzyme inhibition by orange juice and hesperetin participates in preventing oxidative stress by enhancing total antioxidant capacity and decreasing lipid peroxidation, overview
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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
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additional information
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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
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purified recombinant wild-type and DELTAC mutant enzymes both exhibit mostly xanthine oxidase activity
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additional information
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The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
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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
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additional information
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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
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xanthine and 2-hydroxy-6-methylpurine are substrates. Substrate binding structures, overview
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ionized Glu232 of wild-type enzyme plays an important role in catalysis by discriminating against the monoanionic form of xanthine
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pH-dependent bioelectrocatalytic activity of the redox enzyme xanthine dehydrogenase (XDH) in the presence of sulfonated polyaniline PMSA1 (poly(2-methoxyaniline-5-sulfonic acid)-co-aniline), electron transfer from the hypoxanthine (HX)-reduced enzyme to the polymer. The enzyme shows bioelectrocatalytic activity on indium tin oxide (ITO) electrodes, when the polymer is present. Depending on solution pH, different processes can be identified. Not only product-based communication with the electrode but also efficient polymer-supported bioelectrocatalysis occur. Substrate-dependent catalytic currents can be obtained in acidic and neutral solutions, although the highest activity of XDH with natural reaction partners is in the alkaline region. Operation of the enzyme electrode without addition of the natural cofactor of XDH is feasible. Method development and evaluation, overview
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The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
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Rhodobacter capsulatus B10XDHB
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The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
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additional information
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The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
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additional information
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in the presence of xanthine and NAD+ the enzyme catalyses the oxidation of cyadox (2-cyano-N'-((E)-1,4-dioxido-2-quinazolinyl)methylene)acetohydrazide to the respective N-oxide
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