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1-methylhypoxanthine + NAD+ + H2O
1-methylxanthine + NADH
-
10% of the activity compared to hypoxanthine
-
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH + H+
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-diaminopurine + NAD+ + H2O
? + NADH + H+
-
poor substrate
-
-
?
2,6-dichloroindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
2,6-dithiopurine + NAD+ + H2O
? + NADH
-
26% of the activity compared to hypoxanthine
-
?
2-amino-4-hydroxy-pterin + methylene blue + H2O
isoxanthopterin + reduced methylene blue
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
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-OH-purine + ferricyanide + H2O
? + ferrocyanide
-
-
-
?
2-thioxanthine + NAD+ + H2O
2-thiourate + NADH
-
57% of the activity compared to hypoxanthine
-
?
2-thioxanthine + NAD+ + H2O
2-thiourate + NADH + H+
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
?
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + H+
3-methylxanthine + ferricyanide + H2O
3-methylurate + ferrocyanide
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-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
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
?
6,8-dihydroxypurine + O2
? + H2O2
-
-
-
?
6,8-dihydroxypurine + O2 + H2O
? + H2O2
-
-
-
?
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
-
-
?
6-thioxanthine + NAD+ + H2O
? + NADH + H+
-
good substrate
-
-
?
8-azahypoxanthine + NAD+ + H2O
8-azaxanthine + NADH
8-azaxanthine + NAD+ + H2O
8-aza-urate + NADH
-
very low activity
-
?
9-methylhypoxanthine + O2
9-methylxanthine + H2O2
-
-
-
?
abscisic aldehyde + NAD+ + ?
? + NADH
28.9% of the activity with xanthine
-
-
?
acetaldehyde + 2,6-dichloroindophenol + H2O
?
acetaldehyde + ferricyanide + H2O
acetic acid + ferrocyanide
-
5% of the activity compared to xanthine
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
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 + NAD+ + H2O
? + NADH
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 + NAD+ + H2O
benzoate + NADH + H+
benzaldehyde + nitroblue tetrazolium + H2O
benzoate + reduced nitroblue tetrazolium
-
very low activity
-
?
benzaldehyde + O2
benzoate + H2O2
-
-
-
?
cinnamaldehyde + H2O + acceptor
cinnamic acid + reduced acceptor
-
-
-
?
glyceraldehyde + 2,6-dichloroindophenol + H2O
?
guanine + NAD+ + H2O
? + NADH
-
81.3% of the activity compared to hypoxanthine
-
?
heptaldehyde + NAD+ + ?
? + NADH
12.5% of the activity with xanthine
-
-
?
hypoxanthine + 2 NAD+ + 2 H2O
urate + 2 NADH + 2 H+
hypoxanthine + 2,6-dichlorophenolindophenol + H2O
xanthine + ?
hypoxanthine + cytochrome c + H2O
xanthine + reduced cytochrome c
-
2.1% of the activity compared to NAD+
-
?
hypoxanthine + ferricyanide
xanthine + ferrocyanide
-
-
-
?
hypoxanthine + ferricyanide + H2O
xanthine + ferrocyanide
hypoxanthine + methyl viologen + H2O
xanthine + reduced methyl viologen
hypoxanthine + methylene blue + H2O
xanthine + reduced methylene blue
-
39% of the activity compared to NAD+ as electron acceptor
-
?
hypoxanthine + NAD+ + 2 H2O
urate + NADH + H+
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
hypoxanthine + NAD+ + H2O
urate + ? + NADH
-
149% activity compared to xanthine
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
hypoxanthine + NADH
? + NO2- + NAD+
-
0.1% of the xanthine oxidation rate
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
hypoxanthine + nitroblue tetrazolium
xanthine + ?
hypoxanthine + O2
xanthine + H2O2
hypoxanthine + O2 + H2O
xanthine + O2-
hypoxanthine + phenazine methosulfate + H2O
urate + ?
hypoxanthine + thio-NAD+ + H2O
xanthine + thio-NADH
-
-
-
?
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
-
-
?
inosine + NAD+ + H2O
? + NADH
-
low activity
-
?
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 + electron acceptor + H2O
NAD+ + reduced electron acceptor
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 + nitroblue tetrazolium + H2O
NADP+ + reduced nitroblue tetrazolium
NADPH + O2
NADP+ + O2- + H+
-
high NADPH oxidase activity
-
?
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
-
?
pterin + 2,6-dichloroindophenol + H2O
?
pterin + NAD+ + H2O
? + NADH
-
-
-
-
?
purine + 2,6-dichloroindophenol + H2O
?
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 + NAD+ + H2O
8-hydroxypurine + NADH + H+
purine + NAD+ + H2O
? + NADH
purine + NADP+ + H2O
? + NADPH
-
60% of the activity compared to hypoxanthine
-
?
purine + nitroblue tetrazolium
?
-
low activity
-
-
?
quinazoline + NAD+ + H2O
4-(3H)-quinazolinone + NADH
-
2% activity compared to xanthine
-
-
?
salicylaldehyde + ferricyanide + H2O
salicylate + ferrocyanide
-
2% of the activity compared to xanthine
-
?
salicylaldehyde + O2
salicylate + H2O2
-
-
-
r
theobromine + NAD+ + H2O
? + NADH
-
very low activity
-
?
theophylline + NAD+ + H2O
? + NADH
-
low activity
-
?
urate + NADH
xanthine + NAD+ + H2O
-
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
xanthine + 3-acetylpyridine-adenine dinucleotide+ + H2O
urate + 3-acetylpyridine-adenine dinucleotide(H)
xanthine + benzyl viologen + H2O
urate + reduced benzyl viologen
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
xanthine + DCIP + H2O
urate + reduced DCIP
-
-
-
-
?
xanthine + FAD + H2O
urate + FADH2
-
35% of the activity compared to methylene blue as electron acceptor
-
?
xanthine + ferredoxin + H2O
urate + reduced ferredoxin
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
xanthine + FMN + H2O
urate + FMNH2
-
44% of the activity compared to methylene blue as electron acceptor
-
?
xanthine + iodonitrotetrazolium + H2O
urate + reduced iodonitrotetrazolium
-
-
-
?
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
xanthine + methylene blue + H2O
urate + reduced methylene blue
xanthine + myoglobin + H2O
urate + reduced myoglobin
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
xanthine + NAD+ + H2O
urate + NADH + H+
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
xanthine + NADP+ + H2O
urate + NADPH
xanthine + nitroblue tetrazolium + H2O
urate + ?
xanthine + O2
hypoxanthine + ?
-
dismutation reaction
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
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 + phenazine methosulfate + cytochrome c + H2O
urate + ?
xanthine + phenazine methosulfate + H2O
urate + ?
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 + thio-NAD+ + H2O
urate + thio-NADH
xanthine + trinitrobenzenesulfonate + H2O
urate + ?
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
-
-
?
xanthopterin + NAD+ + H2O
leucopterin + NADH
xanthosine + NAD+ + H2O
? + NADH
-
15.1% of the activity compared to hypoxanthine
-
?
additional information
?
-
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
-
-
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
-
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
-
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
-
-
?
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
-
-
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
-
-
?
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
-
?
adenine + NAD+ + H2O
? + NADH
-
low activity
-
?
adenine + NAD+ + H2O
? + NADH
-
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 NAD+ + 2 H2O
urate + 2 NADH + 2 H+
-
-
-
-
?
hypoxanthine + 2 NAD+ + 2 H2O
urate + 2 NADH + 2 H+
-
-
-
?
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
-
-
-
-
?
hypoxanthine + ferricyanide + H2O
xanthine + ferrocyanide
-
-
-
-
?
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+ + 2 H2O
urate + NADH + H+
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
r
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
more rapidly oxidized than xanthine
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
-
-
?
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+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
44% of the activity with xanthine
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
preferred substrate
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
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
-
-
-
?
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 + nitroblue tetrazolium
xanthine + ?
-
-
-
?
hypoxanthine + O2
xanthine + H2O2
-
very low activity
-
?
hypoxanthine + O2
xanthine + H2O2
-
-
-
?
hypoxanthine + O2 + H2O
xanthine + O2-
-
-
no production of H2O2
-
?
hypoxanthine + O2 + H2O
xanthine + O2-
-
-
no production of H2O2
-
?
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
?
-
22.7% of activity with xanthine
-
-
?
pterin + 2,6-dichloroindophenol + H2O
?
-
9.7% of activity with xanthine
-
-
?
purine + 2,6-dichloroindophenol + H2O
?
-
18.7% 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
-
-
?
purine + NAD+ + H2O
8-hydroxypurine + NADH + H+
-
-
-
?
purine + NAD+ + H2O
? + NADH
-
-
-
?
purine + NAD+ + H2O
? + NADH
-
poor substrate
-
?
purine + NAD+ + H2O
? + NADH
-
poor substrate
-
?
purine + NAD+ + H2O
? + NADH
-
poor substrate
-
?
purine + NAD+ + H2O
? + NADH
-
poor substrate
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
-
-
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
-
-
?
