Any feedback?
No. of entries
Information on EC 1.17.1.4 - xanthine dehydrogenase
for references in articles please use BRENDA:EC1.17.1.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.17 Acting on CH or CH2 groups
1.17.1 With NAD+ or NADP+ as acceptor
1.17.1.4 xanthine dehydrogenase
IUBMB Comments
Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein . The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [2,6,8,15] [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo [2,7,15].
The enzyme appears in viruses and cellular organisms
- 1.17.1.4
-
uric
-
1.2.1.37
-
1.1.1.204
- allopurinol
- environmental protection
-
ureide
-
1.1.3.22
- medicine
-
1.2.3.1
-
xanthinuria
-
oxypurines
-
butyrophilins
- synthesis
-
hypouricemic
- agriculture
- biotechnology
- analysis
- nutrition
- molecular biology
showSynonyms
xdh/xo, xanthine dehydrogenase/oxidase, atxdh1, paoabc, xanthine:nad+ oxidoreductase, xanthine-nad oxidoreductase, xanthine/nad+ oxidoreductase, xanthine dehydrogenase-1, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.1.1.204
-
-
formerly
-
EC 1.2.1.37
-
-
formerly
-
NAD-xanthine dehydrogenase
-
-
-
-
Rosy locus protein
-
-
-
-
xanthine dehydrogenase
xanthine oxidoreductase
xanthine-NAD oxidoreductase
-
-
-
-
xanthine/NAD+ oxidoreductase
-
-
-
-
XDH
XDH/XO
-
-
-
-
XDH1
XdhC
XOR
additional information
xanthine oxidoreductase
-
-
-
-
XOR
-
-
-
-
additional information
-
mammalian XOR exists in two interconvertible forms, the xanthine dehydrogenase, XDH, form and the xanthine oxidase, XO, form. The primary gene product is XDH, which can be converted into XO
additional information
-
XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4
additional information
XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
xanthine + NAD+ + H2O = urate + NADH + H+
Acts on a variety of purines and aldehydes. The animal enzyme can be interconverted to EC 1.1.3.22 xanthine oxidase, the oxidase form. That from liver exists in vivo mainly in the dehydrogenase form, but can be converted into EC 1.1.3.22 by storage at -20°C, by treatment with proteolytic agents or organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate. The effect of thiol reagents can be reversed by thiols such as 1,4-dithioerythritol. EC 1.1.1.204 can also be converted into EC 1.1.3.22 by EC 1.8.4.7 enzyme-thiol transhydrogenase (oxidized-glutathione) in the presence of the oxidized glutathione. In other animal tissues, the enzyme exists almost entirely as EC 1.1.3.22, but can be converted into the dehydrogenase form by 1,4-dithioerythritol. Formerly EC 1.2.1.37
-
-
-
xanthine + NAD+ + H2O = urate + NADH + H+
catalytically labile Mo-OH oxygen forms a bond with a carbon atom of substrate, the Mo=S group of the oxidized enzyme becomes protonated to afford Mo-SH on reduction of the molybdenum center
xanthine + NAD+ + H2O = urate + NADH + H+
mechanism of conversion of dehydrogenase form to oxidase form
-
xanthine + NAD+ + H2O = urate + NADH + H+
the catalytic sequence of Rhodobacter capsulatus XDH is initiated by abstraction of a proton from the Mo-OH group by the highly conserved active site subunit B residue Glu730, followed by nucleophilic attack of the resulting Mo-O on the carbon center of the substrate (C-2 in hypoxanthine and C-8 in xanthine) and concomitant hydride transfer to the Mo-S of the molybdenum center, reaction and substrate binding mechanisms, overview
xanthine + NAD+ + H2O = urate + NADH + H+
reaction mechanism with substrate all-trans-retinol, overview
-
xanthine + NAD+ + H2O = urate + NADH + H+
reaction mechanism, The reaction is initiated by proton abstraction from the Mo-OH group by Glu730, the active-site base, followed by nucleophilic attack on the carbon to be hydroxylated, and hydride transfer to the Mo-S double bond. Suitable substrate orientation, overview. Arg310 is involved in stablizing the transition state in the course of nucleophilic attack, overview
-
xanthine + NAD+ + H2O = urate + NADH + H+
reaction mechanism of XOR and binding modes of the substrate xanthine, overview. The oxidative hydroxylation of purine substrates takes place at the molybdenum center. Reducing equivalents introduced there are then transferred via two [2Fe-2S] centers to the FAD cofactor where reduction of the physiological electron acceptors occurs, NAD+ in the case of the dehydrogenase form, XDH, or O2 in the oxidase form, XO, of the enzyme occur
xanthine + NAD+ + H2O = urate + NADH + H+
reaction mechanism of XOR and binding modes of the substrate xanthine, overview. The oxidative hydroxylation of purine substrates takes place at the molybdenum center. Reducing equivalents introduced there are then transferred via two [2Fe-2S] centers to the FAD cofactor where reduction of the physiological electron acceptors occurs, NAD+ in the case of the dehydrogenase form, XDH, or O2 in the oxidase form, XO, of the enzyme occur
-
xanthine + NAD+ + H2O = urate + NADH + H+
a reaction mechanism for XDH is suggested in which an initial oxo rather than a hydroxo group and the sulfido ligand are essential for xanthine oxidation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
adenosine nucleotides degradation I, adenosine nucleotides degradation II, caffeine degradation III (bacteria, via demethylation), guanosine nucleotides degradation I, guanosine nucleotides degradation II, guanosine nucleotides degradation III, inosine 5'-phosphate degradation, purine nucleobases degradation II (anaerobic), theophylline degradation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
xanthine:NAD+ oxidoreductase
Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein [14]. The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [2,6,8,15] [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo [2,7,15].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9054-84-6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-methylhypoxanthine + NAD+ + H2O
1-methylxanthine + NADH
-
Substrates: 10% of the activity compared to hypoxanthine
Products: -
Products: -
?
1-naphthaldehyde + NAD+ + ?
? + NADH
Substrates: 27.5% of the activity with xanthine
Products: -
Products: -
?
2 2-hydroxypurine + 2 NAD+ + 2 H2O
xanthine + 2,8-dihydroxypurine + 2 NADH + 2 H+
-
Substrates: considerable activity
Products: 84% xanthine, 8% 2,8-dihydroxypurine formed
Products: 84% xanthine, 8% 2,8-dihydroxypurine formed
?
2 hypoxanthine + 2 NAD+ + 2 H2O
xanthine + 6,8-dihydroxypurine + 2 NADH + 2 H+
-
Substrates: preferred substrate
Products: 100% xanthine, 51% 6,8-dihydroxypurine formed
Products: 100% xanthine, 51% 6,8-dihydroxypurine formed
?
2,6-diaminopurine + NAD+ + H2O
? + NADH + H+
-
Substrates: poor substrate
Products: -
Products: -
?
2,6-dithiopurine + NAD+ + H2O
? + NADH
-
Substrates: 26% of the activity compared to hypoxanthine
Products: -
Products: -
?
2-amino-4-hydroxypterin + nitroblue tetrazolium + H2O
isoxanthopterin + reduced nitroblue tetrazolium
2-hydroxy-6-methylpurine + NAD+ + H2O
? + NADH + H+
-
Substrates: poor substrate
Products: -
Products: -
?
2-hydroxypurine + NAD+ + H2O
? + NADH
-
Substrates: 35% of the activity compared to hypoxanthine, purine not oxidized
Products: -
Products: -
?
2-OH-purine + ferricyanide + H2O
? + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
2-thioxanthine + NAD+ + H2O
2-thiourate + NADH
-
Substrates: 57% of the activity compared to hypoxanthine
Products: -
Products: -
?
3 purine + 3 NAD+ + 3 H2O
hypoxanthine + 8-hydroxypurine + 2-hydroxypurine + 3 NADH + 3 H+
-
Substrates: poor substrate
Products: 2.3% hypoxanthine, 2.3% 8-hydroxypurine and traces of 2-hydroxypurine formed
Products: 2.3% hypoxanthine, 2.3% 8-hydroxypurine and traces of 2-hydroxypurine formed
?
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + H+
-
Substrates: 1.2% activity compared to xanthine
Products: -
Products: -
?
4-aminoimidazole-5-carboxamide + NADP+ + H2O
? + NADPH
-
Substrates: 38% of the activity compared to hypoxanthine-NADP+
Products: -
Products: -
?
4-dimethylaminobenzaldehyde + NAD+ + H2O
4-dimethylaminobenzoate + NADH
-
Substrates: 0.3% activity compared to xanthine
Products: -
Products: -
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
-
Substrates: 0.7% activity compared to xanthine
Products: -
Products: -
?
4-hydroxypyrazolo(3,4-d)pyrimidine + ferricyanide + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + ferrocyanide
-
Substrates: i.e. allopurinol
Products: -
Products: -
?
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
-
Substrates: 1.1% of the activity compared to xanthine
Products: -
Products: -
?
6,8-dihydropurine + NAD+ + H2O
? + NADH
-
Substrates: 50% of the activity compared to hypoxanthine
Products: -
Products: -
?
6,8-dihydroxypurine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: 18% urate formed
Products: 18% urate formed
?
6-mercaptopurine + methyl viologen + H2O
? + reduced methyl viologen
-
Substrates: 9.5% of the activity compared to xanthine
Products: -
Products: -
?
6-thioxanthine + NAD+ + H2O
6-thiourate + NADH
-
Substrates: 63% of the activity compared to hypoxanthine
Products: -
Products: -
?
6-thioxanthine + NAD+ + H2O
6-thiourate + NADH + H+
-
Substrates: effective substrate
Products: -
Products: -
?
6-thioxanthine + NAD+ + H2O
? + NADH + H+
-
Substrates: good substrate
Products: -
Products: -
?
8-azaxanthine + NAD+ + H2O
8-aza-urate + NADH
-
Substrates: very low activity
Products: -
Products: -
?
9-methylhypoxanthine + O2
9-methylxanthine + H2O2
-
Substrates: -
Products: -
Products: -
?
abscisic aldehyde + NAD+ + ?
? + NADH
Substrates: 28.9% of the activity with xanthine
Products: -
Products: -
?
acetaldehyde + ferricyanide + H2O
acetic acid + ferrocyanide
-
Substrates: 5% of the activity compared to xanthine
Products: -
Products: -
?
acetaldehyde + nitroblue tetrazolium + H2O
acetic acid + reduced nitroblue tetrazolium
-
Substrates: very low activity
Products: -
Products: -
?
adenine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: 12% of the activity compared to xanthine
Products: -
Products: -
?
adenine-N1-oxide + NAD+ + H2O
? + NADH
-
Substrates: 3.4% of the activity compared to hypoxanthine
Products: -
Products: -
?
benzaldehyde + 2 ferricyanide + H2O
benzoate + 2 ferrocyanide + 2 H+
-
Substrates: 4% of the activity compared to xanthine
Products: -
Products: -
?
benzaldehyde + ferricyanide + H2O
benzoate + 2 ferrocyanide + 2 H+
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: 1.3% activity compared to xanthine
Products: -
Products: -
?
benzaldehyde + nitroblue tetrazolium + H2O
benzoate + reduced nitroblue tetrazolium
-
Substrates: very low activity
Products: -
Products: -
?
cinnamaldehyde + H2O + acceptor
cinnamic acid + reduced acceptor
Substrates: -
Products: -
Products: -
?
guanine + NAD+ + H2O
? + NADH
-
Substrates: 81.3% of the activity compared to hypoxanthine
Products: -
Products: -
?
heptaldehyde + NAD+ + ?
? + NADH
Substrates: 12.5% of the activity with xanthine
Products: -
Products: -
?
hypoxanthine + cytochrome c + H2O
xanthine + reduced cytochrome c
-
Substrates: 2.1% of the activity compared to NAD+
Products: -
Products: -
?
hypoxanthine + ferricyanide
xanthine + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + methylene blue + H2O
xanthine + reduced methylene blue
-
Substrates: 39% of the activity compared to NAD+ as electron acceptor
Products: -
Products: -
?
hypoxanthine + NADH
? + NO2- + NAD+
-
Substrates: 0.1% of the xanthine oxidation rate
Products: -
Products: -
?
hypoxanthine + thio-NAD+ + H2O
xanthine + thio-NADH
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + urate
xanthine + 6,8-dihydroxypurine
-
Substrates: oxygen-free assay
Products: -
Products: -
r
hypoxanthine + uric acid imine
?
