1.17.1.4: xanthine dehydrogenase
This is an abbreviated version!
For detailed information about xanthine dehydrogenase, go to the full flat file.
Word Map on EC 1.17.1.4
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1.17.1.4
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uric
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1.2.1.37
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1.1.1.204
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allopurinol
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environmental protection
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ureide
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1.1.3.22
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medicine
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1.2.3.1
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xanthinuria
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oxypurines
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butyrophilins
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synthesis
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hypouricemic
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agriculture
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biotechnology
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analysis
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nutrition
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molecular biology
- 1.17.1.4
-
uric
-
1.2.1.37
-
1.1.1.204
- allopurinol
- environmental protection
-
ureide
-
1.1.3.22
- medicine
-
1.2.3.1
-
xanthinuria
-
oxypurines
-
butyrophilins
- synthesis
-
hypouricemic
- agriculture
- biotechnology
- analysis
- nutrition
- molecular biology
Reaction
Synonyms
AtXDH1, EC 1.1.1.204, EC 1.2.1.37, IAO1, More, NAD-xanthine dehydrogenase, PaoABC, Retinol dehydrogenase, Rosy locus protein, VvXDH, xanthine dehydrogenase, xanthine dehydrogenase-1, xanthine dehydrogenase-2, xanthine dehydrogenase/oxidase, xanthine oxidoreductase, xanthine-NAD oxidoreductase, xanthine/NAD+ oxidoreductase, xanthine:NAD+ oxidoreductase, XDH, XDH/XO, XDH1, XDH2, XdhC, XOR, YagR, YagS, YagT
ECTree
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Natural Substrates Products
Natural Substrates Products on EC 1.17.1.4 - xanthine dehydrogenase
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REACTION DIAGRAM
2 2-hydroxypurine + 2 NAD+ + 2 H2O
xanthine + 2,8-dihydroxypurine + 2 NADH + 2 H+
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considerable activity
84% xanthine, 8% 2,8-dihydroxypurine formed
?
2 hypoxanthine + 2 NAD+ + 2 H2O
xanthine + 6,8-dihydroxypurine + 2 NADH + 2 H+
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preferred substrate
100% xanthine, 51% 6,8-dihydroxypurine formed
?
3 purine + 3 NAD+ + 3 H2O
hypoxanthine + 8-hydroxypurine + 2-hydroxypurine + 3 NADH + 3 H+
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poor substrate
2.3% hypoxanthine, 2.3% 8-hydroxypurine and traces of 2-hydroxypurine formed
?
6,8-dihydroxypurine + NAD+ + H2O
urate + NADH
-
-
18% urate formed
?
guanine + NAD+ + H2O
? + NADH
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81.3% of the activity compared to hypoxanthine
-
?
hypoxanthine + NADH
? + NO2- + NAD+
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0.1% of the xanthine oxidation rate
-
?
hypoxanthine + urate
xanthine + 6,8-dihydroxypurine
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oxygen-free assay
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r
purine + NADP+ + H2O
? + NADPH
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60% of the activity compared to hypoxanthine
-
?
xanthopterin + NAD+ + H2O
leucopterin + NADH
-
regulation of the pteridine pathway by competitive inhibition of reaction products and the precursor of xanthopterin, 7,8-dihydroxanthopterin
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?
isoxanthopterin + NADH
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i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
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i.e. pterin
precursor of the eye pigment drosopterin
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
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i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
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i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
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i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
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i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
r
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
conversion of xanthine dehydrogenase to xanthine oxidase is strongly influenced by in vitro cell culture of alveolar epithelial cells
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
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i.e. pterin
-
?