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 + ?
-
-
-
?
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 + ?
-
-
-
?
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
-
-
-
?
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
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
-
-
?
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
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
-
-
?
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
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
-
-
?
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 + ferricyanide + H2O
urate + ferrocyanide
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
-
-
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
-
-
?
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
-
-
-
r
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
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
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 + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
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
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
involved in pteridine metabolism, 40% of activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
only dehydrogenase type D present
-
?
xanthine + NAD+ + H2O
urate + NADH
-
ping-pong reaction mechanism
-
r
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
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
-
subtilisin treatment leads to an active component I of 120000 kDa
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
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
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
only present as stable dehydrogenase from, no conversion to the oxidase form
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
100% activity
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
NAD+-linked activity, very low activity towards molecular oxygen
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
75% of the activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
r
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
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
67% of the activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
61% of the activity compared to hypoxanthine
91% urate formed
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
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+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
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+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
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+
-
-
-
?
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+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
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+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
-
-
-
?
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 + ?
-
-
-
?
xanthine + nitroblue tetrazolium + H2O
urate + ?
-
32% of the activity compared to methyl viologen as electron acceptor
-
?
xanthine + nitroblue tetrazolium + H2O
urate + ?
-
-
-
?
xanthine + nitroblue tetrazolium + H2O
urate + ?
-
-
-
?
xanthine + nitroblue tetrazolium + H2O
urate + ?
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
no production of H2O2
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
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+
-
low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
low activity
-
r
xanthine + O2 + H2O
urate + O2- + 2 H+
-
very low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
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+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
very low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
4% of the activity compared to xanthine-NAD+
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
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+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
no production of H2O2
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
very low activity
-
?
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 + ?
-
-
-
r
xanthine + phenazine methosulfate + H2O
urate + ?
-
5fold higher activity compared to NAD+ as electron acceptor
-
?
xanthine + phenazine methosulfate + H2O
urate + ?
-
-
-
?
xanthine + phenazine methosulfate + H2O
urate + ?
-
-
-
?
xanthine + thio-NAD+ + H2O
urate + thio-NADH
-
-
-
?
xanthine + thio-NAD+ + H2O
urate + thio-NADH
-
same activity compared to NAD+
-
r
xanthine + trinitrobenzenesulfonate + H2O
urate + ?
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
-
-
?
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. 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 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
?
-
-
xanthine oxidoreductase is a regulator of adipogenesis and of nuclear recptor PPARgamma activityand is essential for the regulation of fat accretion
-
-
?
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
?
-
-
NAD+ is the most effcient electron acceptor, followed by 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyl-2H-tetrazolium chloride and ferricyanide
-
-
?
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
?
-
-
NAD+ is the most effcient electron acceptor, followed by 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyl-2H-tetrazolium chloride and ferricyanide
-
-
?
additional information
?
-
-
major function of enzyme in liver parenchymal and sinusoidal cells is the 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
?
-
-
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
?
-
-
enzyme inhibition by orange juice and hesperetin participates in preventing oxidative stress by enhancing total antioxidant capacity and decreasing lipid peroxidation, overview
-
-
?
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, 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
?
-
purified recombinant wild-type and DELTAC mutant enzymes both exhibit mostly xanthine oxidase activity
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
xanthine and 2-hydroxy-6-methylpurine are substrates. Substrate binding structures, overview
-
-
?
additional information
?
-
ionized Glu232 of wild-type enzyme plays an important role in catalysis by discriminating against the monoanionic form of xanthine
-
-
?
additional information
?
-
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
-
-
?
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
?
-
-
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
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
?
6,8-dihydroxypurine + NAD+ + H2O
urate + NADH
-
-
18% urate formed
?
6,8-dihydroxypurine + O2
? + H2O2
-
-
-
?
guanine + NAD+ + H2O
? + NADH
-
81.3% of the activity compared to hypoxanthine
-
?
hypoxanthine + 2 NAD+ + 2 H2O
urate + 2 NADH + 2 H+
hypoxanthine + NAD+ + 2 H2O
urate + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
hypoxanthine + NADH
? + NO2- + NAD+
-
0.1% of the xanthine oxidation rate
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
hypoxanthine + O2
xanthine + H2O2
hypoxanthine + urate
xanthine + 6,8-dihydroxypurine
-
oxygen-free assay
-
r
NADPH + O2
NADP+ + O2- + H+
-
high NADPH oxidase activity
-
?
purine + NAD+ + H2O
8-hydroxypurine + NADH + H+
-
-
-
?
purine + NAD+ + H2O
? + NADH
purine + NADP+ + H2O
? + NADPH
-
60% of the activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
xanthine + NAD+ + H2O
urate + NADH + H+
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
xanthine + NADP+ + H2O
urate + NADPH
xanthine + O2
hypoxanthine + ?
-
dismutation reaction
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
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
?
-
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
-
?
hypoxanthine + 2 NAD+ + 2 H2O
urate + 2 NADH + 2 H+
-
-
-
-
?
hypoxanthine + 2 NAD+ + 2 H2O
urate + 2 NADH + 2 H+
-
-
-
?
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
-
-
-
?
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
-
-
-
r
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
more rapidly oxidized than xanthine
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
preferred substrate
-
ir
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
preferred substrate
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
-
-
-
?
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 + O2
xanthine + H2O2
-
very low activity
-
?
hypoxanthine + O2
xanthine + H2O2
-
-
-
?
purine + NAD+ + H2O
? + NADH
-
-
-
?
purine + NAD+ + H2O
? + NADH
-
poor substrate
-
?
purine + NAD+ + H2O
? + NADH
-
poor substrate
-
?
purine + NAD+ + H2O
? + NADH
-
poor substrate
-
?
purine + NAD+ + H2O
? + NADH
-
poor substrate
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
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 + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
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
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
involved in pteridine metabolism, 40% of activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
only dehydrogenase type D present
-
?
xanthine + NAD+ + H2O
urate + NADH
-
ping-pong reaction mechanism
-
r
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
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
-
-
-
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
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
-
-
-
r
xanthine + NAD+ + H2O
urate + NADH
-
only present as stable dehydrogenase from, no conversion to the oxidase form
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
NAD+-linked activity, very low activity towards molecular oxygen
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
75% of the activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
r
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
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
67% of the activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
61% of the activity compared to hypoxanthine
91% urate formed
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
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+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
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+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
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+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
-
-
-
?
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 + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
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+
-
low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
low activity
-
r
xanthine + O2 + H2O
urate + O2- + 2 H+
-
very low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
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+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
very low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
4% of the activity compared to xanthine-NAD+
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
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+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
very low activity
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
presence of ferredoxin enhances rate of oxygen reduction
-
?
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
?
-
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
?
-
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
?
-
-
xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
-
-
?
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 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
?
-
-
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
?
-
xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
-
-
?
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. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms
-
-
?
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
?
-
-
major function of enzyme in liver parenchymal and sinusoidal cells is the 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
?
-
-
enzyme inhibition by orange juice and hesperetin participates in preventing oxidative stress by enhancing total antioxidant capacity and decreasing lipid peroxidation, overview
-
-
?