-
Substrates: 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
Products: -
Products: -
?
indole-3-acetaldehyde + NAD+ + H2O
indole-3-acetate + NADH + H+
-
Substrates: and similar aldehydes, 2-3% of the activity with xanthine
Products: -
Products: -
?
indole-3-carboxaldehyde + NAD+ + ?
? + NADH
Substrates: 31.3% of the activity with xanthine
Products: -
Products: -
?
inosine + NAD+ + H2O
? + NADH
-
Substrates: low activity
Products: -
Products: -
?
isoguanine + NAD+ + H2O
? + NADH
-
Substrates: 7.3% of the activity compared to hypoxanthine
Products: -
Products: -
?
N-methylnicontinamide + NADP+ + H2O
? + NADPH
-
Substrates: low activity, only a substrate at pH values above 8.0
Products: -
Products: -
?
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
r
NADH + O2 + H+
NAD+ + O2- + H2O2
-
Substrates: 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
Products: -
Products: -
?
NADH + reduced phenazine methosulfate + cytochrome c
NAD+ + ?
-
Substrates: no activity for the mutant E89K
Products: -
Products: -
?
NADPH + electron acceptor + H2O
NADP+ + reduced electron acceptor
-
Substrates: electron acceptors: 2,6-dichlorophenolindophenol, methyl viologen, benzyl viologen, methylene blue
Products: -
Products: -
?
NADPH + O2
NADP+ + O2- + H+
-
Substrates: high NADPH oxidase activity
Products: -
Products: -
?
NADPH + phenazine methosulfate + cytochrome c
NADP+ + ?
-
Substrates: -
Products: -
Products: -
?
phthalazine + NAD+ + H2O
1-(2H)-phthalazinone + NADH
-
Substrates: 0.4% activity compared to xanthine
Products: -
Products: -
?
propionaldehyde + NAD+ + H2O
propionic acid + NADH
-
Substrates: low activity
Products: -
Products: -
?
purine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: 108% of the activity compared to xanthine
Products: -
Products: -
?
purine + methyl viologen + H2O
? + reduced methyl viologen
-
Substrates: 2% of the activity compared to xanthine
Products: -
Products: -
?
purine + NAD+ + ?
? + NADH
Substrates: 10.3% of the activity with xanthine
Products: -
Products: -
?
purine + NADP+ + H2O
? + NADPH
-
Substrates: 60% of the activity compared to hypoxanthine
Products: -
Products: -
?
quinazoline + NAD+ + H2O
4-(3H)-quinazolinone + NADH
-
Substrates: 2% activity compared to xanthine
Products: -
Products: -
?
salicylaldehyde + ferricyanide + H2O
salicylate + ferrocyanide
-
Substrates: 2% of the activity compared to xanthine
Products: -
Products: -
?
theobromine + NAD+ + H2O
? + NADH
-
Substrates: very low activity
Products: -
Products: -
?
theophylline + NAD+ + H2O
? + NADH
-
Substrates: low activity
Products: -
Products: -
?
xanthine + 3-acetylpyridine-adenine dinucleotide+ + H2O
urate + 3-acetylpyridine-adenine dinucleotide(H)
xanthine + DCIP + H2O
urate + reduced DCIP
-
Substrates: -
Products: -
Products: -
?
xanthine + FAD + H2O
urate + FADH2
-
Substrates: 35% of the activity compared to methylene blue as electron acceptor
Products: -
Products: -
?
xanthine + ferredoxin + H2O
urate + reduced ferredoxin
-
Substrates: -
Products: -
Products: -
?
xanthine + FMN + H2O
urate + FMNH2
-
Substrates: 44% of the activity compared to methylene blue as electron acceptor
Products: -
Products: -
?
xanthine + iodonitrotetrazolium + H2O
urate + reduced iodonitrotetrazolium
-
Substrates: -
Products: -
Products: -
?
xanthine + myoglobin + H2O
urate + reduced myoglobin
-
Substrates: -
Products: -
Products: -
?
xanthine + O2
hypoxanthine + ?
-
Substrates: dismutation reaction
Products: -
Products: -
?
xanthine + p-benzoquinone + H2O
hypoxanthine + hydroquinone + ?
-
Substrates: electron donor only for oxidase type
Products: -
Products: -
?
xanthine + p-benzoquinone + H2O
p-benzosemiquinone + urate
-
Substrates: electron acceptor p-benzoquinone for both dehydrogenase and oxidase types
Products: -
Products: -
?
xanthine + pyridinealdehyde-NAD+ + H2O
urate + pyridinealdehyde-NADH
-
Substrates: 53% of the activity compared to NAD+, low reverse activity
Products: -
Products: -
r
xanthine + riboflavin + H2O
urate + reduced riboflavin
-
Substrates: 41% of the activity compared to methylene blue as electron acceptor
Products: -
Products: -
?
xanthine + ureic acid imine
?
-
Substrates: 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
Products: -
Products: -
?
xanthosine + NAD+ + H2O
? + NADH
-
Substrates: 15.1% of the activity compared to hypoxanthine
Products: -
Products: -
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + ferricyanide + H2O
1-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
Substrates: 10% of the activity compared to hypoxanthine
Products: -
Products: -
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
Substrates: -
Products: -
Products: -
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH + H+
-
Substrates: 10fold reduced kred-value compared to xanthine
Products: -
Products: -
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH + H+
-
Substrates: rather less effective than xanthine as a substrate
Products: -
Products: -
?
2,6-dichloroindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
Substrates: -
Products: -
Products: -
r
2,6-dichloroindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
Substrates: -
Products: -
Products: -
r
2-amino-4-hydroxy-pterin + methylene blue + H2O
isoxanthopterin + reduced methylene blue
-
Substrates: -
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + methylene blue + H2O
isoxanthopterin + reduced methylene blue
-
Substrates: -
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: precursor of the eye pigment drosopterin
Products: precursor of the eye pigment drosopterin
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
r
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: conversion of xanthine dehydrogenase to xanthine oxidase is strongly influenced by in vitro cell culture of alveolar epithelial cells
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: 11% of the activity compared to xanthine
Products: -
Products: -
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: precursor of the eye pigment drosopterin
Products: precursor of the eye pigment drosopterin
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
r
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: conversion of xanthine dehydrogenase to xanthine oxidase is strongly influenced by in vitro cell culture of alveolar epithelial cells
Products: -
Products: -
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: 11% of the activity compared to xanthine
Products: -
Products: -
?
2-amino-4-hydroxypterin + nitroblue tetrazolium + H2O
isoxanthopterin + reduced nitroblue tetrazolium
-
Substrates: very low activity
Products: -
Products: -
?
2-amino-4-hydroxypterin + nitroblue tetrazolium + H2O
isoxanthopterin + reduced nitroblue tetrazolium
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-thioxanthine + NAD+ + H2O
2-thiourate + NADH + H+
-
Substrates: good substrate
Products: -
Products: -
?
2-thioxanthine + NAD+ + H2O
2-thiourate + NADH + H+
-
Substrates: effective substrate
Products: -
Products: -
?
3-methylxanthine + ferricyanide + H2O
3-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
3-methylxanthine + ferricyanide + H2O
3-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
3-methylxanthine + ferricyanide + H2O
3-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
3-methylxanthine + ferricyanide + H2O
3-methylurate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
4-hydroxypyrazolo(3,4-d)pyrimidine + methyl viologen + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced methyl viologen
-
Substrates: i.e. allopurinol
Products: -
Products: -
?
4-hydroxypyrazolo(3,4-d)pyrimidine + methyl viologen + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced methyl viologen
-
Substrates: 8% of the activity compared to xanthine
Products: -
Products: -
?
4-hydroxypyrazolo(3,4-d)pyrimidine + NAD+ + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + NADH
-
Substrates: best substrate tested
Products: -
Products: -
?
4-hydroxypyrazolo(3,4-d)pyrimidine + NAD+ + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + NADH
-
Substrates: i.e. allopurinol
Products: -
Products: -
?
4-hydroxypyrazolo(3,4-d)pyrimidine + NAD+ + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + NADH
-
Substrates: i.e. allopurinol
Products: -
Products: -
?
4-hydroxypyrazolo(3,4-d)pyrimidine + nitroblue tetrazolium + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced nitroblue tetrazolium
-
Substrates: i.e. allopurinol
Products: -
Products: -
?
4-hydroxypyrazolo(3,4-d)pyrimidine + nitroblue tetrazolium + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced nitroblue tetrazolium
-
Substrates: very low activity
Products: -
Products: -
?
4-hydroxypyrazolo(3,4-d)pyrimidine + nitroblue tetrazolium + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced nitroblue tetrazolium
-
Substrates: i.e. allopurinol
Products: -
Products: -
?
8-azahypoxanthine + NAD+ + H2O
8-azaxanthine + NADH
-
Substrates: 42% of the activity compared to hypoxanthine
Products: -
Products: -
?
8-azahypoxanthine + NAD+ + H2O
8-azaxanthine + NADH
-
Substrates: 39% 0f the activity compared to hypoxanthine
Products: -
Products: -
?
acetaldehyde + 2,6-dichloroindophenol + H2O
?
-
Substrates: 1.2% of activity with xanthine
Products: -
Products: -
?
acetaldehyde + 2,6-dichloroindophenol + H2O
?
-
Substrates: 0.1% of activity with xanthine
Products: -
Products: -
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: very low activity
Products: -
Products: -
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: considerable activity for the recombinant enzyme
Products: -
Products: -
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: very low activity
Products: -
Products: -
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: very low activity
Products: -
Products: -
?
adenine + NAD+ + H2O
? + NADH
-
Substrates: low activity
Products: -
Products: -
?
glyceraldehyde + 2,6-dichloroindophenol + H2O
?
-
Substrates: 12.1% of activity with xanthine
Products: -
Products: -
?
glyceraldehyde + 2,6-dichloroindophenol + H2O
?
-
Substrates: 0.3% of activity with xanthine
Products: -
Products: -
?
hypoxanthine + 2 NAD+ + 2 H2O
urate + 2 NADH + 2 H+
Substrates: -
Products: -
Products: -
?
hypoxanthine + 2,6-dichlorophenolindophenol + H2O
xanthine + ?
-
Substrates: considerable activity
Products: -
Products: -
?
hypoxanthine + 2,6-dichlorophenolindophenol + H2O
xanthine + ?
-
Substrates: 12.2% of the activity compared to NAD+
Products: -
Products: -
?
hypoxanthine + ferricyanide + H2O
xanthine + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + ferricyanide + H2O
xanthine + ferrocyanide
-
Substrates: 17.2% of the activity compared to NAD+
Products: -
Products: -
?
hypoxanthine + ferricyanide + H2O
xanthine + ferrocyanide
-
Substrates: 98% of the activity compared to xanthine
Products: -
Products: -
?
hypoxanthine + methyl viologen + H2O
xanthine + reduced methyl viologen
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + methyl viologen + H2O
xanthine + reduced methyl viologen
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + methyl viologen + H2O
xanthine + reduced methyl viologen
-
Substrates: 7% of the activity compared to xanthine
Products: -
Products: -
?
hypoxanthine + NAD+ + 2 H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + 2 H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + 2 H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
Substrates: 94.7% of the activity with xanthine
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: 12.4% of activity with xanthine
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: NAD+-O2- dependent xanthine oxidase activity
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: NAD+-O2- dependent xanthine oxidase activity
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: predominant reaction
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: subtilisin treatment leads to an active component I of 120000 kDa
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
r
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: more rapidly oxidized than xanthine
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: preferred substrate
Products: -
Products: -
ir
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: 19% of activity with xanthine
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
urate + ? + NADH
-
Substrates: 149% activity compared to xanthine
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
urate + ? + NADH
-
Substrates: 149% activity compared to xanthine
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: 44% of the activity with xanthine
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: preferred substrate
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
Substrates: 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
Products: -
Products: -
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
-
Substrates: strict specificity for NADP+
Products: -
Products: -
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
-
Substrates: 40% of the activity compared to NAD+
Products: -
Products: -
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
-
Substrates: 2.4% of the activity compared to NAD+
Products: -
Products: -
?
hypoxanthine + nitroblue tetrazolium
xanthine + ?
