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Information on EC 1.17.1.4 - xanthine dehydrogenase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8GUQ8
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1.17.1.4 xanthine dehydrogenaseIUBMB 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].
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Word Map
- 1.17.1.4
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uric
-
1.2.1.37
-
1.1.1.204
- allopurinol
- environmental protection
-
ureide
-
1.1.3.22
- medicine
-
1.2.3.1
-
xanthinuria
-
oxypurines
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butyrophilins
- synthesis
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hypouricemic
- agriculture
- biotechnology
- analysis
- nutrition
- molecular biology
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
xdh/xo, xanthine dehydrogenase/oxidase, atxdh1, paoabc, xanthine:nad+ oxidoreductase, xanthine-nad oxidoreductase, xanthine/nad+ oxidoreductase, xanthine dehydrogenase-1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NAD-xanthine dehydrogenase
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-
-
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Rosy locus protein
-
-
-
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xanthine oxidoreductase
-
-
-
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xanthine-NAD oxidoreductase
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-
-
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xanthine/NAD+ oxidoreductase
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-
-
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XDH/XO
-
-
-
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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
XOR
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
-
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oxidation
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-
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -, -
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].
CAS REGISTRY NUMBER
COMMENTARY
9054-84-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-naphthaldehyde + NAD+ + ?
? + NADH
27.5% of the activity with xanthine
-
-
?
abscisic aldehyde + NAD+ + ?
? + NADH
28.9% of the activity with xanthine
-
-
?
heptaldehyde + NAD+ + ?
? + NADH
12.5% of the activity with xanthine
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
94.7% of the activity with xanthine
-
-
?
indole-3-carboxaldehyde + NAD+ + ?
? + NADH
31.3% of the activity with xanthine
-
-
?
purine + NAD+ + ?
? + NADH
10.3% of the activity with xanthine
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
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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%
-
-
?
additional information
?
-
XDH can be converted into XO, EC 1.17.3.2, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20%
-
-
?
additional information
?
-
-
AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher than the activity with xanthine accompanied by a doubling in superoxide production and is dependent on sulfurated molybdenum cofactor, overview. FAD is crucial for NADH-based superoxide formation of AtXDH1, whereas the molybdenum cofactor has only little or no influence on the activity, residues E831, R909, E1297, W364, and Y421 are involved
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-
?
additional information
?
-
AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher than the activity with xanthine accompanied by a doubling in superoxide production and is dependent on sulfurated molybdenum cofactor, overview. FAD is crucial for NADH-based superoxide formation of AtXDH1, whereas the molybdenum cofactor has only little or no influence on the activity, residues E831, R909, E1297, W364, and Y421 are involved
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-
?
additional information
?
-
autofluorescent objects (AFOs) formation within mesophyll cells of the mutant plants is a marker for xanthine accumulation with both spatial and temporal resolution, AFOs are highly enriched in xanthine
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-
?
additional information
?
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The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
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-
?
additional information
?
-
-
by an alternative activity, AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide. In comparison to the specific activity with xanthine as substrate, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher. Each sub-activity is determined by specific conditions such as the availability of substrates and co-substrates, which allows regulation of superoxide production by AtXDH1
-
-
?
additional information
?
-
by an alternative activity, AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide. In comparison to the specific activity with xanthine as substrate, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher. Each sub-activity is determined by specific conditions such as the availability of substrates and co-substrates, which allows regulation of superoxide production by AtXDH1
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
xanthine + NAD+ + H2O
urate + NADH + H+
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-
-
?
additional information
?
-
-
XDH can be converted into XO, EC 1.17.3.2, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20%
-
-
?
additional information
?
-
XDH can be converted into XO, EC 1.17.3.2, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20%
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-
?
additional information
?