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, 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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
FMN
-
primarily flavin cofactor
heme
-
ferricyanide-linked activity, no FAD
molybdopterin cytosine dinucleotide
localized in subunit PaoC
[4Fe-4S]-center
cluster is anchored to an additional 40 residues subdomain of subunit PaoB
FAD
-
-
FAD
-
1 mol per mol of subunit
FAD
1 mol per mol of subunit
FAD
-
2 mol per mol enzyme
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
-
one FAD per hemimolecule
FAD
-
generally viewed as the site at which NADH reacts
FAD
-
substitutions G348E, G353D, S357F located within the flavin/NAD+/NADH-domain
FAD
-
one FAD per subunit, central 40 kDa FAD-domain
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
-
0.9 mol per subunit
FAD
-
1.0-1.1 molecules per alphabeta protomer
FAD
a molybdenum-iron-flavoenzyme
FAD
-
the FAD cofactor is open to solvent in XO, but much less accessible in XDH, binding site structure, overview
FAD
a molybdenum-iron-flavoenzyme, activity-to-flavin ratio of 8 with xanthine as substrate and NAD+ as final electron acceptor, recombinant enzyme
FAD
role of Asp428 in the FAD reactivity, overview
FAD
subunit PaoB exhibits a typical FAD binding motif
FAD
a molybdenum-containing flavoenzyme
FAD
-
a molybdenum-containing flavoprotein
FAD
-
a molybdenum-containing flavoprotein
FAD
-
a molybdenum-containing flavoprotein
FAD
-
a molybdenum-containing flavoprotein
FAD
-
a molybdenum-containing flavoprotein
FAD
-
a molybdenum-containing flavoprotein
FAD
-
a molybdenum-containing flavoprotein
FAD
-
a molybdenum-containing flavoprotein
FAD
-
a molybdenum-containing flavoprotein
FAD
-
a molybdenum-containing flavoprotein
FAD
-
a molybdenum-containing flavoprotein
FAD
-
a molybdenum-containing flavoprotein
FAD
-
a molybdenum-containing flavoprotein
FAD
a molybdenum-containing flavoprotein
FAD
a molybdenum-containing flavoprotein
FAD
-
a molybdenum-containing flavoprotein
FAD
-
a molybdenum-containing flavoprotein
FAD
one FAD per enzyme molecule
ferricyanide
-
does not act with NAD+ or NADP+
ferricyanide
-
specific xanthine oxidizing activity
flavin
-
-
molybdenum cofactor
-
molybdenum cofactor
-
the enzyme contains molybdenum cofactor comprising only molybdopterin and molybdenum
molybdenum cofactor
-
binding involves residues GluB730, GlnA102, CysA103, CysA106, CysA134, and CysA13 of the alpha and beta subunits
molybdenum cofactor
C-terminal
molybdenum cofactor
-
molybdenum-containing enzyme
molybdenum cofactor
-
structure-function analysis, mechanism, overview
molybdenum cofactor
-
structure-function analysis, mechanism, overview
molybdenum cofactor
-
structure-function analysis, mechanism, overview
molybdenum cofactor
-
structure-function analysis, mechanism, overview
molybdenum cofactor
-
structure-function analysis, mechanism, overview
molybdenum cofactor
-
cofactor geometry, overview
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
a molybdenum-containing flavoprotein
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
a molybdenum-containing flavoprotein, biosynthesis of sulfurated molybdenum cofactor, overview
molybdenum cofactor
-
MoCo, the metal ion binds a molybdopterin (MPT) molecule via its dithiolene function and terminal sulfur and oxygen groups
molybdopterin
-
enzyme contains molybdopterin
molybdopterin
0.09 molecules per subunit
molybdopterin
-
0.62 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
molybdopterin
cofactor geometry, overview
molybdopterin
one molybdopterin per enzyme molecule
molybdopterin
protein contains a molybdopterin-binding domain
NAD+
-
-
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+
-
cannot be replaced by NADP+
NAD+
-
cannot be replaced by NADP+
NAD+
-
cannot be replaced by NADP+
NAD+
-
cannot be replaced by NADP+
NAD+
-
physiological cofactor
NAD+
-
activity different from ferricyanide-linked activity
NAD+
NAD+ inhibits NADH oxidase activity of AtXDH1
NADH
-
-
NADH
-
reduces xanthine oxidase to reductase activity
NADH
suppresses NAD+-dependent xanthine oxidation
NADH
crystal structures of the NAD(H) complexes of XDH reveal that, given the proper oxidation states, the nicotinamide rings of the dinucleotides locate at van der Waals distance to the flavin ring
NADP+
-
-
NADP+
-
40% of the activity compared to NAD+
NADP+
-
11% of the activity compared to NAD+
[2Fe-2S] cluster
-
-
[2Fe-2S] cluster
two N-terminal non-identical iron-sulfur clusters of the [2Fe-2S]-type
[2Fe-2S]-center
-
-
[2Fe-2S]-center
iron-sulfur subunit PaoA can be divided into two subdomains, each carrying one [2Fe-2S] cluster
[2Fe-2S]-center
two nonidentical [2Fe-2S] clusters designated as Fe/SI and Fe/SII, distinguished by redox potential and EPR signal
[2Fe-2S]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
protein contains 2 2Fe-2S iron-sulfur-cluster-binding domains
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
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
-
iron-containing flavoprotein
-
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
-
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
-
molar ratio of FAD to iron to labile sulfide per mol enzyme is 2 : 14 : 2
-
additional information
-
one molybdopterin-cofactor, two Fe2-S2-cluster, one FAD per subunit
-
additional information
-
molybdoironflavoprotein: 1 : 1 : 4 ratio of molybdenum to FAD to iron
-
additional information
-
molybdoironflavoprotein: ratio of iron to FAD to molybdenum is 4 : 1 : 1
-
additional information
-
cofactor compostion similar to eukaryotic enzymes
-
additional information
-
non-heme flavoprotein
-
additional information
-
molybdoironflavoprotein: ratio of 2 : 1.4 : 7.6 of FAD to molybdenum to Fe-S
-
additional information
-
both NAD+ and NADH compete for the same binding site
-
additional information
both NAD+ and NADH compete for the same binding site
-
additional information
-
cofactor conformation, binding structure analysis and mechanism, overview
-
additional information
cofactor conformation, binding structure analysis and mechanism, overview
-
additional information
-
cofactor domain amino acid sequence comparisons, overview
-
additional information
-
cofactor domain amino acid sequence comparisons, overview
-
additional information
-
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
-
additional information
-
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
-
additional information
-
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
-
additional information
-
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
-
additional information
-
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
-
additional information
-
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
-
additional information
-
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
-
additional information
-
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
-
additional information
-
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
-
additional information
-
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
-
additional information
-
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
-
additional information
-
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
-
additional information
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
-
additional information
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
-
additional information
-
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species. Rhodobacter capsulatus alpha2beta2 XDH arranges the FAD and [2Fe-2S] domains and the Moco domain into 2 separate subunits
-
additional information
the purified wild-type XDH contains 2.80 iron, 0.94 FAD, and 0.72 Moco per (alphabeta)2 tetrameric subunit, Split178 has 2.73 iron, 0.95 FAD, and 0.70 Moco per (alphabetagamma)2 hexameric subunit, while Split166 incorporates 3.51 iron, 0.95 FAD, and 0.95 Moco per (alphabetagamma)2 hexamer
-
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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-(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
2-amino-4-hydroxypterin
-
substrate inhibition above 0.01 mM
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-chloromercuriphenyl sulfonic acid
-
98% inhibition at 0.001 mM
4-hydroxypyrazolo(3,4-d)pyrimidine
5,5-dithiobis-(2-nitrobenzoate)
6-chloro-2-[3-(4-hydroxyphenyl)-1-phenyl-1-H-pyrazol-4-yl]-chromen-4-one
6-chloro-7-methyl-2-[3-(4-chlorophenyl)-1-phenyl-1-H-pyrazol-4-yl]-chromen-4-one
6-Mercaptopurine
-
90% inhibition of hypoxanthine-NADP+-activity at 1 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
Ag2+
-
complete inhibition of hypoxanthine oxidation at 0.01 mM
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
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
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
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
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
Leucopterin
-
competitive inhibition of xanthopterin oxidation, Ki: 0.0109 mM
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
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
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
p-hydroxymercuribenzoate
strong
pterin-6-aldehyde
competitive inhibition pattern, mechanism of inhibitor binding at the active site, overview
pyridoxal
-
Ki for 2-amino-4-hydroxypterine oxidation: 0.08 mM at 30 and 50°C, competitive; Ki for xanthine oxidation: 0.05 mM at 30°C, 0.11 mM at 50°C, competitive
Quinacrine
-
29.7% inhibition of hypoxanthine oxidation at 1 mM
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
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-Iodosobenzoic acid
-
effective inhibition of xanthine and pterine oxidation
2-Iodosobenzoic acid
-
50% inhibition at 0.0025 mM of NAD+-dependent activity by enzyme inactivation, not by conversion to the O2-dependent activity
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-hydroxymercuribenzoate
-
effective inhibition of xanthine and pterine oxidation
4-hydroxymercuribenzoate
-
76% inhibition of xanthine-NAD+-activity at 0.002 mM
4-hydroxypyrazolo(3,4-d)pyrimidine
-
i.e. allopurinol; rapid inactivation under anaerobic conditions at 0.1 mM
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; inhibition of pterine oxidation at 0.0003 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
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)
-