-
Substrates: 18% of the activity compared to NAD+
Products: -
Products: -
?
hypoxanthine + nitroblue tetrazolium
xanthine + ?
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + O2
xanthine + H2O2
-
Substrates: very low activity
Products: -
Products: -
?
hypoxanthine + O2 + H2O
xanthine + O2-
-
Substrates: -
Products: no production of H2O2
Products: no production of H2O2
?
hypoxanthine + O2 + H2O
xanthine + O2-
-
Substrates: -
Products: no production of H2O2
Products: no production of H2O2
?
hypoxanthine + phenazine methosulfate + H2O
urate + ?
-
Substrates: effective electron acceptor
Products: -
Products: -
?
hypoxanthine + phenazine methosulfate + H2O
urate + ?
-
Substrates: low activity
Products: -
Products: -
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
Substrates: electron acceptor: nitroblue tetrazolium
Products: -
Products: -
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
Substrates: extremely slow reoxidation rate
Products: -
Products: -
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
Substrates: NADH diaphorase activity with several acceptors
Products: -
Products: -
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
Substrates: electron acceptors: 2,6-dichlorphenolindophenol or methyl viologen
Products: -
Products: -
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
Substrates: electron acceptor: 2,6-dichlorophenolindophenol, no activity for mutant E89K
Products: -
Products: -
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
Substrates: NADH diaphorase activity with several acceptors
Products: -
Products: -
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
Substrates: 2,6-dichloroindophenol, 3-acetylpyridine-adenine dinucleotide, methylene blue, phenazine methosulfate or trinitrobenzene sulfonate
Products: -
Products: -
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
Substrates: subtilisin treatment leads to an active component of 120000 kDa with enhanced activity
Products: -
Products: -
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
Substrates: NADH diaphorase activity with several acceptors
Products: -
Products: -
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
Substrates: 2,6-dichloroindophenol as electron acceptor
Products: -
Products: -
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
Substrates: 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
Products: -
Products: -
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
Substrates: only dehydrogenase type D shows considerable activities, not oxidase type O
Products: -
Products: -
?
NADH + electron acceptor + H2O
NAD+ + reduced electron acceptor
-
Substrates: electron acceptor: nitroblue tetrazolium
Products: -
Products: -
?
NADPH + nitroblue tetrazolium + H2O
NADP+ + reduced nitroblue tetrazolium
-
Substrates: diaphorase activity
Products: -
Products: -
?
NADPH + nitroblue tetrazolium + H2O
NADP+ + reduced nitroblue tetrazolium
-
Substrates: diaphorase activity
Products: -
Products: -
?
pterin + 2,6-dichloroindophenol + H2O
?
-
Substrates: 22.7% of activity with xanthine
Products: -
Products: -
?
pterin + 2,6-dichloroindophenol + H2O
?
-
Substrates: 9.7% of activity with xanthine
Products: -
Products: -
?
purine + 2,6-dichloroindophenol + H2O
?
-
Substrates: 18.7% of activity with xanthine
Products: -
Products: -
?
purine + 2,6-dichloroindophenol + H2O
?
-
Substrates: 8.5% of activity with xanthine
Products: -
Products: -
?
purine + NAD+ + H2O
8-hydroxypurine + NADH + H+
-
Substrates: 5% activity compared to xanthine
Products: -
Products: -
?
purine + NAD+ + H2O
8-hydroxypurine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
purine + NAD+ + H2O
? + NADH
-
Substrates: poor substrate
Products: -
Products: -
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
Substrates: -
Products: -
Products: -
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
Substrates: -
Products: -
Products: -
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
Substrates: -
Products: -
Products: -
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
Substrates: very low activity for the mutant E89K
Products: -
Products: -
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
Substrates: same activity compared to NAD+ as electron acceptor
Products: -
Products: -
r
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
Substrates: 2.5% of the activity compared to methyl viologen as electron acceptor
Products: -
Products: -
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
Substrates: -
Products: -
Products: -
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
Substrates: subtilisin treatment leads to an active component of 120000 kDa
Products: -
Products: -
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
Substrates: -
Products: -
Products: -
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
Substrates: 11% of the activity compared to ferricyanide as electron acceptor
Products: -
Products: -
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
Substrates: greatly enhanced activity for dehydrogenase type D and trypsin- or heat-treated oxidase types O
Products: -
Products: -
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
Substrates: -
Products: -
Products: -
?
xanthine + 2,6-dichlorophenolindophenol + H2O
urate + ?
-
Substrates: 13% of the activity compared to methylene blue as electron acceptor
Products: -
Products: -
?
xanthine + 3-acetylpyridine-adenine dinucleotide+ + H2O
urate + 3-acetylpyridine-adenine dinucleotide(H)
-
Substrates: same activity compared to NAD+
Products: -
Products: -
r
xanthine + 3-acetylpyridine-adenine dinucleotide+ + H2O
urate + 3-acetylpyridine-adenine dinucleotide(H)
-
Substrates: low reverse activity
Products: -
Products: -
r
xanthine + 3-acetylpyridine-adenine dinucleotide+ + H2O
urate + 3-acetylpyridine-adenine dinucleotide(H)
-
Substrates: same activity compared to NAD+
Products: -
Products: -
r
xanthine + benzyl viologen + H2O
urate + reduced benzyl viologen
-
Substrates: 52% of the activity compared to methyl viologen as electron acceptor
Products: -
Products: -
?
xanthine + benzyl viologen + H2O
urate + reduced benzyl viologen
-
Substrates: 18% of the activity compared to methylene blue as electron acceptor
Products: -
Products: -
?
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
-
Substrates: -
Products: -
Products: -
?
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
-
Substrates: enhanced activity for heat- and trypsin-treated oxidase types O
Products: -
Products: -
?
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
-
Substrates: low activity
Products: -
Products: -
?
xanthine + cytochrome c + H2O
urate + reduced cytochrome c
-
Substrates: presence of ferredoxin enhances cytochrom c reduction
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: 99% of the activity compared to methyl viologen as electron acceptor
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: preferred substrates, does not act with NAD+ or NADP+
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: specific ferricyanide-dependent activity, no activity with NAD+, NADP+, oxygen, cytochrome c, FAD or FMN
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: 58% of the activity compared to xanthine-NAD+
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: 58% of the activity compared to xanthine-NAD+
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: low activity for both dehydrogenase type D and oxidase type O
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + ferricyanide + H2O
urate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
-
Substrates: -
Products: -
Products: -
?
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
-
Substrates: -
Products: -
Products: -
?
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
-
Substrates: best substrates tested, no activity with NAD+ or NADP+, 40% of the activity in the reverse reaction
Products: -
Products: -
r
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
-
Substrates: -
Products: -
Products: -
?
xanthine + methyl viologen + H2O
urate + reduced methyl viologen
-
Substrates: low activity
Products: -
Products: -
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
Substrates: -
Products: -
Products: -
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
Substrates: -
Products: -
Products: -
r
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
Substrates: 87% of the activity compared to methyl viologen as electron acceptor
Products: -
Products: -
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
Substrates: -
Products: -
Products: -
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
Substrates: subtilisin treatment leads to an active component of 120000 kDa
Products: -
Products: -
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
Substrates: same activity for dehydrogenase type D and oxidase type O
Products: -
Products: -
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
Substrates: enhanced oxidation of xanthine for dehydrogenase type D and trypsin- or heat-treated oxidase type O
Products: -
Products: -
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
Substrates: 3fold higher activity compared to NAD+ as electron acceptor
Products: -
Products: -
?
xanthine + methylene blue + H2O
urate + reduced methylene blue
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: regulation of xanthine dehydrogenase expression is subjected to nitrogen catabolite repression mediated through the GlnA-dependent signaling pathway
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: xanthine dehydrogenase form has distinct xanthine/oxygen activity, 35-42% of electrons transferred to O2 to form O2-
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: conversion of dehydrogenase to oxidase type due to oxidation of sulfhydryl groups by molecular oxygen, dehydrogenase activity recovered by treatment with dithiothreitol
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: NAD+-dependent dehydrogenase type D
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: involved in pteridine metabolism, 40% of activity compared to hypoxanthine
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: only dehydrogenase type D present
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: ping-pong reaction mechanism
Products: -
Products: -
r
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: 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
Products: -
Products: -
r
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: 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
Products: 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
Products: 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
-
Substrates: only present as stable dehydrogenase from, no conversion to the oxidase form
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: subtilisin treatment leads to an active component I of 120000 kDa
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: 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
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: degradative pathway of conversion of purines to ammonia
Products: -
Products: -
r
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
r
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: NAD+-linked activity, very low activity towards molecular oxygen
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: 100% activity
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: 75% of the activity compared to hypoxanthine
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: NAD+-dependent form is postulated to play a regulatory role in purine metabolism
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: conversion of xanthine dehydrogenase to the oxidase type by thiol-disulfide oxidoreductase, thiol reagents or oxidized glutathione
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: trypsin treatment leads to a complete conversion of xanthine dehydrogenase to xanthine oxidase activity
Products: -
Products: -
r
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: NAD+-dependent dehydrogenase type D
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: 67% of the activity compared to hypoxanthine
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: 61% of the activity compared to hypoxanthine
Products: 91% urate formed
Products: 91% urate formed
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: strict dehydrogenase activity, no utilization of O2
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: catalytically relevant binding mode of the substrate xanthine, overview
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: catalytically relevant binding mode of the substrate xanthine, overview
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: 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
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: when catalyzing the sequential oxidation of hypoxanthine to xanthine to uric acid, XDH uses the NAD+ as final electron receptor to produce NADH
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: product release is principally rate-limiting in catalysis
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Rhodobacter capsulatus B10XDHB
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Rhodobacter capsulatus CGMCC 1.3366
Substrates: when catalyzing the sequential oxidation of hypoxanthine to xanthine to uric acid, XDH uses the NAD+ as final electron receptor to produce NADH
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Rhodobacter capsulatus CGMCC 1.3366
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Rhodobacter capsulatus CGMCC 1.3366
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
-
Substrates: heat-treated intermediate dehydrogenase/oxidase type O
Products: -
Products: -
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
-
Substrates: intermediate form of dehydrogenase/oxidase type D/O
Products: -
Products: -
?
xanthine + NADP+ + H2O
urate + NADPH
-
Substrates: 11% of the activity compared to NAD+
Products: -
Products: -
?
xanthine + NADP+ + H2O
urate + NADPH
-
Substrates: strict specificity for NADP+
Products: -
Products: -
?
xanthine + nitroblue tetrazolium + H2O
urate + ?
-
Substrates: -
Products: -
Products: -
?
xanthine + nitroblue tetrazolium + H2O
urate + ?
-
Substrates: 32% of the activity compared to methyl viologen as electron acceptor
Products: -
Products: -
?
xanthine + nitroblue tetrazolium + H2O
urate + ?
-
Substrates: -
Products: -
Products: -
?
xanthine + nitroblue tetrazolium + H2O
urate + ?
-
Substrates: -
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: -
Products: no production of H2O2
Products: no production of H2O2
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: xanthine oxidase form transfers 22% electrons to oxygen to form superoxide
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: low activity
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: -
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: low activity
Products: -
Products: -
r
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: very low activity
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: low activity
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: subtilisin treatment leads to an active component I of 120000 kDa
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: -
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: very low activity
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: 4% of the activity compared to xanthine-NAD+
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: 4% of the activity compared to xanthine-NAD+
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: toxic reactions of xanthine oxidase-derived radicals are critical factors in several mechanisms of tissue pathology
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: NAD+-independent trypsin-treated oxidase type O
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: 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
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: -
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: -
Products: no production of H2O2
Products: no production of H2O2
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: very low activity
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: presence of ferredoxin enhances rate of oxygen reduction
Products: -
Products: -
?
xanthine + phenazine methosulfate + cytochrome c + H2O
urate + ?
-
Substrates: -
Products: -
Products: -
?
xanthine + phenazine methosulfate + cytochrome c + H2O
urate + ?
-
Substrates: very low activity for the mutant E89K
Products: -
Products: -
?
xanthine + phenazine methosulfate + H2O
urate + ?
-
Substrates: -
Products: -
Products: -
r
xanthine + phenazine methosulfate + H2O
urate + ?