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
11% of the activity compared to xanthine
-
?
xanthine + NADH + H2O2
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NAD+-O2- dependent xanthine oxidase activity
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
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NAD+-O2- dependent xanthine oxidase activity
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
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predominant reaction
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?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
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subtilisin treatment leads to an active component I of 120000 kDa
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?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
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more rapidly oxidized than xanthine
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?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
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preferred substrate
-
ir
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
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preferred substrate
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
-
strict specificity for NADP+
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?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
-
40% of the activity compared to NAD+
-
?
hypoxanthine + NADP+ + H2O
xanthine + NADPH
-
2.4% of the activity compared to NAD+
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?
xanthine + NAD+ + H2O
urate + NADH
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regulation of xanthine dehydrogenase expression is subjected to nitrogen catabolite repression mediated through the GlnA-dependent signaling pathway
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?
xanthine + NAD+ + H2O
urate + NADH
-
xanthine dehydrogenase form has distinct xanthine/oxygen activity, 35-42% of electrons transferred to O2 to form O2-
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?
xanthine + NAD+ + H2O
urate + NADH
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conversion of dehydrogenase to oxidase type due to oxidation of sulfhydryl groups by molecular oxygen, dehydrogenase activity recovered by treatment with dithiothreitol
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?
xanthine + NAD+ + H2O
urate + NADH
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NAD+-dependent dehydrogenase type D
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?
xanthine + NAD+ + H2O
urate + NADH
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NAD+-dependent dehydrogenase type D
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?
xanthine + NAD+ + H2O
urate + NADH
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involved in pteridine metabolism, 40% of activity compared to hypoxanthine
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?
xanthine + NAD+ + H2O
urate + NADH
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only dehydrogenase type D present
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?
xanthine + NAD+ + H2O
urate + NADH
-
minimum degree of 1 : 1 for xanthine, 2 : 2 for NAD, 1 : 1 for urate and 1 : 2 for NADH in the xanthine/NAD+ oxidoreductase reaction required
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r
xanthine + NAD+ + H2O
urate + NADH
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xanthine dehydrogenase can be partially reduced in a triphasic reaction by either xanthine or NADH, oxidation of fully, 6-electron-reduced xanthine dehydrogenase by either urate or NAD+ is monophasic and depends on the oxidant concentration
NADH-binding to the 2-electron reduced enzyme is implicated in fixing end-point position in reactions involving pyridine nucleotides, urate-binding is involved in fixing end-point reactions involving xanthine and urate
r
xanthine + NAD+ + H2O
urate + NADH
-
subtilisin treatment leads to an active component I of 120000 kDa
-
?
xanthine + NAD+ + H2O
urate + NADH
-
xanthine oxidase form is the principle major form in fresh mouse milk, dehydrogenase form is the major form in mammary gland, conversion to the dehydrogenase form by thiol active compounds
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?
xanthine + NAD+ + H2O
urate + NADH
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degradative pathway of conversion of purines to ammonia
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r
xanthine + NAD+ + H2O
urate + NADH
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only present as stable dehydrogenase from, no conversion to the oxidase form
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?
xanthine + NAD+ + H2O
urate + NADH
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NAD+-linked activity, very low activity towards molecular oxygen
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?
xanthine + NAD+ + H2O
urate + NADH
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75% of the activity compared to hypoxanthine
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?
xanthine + NAD+ + H2O
urate + NADH
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NAD+-dependent form is postulated to play a regulatory role in purine metabolism
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?
xanthine + NAD+ + H2O
urate + NADH
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conversion of xanthine dehydrogenase to the oxidase type by thiol-disulfide oxidoreductase, thiol reagents or oxidized glutathione
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?
xanthine + NAD+ + H2O
urate + NADH
-
trypsin treatment leads to a complete conversion of xanthine dehydrogenase to xanthine oxidase activity
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r
xanthine + NAD+ + H2O
urate + NADH
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NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH
-
NAD+-dependent dehydrogenase type D
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?
xanthine + NAD+ + H2O
urate + NADH
-
67% of the activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH
-
61% of the activity compared to hypoxanthine
91% urate formed
?
xanthine + NAD+ + H2O
urate + NADH
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strict dehydrogenase activity, no utilization of O2
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?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
catalytically relevant binding mode of the substrate xanthine, overview
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-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
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?