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)
-
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, 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-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-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
-
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
-
broad spectrum antifungal activity against Trichoderma viridae, Penicillium chrysogenum, Fusarium moniliformae, Microsporum cannis, Serratia marcescens, Staphylococcus aureus
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
adenine
-
competitive inhibition of xanthine oxidation, Ki: 0.13 mM
adenine
-
some non-competitive inhibition
adenine
-
96% inhibition of hypoxanthine-NADP+-activity at 1 mM
adenine
-
effective inhibition of xanthine oxidation at 0.001 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
adenine
-
competitive inhibition, Ki: 0.05 mM
adenine
-
62.8% inhibition of hypoxanthine oxidation at 0.5 mM
allopurinol
-
allopurinol
-
mechanism-based inhibitor. Allopurinol is oxidized by xanthine oxidoreductase itself to oxypurinol which forms a covalent bond with the reduced molybdenium atom
allopurinol
-
blocks xanthine dehydrogenase activity, without influencing xanthine oxidase activity
allopurinol
-
inhibits xanthine and hypoxanthine oxidation in vivo in intestine and pancreas, but enhances the activity in liver, tissue-dependent effects, overview
allopurinol
-
XOR activity in liver reduced by allopurinol treatment, no effect in kidney. Birds fed with inosine and allopurinol show lower total XOR activity in liver but no effect in kidney
allopurinol
-
inhibition of xanthine oxidoreductase also suppresses high tidal volume mechanical ventilation-induced alveolar apoptosis
allopurinol
-
treatment of normal fruit in linear phase of growth arrests fruit growth
allopurinol
-
0.1 mM, complete inhibition
allopurinol
-
shows strong enzyme inhibition and hypouricemic effect
allopurinol
i.e. 1-H-pyrazolo [3,4-d] pyrimidine-4-one
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
ammeline
-
competitive inhibition of xanthine oxidation Ki: 0.083 mM, uncompetitive inhibition of NADH oxidation Ki: 0.063 mM
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
-
inhibition of xanthine or pterine oxidation at 0.3 mM, diaphorase activity unaffected
arsenite
-
90% loss of the ferricyanide-linked activity in the presence of 1.78 mM
diphenylen iodinium
-
-
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
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
KCN
-
irreversible inactivation
KCN
-
addition of selenide in the presence of dithionite reactivates the inhibited enzyme
KCN
-
complete inhibition of xanthine dehydrogenase activity, 70% reduction of diaphorase activity
KCN
-
cyanolyzable selenium, 75% inhibition at 15 mM
KCN
-
35% inhibition of pterine oxidation, 60% inhibition of diaphorase activity at 5 mM
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
-
37% inhibition at 1 mM
KCN
-
complete inhibition of hypoxanthine oxidation at 1 mM
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
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
methanol
-
develops inhibition during course of catalysis, enhanced inhibition in the presence of ferricyanide in the oxygen-dependent oxidation of xanthine
NADH
suppresses NAD+-dependent xanthine oxidation
NADH
-
partial reduction of dehydrogenase activity under anaeroboic conditions, oxidase activity more slowly reduced
NADH
-
inactivation closely related to associated diaphorase activity
NADH
-
varied substrate: xanthine, product inhibition, Ki 0.05 mM, varied substrate: NAD+, dead-end inhibition type, Ki 0.022 mM
NADH
-
accumulation of produced NADH inhibits activity to 50%
NADH
-
product inhibition
o-phenanthroline
-
50% inhibition at 5-15 mM
o-phenanthroline
-
19.5% inhibition of hypoxanthine oxidation at 10 mM
o-phenanthroline
-
12% inhibition of xanthine-NAD+-activity at 7.5 mM
oxypurinol
-
blocks xanthine dehydrogenase activity, without influencing xanthine oxidase activity
oxypurinol
-
complete inhibition at 0.004 mM
Salicylhydroxamic acid
-
82% inhibition of hypoxanthine oxidation at 2.5 mM
Salicylhydroxamic acid
-
71% inhibition of xanthine-NAD+-activity at 5 mM
Sodium dithionite
-
irreversible inactivation by reduction of xanthine dehydrogenase, no recovery after dithionite elimination
Sodium dithionite
-
reduction of enzyme
Sodium dithionite
-
reduction of enzyme
Urate
-
competitive inhibition of xanthine oxidation, Ki: 0.064 mM
Urate
-
varied substrate: xanthine, dead-end inhibition type, Ki 0.18 mM, varied substrate: NAD+, product inhibition, Ki 0.45 mM
Urate
-
inhibition of xanthine oxidation at 0.06 mM
Urate
-
competitive inhibition of xanthine dehydrogenase, Ki: 0.144 mM
Urate
-
36.6% inhibition of hypoxanthine oxidation at 0.5 mM
Urate
-
15% inhibition of xanthine-NAD+-activity
Urate
-
50% inhibition of xanthine oxidation at 0.5 mM
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
Urea
-
competitive inhibition of xanthine oxidation Ki: 0.28 M, uncompetitive inhibition of NADH oxidation Ki: 1 M
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
-
reduction of enzyme
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
additional information
-
NAD+ inhibits NADH-dependent superoxide formation of AtXDH1
-
additional information
NAD+ inhibits NADH-dependent superoxide formation of AtXDH1
-
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
-
no substrate inhibition
-
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0.021
2,6-dichloroindophenol
-
diaphorase activity
0.001 - 0.011
2-amino-4-hydroxypterin
0.102
3-acetylpyridine adenine dinucleotide+
-
NADH oxidation
0.021
3-acetylpyridine-adenine dinucleotide
-
xanthine oxidation
0.0258 - 1
4-hydroxypyrazolo(3,4-d)pyrimidine
0.0071
adenine
-
cosubstrate: NAD+
0.06 - 1.517
benzaldehyde
0.0041 - 0.5
hypoxanthine
0.44
methyl viologen
-
electron donor: xanthine
0.00083
methylene blue
-
electron donor: 2-amino-4-hydroxy-pterine
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
0.0018
Xanthopterin
-
cosubstrate: NAD+
additional information
?
-
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
0.0258
4-hydroxypyrazolo(3,4-d)pyrimidine
-
cosubstrate: NAD+
1
4-hydroxypyrazolo(3,4-d)pyrimidine
-
electron acceptor: 2,6-dichlorophenolindophenol
1
4-hydroxypyrazolo(3,4-d)pyrimidine
-
i.e. allopurinol
0.06
benzaldehyde
mutant R440H, pH 5.5, 22°C
0.129
benzaldehyde
wild-type, pH 5.5, 22°C
0.159
benzaldehyde
wild-type, pH 5.0, 22°C
0.204
benzaldehyde
mutant R440K, pH 5.5, 22°C
0.288
benzaldehyde
mutant R440H, pH 5.0, 22°C
0.307
benzaldehyde
wild-type, pH 4.5, 22°C
0.361
benzaldehyde
mutant R440K, pH 5.0, 22°C
0.396
benzaldehyde
mutant R440H, pH 4.5, 22°C
0.514
benzaldehyde
mutant R440H, pH 4.0, 22°C
0.52
benzaldehyde
mutant R440K, pH 4.5, 22°C
0.659
benzaldehyde
wild-type, pH 4.0, 22°C
1.517
benzaldehyde
mutant R440K, pH 4.0, 22°C
0.0809
DCPIP
-
pH 7.8, 25°C, mutants Q102A and Q102G
0.0823
DCPIP
-
pH 7.8, 25°C, wild-type enzyme
0.0041
hypoxanthine
-
electron acceptor: NAD+
0.0075
hypoxanthine
-
electron acceptor: nitroblue tetrazolium
0.0088
hypoxanthine
-
wild-type, pH 8.5, 25°C
0.018
hypoxanthine
-
pH 8.5
0.02
hypoxanthine
-
cosubstrate: NAD+
0.021
hypoxanthine
-
xanthine dehydrogenase activity
0.0451
hypoxanthine
-
co substrate: NAD+
0.047 - 0.079
hypoxanthine
-
measured in the pH range from 6 to 8.9, pH-independent Km
0.072
hypoxanthine
-
mutant R881M, pH 8.5, 25°C
0.21
hypoxanthine
-
electron acceptor: NADP+
0.29
hypoxanthine
-
cosubstrate: NAD+
0.5
hypoxanthine
-
electron acceptor: 2,6-dichlorophenolindophenol
0.00219
NAD+
-
pH 7.2, 25°C
0.0022
NAD+
-
oxidation of 2-amino-4-hydroxy-pterin
0.00252
NAD+
-
pH 7.2, 25°C
0.00274
NAD+
-
pH 7.2, 25°C
0.0033
NAD+
-
electron donor: 2-amino-4-hydroxypterine
0.00412
NAD+
-
pH 7.2, 25°C
0.0052
NAD+
DTT-treated C-terminally truncated enzyme mutant, pH 7.8, 25°C
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
0.028
NAD+
-
xanthine dehydrogenase activity
0.0328
NAD+
-
pH 7.8, 25°C, wild-type enzyme
0.033
NAD+
-
increased Km for mutant G353D, electron acceptor: pterin
0.036
NAD+
pH 8.5, 40°C, Split166 mutant
0.036
NAD+
pH 8.5, 40°C, Split178 mutant
0.0373
NAD+
-
pH 7.8, 25°C, mutant Q102G
0.04
NAD+
-
ping-pong reaction mechanism
0.0402
NAD+
-
pH 7.8, 25°C, mutant Q102A
0.044
NAD+
pH 8.5, 40°C, wild-type enzyme
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+
coexpression of genes xdhABC, conditions of high aeration, pH 7.8, 25°C
0.103
NAD+
-
wild-type, pH 7.8, 25°C
0.1065
NAD+
-
cosubstrate: hypoxanthine
0.113
NAD+
coexpression of genes xdhABC, conditions of low aeration, pH 7.8, 25°C
0.12
NAD+
-
cosubstrate: xanthine
0.124
NAD+
-
cosubstrate: xanthine
0.148
NAD+
coexpression of genes xdhAB, conditions of high aeration, pH 7.8, 25°C
0.156
NAD+
coexpression of genes xdhAB, conditions of low aeration, pH 7.8, 25°C
0.16
NAD+
-
electron donor: xanthine
0.16
NAD+
-
cosubstrate: hypoxanthine
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
0.0003
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, 25°C
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, 25°C
0.00714
xanthine
-
pH 7.2, 25°C
0.00774
xanthine
-
pH 7.2, 25°C
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, 25°C
0.012
xanthine
-
electron acceptor: oxygen
0.017
xanthine
-
electron acceptor: ferricyanide
0.017
xanthine
-
pH 7.9, increasing Km with increasing pH
0.018
xanthine
-
electron acceptor: NAD+, 30°C
0.0213
xanthine
-
pH 7.4, 37°C, mutant D430H, Vmax (micromol/min/mg): 7.47
0.02169
xanthine
-
pH 7.4, 37°C, wild-type, Vmax (micromol/min/mg): 7.74
0.02172
xanthine
-
pH 7.4, 37°C, mutant D431A, Vmax (micromol/min/mg): 8.52
0.02227
xanthine
-
pH 7.4, 37°C, mutant N352A, Vmax (micromol/min/mg): 7.69
0.0227
xanthine
-
pH 7.8, 25°C, mutant Q102G, with NAD+
0.02324
xanthine
-
pH 7.4, 37°C, mutant R427E, Vmax (micromol/min/mg): 7.75
0.0236
xanthine
-
cosubstrate: NAD+
0.024
xanthine
-
ping-pong reaction mechanism
0.02413
xanthine
-
pH 7.4, 37°C, mutant G47A, Vmax (micromol/min/mg): 7.91
0.029
xanthine
-
electron acceptors: phenazine methosulfate/cytochrome c
0.0293
xanthine
-
pH 7.8, 25°C, mutant Q102A, with NAD+
0.032
xanthine
-
electron acceptor: NAD+
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 30°C
0.039
xanthine
-
pH 7.4, 37°C, mutant K1230A, Vmax (micromol/min/mg): 4.02
0.04
xanthine
-
electron acceptor: NAD+, 50°C
0.0442
xanthine
-
pH 7.8, 25°C, wild-type enzyme, with NAD+