-
Substrates: 5fold higher activity compared to NAD+ as electron acceptor
Products: -
Products: -
?
xanthine + phenazine methosulfate + H2O
urate + ?
-
Substrates: -
Products: -
Products: -
?
xanthine + thio-NAD+ + H2O
urate + thio-NADH
-
Substrates: -
Products: -
Products: -
?
xanthine + thio-NAD+ + H2O
urate + thio-NADH
-
Substrates: same activity compared to NAD+
Products: -
Products: -
r
xanthine + trinitrobenzenesulfonate + H2O
urate + ?
-
Substrates: -
Products: -
Products: -
r
xanthine + trinitrobenzenesulfonate + H2O
urate + ?
-
Substrates: subtilisin treatment leads to an active component of 120000 kDa
Products: -
Products: -
?
xanthopterin + NAD+ + H2O
leucopterin + NADH
-
Substrates: regulation of the pteridine pathway by competitive inhibition of reaction products and the precursor of xanthopterin, 7,8-dihydroxyxanthopterin
Products: -
Products: -
?
xanthopterin + NAD+ + H2O
leucopterin + NADH
-
Substrates: regulation of the pteridine pathway by competitive inhibition of reaction products and the precursor of xanthopterin, 7,8-dihydroxanthopterin
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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%
Products: -
Products: -
?
additional information
?
-
Substrates: 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%
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the dehydrogenase form of enzyme reacts significantly faster than the oxidase form
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: xanthine oxidoreductase is a regulator of adipogenesis and of nuclear recptor PPARgamma activityand is essential for the regulation of fat accretion
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: NAD+ is the most effcient electron acceptor, followed by 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyl-2H-tetrazolium chloride and ferricyanide
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: major function of enzyme in liver parenchymal and sinusoidal cells is the production of uric acid as a antioxidant
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme inhibition by orange juice and hesperetin participates in preventing oxidative stress by enhancing total antioxidant capacity and decreasing lipid peroxidation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: purified recombinant wild-type and DELTAC mutant enzymes both exhibit mostly xanthine oxidase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: xanthine and 2-hydroxy-6-methylpurine are substrates. Substrate binding structures, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: ionized Glu232 of wild-type enzyme plays an important role in catalysis by discriminating against the monoanionic form of xanthine
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Rhodobacter capsulatus B10XDHB
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 2-hydroxypurine + 2 NAD+ + 2 H2O
xanthine + 2,8-dihydroxypurine + 2 NADH + 2 H+
-
Substrates: considerable activity
Products: 84% xanthine, 8% 2,8-dihydroxypurine formed
Products: 84% xanthine, 8% 2,8-dihydroxypurine formed
?
2 hypoxanthine + 2 NAD+ + 2 H2O
xanthine + 6,8-dihydroxypurine + 2 NADH + 2 H+
-
Substrates: preferred substrate
Products: 100% xanthine, 51% 6,8-dihydroxypurine formed
Products: 100% xanthine, 51% 6,8-dihydroxypurine formed
?
3 purine + 3 NAD+ + 3 H2O
hypoxanthine + 8-hydroxypurine + 2-hydroxypurine + 3 NADH + 3 H+
-
Substrates: poor substrate
Products: 2.3% hypoxanthine, 2.3% 8-hydroxypurine and traces of 2-hydroxypurine formed
Products: 2.3% hypoxanthine, 2.3% 8-hydroxypurine and traces of 2-hydroxypurine formed
?
6,8-dihydroxypurine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: 18% urate formed
Products: 18% urate formed
?
guanine + NAD+ + H2O
? + NADH
-
Substrates: 81.3% of the activity compared to hypoxanthine
Products: -
Products: -
?
hypoxanthine + NAD+ + 2 H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
hypoxanthine + NADH
? + NO2- + NAD+
-
Substrates: 0.1% of the xanthine oxidation rate
Products: -
Products: -
?
hypoxanthine + urate
xanthine + 6,8-dihydroxypurine
-
Substrates: oxygen-free assay
Products: -
Products: -
r
NADPH + O2
NADP+ + O2- + H+
-
Substrates: high NADPH oxidase activity
Products: -
Products: -
?
purine + NAD+ + H2O
8-hydroxypurine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
purine + NADP+ + H2O
? + NADPH
-
Substrates: 60% of the activity compared to hypoxanthine
Products: -
Products: -
?
xanthine + O2
hypoxanthine + ?
-
Substrates: dismutation reaction
Products: -
Products: -
?
xanthopterin + NAD+ + H2O
leucopterin + NADH
-
Substrates: regulation of the pteridine pathway by competitive inhibition of reaction products and the precursor of xanthopterin, 7,8-dihydroxanthopterin
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: precursor of the eye pigment drosopterin
Products: precursor of the eye pigment drosopterin
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
r
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: conversion of xanthine dehydrogenase to xanthine oxidase is strongly influenced by in vitro cell culture of alveolar epithelial cells
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: i.e. pterin
Products: -
Products: -
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
Substrates: 11% of the activity compared to xanthine
Products: -
Products: -
?
hypoxanthine + 2 NAD+ + 2 H2O
urate + 2 NADH + 2 H+
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: NAD+-O2- dependent xanthine oxidase activity
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: NAD+-O2- dependent xanthine oxidase activity
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: predominant reaction
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: subtilisin treatment leads to an active component I of 120000 kDa
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
r
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: more rapidly oxidized than xanthine
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
Substrates: preferred substrate
Products: -
Products: -
ir
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: preferred substrate
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
Substrates: -
Products: -
Products: -
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
-
Substrates: -
Products: -
Products: -
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
-
Substrates: strict specificity for NADP+
Products: -
Products: -
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
-
Substrates: 40% of the activity compared to NAD+
Products: -
Products: -
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
-
Substrates: 2.4% of the activity compared to NAD+
Products: -
Products: -
?
hypoxanthine + O2
xanthine + H2O2
-
Substrates: very low activity
Products: -
Products: -
?
purine + NAD+ + H2O
? + NADH
-
Substrates: poor substrate
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: regulation of xanthine dehydrogenase expression is subjected to nitrogen catabolite repression mediated through the GlnA-dependent signaling pathway
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: xanthine dehydrogenase form has distinct xanthine/oxygen activity, 35-42% of electrons transferred to O2 to form O2-
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: conversion of dehydrogenase to oxidase type due to oxidation of sulfhydryl groups by molecular oxygen, dehydrogenase activity recovered by treatment with dithiothreitol
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: NAD+-dependent dehydrogenase type D
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: involved in pteridine metabolism, 40% of activity compared to hypoxanthine
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: only dehydrogenase type D present
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: ping-pong reaction mechanism
Products: -
Products: -
r
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: 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
Products: -
Products: -
r
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: 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
Products: 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
Products: 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
-
Substrates: only present as stable dehydrogenase from, no conversion to the oxidase form
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: subtilisin treatment leads to an active component I of 120000 kDa
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: 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
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: degradative pathway of conversion of purines to ammonia
Products: -
Products: -
r
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
r
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: NAD+-linked activity, very low activity towards molecular oxygen
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: 75% of the activity compared to hypoxanthine
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: NAD+-dependent form is postulated to play a regulatory role in purine metabolism
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: conversion of xanthine dehydrogenase to the oxidase type by thiol-disulfide oxidoreductase, thiol reagents or oxidized glutathione
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: trypsin treatment leads to a complete conversion of xanthine dehydrogenase to xanthine oxidase activity
Products: -
Products: -
r
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: NAD+-dependent dehydrogenase type D
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: 67% of the activity compared to hypoxanthine
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: 61% of the activity compared to hypoxanthine
Products: 91% urate formed
Products: 91% urate formed
?
xanthine + NAD+ + H2O
urate + NADH
-
Substrates: strict dehydrogenase activity, no utilization of O2
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: catalytically relevant binding mode of the substrate xanthine, overview
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: catalytically relevant binding mode of the substrate xanthine, overview
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: when catalyzing the sequential oxidation of hypoxanthine to xanthine to uric acid, XDH uses the NAD+ as final electron receptor to produce NADH
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Rhodobacter capsulatus B10XDHB
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Rhodobacter capsulatus CGMCC 1.3366
Substrates: when catalyzing the sequential oxidation of hypoxanthine to xanthine to uric acid, XDH uses the NAD+ as final electron receptor to produce NADH
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
Rhodobacter capsulatus CGMCC 1.3366
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
-
Substrates: heat-treated intermediate dehydrogenase/oxidase type O
Products: -
Products: -
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
-
Substrates: intermediate form of dehydrogenase/oxidase type D/O
Products: -
Products: -
?
xanthine + NADP+ + H2O
urate + NADPH
-
Substrates: 11% of the activity compared to NAD+
Products: -
Products: -
?
xanthine + NADP+ + H2O
urate + NADPH
-
Substrates: strict specificity for NADP+
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: xanthine oxidase form transfers 22% electrons to oxygen to form superoxide
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: low activity
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: -
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: low activity
Products: -
Products: -
r
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: very low activity
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: low activity
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: subtilisin treatment leads to an active component I of 120000 kDa
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: -
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: very low activity
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: 4% of the activity compared to xanthine-NAD+
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: 4% of the activity compared to xanthine-NAD+
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: toxic reactions of xanthine oxidase-derived radicals are critical factors in several mechanisms of tissue pathology
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: NAD+-independent trypsin-treated oxidase type O
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: 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
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: -
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: very low activity
Products: -
Products: -
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
Substrates: presence of ferredoxin enhances rate of oxygen reduction
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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%
Products: -
Products: -
?
additional information
?
-
Substrates: 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%
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: xanthine oxidoreductase is a regulator of adipogenesis and of nuclear recptor PPARgamma activityand is essential for the regulation of fat accretion
Products: -
Products: -
?
additional information
?