xanthine + NAD+ + H2O
urate + NADH + H+
catalytically relevant binding mode of the substrate xanthine, overview
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-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
when catalyzing the sequential oxidation of hypoxanthine to xanthine to uric acid, XDH uses the NAD+ as final electron receptor to produce NADH
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-
?
xanthine + NAD+ + H2O
urate + NADH + H+
Rhodobacter capsulatus CGMCC 1.3366
when catalyzing the sequential oxidation of hypoxanthine to xanthine to uric acid, XDH uses the NAD+ as final electron receptor to produce NADH
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-
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
-
heat-treated intermediate dehydrogenase/oxidase type O
-
?
xanthine + NAD+ + O2 + H2O + H+
urate + NADH + H2O2
-
intermediate form of dehydrogenase/oxidase type D/O
-
?
urate + NADPH
-
11% of the activity compared to NAD+
-
?
xanthine + NADP+ + H2O
urate + NADPH
-
strict specificity for NADP+
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
xanthine oxidase form transfers 22% electrons to oxygen to form superoxide
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
subtilisin treatment leads to an active component I of 120000 kDa
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
4% of the activity compared to xanthine-NAD+
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
toxic reactions of xanthine oxidase-derived radicals are critical factors in several mechanisms of tissue pathology
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
NAD+-independent trypsin-treated oxidase type O
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
NAD+-independent xanthine oxidase activity, low activity present in the enzyme preparation, conversion of the NAD+-dependent to NAD+-independent activity by some thiol reagents
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
presence of ferredoxin enhances rate of oxygen reduction
-
?
?
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-
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%
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-
?
additional information
?
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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%
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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-
xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
-
-
?
additional information
?
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-
xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms
-
-
?
additional information
?
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-
the enzyme is responsible for the synthesis of uric acid, the major end product of the metabolism of nitrogen compounds in birds, uric acid functions as an antioxidant to reduce oxidative stress
-
-
?
additional information
?
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-
xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms
-
-
?
additional information
?
-
xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
-
-
?
additional information
?
-
-
xanthine dehydrogenase is the native form of xanthine oxidase, EC 1.17.3.2, conversion causes a loss of the NAD+ binding activity and of the retinol oxidation activity, the conversion with conformational changes is reversible, except for alteration due to proteolytic cleavage
-
-
?
additional information
?
-
-
xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms
-
-
?
additional information
?
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-
xanthine oxidoreductase is a regulator of adipogenesis and of nuclear recptor PPARgamma activityand is essential for the regulation of fat accretion
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-
?
additional information
?
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-
major function of enzyme in liver parenchymal and sinusoidal cells is the production of uric acid as a antioxidant
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-
?
additional information
?
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NADH oxidation by xanthine oxidoreductase may constitute an important pathway for reactive oxygen species-mediated tissue injuries. Xanthine oxidoreductase and xanthine oxidase catalyze the NADH oxidation, generating O2- radicals and inducing the peroxidation of liposomes, in a NADH and enzyme dependent manner
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-
?
additional information
?
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-
enzyme inhibition by orange juice and hesperetin participates in preventing oxidative stress by enhancing total antioxidant capacity and decreasing lipid peroxidation, overview
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-
?
additional information
?
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with the supply of molecular oxygen upon reperfusion of ischemic tissues, xanthine oxidoreductase metabolizes xanthine and hypoxanthine to uric acid, free radicals are generated, overview. Decrease in xanthine oxidoreductase expression is one of the beneficial mechanisms of trimetazidine on ischemia/reperfusion injury, preventing the degradation of purine nucleotides during the oxidation of hypoxanthine to xanthine and uric acid and formation of free radicals
-
-
?
additional information
?
-
-
xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. The difference in three-dimensional structures is centered on Ala535. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms
-
-
?
additional information
?
-
-
xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms
-
-
?