0.0508
xanthine
-
pH 7.4, 37°C, mutant S1227A, Vmax (micromol/min/mg): 3.94
0.055
xanthine
pH 8.5, 40°C, Split178 mutant
0.059
xanthine
-
increased Km in the presence of pyridoxal at 50°C
0.061
xanthine
-
wing preparation, cosubstrate: NAD+
0.064
xanthine
-
wild-type, pH 7.8, 25°C
0.06428
xanthine
-
pH 7.4, 37°C, mutant S360P, Vmax (micromol/min/mg): 2.83
0.0647
xanthine
-
body preparation, cosubstrate: NAD+
0.066
xanthine
-
electron acceptor: NAD+
0.066
xanthine
coexpression of genes xdhAB, conditions of high aeration, pH 7.8, 25°C
0.067
xanthine
-
electron acceptor: NADP+
0.067
xanthine
coexpression of genes xdhAB, conditions of low aeration, pH 7.8, 25°C
0.068
xanthine
pH 8.5, 40°C, wild-type enzyme
0.07
xanthine
-
cosubstrate
0.072
xanthine
-
mutant E803V, pH 8.5, 25°C
0.085
xanthine
coexpression of genes xdhABC, conditions of high aeration, pH 7.8, 25°C
0.096
xanthine
pH 8.5, 40°C, Split166 mutant
0.163
xanthine
-
mutant E232A, pH 7.8, 25°C
1.35
xanthine
-
electron acceptor: methyl viologen
80.09
xanthine
coexpression of genes xdhABC, conditions of low aeration, pH 7.8, 25°C
additional information
?
-
KM (mM) (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) (pH 7.4, 37°C), wild-type: 0.0582, mutant G47A: 0.06568, mutant N352A: 0.0601, mutant S360P: 0.09353, mutant R427E: 0.02086, mutant D430H: 0.06468, mutant D431A: 0.06129, mutant S1227A: 0.148, mutant K1230A: 0.162
-
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
-
Km-value is 0.0025 mg/ml xanthine
-
additional information
additional information
-
Km-value is 0.0025 mg/ml xanthine
-
additional information
additional information
-
Km-value is 0.0025 mg/ml xanthine
-
additional information
additional information
-
Km-value is 0.0025 mg/ml xanthine
-
additional information
additional information
-
Km-value is 0.0025 mg/ml xanthine
-
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
-
additional information
additional information
Michaelis-Menten steady-state kinetics, overview
-
additional information
additional information
steady-state kinetics and reductive half-reaction, stopped flow kinetics, kinetic analysis of wild-type and mutant xanthine dehydrogenases, overview. kred, the limiting rate constant for reduction at high [xanthine], is significantly compromised in the mutant variant E232Q, a result that is inconsistent with Glu232 being neutral in the active site of the wild-type enzyme. The ionized Glu232 of wild-type enzyme plays an important role in catalysis by discriminating against the monoanionic form of substrate, effectively increasing the pKa of the substrate by two pH units and ensuring that at physiological pH the neutral form of the substrate predominates in the Michaelis complex. The product release is principally rate-limiting in catalysis. The disparity in rate constants for the chemical step of the reaction and product release is not as great in the bacterial enzyme as compared with the vertebrate forms. The faster turnover observed with the bacterial enzyme isdue to a faster rate constant for product release than is seen with the vertebrate enzyme
-
additional information
additional information
steady-state kinetics of DTT-treated and untreated C-terminally truncated enzyme mutant
-
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evolution
-
the enzyme belongs to the xanthine oxidase family
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis. The page XDH sequence shows 100% identity to the genomic XDH genes of Acinetobacter baumannii. It seems plausible that the similarity is a result of horizontal gene transfer
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis. The unique industrially applicable Acinetobacter baumannii XDH shows only modest similarity to all the previous already-characterized XDHs
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
-
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
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
disruption of XDH by allopurinol or XDH1 by RNA interference significantly affect mosquito survival, causing a disruption in blood digestion, excretion, oviposition, and reproduction. XDH1-deficient mosquitoes show a persistence of serine proteases in the midgut at 48 h after blood feeding and a reduction in the uptake of vitellogenin by the ovaries. Analysis of the fat body from dsRNA-XDH1-injected mosquitoes fall into 2 groups: one group is characterized by a reduction of the XDH1 transcript, whereas the other group is characterized by an upregulation of several transcripts, including XDH1, glutamine synthetase, alanine aminotransferase, catalase, superoxide dismutase, ornithine decarboxylase, glutamate receptor, and ammonia transporter. Depletion of XDH1 activity is lethal to bloodfed mosquitoes. Silencing of XDH1 reduces protein expression and delays synthesis and excretion of nitrogen waste, XDH1 deficiency slows digestion, vitellogenesis, and oviposition, and reduces fecundity
malfunction
dysfunction of purine degradation is a result of knocking down the key enzyme xanthine dehydrogenase, leading to severely reduced survival of Arabidopsis thaliana under progressive drought conditions and to significantly decreased tolerance to superoxide-mediated oxidative stress. The enhanced stress sensitivity of the knockdown mutants likely results from defective stress responses, because the drought-induced accumulation of the cellular protectant proline is compromised in the knockdown plants, which also show lower mRNA levels of P5CS1, the gene encoding the rate-limiting enzyme for proline biosynthesis, DELTA1-pyrroline-5-carboxylate synthase 1
malfunction
RNAi silencing of XDH1 in ecotype Col-0 results in autofluorescent object formation and infiltration of allopurinol, an inhibitor of XDH. drf1 Mutants contain missense mutations in XDH1, whole-cell and haustorial complex-confined H2O2 is significantly reduced in the mutants compared with the parental line
malfunction
the powdery mildew fungus Golovinomyces cichoracearum triggers defense responses in Arabidopsis mediated by the R gene RPW8.2. In a screen for mutants defective in RPW8.2-related resistance to powdery mildew, three plants with point mutations in xanthine dehydrogenase 1 (XDH1), including two that alter residues strictly conserved among xanthine dehydrogenases. The mutants show impaired resistance to powdery mildew and accumulate less H2O2 in the haustorial complex in epidermal cells invaded by the fungus. These point mutations decrease the activity of recombinant XDH1 proteins, in terms of both dehydrogenase activity and ROS production. Xanthine accumulation in the mutants is further induced by pathogen inoculation due to increased purine catabolism (mediated at least in part by XDH1) upon infection. Feeding uric acid suppressed the H2O2 accumulation normally observed in mesophyll cells of infected xdh1 mutant plants
malfunction
-
dysfunction of purine degradation is a result of knocking down the key enzyme xanthine dehydrogenase, leading to severely reduced survival of Arabidopsis thaliana under progressive drought conditions and to significantly decreased tolerance to superoxide-mediated oxidative stress. The enhanced stress sensitivity of the knockdown mutants likely results from defective stress responses, because the drought-induced accumulation of the cellular protectant proline is compromised in the knockdown plants, which also show lower mRNA levels of P5CS1, the gene encoding the rate-limiting enzyme for proline biosynthesis, DELTA1-pyrroline-5-carboxylate synthase 1
-
malfunction
-
the powdery mildew fungus Golovinomyces cichoracearum triggers defense responses in Arabidopsis mediated by the R gene RPW8.2. In a screen for mutants defective in RPW8.2-related resistance to powdery mildew, three plants with point mutations in xanthine dehydrogenase 1 (XDH1), including two that alter residues strictly conserved among xanthine dehydrogenases. The mutants show impaired resistance to powdery mildew and accumulate less H2O2 in the haustorial complex in epidermal cells invaded by the fungus. These point mutations decrease the activity of recombinant XDH1 proteins, in terms of both dehydrogenase activity and ROS production. Xanthine accumulation in the mutants is further induced by pathogen inoculation due to increased purine catabolism (mediated at least in part by XDH1) upon infection. Feeding uric acid suppressed the H2O2 accumulation normally observed in mesophyll cells of infected xdh1 mutant plants
-
malfunction
-
RNAi silencing of XDH1 in ecotype Col-0 results in autofluorescent object formation and infiltration of allopurinol, an inhibitor of XDH. drf1 Mutants contain missense mutations in XDH1, whole-cell and haustorial complex-confined H2O2 is significantly reduced in the mutants compared with the parental line
-
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
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
metabolism
dual and opposing roles of XDH1 in reactive oxygen species metabolism, detailed overview
metabolism
-
dual and opposing roles of XDH1 in reactive oxygen species metabolism, detailed overview
-
physiological function
-
xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation
physiological function
-
xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation
physiological function
-
xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation
physiological function
-
xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation
physiological function
-
xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation
physiological function
xanthine 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
AtXDH1 is a key enzyme in purine degradation where it oxidizes hypoxanthine to xanthine and 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
physiological function
-
dual and opposing roles of XDH1 in reactive oxygen species metabolism, detailed overview. The enzyme's basic function is in purine catabolism, catalyzing the conversion of hypoxanthine to xanthine and xanthine to uric acid. In mammals, xanthine dehydrogenases, which use NAD+ as electron acceptor to produce uric acid, can be posttranslationally modified to become xanthine oxidases, which use O2 as electron acceptor to produce reactive oxygen species (ROS). Because uric acid is a scavenger of ROS, the resulting influence of xanthine dehydrogenase on ROS status is likely responsible for its importance in a remarkably wide range of processes in mammals, including immunity