-
-
Substrates: major function of enzyme in liver parenchymal and sinusoidal cells is the production of uric acid as a antioxidant
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme inhibition by orange juice and hesperetin participates in preventing oxidative stress by enhancing total antioxidant capacity and decreasing lipid peroxidation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
molybdopterin cytosine dinucleotide
localized in subunit PaoC
[4Fe-4S]-center
cluster is anchored to an additional 40 residues subdomain of subunit PaoB
FAD
-
trypsin-treated oxidase type O shows absence of FAD, heat-treated oxidase type O shows small measurable FAD
FAD
-
substitutions G348E, G353D, S357F located within the flavin/NAD+/NADH-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
-
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
subunit PaoB exhibits a typical FAD binding motif
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
-
structure-function analysis, mechanism, overview
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
-
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
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
[2Fe-2S] cluster
two N-terminal non-identical iron-sulfur clusters of the [2Fe-2S]-type
[2Fe-2S]-center
iron-sulfur subunit PaoA can be divided into two subdomains, each carrying one [2Fe-2S] cluster
[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
two nonidentical [2Fe-2S] clusters designated as Fe/SI and Fe/SII, distinguished by redox potential and EPR signal
[2Fe-2S]-center
protein contains 2 2Fe-2S iron-sulfur-cluster-binding domains
additional information
-
molybdoironflavoprotein: molar ratio of molybdenum to iron to acid-labile-sulfur to FAD is 1 : 2 : 1.9 : 0.8
-
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
-
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. 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
-
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
-
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, 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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Fe2+
Iron
Iron-sulfur-center
Mo
Molybdenum
molybdenum-center
Se
selenium
Tungsten
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
Fe
-
non-heme iron-sulfur groups, 7.7 g-atom Fe, 7.5 g- atom S2- per mol enzyme
Iron
enzyme is about 30% deficient in iron-sulfur centers on basis of UV/vis and CD spectra
Iron
-
FeS center, EPR spectra, wild type 3.7 mol per subunit, active form of mutant R135C 2.8 mol per subunit, inactive form of mutant R135C 1.2 mol per subunit
Iron
-
the enzyme is a molybdo-flavoprotein, the enzyme tetramer contains two [2Fe-2S] clusters
Iron-sulfur-center
-
2 Fe2-S2-clusters, located at the N-terminal 20 kDa domain
Iron-sulfur-center
-
substitutions G42E, E89K, L127F located within the iron-sulfur domain
Molybdenum
-
superoxide production depends on sulfuration of molybdenum cofactor
Molybdenum
a molybdenum-iron-flavo enzyme, which contains a C-terminal molybdenum cofactor-binding domain of 85 kDa
Molybdenum
a molybdenum-containing flavoprotein, biosynthesis of sulfurated molybdenum cofactor, overview
Molybdenum
-
in milk, more than 90% of enzyme exists in the inactive demolybdo form
Molybdenum
-
1.1 atoms per alphabeta protomer in wild-type, 0.89 atoms per alphabeta protomer after expression of xdhABC genes, 0.24 atoms per alphabeta protomer after expression of xdhAB genes
Molybdenum
molybdopterin-cytosine-dinucleotide localized in subunit PaoC
Molybdenum
-
the enzyme contains molybdenum cofactor comprising only molybdopterin and molybdenum
Molybdenum
XOR is a molybdenum-containing enzyme, cofactor geometry, overview
Molybdenum
-
active form of mutant R135C Moco content 97%, inactive form of mutant R135C Moco content 3.8%
Molybdenum
-
protein XdhC binds molybdenum cofactor in stoichiometric amounts, which subsequently can be inserted into molybdenum-free apoxanthine dehydrogenase. Protein XdhC is required for the stabilization of the sulfurated form of molybdenum cofactor
Molybdenum
-
the enzyme is molybdo-flavoprotein, one cofactor molecule per enzyme tetramer
Molybdenum
-
in the molybdenum cofactor, the metal ion binds a molybdopterin (MPT) molecule via its dithiolene function and terminal sulfur and oxygen groups. 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
Molybdenum
molybdenum-containing flavoenzyme, in the molybdenum cofactor (Moco)
Molybdenum
-
superoxide production depends on sulfuration of molybdenum cofactor
molybdenum-center
-
contains molybdopterin mononucleotide rather than molybdopterin dinucleotide
molybdenum-center
-
substitutions G800E, G1011E, G1164R, G1266D, S1275F located within the pterin molybdenum cofactor domain
molybdenum-center
-
urate, xanthine and 8-bromoxanthine interact with the molybdenum-site of fully reduced xanthine oxidase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-methylhypoxanthine
-
17% inhibition of xanthine dehydrogenase at 0.25 mM
17beta-estradiol
-
inhibition of enzyme activity in malignant and non-malignant mammary epithelial cells
2-(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
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
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
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
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
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
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
hypoxanthine
-
inactivation of xanthine oxidase activity, not in the presence of NAD+
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
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
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
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
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
-
51% inhibition of hypoxanthine oxidation at 0.0001 mM
4-hydroxypyrazolo(3,4-d)pyrimidine
-
i.e. allopurinol; inhibition of pterine oxidation at 0.0003 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
-
treatment of normal fruit in linear phase of growth arrests fruit growth
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
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
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
-
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
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
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
-
35% inhibition of pterine oxidation, 60% inhibition of diaphorase activity at 5 mM
KCN
-
complete inactivation of oxygen-linked activity in 15 min, decline of NAD+-linked activity in 75 min, ferricyanide-linked activity completely stable
KCN
-
10-50% inhibition of xanthine oxidation only in the presence of Tris or phosphate buffers from 0.01 to 0.1 M inhibitor concentration
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
-
develops inhibition during course of catalysis, enhanced inhibition in the presence of ferricyanide in the oxygen-dependent oxidation of xanthine
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
o-phenanthroline
-
19.5% inhibition of hypoxanthine oxidation at 10 mM
oxypurinol
-
blocks xanthine dehydrogenase activity, without influencing xanthine oxidase activity
Salicylhydroxamic acid
-
82% inhibition of hypoxanthine oxidation at 2.5 mM
Sodium dithionite
-
irreversible inactivation by reduction of xanthine dehydrogenase, no recovery after dithionite elimination
Urate
-
varied substrate: xanthine, dead-end inhibition type, Ki 0.18 mM, varied substrate: NAD+, product inhibition, Ki 0.45 mM
Urate
-
competitive inhibition of xanthine dehydrogenase, Ki: 0.144 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
-
substrate inhibition above 0.05 mM, but in the presence of NAD+
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
allopurinol
-
inhibits xanthine and hypoxanthine oxidation in vivo in intestine and pancreas, but enhances the activity in liver, tissue-dependent effects, overview
Ferredoxin
-
26fold increase of cytochrome c reduction, 2fold increase of oxygen reduction
-
PD98059
-
inhibitor used to block MEK-1/2 kinase, activates the promoter of xanthine oxidoreductase and significantly enhances expression of enzyme induced by insulin, acute phase cytokines, or growth factors
sodium nitroprusside
-
i.e. SNP, a NO donor, activates at concentrations of up to 3 mM, preventable by hemoglobin, overview
sulfide/dithionite
treatment increases the specific activity of AtXDH1
-
additional information
-
activation mechanism based on the results of mutations at the positions of the second Glu and Arg residues, overview
-
thiol active compounds
-
reversible conversion of xanthine dehydrogenase to xanthine oxidase by modification of C535 and C992 and formation of a disulfide bond, that induces a conformational change
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
adenine phosphoribosyltransferase deficiency
[2,8-dihydroxyadenine nephrolithiasis: from diagnosis to therapy]
Amyotrophic Lateral Sclerosis
Analysis of aldehyde oxidase and xanthine dehydrogenase/oxidase as possible candidate genes for autosomal recessive familial amyotrophic lateral sclerosis.
Bacterial Infections
Enzymes involved in purine metabolism--a review of histochemical localization and functional implications.
Carcinoma, Hepatocellular
Decreased concentration of xanthine dehydrogenase (EC 1.1.1.204) in rat hepatomas.
Chagas Disease
Inhibition of xanthine dehydrogenase from Triatoma infestans by some purine analogues.
d-xylulose reductase deficiency
The RNAi-Mediated Silencing of Xanthine Dehydrogenase Impairs Growth and Fertility and Accelerates Leaf Senescence in Transgenic Arabidopsis Plants.
Lung Injury
Effect of hypoxia and reoxygenation on the formation and release of reactive oxygen species by porcine pulmonary artery endothelial cells.
Lung Injury
Upregulation of xanthine oxidase by lipopolysaccharide, interleukin-1, and hypoxia. Role in acute lung injury.
Neoplasms
Dissecting the role of multiple reductases in bioactivation and cytotoxicity of the antitumor agent 2,5-diaziridinyl-3-(hydroxymethyl)-6-methyl-1,4-benzoquinone (RH1).
Neoplasms
Responses of vascular endothelial oxidant metabolism to lipopolysaccharide and tumor necrosis factor-alpha.
Pneumonia, Viral
Molecular cloning and characterization of the human xanthine dehydrogenase gene (XDH).
Proteinuria
Renal purine efflux and xanthine oxidase activity during experimental nephrosis in rats: difference between puromycin aminonucleoside and adriamycin nephrosis.
Pulmonary Edema
Upregulation of xanthine oxidase by lipopolysaccharide, interleukin-1, and hypoxia. Role in acute lung injury.
Renal Insufficiency
Molecular cloning and characterization of the human xanthine dehydrogenase gene (XDH).
Stomach Ulcer
Upregulation of xanthine oxidase by tobacco smoke condensate in pulmonary endothelial cells.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004
2-amino-4-hydroxypterin
-
pH 7.0, electron acceptor: methylene blue
0.0071
2-amino-4-hydroxypterin
-
pH 8.0, electron acceptor: methylene blue
0.011
2-amino-4-hydroxypterin
-
increased Km in the presence of pyridoxal
1
4-hydroxypyrazolo(3,4-d)pyrimidine
-
electron acceptor: 2,6-dichlorophenolindophenol
0.047 - 0.079
hypoxanthine
-
measured in the pH range from 6 to 8.9, pH-independent Km
0.0052
NAD+
DTT-treated C-terminally truncated enzyme mutant, pH 7.8, 25°C
0.033
NAD+
-
increased Km for mutant G353D, electron acceptor: pterin
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
0.113
NAD+
coexpression of genes xdhABC, conditions of low aeration, pH 7.8, 25°C
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
0.048
NADH
-
increased Km for mutant G353D, electron acceptor: 2,6-dichlorophenolindophenol
0.029
xanthine
-
electron acceptors: phenazine methosulfate/cytochrome c
0.035
xanthine
-
immobilized enzyme preparation, pH 7.9, pH dependence, minimum Km at pH 8.1, increasing values below and above
0.066
xanthine
coexpression of genes xdhAB, conditions of high aeration, pH 7.8, 25°C
0.067
xanthine
coexpression of genes xdhAB, conditions of low aeration, pH 7.8, 25°C
0.085
xanthine
coexpression of genes xdhABC, conditions of high aeration, pH 7.8, 25°C
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
-
kinetics in presence and absence of cellular retinol binding proteins, apo-CRBP and apo-CRABP, overview
-
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
steady-state kinetics of DTT-treated and untreated C-terminally truncated enzyme mutant
-
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
Michaelis-Menten steady-state kinetics, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.1
NADH
-
activation of mutant G1011E activity after preincubation with phenazine methosulfate and cytochrome c, electron acceptor: methylene blue
29
NADH
-
activation of mutant G1011E activity after preincubation with ferricyanide, electron acceptor: methylene blue
0.4
xanthine
coexpression of genes xdhAB, conditions of low aeration, pH 7.8, 25°C
27
xanthine
coexpression of genes xdhAB, conditions of high aeration, pH 7.8, 25°C
31
xanthine
-
recombinant enzyme, electron acceptor: phenazine methosulfate-cytochrome c
86
xanthine
coexpression of genes xdhABC, conditions of low aeration, pH 7.8, 25°C
118
xanthine
coexpression of genes xdhABC, conditions of high aeration, pH 7.8, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
6-chloro-2-[3-(4-hydroxyphenyl)-1-phenyl-1-H-pyrazol-4-yl]-chromen-4-one, Ki-value 0.0011 mg/ml, 6-chloro-7-methyl-2-[3-(4-chlorophenyl)-1-phenyl-1-H-pyrazol-4-yl]-chromen-4-one, Ki-value 0.00022 mg/ml, respectively
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.22
0.27
1.712
purified recombinant enzyme, in presence of sulfide/dithionite
1.8
10
-
purified native enzyme, pH and temperature not specified in the publication
17.5
2.8
-
highest activity if growth medium contains urate and is supplemented with 0.0001 mM selenite and 0.0001 mM tungstate
29.1
-
purified recombinant enzyme, pH and temperature not specified in the publication
3.7
-
highest activity if growth medium contains urate and is supplemented with 0.0001 mM selenite and 0.0001 mM molybdate
7
purified recombinant enzyme, pH and temperature not specified in the publication
7.5
-
purified native enzyme, pH and temperature not specified in the publication
additional information
17.5
-
purified enzyme, pH and temperature not specified in the publication
additional information
-
enzymic activity is only detectable after resulfuration of purified enzyme
additional information
-
serum uric acid levels in healthy and hypeuricemic rats, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7.5 - 8
7.8
7.9
8 - 8.6
-
xanthine-NAD+, NADH-nitroblue tetrazolium or xanthine-nitroblue tetrazolium assay
8.5
7
-
optimum value in the reverse reaction with urate and reduced methyl viologen
8.5
-
optimum value for oxidation of xanthine and reduction of methyl viologen
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11.5
activity range, bell-shaped pH-activity relationships for both the recombinant split variants
4.5 - 9
the enzyme is highly active at pH 5.0-8.0, shows low activity at pH 9.0, and is inactive above
additional information
additional information
-
Acinetobacter baumannii XDH extends the pH tolerance to pH 11.0
additional information
comparison of the pH dependence of both kred and kred/Kd from reductive half-reaction experiments between wild-type enzyme and mutant E232Q, overview. 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
40
41
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
-
-
brenda
Rhodobacter capsulatus CGMCC 1.3366