physiological function
in leaf mesophyll cells, XDH1 carries out xanthine dehydrogenase activity to produce uric acid in local and systemic tissues to scavenge H2O2 from stressed chloroplasts, thereby protecting plants from stress-induced oxidative damage. XDH1-derived uric acid is essential for removing H2O2 from stressed chloroplasts in leaf mesophyll cells. XDH1 plays spatially specified dual and opposing roles in modulation of ROS metabolism during defense responses in Arabidopsis thaliana as xanthine dehydrogenase and as xanthine oxidase, EC 1.17.3.2. XDH1 is required for scavenging age-dependent and pathogen-induced H2O2 in chloroplasts. XDH1 plays opposing roles in H2O2 metabolism in Golovinomyces cichoracearum GcUCSC1 haustorium-affected epidermal and mesophyll cells. XDH1-derived H2O2 is also required for RPW8-dependent and -independent basal resistance
physiological function
isozyme XDH1 plays an essential role in Aedes aegypti vector control
physiological function
mammalian xanthine oxidoreductase can exist in both dehydrogenase and oxidase forms. The C-terminal peptide plays a role in the formation of an intermediate form during the transition between xanthine dehydrogenase and xanthine oxidase. Conversion between the two is implicated in such diverse processes as lactation, anti-bacterial activity, reperfusion injury and a growing number of diseases. The dehydrogenase-oxidase transformation occurs rather readily and the insertion of the C-terminal peptide into the active site cavity of its subunit stabilizes the dehydrogenase form. The intermediate form can be generated (e.g. in endothelial cells) upon interaction of the C-terminal peptide portion of the enzyme with other proteins or the cell membrane. Residues Cys535 and Cys992 are involved in the rapid phase and Cys1316 and Cys1324 in the slow phase of the modification reaction. The irreversible conversion of XDH to XOR by trypsin involves limited proteolysis at the same linker peptide. Triggering events, such as the formation of a disulfide bond between Cys535 and Cys992 or proteolysis of the linker, reorient Phe549 (also a part of the long linker), resulting in disruption of a four amino acid cluster. Arg426 is then released from the cluster and moves the A-loop that blocks the approach of NAD+ to the flavin ring of the FAD moiety, as well as changing the electrostatic environment
physiological function
plant xanthine dehydrogenases do not undergo a posttranslational modification, las in mammals becoming xanthine oxidases, which use O2 as electron acceptor to produce reactive oxygen species. Plant enzymes appear capable of using both O2 and NAD+ as electron acceptors, as well as of producing high levels of ROS. In leaf mesophyll cells, XDH1 carries out xanthine dehydrogenase activity to produce uric acid in local and systemic tissues to scavenge H2O2 from stressed chloroplasts, thereby protecting plants from stress-induced oxidative damage. XDH1-derived uric acid is essential for removing H2O2 from stressed chloroplasts in leaf mesophyll cells. XDH1 plays spatially specified dual and opposing roles in modulation of ROS metabolism during defense responses in Arabidopsis thaliana as xanthine dehydrogenase and as xanthine oxidase, EC 1.17.3.2. XDH1 is required for scavenging age-dependent and pathogen-induced H2O2 in chloroplasts. XDH1 activity appears to be important for RPW8.2-mediated powdery mildew resistance. XDH1 appears to be an important tool allowing plants to harness and direct the power of ROS
physiological function
role for purine metabolites in stress responses, supporting the possible contribution of purine degradation to plant acclimation to changing environments, overview
physiological function
xanthine dehydrogenase plays an important role in purine catabolism catalyzing the oxidative hydroxylation of hypoxanthine to xanthine and of xanthine to uric acid, it plays a role in recycling and remobilization of nitrogen, and XDH is implicated in plant stress responses and acclimation. Explicit function of VvXDH in conferring salt stress by increasing allantoin accumulation and activating abscisic acid signaling pathway, enhancing ROS scavenging in transgenic Arabidopsis thaliana. VvXDH application results in increased tolerance to abiotic stresses by elevating allantoin accumulation
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
physiological function
XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
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physiological function
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role for purine metabolites in stress responses, supporting the possible contribution of purine degradation to plant acclimation to changing environments, overview
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physiological function
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plant xanthine dehydrogenases do not undergo a posttranslational modification, las in mammals becoming xanthine oxidases, which use O2 as electron acceptor to produce reactive oxygen species. Plant enzymes appear capable of using both O2 and NAD+ as electron acceptors, as well as of producing high levels of ROS. In leaf mesophyll cells, XDH1 carries out xanthine dehydrogenase activity to produce uric acid in local and systemic tissues to scavenge H2O2 from stressed chloroplasts, thereby protecting plants from stress-induced oxidative damage. XDH1-derived uric acid is essential for removing H2O2 from stressed chloroplasts in leaf mesophyll cells. XDH1 plays spatially specified dual and opposing roles in modulation of ROS metabolism during defense responses in Arabidopsis thaliana as xanthine dehydrogenase and as xanthine oxidase, EC 1.17.3.2. XDH1 is required for scavenging age-dependent and pathogen-induced H2O2 in chloroplasts. XDH1 activity appears to be important for RPW8.2-mediated powdery mildew resistance. XDH1 appears to be an important tool allowing plants to harness and direct the power of ROS
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physiological function
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in leaf mesophyll cells, XDH1 carries out xanthine dehydrogenase activity to produce uric acid in local and systemic tissues to scavenge H2O2 from stressed chloroplasts, thereby protecting plants from stress-induced oxidative damage. XDH1-derived uric acid is essential for removing H2O2 from stressed chloroplasts in leaf mesophyll cells. XDH1 plays spatially specified dual and opposing roles in modulation of ROS metabolism during defense responses in Arabidopsis thaliana as xanthine dehydrogenase and as xanthine oxidase, EC 1.17.3.2. XDH1 is required for scavenging age-dependent and pathogen-induced H2O2 in chloroplasts. XDH1 plays opposing roles in H2O2 metabolism in Golovinomyces cichoracearum GcUCSC1 haustorium-affected epidermal and mesophyll cells. XDH1-derived H2O2 is also required for RPW8-dependent and -independent basal resistance
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additional information
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active site structure, overview
additional information
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biofilm formation is stimulated in the presence of uric acid, Se, and Mo and inhibited by auranofin or tungstate
additional information
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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
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
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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
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
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analysis of the mechanism of transfer of an oxygen atom to the substrate
additional information
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Glu802 binds the substrate and stabilizes the transition state, Glu1261 is the catalytic base, Arg880 and Thr1010 bind the substrate and decrease the reaction activation energy, Phe914 and Phe1009 orientate the substrate via pi-pi stacking, Val1011 is the key residue channeling the substrate, and Gln758 is responsible for releasing the product. There is an obvious variation of key residues channeling the substrate and binding pocket, which affect the substrate entry and product release, resulting in different catalytic activity and enzymatic properties. Surprisingly, the 2 pairs of cysteines, C535 and C992, and C1316 and C1324 numbering in bovine XDH, which are proposed to control the reversible post-translational conversion from XDH to XOD, EC 1.17.3.2, by forming 2 cysteine disulfide bonds, are totally absent in other XDHs. Bovine milk XDH can be converted reversibly into active XOD form by forming disulfide bond or irreversibly by limited proteolysis, overview
additional information
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rat liver XDH can be converted reversibly into active XOD form by forming disulfide bond or irreversibly by limited proteolysis, overview
additional information
the Arabidopsis thaliana XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
additional information
the biosynthesis of functionally active XDH is a multi-step process requiring a series of helper proteins to aid the formation of cofactors and apoproteins and their ordered assembly, in vivo biosynthetic mechanism of active xanthine dehydrogenase in schematic overview. NifS is a cysteine desulfurase, which catalyzes the sulfur transfer from L-cysteine to Moco to form Mo-S bond. Chaperone XDHC binds stoichiometric amount of Moco as a scaffold protein, interacts with NifS for the sulfuration of Moco, protects sulfurated Moco from oxidation, and further transfers to XDH
additional information
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the chicken XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
additional information
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the Rhodobacter capsulatus XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
additional information
XDH active site structure with conserved Glu232 and Arg310 residues. Analysis of crystal structure of xanthine dehydrogenase, PDB ID 2W3S, where an ionized glutamate 802/232 acts as a hydrogen bonding acceptor from the substrate N3 nitrogen
additional information
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the Rhodobacter capsulatus XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
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additional information
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the biosynthesis of functionally active XDH is a multi-step process requiring a series of helper proteins to aid the formation of cofactors and apoproteins and their ordered assembly, in vivo biosynthetic mechanism of active xanthine dehydrogenase in schematic overview. NifS is a cysteine desulfurase, which catalyzes the sulfur transfer from L-cysteine to Moco to form Mo-S bond. Chaperone XDHC binds stoichiometric amount of Moco as a scaffold protein, interacts with NifS for the sulfuration of Moco, protects sulfurated Moco from oxidation, and further transfers to XDH
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E1297A
site-directed mutagenis
E831A
site-directed mutagenis
G48D
naturally occuring mutation, drf mutant, missense mutation G143A, i.e. drf1-1 or xdh1-3
G48D/R941Q/T1061I
naturally occuring mutation, identification of 15 potential drf mutants, drf1 mutants contain missense mutations in XDH1, the mutant phenotypes cosegregate with a single missense mutation G143A. Targeted sequencing of XDH1 revealed missense mutations G2822A (resulting in R941Q) and C3182T (resulting in T1061I) in the remaining two mutants, respectively. Identification of a knockout mutant GK-049D04, i.e. xdh1-2, and of knockdown allele in SALK_148364 where a T-DNA is inserted in the 11th intron of XDH1, i.e. xdh1-1. Defense phenotypes of drf mutants, general phenotypes, overview. The loss-of-function single and double mutant lines for atrobhD and atrbohF and the eds1-2 null allele in the Col-0 background are crossed with xdh1-2 to make xdh1 rbohD and xdh1 rbohF, xdh1 eds1 double, and xdh1 rbohD rbohF triple mutant lines
R909A
site-directed mutagenis
R941Q
naturally occuring mutation, drf mutant, missense mutation G2822A, i.e. drf1-2 or xdh1-4
T1061I
naturally occuring mutation, drf mutant, missense mutation C3182T, i.e. drf1-3 or xdh1-5
W364A
site-directed mutagenis
Y421A
site-directed mutagenis
G48D
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naturally occuring mutation, drf mutant, missense mutation G143A, i.e. drf1-1 or xdh1-3
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G48D/R941Q/T1061I
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naturally occuring mutation, identification of 15 potential drf mutants, drf1 mutants contain missense mutations in XDH1, the mutant phenotypes cosegregate with a single missense mutation G143A. Targeted sequencing of XDH1 revealed missense mutations G2822A (resulting in R941Q) and C3182T (resulting in T1061I) in the remaining two mutants, respectively. Identification of a knockout mutant GK-049D04, i.e. xdh1-2, and of knockdown allele in SALK_148364 where a T-DNA is inserted in the 11th intron of XDH1, i.e. xdh1-1. Defense phenotypes of drf mutants, general phenotypes, overview. The loss-of-function single and double mutant lines for atrobhD and atrbohF and the eds1-2 null allele in the Col-0 background are crossed with xdh1-2 to make xdh1 rbohD and xdh1 rbohF, xdh1 eds1 double, and xdh1 rbohD rbohF triple mutant lines
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R941Q
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naturally occuring mutation, drf mutant, missense mutation G2822A, i.e. drf1-2 or xdh1-4
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T1061I
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naturally occuring mutation, drf mutant, missense mutation C3182T, i.e. drf1-3 or xdh1-5
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G1011E
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within the molybdenum domain, no activity without oxidative activation
G353D
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modifications to the NAD+-NADH-binding sites
S357F
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modifications to the NAD+-NADH-binding sites
R40K
mutation in subunit PaoC, strong decrease in activity
R440H
mutation in subunit PaoC, strong decrease in activity, crystallization data
C535A
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resistant to conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine
C992R
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resistant to conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine
W335A/F336L
mutant oxidoreductase displaying xanthine oxidase activity
C134A/C136A
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site-directed mutagenesis, an inactive subunit A mutant
C44A/C47A
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site-directed mutagenesis, an instable subunit A mutant that cannot be purified
E220R/D517R
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site-directed mutagenesis, a subunit B mutant that is mainly dimeris incontrast to the tetrameric wild-type enzyme, inactive mutant
E232Q
site-directed mutagenesis, kred, the limiting rate constant for reduction at high [xanthine], is significantly compromised in the mutant variant E232Q, the mutant exhibits a 12fold decrease in kred, a result that is inconsistent with Glu232 being neutral in the active site of the wild-type enzyme
E730D
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no enzymic activity
E730Q
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no enzymic activity
E730R
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no enzymic activity
EB232Q
catalytically inactive active site mutant, inactive desulfo enzyme form
Q102A
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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
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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
Q179A
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crystal structure determination and analysis, comparison with wild-type enzyme structure, a similar acidic pK for the wild-type and Q179A variants, as well as the metrical parameters of the Mo site and density functional theory calculations, suggested protonation at the equatorial oxo group. Oxidized wild-type and mutant Q179A reveal a similar Mo(VI) ion with each one molybdopterin, Mo=O, Mo-O-, and Mo=S ligand, and a weak Mo-O(E730) bond at alkaline pH
R135C
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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
R330M
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the activity with substrate 2-hydroxy-6-methylpurine is only slightly affected
D430H
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Km (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) slightly increased compared to wild-type, Vmax (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) decreased compared to wild-type, Km (xanthine) slightly decreased compared to wild-type, Vmax (xanthine) slightly decreased to wild-type
D431A
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Km (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) slightly increased compared to wild-type, Vmax (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) increased compared to wild-type, Km (xanthine) slightly increased compared to wild-type, Vmax (xanthine) increased to wild-type
G47A
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Km and Vmax (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) increased compared to wild-type, Km and Vmax (xanthine) slightly increased compared to wild-type
K1230A
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Km (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) 2.5fold increased compared to wild-type, Vmax (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) decreased compared to wild-type, Km (xanthine) 2fold increased compared to wild-type, Vmax (xanthine) 2fold decreased to wild-type
N352A
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Km (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) slightly increased compared to wild-type, Vmax (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) slightly decreased compared to wild-type, Km (xanthine) slightly increased compared to wild-type, Vmax (xanthine) slightly decreased compared to wild-type
R427E
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Km (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) decreased compared to wild-type, Vmax (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) decreased compared to wild-type, Km (xanthine) slightly increased compared to wild-type, Vmax (xanthine) comparable to wild-type
S1227A
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Km (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) 2.5fold increased compared to wild-type, Vmax (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) decreased compared to wild-type, Km (xanthine) 2fold increased compared to wild-type, Vmax (xanthine) 2fold decreased to wild-type
S360P
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Km (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) increased compared to wild-type, Vmax (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) decreased compared to wild-type, Km (xanthine) 3fold increased compared to wild-type, Vmax (xanthine) 3fold decreased compared to wild-type
E89K
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E89K
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natural mutant strain, lacking iron-sulfur centers, activity to xanthine/NAD+ or xanthine/pterin not affected, but xanthine/phenazine methosulfate activity abolished
E803V
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almost complete loss of activity with hypoxanthine, weak activity with xanthine, significant aldehyde oxidase activity
E803V
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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
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almost complete loss of activity with xanthine, weak activity with hypoxanthine, significant aldehyde oxidase activity
R881M
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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
C535A/C992R
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slow conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine, conversion is blocked by NADH
C535A/C992R
site-directed mutagenesis, the mutant activity in the presence of sulfhydryl residue modifiers is very low