induction by application of abscisic acid and in water-stressed leaves and roots
-
-
brenda
induction by application of abscisic acid and in water-stressed leaves and roots
-
-
brenda
expression in Pseudomonas aeruginosa, for maximal level of functional expression, co-expression of xdhC gene is required which increases level of molybdenum incorporation. Iron and FAD content of expressed enzymes are independent of xdhC expression
-
-
brenda
large subunit; expression of genes xdhAB encoding the two subunits of enzyme, in Escherichia coli, produces active enzyme. Coexpression of xdhAB genes with Pseudomonas aeruginosa xdhC gene results in high levels of functional protein
Swissprot
brenda
small subunit; expression of genes xdhAB encoding the two subunits of enzyme, in Escherichia coli, produces active enzyme. Coexpression of xdhAB genes with Pseudomonas aeruginosa xdhC gene results in high levels of functional protein
Swissprot
brenda
P77165 i.e. alpha-subunit, P77324 i.e. beta-subnit, P77489 i.e. gamma-subunit
UniProt
brenda
increase in activity upon growth on selenite or molybdate, xanthine or uric acid
-
-
brenda
-
-
-
brenda
expression of enzyme in baculovirus-insect cell system, yields a mixture of native dimeric, demolydbo-dimeric and monomeric forms. All forms contain flavin, the monomeric forms lack molybdopterin and the iron-sulfur centers. Monomeric forms require only three electrons for complete reduction
-
-
brenda
male Sprague-Dawley rats, potassium oxonate-induced hyperuricemic rats
-
-
brenda
treated for 7 days with cocaine, or cocaine with a NADPH oxidase inhibitor apocynin, or cocaine with a xanthine oxidoreductase inhibitor allopurinol
-
-
brenda
small and large subunits encoded by genes xdhA and xdhB
UniProt
brenda
small and large subunits encoded by genes xdhA and xdhB, and chaperone encoded by gene xdhC
UniProt
brenda
Rhodobacter capsulatus CGMCC 1.3366
small and large subunits encoded by genes xdhA and xdhB, and chaperone encoded by gene xdhC
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
mRNA expression increases 8-fold during the first 12 hr postinduction and subsequently declines to preinduction levels by day 3. Xanthine dehydrogenase activity is maximally induced at 24 hr postinduction, while xanthine oxidase activity remains relatively unchanged
brenda
-
xanthine oxidoreductase is activated in a p38 MAP kinase-dependent manner following high tidal volume mechanical ventilation and is involved in resulting increased alveolar cell apoptosis
brenda
-
enzyme activity is maximal in late linear phase of fruit growth
brenda
-
exists preliminary as oxidase form, promotes oxidative incorporation of iron into mucosal transferrin, facilitates dietary iron absorption
brenda
-
identification of zinc-binding protein identical to xanthine oxidoreductase of 85 kDa
brenda
additional information
-
selenium is needed for xanthine dehydrogenase formation
brenda
-
0.0025 mg/ml sodium tungstate in the growth medium reduces level of ferricyanide-linked enzyme to 3%
brenda
XDH1 is expressed in epidermal cells albeit at relatively lower levels compared with mesophyll cells
brenda
-
XDH1 is expressed in epidermal cells albeit at relatively lower levels compared with mesophyll cells
-
brenda
-
only oxidase type O form, can be converted to dehydrogenase type D by dithioerythritol
brenda
cold stress causes decrease, desiccation and senesence cause strong increase in activity
brenda
in leaf peroxisomes, the superoxide-generating form, xanthine oxidase XOD is predominant over the xanthine dehydrogenase form XDH, with a XDH/XOD ratio of 0.5. In crude extracts of pea leaves, the XDH form is more abundant, with a XDH/XOD ratio of 1.6
brenda
-
XOR activity reduced by allopurinol treatment. Birds fed with inosine and allopurinol show lower total XOR activity in liver but no effect in kidney
brenda
-
high oxidase and reductase activities at nearly the same rates
brenda
-
high oxidase and reductase activities at nearly the same rates
brenda
-
the dehydrogenase form of liver xanthine oxidoreduxtase is intrinsically more efficient at generating superoxide anion radicals than the oxidase form, independently of the reducing substrat
brenda
-
exists preliminary as dehydrogenase form, participates in mobilization of iron from ferritin stores
brenda
-
lung xanthine oxidoreductase activity is significantly increased after 2 h of mechanical ventilation without changes in enzyme expression. Increase occurs via activation of p38 MAP kinase and ERK and plays a critical role in the pathogenesis of pulmonary edema associated with ventilator-induced lung injury
brenda
-
constitutive expression and high activity of XDH in non-malignant cells
brenda
-
only oxidase type in stored milk, 94% NAD+-dependent dehydrogenase type in fresh milk
brenda
-
xanthine oxidoreductase associated with milk phospholipid membranes was found to be distributed among an intra-membranous pool in which it takes the form of a mixture of xanthine oxidase and xanthine dehydrogenase, with a clear predominance of xanthine dehydrogenase, and a free pool of xanthine oxidase, of which 33% is found in the outer surface of milk fat globule membrane, 20.5% in the outer surface of whey membrane particles, and the remaining 46.7% in apparent solution. The inner-membrane xanthine oxidoreductase may play a nonenzymatic role in fat secretion, whereas extramembranous xanthine oxidase is freely available for a role in the innate gland immune system and may affect milk quality
brenda
-
in milk, more than 90% of enzyme exists in the inactive demolybdo form
brenda
-
five different forms in electrophoretic mobility, but no differences in kinetic constants
brenda
-
selection of 11 rosy mutant strain, corresponding to single amino acid substitutions for detailed studies on the activities
brenda
additional information
tissue expression profile of gene XDH1, differential isozymes XDH1 and XDH2 gene tissue expression, transcripts for XDH2 are much less abundant compared to XDH1 in most of the tissues, overview. XDH1 gene expression is immediately upregulated after a blood meal in the fat body, midgut, and thorax. In the midgut, XDH1 transcript levels increase 10fold. In malpighian tubules, the XDH1 mRNA levels increase after blood feeding, reaching a peak at 18 h PBM, while XDH1 transcript levels in the ovary are constitutively expressed during the first gonotrophic cycle, with a slight increase occurring between 24 and 48 h and a decrease thereafter
brenda
additional information
tissue expression profile of gene XDH1, differential isozymes XDH1 and XDH2 gene tissue expression, transcripts for XDH2 are much less abundant compared to XDH1 in most of the tissues, overview. XDH1 gene expression is immediately upregulated after a blood meal in the fat body, midgut, and thorax. In the midgut, XDH1 transcript levels increase 10fold. In malpighian tubules, the XDH1 mRNA levels increase after blood feeding, reaching a peak at 18 h PBM, while XDH1 transcript levels in the ovary are constitutively expressed during the first gonotrophic cycle, with a slight increase occurring between 24 and 48 h and a decrease thereafter
brenda
additional information
-
tissue expression profile of gene XDH1, differential isozymes XDH1 and XDH2 gene tissue expression, transcripts for XDH2 are much less abundant compared to XDH1 in most of the tissues, overview. XDH1 gene expression is immediately upregulated after a blood meal in the fat body, midgut, and thorax. In the midgut, XDH1 transcript levels increase 10fold. In malpighian tubules, the XDH1 mRNA levels increase after blood feeding, reaching a peak at 18 h PBM, while XDH1 transcript levels in the ovary are constitutively expressed during the first gonotrophic cycle, with a slight increase occurring between 24 and 48 h and a decrease thereafter
brenda
additional information
tissue expression profile of gene XDH2, differential isozymes XDH1 and XDH2 gene tissue expression, for XDH2 ae much less abundant compared to XDH1 in most of the tissues, overview. In the midgut and malpighian tubules, XDH2 mRNA levels increase over time, with peaks at 36 and 18 h, respectively. XDH2 gene expression in the fat body has peaks at 6, 18, 48, and 72 h PBM, whereas the XDH2 transcript levels in the thorax are significantly upregulated at 12, 24, 36, and 48 h PBM. In the ovary, XDH2 gene expression does not change significantly during the first gonotrophic cycle
brenda
additional information
tissue expression profile of gene XDH2, differential isozymes XDH1 and XDH2 gene tissue expression, for XDH2 ae much less abundant compared to XDH1 in most of the tissues, overview. In the midgut and malpighian tubules, XDH2 mRNA levels increase over time, with peaks at 36 and 18 h, respectively. XDH2 gene expression in the fat body has peaks at 6, 18, 48, and 72 h PBM, whereas the XDH2 transcript levels in the thorax are significantly upregulated at 12, 24, 36, and 48 h PBM. In the ovary, XDH2 gene expression does not change significantly during the first gonotrophic cycle
brenda
additional information
-
tissue expression profile of gene XDH2, differential isozymes XDH1 and XDH2 gene tissue expression, for XDH2 ae much less abundant compared to XDH1 in most of the tissues, overview. In the midgut and malpighian tubules, XDH2 mRNA levels increase over time, with peaks at 36 and 18 h, respectively. XDH2 gene expression in the fat body has peaks at 6, 18, 48, and 72 h PBM, whereas the XDH2 transcript levels in the thorax are significantly upregulated at 12, 24, 36, and 48 h PBM. In the ovary, XDH2 gene expression does not change significantly during the first gonotrophic cycle
brenda
additional information
-
enzyme tissue distribution, no age-dependent differences, overview
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
milk phospholipid membrane, mixture of xanthine oxidase and xanthine dehydrogenase, with a clear predominance of xanthine dehydrogenase
brenda
in leaf peroxisomes, the superoxide-generating form, xanthine oxidase XOD is predominant over the xanthine dehydrogenase form XDH, with a XDH/XOD ratio of 0.5. Enzyme is localized to the matrix of peroxisome
brenda
-
matrix and core, of parenchymal cells, both oxidase and dehydrogenase activity
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
Rhodobacter capsulatus B10XDHB
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
-
malfunction
-
the retinoic acid deficiency in breast tumour epithelial cells has been ascribed to an insufficient expression of either the enzyme(s) involved in its biosynthesis or the cellular retinol binding protein or both, overview
malfunction
-
potassium oxonate-induced hyperuricemia can be reduced by oral application of onions reducing serum uric acid levels in hyperuricemic rats. The compound probably does not act via simple enzyme inhibition mechanism
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
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
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
-
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 is a ubiquitous molybdenum-iron-flavo enzyme with a central role in purine catabolism where it catalyzes the oxidation of hypoxanthine to xanthine and of xanthine to uric acid
physiological function
-
xanthine 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 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
AtXDH1 is a key enzyme in purine degradation where it oxidizes hypoxanthine to xanthine and xanthine to uric acid
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
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
-
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
-
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
-
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
-
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
-
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 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
-
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 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
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 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
-
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
isozyme XDH1 plays an essential role in Aedes aegypti vector control
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
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
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
-
the enzyme is involved in the regulation of normal and abiotic stress-induced ageing processes in rice
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
-
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
-
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
Rhodobacter capsulatus B10XDHB
-
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
-
additional information
-
biofilm formation is stimulated in the presence of uric acid, Se, and Mo and inhibited by auranofin or tungstate
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
mammalian XOR exists in two interconvertible forms, the xanthine dehydrogenase, XDH, form and the xanthine oxidase, XO, form. The primary gene product is XDH, which can be converted into XO
additional information
XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4
additional information
-
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
-
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
-
the chicken XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
additional information
-
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 Rhodobacter capsulatus 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
-
analysis of the mechanism of transfer of an oxygen atom to the substrate
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
Rhodobacter capsulatus CGMCC 1.3366
-
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
Rhodobacter capsulatus B10XDHB
-
the Rhodobacter capsulatus XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
-
Show AA Sequence and Transmembrane Helices (3673 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
-
1 * 110000 + 1 * 83000 + 1 * 56000 + 1 * 53000 + 1 * 26000, SDS-PAGE
140000
150000
155000
16000
-
alpha4, 4 * 80000 + beta4, 4 * 35000 + gamma4, 4 * 16000, SDS-PAGE
160000
17500
-
tetramer of alpha/beta/gamma-protomers, alpha4, 4 * 81300 + beta4, 4 * 30000 + gamma4, 4 * 17500, SDS-PAGE
26000
-
1 * 110000 + 1 * 83000 + 1 * 56000 + 1 * 53000 + 1 * 26000, SDS-PAGE
290000
30000
-
tetramer of alpha/beta/gamma-protomers, alpha4, 4 * 81300 + beta4, 4 * 30000 + gamma4, 4 * 17500, SDS-PAGE
300000
35000
-
alpha4, 4 * 80000 + beta4, 4 * 35000 + gamma4, 4 * 16000, SDS-PAGE
350000
53000
-
1 * 110000 + 1 * 83000 + 1 * 56000 + 1 * 53000 + 1 * 26000, SDS-PAGE
56000
-
1 * 110000 + 1 * 83000 + 1 * 56000 + 1 * 53000 + 1 * 26000, SDS-PAGE
80000
-
alpha4, 4 * 80000 + beta4, 4 * 35000 + gamma4, 4 * 16000, SDS-PAGE
81300
-
tetramer of alpha/beta/gamma-protomers, alpha4, 4 * 81300 + beta4, 4 * 30000 + gamma4, 4 * 17500, SDS-PAGE
83000
-
1 * 110000 + 1 * 83000 + 1 * 56000 + 1 * 53000 + 1 * 26000, SDS-PAGE
90000
140000
-
x * 140000, SDS-PAGE, trypsin-treated: x * 90000, SDS-PAGE, conversion of dehydrogenase to oxidase activity
90000
-
x * 140000, SDS-PAGE, trypsin-treated: x * 90000, SDS-PAGE, conversion of dehydrogenase to oxidase activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dodecamer
heterohexamer
heterooctamer
heterotetramer
homodimer
pentamer
-
1 * 110000 + 1 * 83000 + 1 * 56000 + 1 * 53000 + 1 * 26000, SDS-PAGE
tetramer
additional information
?
x * 150000, about, C-terminally truncated mutant enzyme DELTAC, SDS-PAGE
?
-
x * 140000, SDS-PAGE, trypsin-treated: x * 90000, SDS-PAGE, conversion of dehydrogenase to oxidase activity
dodecamer
-
tetramer of alpha/beta/gamma-protomers, alpha4, 4 * 81300 + beta4, 4 * 30000 + gamma4, 4 * 17500, SDS-PAGE
dodecamer
-
alpha4, 4 * 80000 + beta4, 4 * 35000 + gamma4, 4 * 16000, SDS-PAGE
heterohexamer
an (alphabetagamma)2 heterohexameric enzyme
heterotetramer
-
(alphabeta)2 structure, mechanism of assembly and cofactor insertion on two different polypeptides: dimerization of the (alphabeta) subunits has to precede molybdenum cofactor insertion, the two subunits act independently without cooperativity, incomplete assembly of FeSI impairs the formation of the XDH (alphabeta)2 heterotetramer and, thus, insertion of the molybdenum cofactor into the enzyme, overview
homodimer
composed of two identical subunits of about 145 kDa, each being subdivided into three domains: a N-terminal iron-sulfur-binding domain of 20 kDa, a 40 kDa domain harboring a FAD-binding site, and a C-terminal molybdenum cofactor-binding domain of 85 kDa
tetramer
-
2 * 87000, alpha-subunit, + 2 * 56000, beta-subunit, alpha2beta2
tetramer
-
2 * 50000, alpha-subunit, + 2 * 80000, beta-subunit, alpha2beta2
tetramer
Rhodobacter capsulatus B10XDHB
-
2 * 50000, alpha-subunit, + 2 * 80000, beta-subunit, alpha2beta2
-
additional information
-
structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview
additional information
-
structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview
additional information
-
structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview
additional information
-
bacterial XDHs, including Rhodobacter capsulatus, Pseudomonas putida and Streptomyces cyanogenus, are found in the alpha2, alpha4, (alphabeta)2, (alphabeta)4, and alphabetagamma forms
additional information
-
structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview
additional information
-
structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview
additional information
-
bacterial XDHs, including Rhodobacter capsulatus, Pseudomonas putida and Streptomyces cyanogenus, are found in the alpha2, alpha4, (alphabeta)2, (alphabeta)4 and alphabetagamma forms
additional information
enzyme structure comparisons, overview
additional information
Rhodobacter capsulatus B10XDHB
-
bacterial XDHs, including Rhodobacter capsulatus, Pseudomonas putida and Streptomyces cyanogenus, are found in the alpha2, alpha4, (alphabeta)2, (alphabeta)4 and alphabetagamma forms
-
additional information
Rhodobacter capsulatus CGMCC 1.3366
-
enzyme structure comparisons, overview
-
additional information
-
bacterial XDHs, including Rhodobacter capsulatus, Pseudomonas putida and Streptomyces cyanogenus, are found in the alpha2, alpha4, (alphabeta)2, (alphabeta)4, and alphabetagamma forms
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
flavoprotein
additional information
-
conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.1 A resolution for both xanthine oxidase and dehydrogenase forms, irreversible pancreatin cleaved xanthine oxidase form results in blocking access of substrate NAD+ to the FAD cofactor
-
batch method, 2.5 and 3.3 A resolution for irreversible proteolytically cleaved xanthine oxidase form, 2.1 A resolution for dehydrogenase form
-
high-resolution crystal structure of XDH at 1.65 A resolution confirms the overall fold of the dimeric protein, the location of the cofactors and the mobile stretches of the polypeptide chain. 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
highly active bovine XOR in its XDH form is soaked in a large excess of NADH under strictly anaerobic conditions in order to reduce both FAD cofactor and iron sulfur centers and to block any electron transfer from the Mo center. The Mo ions in the crystal are fully reduced by soaking in 4 mM titanium citrate solution followed by 0.25 mM urate, crystal structure determination and analysis, superimposition, modelling
-
in complex with inhibitor FYX051, which is slowly hydroxylated by the enzyme
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
-
to 1.7 A resolution. The active site of PaoABC is highly exposed to the surface with no aromatic residues and an arginine (subunit PaoC-R440) making a direct interaction with subunit PaoC-E692, which acts as a base catalyst
mutant E803V, decrease in activity towards purine substrates is not due to large conformational change in the mutant protein
-
mutant W335A/F336L, showing two similar, but not identical subunits. The cluster involved in conformation-switching is completely disrupted in one subunit, but remains partly associated in the other. Xanthine oxidase and oxidoreductase forms of the mutant are in equilibrium that greatly favors the oxidase form, but upon incubation with dithiothreitol equilibrium is partly shifted towards the oxidoreductase form
purified recombinant C-terminally truncated mutant enzyme, crystals of the mutant protein are prepared in two ways: (a) crystallization of the protein directly after DTT treatment and (b) crystallization in the presence of DTT followed by extended soaks in mother liquor devoid of DTT to convert most of the protein to the XO form, X-ray diffraction structure determination and analysis at 2.0 A resolution. Comparisons of crystal structures of a stable wild-type XDH enzyme form, the triple mutant C535A/C992R/C1324, and the DELTAC truncated mutant XOR
XOR complexed with the artificial substrate 4-[5-pyridine-4-yl-1H-[1,2,4]triazol-3-yl]pyridine-2-carbonitril, FYX-051, crystal structure analysis. Urate complexes of the purified recombinant demolybdo-form of mutant D428A, X-ray diffraction structure determination and analysis at 1.7 A resolution
2.7 A resolution, direct coordination of alloxanthine to the molybdenum via a nitrogen atom
-
crystal structure determination of the free enzyme and the enzyme in complex with inhibitor alloxanthine
-
purified recombinant wild-type enzyme and subunit beta mutants E232A and E232Q with or without molybdenum cofactor, hanging drop vapor diffusion method, 15 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 1 mM EDTA, 200 mM NaCl,and 2.5 mM dithiothreitol are mixed 1 mM NAD+ and inhibitor pterin-6-aldehyde and with the reservoir solution containing 6-8 mM BaCl2, 6-8% polyethylene glycol 8000, 100 mM Tris-HCl, pH 8.3, 5-25mM dithiothreitol, and 3-4% isopropanol, whereas the EB232Q variant is mixed in a 1:2 ratio with the same reservoir solution, X-ray diffraction structure determination and analysis at 2.6-3.4 A resolution, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
-
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
-
E89K
G1011E
-
within the molybdenum domain, no activity without oxidative activation
R40K
mutation in subunit PaoC, strong decrease in activity
R440H
mutation in subunit PaoC, strong decrease in activity, crystallization data
E803V
R881M
C535A
-
resistant to conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine
C535A/C992R
C535A/C992R/C1316S
C535A/C992R/C1324S
C992R
-
resistant to conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine
W335A/F336L
mutant oxidoreductase displaying xanthine oxidase activity
C44A/C47A
-
site-directed mutagenesis, an instable subunit A mutant that cannot be purified
E220R/D517R
-
site-directed mutagenesis, a subunit B mutant that is mainly dimeris incontrast to the tetrameric wild-type enzyme, inactive mutant
E232A
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
E730A
EB232Q
catalytically inactive active site mutant, inactive desulfo enzyme form
Q102A
-
site-directed mutagenesis, a subunit A mutant that shows altered metal content and reduced KM and Kcat with xanthine compared to the wild-type enzyme
Q102G
-
site-directed mutagenesis, a subunit A mutant that shows altered metal content and reduced KM and Kcat with xanthine compared to the wild-type enzyme
Q179A
-
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
-
mutation corresponding to human protein variant of a patient suffering from xanthinuria I. Mutation results in an active (alphabeta)2 heterotetrameric form besides an inactive alphabeta heterodimeric form missing the FeSI center
R310K
R310M
R330M
-
the activity with substrate 2-hydroxy-6-methylpurine is only slightly affected
D430H
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
additional information
E89K
-
natural mutant strain, lacking iron-sulfur centers, activity to xanthine/NAD+ or xanthine/pterin not affected, but xanthine/phenazine methosulfate activity abolished
E803V
-
almost complete loss of activity with hypoxanthine, weak activity with xanthine, significant aldehyde oxidase activity
E803V
-
very low steady-state activity towards xanthine or hypoxanthine, loss of hydrogen bonding with one of these residues greatly influences the electron transfer process to the molybdenum center, changing the rate-limiting step in the reductive half-reaction
R881M
-
almost complete loss of activity with xanthine, weak activity with hypoxanthine, significant aldehyde oxidase activity
R881M
-
very low steady-state activity towards xanthine or hypoxanthine, loss of hydrogen bonding with one of these residues greatly influences the electron transfer process to the molybdenum center, changing the rate-limiting step in the reductive half-reaction
C535A/C992R
-
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
-
completely resistant to conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine
C535A/C992R/C1316S
-
mutation in residues involved in conversion of xanthin dehydrogenase to xanthine oxidase by formation of disulfide bonds. Using guanidine-HCl, the mutant can be converted into the oxidase form
C535A/C992R/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
-
completely resistant to conversion from dehydrogenase to oxidase by incubation with 4,4-dithiodipyridine
C535A/C992R/C1324S
-
an XDH-locked enzyme mutant that cannot be induced by sulfhydryl reagents to adopt the XO form
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
site-directed mutagenesis, the mutant exhibits a 12fold decrease in kred compared to wild-type
E730A
-
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
-
absorption spectra similar to wild-type. 20fold decrease of kred-value
R310K
-
kred, the limiting rate of enzyme reduction by substrate at high substrate concentration is 20-fold decreased
R310M
-
absorption spectra similar to wild-type. 20000fold decrease of kred-value
R310M
-
kred, the limiting rate of enzyme reduction by substrate at high substrate concentration is 20000-fold decreased
additional information
-
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
-
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
-
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
-
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
-
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
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
-
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
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
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
Rhodobacter capsulatus CGMCC 1.3366
-
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
Rhodobacter capsulatus CGMCC 1.3366
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11.5
both the recombinant split variants display similar bell-shaped pH-activity relationships with the optimum activity at pH 8.5 and remain stable in buffers ranging from pH 4.0-11.5 after incubation at 25°C for 24 h
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-20
30
-
enhanced stability of immobilized enzyme preparation if N2 and hemoglobin is included, reaction of oxygen products causes instability of the working enzyme, half-life: 250-560 min, compared to immobilized enzyme without additions of about 145 min
37
38
-
dehydrogenase type unstable, change to oxidase type inhibited under anaerobic conditions
51.6
t1/2 for the wild-type enzyme, pH 8.5, 30 min
63
t1/2 for the mutant Split166 enzyme, pH 8.5, 30 min
63.2
t1/2 for the mutant Split178 enzyme, pH 8.5, 30 min
65
37
-
30 min, increase in activity of both xanthine oxidase and xanthine oxidase plus dehydrogenase. No increase in presence of adenine
4
-
liver extract: conversion of dehydrogenase to oxidase activity, some loss of activity after 7 days, extract from cerebrellum and cerebral cortex: stable for 7 days
65
all the XDHs exhibit a bell-shaped temperature-activity relationship with maximum activity at 40°C, the recombinant split variants are more thermostable than the wild-type. Both Split166 and Split178 maintain about 60% of maximal activity at 65°C, while the wild-type shows below 20% remaining activity after 30 min
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant
crude and purified enzyme preparations form readily insoluble inactive aggregates, not stable to freezing and thawing
-
enzyme from crude extract can be stabilized by addition of nicotinamide, cysteine and EDTA, purified enzyme more stable
-
oxygen-linked activity rather unstable during storage at 4°C, ferricyanide-linked activity stable to freezing and thawing