C535A/C992R/C1316S
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completely resistant to conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine
C535A/C992R/C1316S
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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/C1316S
site-directed mutagenesis, the triple mutant does not undergo conversion from XOR, EC 1.17.3.2, to XDH, EC 1.17.1.4, at all
C535A/C992R/C1324S
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completely resistant to conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine
C535A/C992R/C1324S
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an XDH-locked enzyme mutant that cannot be induced by sulfhydryl reagents to adopt the XO form
C535A/C992R/C1324S
site-directed mutagenesis, the triple mutant does not undergo conversion from XOR, EC 1.17.3.2, to XDH, EC 1.17.1.4, at all
E232A
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decrease in kcat value, increase in KM-value
E232A
site-directed mutagenesis, the mutant exhibits a 12fold decrease in kred compared to wild-type
E730A
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no enzymic activity
E730A
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crystal structure determination and analysis, comparison with wild-type enzyme structure, the sulfido is replaced with an oxo ligand in the inactive E730A mutant, further showing another oxo and one Mo-OH ligand at Mo, which are independent of pH
R310K
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absorption spectra similar to wild-type. 20fold decrease of kred-value
R310K
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kred, the limiting rate of enzyme reduction by substrate at high substrate concentration is 20-fold decreased
R310M
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absorption spectra similar to wild-type. 20000fold decrease of kred-value
R310M
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kred, the limiting rate of enzyme reduction by substrate at high substrate concentration is 20000-fold decreased
additional information
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T-DNA insertion mutant, loss of superoxide producing activity
additional information
generation of XDH-knockdown mutants, analysis of compromised drought-stress responses of proline biosynthesis in Arabidopsis thaliana XDH-knockdown mutants, phenotype, overview
additional information
the powdery mildew fungus Golovinomyces cichoracearum triggers defense responses in Arabidopsis mediated by the R gene RPW8.2. In a screen for mutants defective in RPW8.2-related resistance to powdery mildew, three plants with point mutations in xanthine dehydrogenase 1 (XDH1), including two that alter residues strictly conserved among xanthine dehydrogenases. The mutants show impaired resistance to powdery mildew and accumulate less H2O2 in the haustorial complex in epidermal cells invaded by the fungus. These point mutations decrease the activity of recombinant XDH1 proteins, in terms of both dehydrogenase activity and ROS production
additional information
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generation of XDH-knockdown mutants, analysis of compromised drought-stress responses of proline biosynthesis in Arabidopsis thaliana XDH-knockdown mutants, phenotype, overview
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additional information
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the powdery mildew fungus Golovinomyces cichoracearum triggers defense responses in Arabidopsis mediated by the R gene RPW8.2. In a screen for mutants defective in RPW8.2-related resistance to powdery mildew, three plants with point mutations in xanthine dehydrogenase 1 (XDH1), including two that alter residues strictly conserved among xanthine dehydrogenases. The mutants show impaired resistance to powdery mildew and accumulate less H2O2 in the haustorial complex in epidermal cells invaded by the fungus. These point mutations decrease the activity of recombinant XDH1 proteins, in terms of both dehydrogenase activity and ROS production
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additional information
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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
additional information
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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
additional information
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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
additional information
construction of a variant of the rat liver enzyme that lacks the C-terminal amino acids 1316-1331. The mutant enzymes appears to assume an intermediate form, exhibiting a mixture of dehydrogenase and oxidase activities. The purified mutant protein retains about 50-70% of oxidase activity even after prolonged dithiothreitol treatment. The C-terminal region plays a role in the dehydrogenase to oxidase conversion. In the crystal structure of the protein variant, most of the enzyme stays in an oxidase conformation. But after 15 min of incubation with a high concentration of NADH, the corresponding X-ray structures show a dehydrogenase-type conformation. On the other hand, disulfide formation between Cys535 and Cys992, which can clearly be seen in the electron density map of the crystal structure of the mutant after removal of dithiothreitol, goes in parallel with the complete conversion to oxidase, resulting in structural changes identical to those observed upon proteolytic cleavage of the linker peptide
additional information
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. Macroporous ITO electrodes are used as an immobilization platform for the fabrication of HX-sensitive electrodes. The efficient polymer/enzyme interaction can be advantageously combined with the open structure of an electrode material of controlled pore size, resulting in good processability, stability, and defined signal transfer in the presence of a substrate. Method development and evaluation, overview
additional information
succesfull mechanism-based metabolic engineering of Escherichia coli strain BL21(DE3) cell factory for production of functionally active, highly-producing xanthine dehydrogenase by co-overexpression of enzyme XDH from Rhodobacter capsulatus with three global regulators (IscS, TusA and NarJ) and four chaperone proteins (DsbA, DsbB, NifS and XdhC) to aid the formation and ordered assembly of three redox center cofactors of Rhodobacter capsulatus XDH in Escherichia coli. NifS is a cysteine desulfurase, which catalyzes the sulfur transfer from L-cysteine to Moco to form Mo-S bond. Chaperone XDHC binds stoichiometric amount of Moco as a scaffold protein, interacts with NifS for the sulfuration of Moco, protects sulfurated Moco from oxidation, and further transfers to XDH, method devlopment, overview. Three helper proteins, NifS, IscS and DsbB improve the specific activity of RcXDH significantly by 30%, 94% and 49%, respectively. The combination of NifS and IscS synergistically increases the specific activity by 1.29fold, and enhances the total enzyme activity by an impressive 3.9fold
additional information
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the enzyme mutants show alterations in the Mo site structure, which changes in a pH range of 5-10, and in the influence of amino acids (Glu730 and Gln179) close to molybdenum cofactor in wild-type, and Q179A and E730A mutants, enzyme kinetics and quantum chemical studies, overview
additional information
two (alphabetagamma)2 XDH variants, Split166 and Split178, are designed and constructed by splitting the small subunit (alphabeta)2 XDH at the N- and C-terminal ends of the L167-A178 peptide linking the iron-sulfur clusters and flavin adenine dinucleotide domains, respectively. Subunit composition of recombinant wild-type and split XDHsAs, overview. As for the co-substrate NAD+, mutant Split178 has a 1.07fold increased catalytic efficiency, while Split166 has a 3.8fold decreased catalytic efficiency compared to the wild-type XDH, for the substrate xanthine, the Split178 variant shows 1.21fold increased turnover number and 1.66fold increased catalytic efficiency, while the mutant Split166 shows a 4.31fold decrease in comparison to the wild-type enzyme
additional information
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succesfull mechanism-based metabolic engineering of Escherichia coli strain BL21(DE3) cell factory for production of functionally active, highly-producing xanthine dehydrogenase by co-overexpression of enzyme XDH from Rhodobacter capsulatus with three global regulators (IscS, TusA and NarJ) and four chaperone proteins (DsbA, DsbB, NifS and XdhC) to aid the formation and ordered assembly of three redox center cofactors of Rhodobacter capsulatus XDH in Escherichia coli. NifS is a cysteine desulfurase, which catalyzes the sulfur transfer from L-cysteine to Moco to form Mo-S bond. Chaperone XDHC binds stoichiometric amount of Moco as a scaffold protein, interacts with NifS for the sulfuration of Moco, protects sulfurated Moco from oxidation, and further transfers to XDH, method devlopment, overview. Three helper proteins, NifS, IscS and DsbB improve the specific activity of RcXDH significantly by 30%, 94% and 49%, respectively. The combination of NifS and IscS synergistically increases the specific activity by 1.29fold, and enhances the total enzyme activity by an impressive 3.9fold
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additional information
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two (alphabetagamma)2 XDH variants, Split166 and Split178, are designed and constructed by splitting the small subunit (alphabeta)2 XDH at the N- and C-terminal ends of the L167-A178 peptide linking the iron-sulfur clusters and flavin adenine dinucleotide domains, respectively. Subunit composition of recombinant wild-type and split XDHsAs, overview. As for the co-substrate NAD+, mutant Split178 has a 1.07fold increased catalytic efficiency, while Split166 has a 3.8fold decreased catalytic efficiency compared to the wild-type XDH, for the substrate xanthine, the Split178 variant shows 1.21fold increased turnover number and 1.66fold increased catalytic efficiency, while the mutant Split166 shows a 4.31fold decrease in comparison to the wild-type enzyme
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