-
treatment accelerating conversion of dehydrogenase type D to oxidase type O is lyophilization, storage at -20°C, exposure to 20% ammonium sulfate, 0.5 mM NAD+ or 0.01 mM xanthine
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 24 h, activity of both xanthine oxidase and xanthine oxidase plus dehydrogenase is lower in liver extracts with the combined presence of adenine and dithiotreitol/phenylmethylsulfonyl fluoride
-
-70°C, 0.1 M sodium diphosphate, 0.3 mM EDTA, pH 7.5, 1 mM salicylate, 2.5 mM DTT, 3 months
-
1°C, 1 mM DTT in conjunction with 0.1 M ammonium sulfate, 60-70% retaining activity after 8-12 days
-
4°C, 25 mM Tris-boric acid, pH 8.5, 2.5 mM EDTA, 2 mM 2-mercaptoethanol, 0.2 mM sodium molybdate, one year
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
adenine may play a role in preventing the dehydrogenase to oxidase conversion during extract preparation, storage, overnight dialysis and heat treatment
-
ammonium sulfate precipitation, phenyl-Sepharose column chromatography, DEAE-10 Macro-Prep MP10 column chromatography, and Bio-Prep SE-1000/17 column chromatography
-
during purification conversion from dehydrogenase type D to oxidase type O, reversible by dithioerythritol
-
highly active bovine XOR in its XDH form is prepared by folate affinity chromatography
-
near homogeneity, chromatography techniques
nearly homogenous, dehydrogenase type D, chromatography steps, oxidase type O purified by nearly the same procedure, but heated to 60°C after homogenization
-
partial
purification of native XDH
recombinant His-tagged enzyme from Escherichia coli strain TP1000 by nickel affinity and anion exchange chromatography, followed by gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity and anion exchange chromatography, followed by gel filtration
recombinant His-tagged wild-type and mutant XDH1 variants from Pichia pastoris strain KM71 by nickel affinity chromatography and anion exchange chromatography
recombinant His-tagged wild-type and mutant XDHs from Escherichia coli strain TP1000 by nickel affinity and anion exchange chromatography, followed by ultrafiltration and gel filtration
-
recombinant His-tagged XDH1 from Pichia pastoris by nickel affinity and anion exchange chromatography
recombinant wild-type and mutant enzymes with or without molybdenum cofactor by nickel affinity and anion exchange chromatography, followed by gel filtration
to homogeneity, 2 types: dehydrogenase type, chromatography techniques, oxidase type: affinity chromatography
-
to homogeneity, affinity chromatography
to homogeneity, chromatography techniques
to homogeneity, chromatography techniques, preparative gel electrophoresis
-
to homogeneity, mainly ferricyanide- and NAD+-linked activities, chromatography steps
-
to homogeneity, presence of DTT required for purification of the dehydrogenase form
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminally His6-tagged wild-type and mutant XDHs expression in Escherichia coli strain TP1000
-
expression of enzyme mutant D428A in Spodoptera frugiperda Sf9 cells via the baculovirus transfection system in mostly the demolybdo-form
expression of His-tagged wild-type and mutant XDH1 variants in Pichia pastoris strain KM71
gene VvXDH, sequence comparisons and phylogenetic analysis, synthesis of gene VvXDH through PCR-based two-step DNA synthesis method, recombinant overexpression in Arabidopsis thaliana ecotype Columbia under control of CaMV 35S promoter from plasmid pYM817 using the Agrobacterium tumefaciens strain GV3101 transfection method. The transgenic Arabidopsis thaliana plants show enhanced salt tolerance, phenotype, overview. 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. Expression of VvXDH results in elevated allantoin accumulation
gene Xdh, recombinant expression in Escherichia coli strain BL21(DE3), co-overexpression with three global regulators from Escherichia coli, IscS, TusA and NarJ and two Escherichia coli as well as two Rhodobacter capsulatus chaperone proteins, i.e. DsbA and DsbB, and NifS and XdhC (UniProt ID Q9X7K2), respectively, to aid the formation and ordered assembly of three redox center cofactors of Rhodobacter capsulatus XDH in Escherichia coli
gene xdh, sequence comparisons and phylogenetic analysis
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Pichia pastoris
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression of liver XDH in insect cell system
-
gene xdh1, genotyping, map-based cloning of drf mutants, recombinant expression of wild-type and mutant enzymes in Pichia pastoris
gene XDH1, quantitative real-time PCR enzyme expression analysis
gene XDH1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
gene XDH2, quantitative real-time PCR enzyme expression analysis
genes xdhA-C, development of a method that translates active Rhodobacter capsulatus (alphabetagamma)2 XDH by directly expressing the iron-sulfur domain, the flavin adenine dinucleotide domain and the sulfurated molybdenum domain as three separate proteins in Escherichia coli, recombinant expression of wild-type enzyme and mutant enzymes, i.e. an (alphabetagamma)2 heterohexameric enzyme and two (alphabetagamma)2 XDH variants, in Escherichia coli
recombinant expression of His-tagged enzyme in Escherichia coli strain TP1000
XOR is cloned and heterologously expressed in Spodoptera frugiperda insect cells
-
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli
-
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
decreased enzyme mRNA expression is detected in human cancers originating from the liver, bladder, breast, colon, bile duct, kidney, and hematolymphoid system
direct binding of ppGpp to a TetR-family transcription factor is responsible for increased enzyme gene expression. H2O2 causes an increase in subunit xdhA expression
-
downregulation of enzyme expression in malignant and non-malignant mammary epithelial cells by 17beta-estradiol
-
enzyme expression increases at the full heading and maturation stages, at drought, high temperature and darkness
-
no significant differences in enzyme expression are observed in the heart and lymphoid organ tissues between the group infected with white spot syndrome virus and Vibrio penaeicida compared to the control
trimetazidine causes no significant differences in XOR expression in kidneys without ischemia, whereas the XOR expression in ischemic kidneys is significantly decreased, overview
-
XDH1 gene expression is immediately upregulated after a blood meal in the fat body, midgut, and thorax. In the midgut, XDH1 transcript levels increase 10fold. In malpighian tubules, the XDH1 mRNA levels increase after blood feeding, reaching a peak at 18 h PBM, while XDH1 transcript levels in the ovary are constitutively expressed during the first gonotrophic cycle, with a slight increase occurring between 24 and 48 h and a decrease thereafter
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant
-
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant. Above 3 M guandine-HCl, even xanthine oxidase activity decreases drastically, but the xanthine oxidase form treated with 1.5 M can be completely reconverted into xanthine dehydrogenase by dialysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
treatment of normal fruit in linear phase of growth with enzyme inhibitors allopurinol or adenine arrests fruit growth
analysis
-
use of rosy mutant strains to probe structure and function of xanthine dehydrogenase
biotechnology
-
the enzyme can be useful in biotechnlogical applications requiring special conditions, e.g. extreme pH values
environmental protection
medicine
molecular biology
isozyme XDH1 has the potential to be used as a metabolic target for controlling populations of Aedes aegypti mosquitoes, which are vectors of public health threats
nutrition
-
xanthine oxidoreductase associated with milk phospholipid membranes is found to be distributed among an intra-membranous pool in which it takes the form of a mixture of xanthine oxidase and xanthine dehydrogenase, with a clear predominance of xanthine dehydrogenase, and a free pool of xanthine oxidase, of which 33% is found in the outer surface of milk fat globule membrane, 20.5% in the outer surface of whey membrane particles, and the remaining 46.7% in apparent solution. The inner-membrane xanthine oxidoreductase may play a nonenzymatic role in fat secretion, whereas extramembranous xanthine oxidase is freely available for a role in the innate gland immune system and may affect milk quality
synthesis
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
environmental protection
Rhodobacter capsulatus B10XDHB
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
-
medicine
-
modification of xanthine oxidoreductase by disulfiram that is used in the management of chronic alcolism
medicine
-
enzyme null mutant mice demonstrate 50% reduction in adipose mass compared to control, while obese mice exhibit increased concentrations of xanthine oxidoreductase mRNA and urate in adipose tissues. In vitro, knockdown of xanthine oxidoreductase inhibits adipogenesis and nuclear receptor PPARgamma activity. Xanthine oxidoreductase is a potential therapeutic target for metabolic abnormalities beyond hyperuricemia
medicine
-
oral adminstration of cassia oil significantly reduces serum and hepatic urate levels in hyperuricemic mice. At 600mg/kg, cassia oil is as potent as allopurinol. This hypouricemic effect is explained by inhibiting activities of liver xanthine oxidase and xanthine oxidoreductase
medicine
-
lung xanthine oxidoreductase activity is significantly increased after 2 h of mechanical ventilation without changes in enzyme expression. Increase occurs via activation of p38 MAP kinase and ERK and plays a critical role in the pathogenesis of pulmonary edema associated with ventilator-induced lung injury
medicine
-
demonstration of a functional link between xanthine oxidoreductase expression and mammary epithelial cell migration, potential role in enzyme in suppressing breast cancer pathogenesis. Level of xanthine oxidoreductase is markedly reduced in highly invasive mammary tumor cells, and over-expression of enzyme cDNA in cell lines possessing weak expression and high migratory capacity inhibits their migration in vitro
medicine
-
demonstration of a functional link between xanthine oxidoreductase expression and mammary epithelial cell migration, potential role in enzyme in suppressing breast cancer pathogenesis. Over-expression of enzyme cDNA in cell lines possessing weak expression and high migratory capacity inhibits their migration in vitro
medicine
-
xanthine oxidoreductase is activated in a p38 MAP kinase-dependent manner following high tidal volume mechanical ventilation and is involved in resulting increased alveolar cell apoptosis
medicine
-
the enzyme inhibitor 4-(5-pyridin-4-yl-1H-[1,2,4]triazol-3-yl) pyridine-2-carbonitrile, i.e. FYX-051, is modified in vivo by N1- and N2-glucuronidation, mainly catalyzed by UDP-glucuronosyltransferase UGT1A9
medicine
-
cocaine-induced cardiac disfunction is associated with an increase in NADPH oxidase and xanthine oxidoreductase activities by 59% and 29%, respectively, and a decrease in catalase activity. Apocynin or allopurinol treatment prevents the cocaine-induced cardiac alteration by restoration of cardiac output, stroke volume and fractional shortening. This is associated with a reduction of the myocardial production of superoxide anions and an enhancement of catalase activity. Apocynin treatment prevents anthine oxidoreductase up-regulation supporting the hypothesis that NADPH oxidase-derived reactive oxygen species play a role in modulating reactive oxygen species production by xanthine oxidoreductase
medicine
in hepatocellular carcinoma, a low enzyme mRNA level predicts poorer overall survival, disease-specific survival, disease-free survival, and progression-free survival
synthesis
-
for maximal level of functional expression, co-expression of xdhC gene is required which increases level of molybdenum incorporation. Iron and FAD content of expressed enzymes are independent of xdhC expression
synthesis
-
expression of enzyme in baculovirus-insect cell system, yields a mixture of native dimeric, demolydbo-dimeric and monomeric forms. All forms contain flavin, the monomeric forms lack molybdopterin and the iron-sulfur centers. Monomeric forms require only three electrons for complete reduction
synthesis
expression of genes xdhAB encoding the two subunits of enzyme, in Escherichia coli, produces active enzyme with moleybdenum content of 0.11-0.16 mol per alphabeta protomer and iron and FAD levels at stoichiometries similar to native enzyme. Coexpression of xdhAB genes with Pseudomonas aeruginosa xdhC gene increases level of molybdenum incorporated to a 1:1 stoichiometry and results in high levels of functional protein, up to 2284 units per mg and 8039 mg per l
EXTERNAL LINKS (specific for EC-Number 1.17.1.4)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