-
autofluorescent objects (AFOs) formation within mesophyll cells of the mutant plants is a marker for xanthine accumulation with both spatial and temporal resolution, AFOs are highly enriched in xanthine
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[2Fe-2S] cluster
two N-terminal non-identical iron-sulfur clusters of the [2Fe-2S]-type
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
FAD
a molybdenum-iron-flavoenzyme, activity-to-flavin ratio of 8 with xanthine as substrate and NAD+ as final electron acceptor, recombinant enzyme
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
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additional information
-
both NAD+ and NADH compete for the same binding site
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additional information
both NAD+ and NADH compete for the same binding site
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Molybdenum
a molybdenum-containing flavoprotein, biosynthesis of sulfurated molybdenum cofactor, overview
Molybdenum
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
NAD+ inhibits NADH-dependent superoxide formation of AtXDH1
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additional information
NAD+ inhibits NADH-dependent superoxide formation of AtXDH1
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
sulfide/dithionite
treatment increases the specific activity of AtXDH1
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.712
purified recombinant enzyme, in presence of sulfide/dithionite
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
XDH1 is expressed in epidermal cells albeit at relatively lower levels compared with mesophyll cells
cold stress causes decrease, desiccation and senesence cause strong increase in activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
malfunction
metabolism
dual and opposing roles of XDH1 in reactive oxygen species metabolism, detailed overview
physiological function
physiological function
AtXDH1 is a key enzyme in purine degradation where it oxidizes hypoxanthine to xanthine and xanthine to uric acid
additional information
malfunction
dysfunction of purine degradation is a result of knocking down the key enzyme xanthine dehydrogenase, leading to severely reduced survival of Arabidopsis thaliana under progressive drought conditions and to significantly decreased tolerance to superoxide-mediated oxidative stress. The enhanced stress sensitivity of the knockdown mutants likely results from defective stress responses, because the drought-induced accumulation of the cellular protectant proline is compromised in the knockdown plants, which also show lower mRNA levels of P5CS1, the gene encoding the rate-limiting enzyme for proline biosynthesis, DELTA1-pyrroline-5-carboxylate synthase 1
malfunction
RNAi silencing of XDH1 in ecotype Col-0 results in autofluorescent object formation and infiltration of allopurinol, an inhibitor of XDH. drf1 Mutants contain missense mutations in XDH1, whole-cell and haustorial complex-confined H2O2 is significantly reduced in the mutants compared with the parental line
malfunction
the powdery mildew fungus Golovinomyces cichoracearum triggers defense responses in Arabidopsis mediated by the R gene RPW8.2. In a screen for mutants defective in RPW8.2-related resistance to powdery mildew, three plants with point mutations in xanthine dehydrogenase 1 (XDH1), including two that alter residues strictly conserved among xanthine dehydrogenases. The mutants show impaired resistance to powdery mildew and accumulate less H2O2 in the haustorial complex in epidermal cells invaded by the fungus. These point mutations decrease the activity of recombinant XDH1 proteins, in terms of both dehydrogenase activity and ROS production. Xanthine accumulation in the mutants is further induced by pathogen inoculation due to increased purine catabolism (mediated at least in part by XDH1) upon infection. Feeding uric acid suppressed the H2O2 accumulation normally observed in mesophyll cells of infected xdh1 mutant plants
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
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
plant xanthine dehydrogenases do not undergo a posttranslational modification, las in mammals becoming xanthine oxidases, which use O2 as electron acceptor to produce reactive oxygen species. Plant enzymes appear capable of using both O2 and NAD+ as electron acceptors, as well as of producing high levels of ROS. In leaf mesophyll cells, XDH1 carries out xanthine dehydrogenase activity to produce uric acid in local and systemic tissues to scavenge H2O2 from stressed chloroplasts, thereby protecting plants from stress-induced oxidative damage. XDH1-derived uric acid is essential for removing H2O2 from stressed chloroplasts in leaf mesophyll cells. XDH1 plays spatially specified dual and opposing roles in modulation of ROS metabolism during defense responses in Arabidopsis thaliana as xanthine dehydrogenase and as xanthine oxidase, EC 1.17.3.2. XDH1 is required for scavenging age-dependent and pathogen-induced H2O2 in chloroplasts. XDH1 activity appears to be important for RPW8.2-mediated powdery mildew resistance. XDH1 appears to be an important tool allowing plants to harness and direct the power of ROS
physiological function
role for purine metabolites in stress responses, supporting the possible contribution of purine degradation to plant acclimation to changing environments, overview
physiological function
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
additional information
the Arabidopsis thaliana XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). XDH1_ARATH
1361
0
149196
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
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
-
T-DNA insertion mutant, loss of superoxide producing activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged XDH1 from Pichia pastoris by nickel affinity and anion exchange chromatography
recombinant His-tagged wild-type and mutant XDH1 variants from Pichia pastoris strain KM71 by nickel affinity chromatography and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Pichia pastoris
gene xdh1, genotyping, map-based cloning of drf mutants, recombinant expression of wild-type and mutant enzymes in Pichia pastoris
expression of His-tagged wild-type and mutant XDH1 variants in Pichia pastoris strain KM71
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hesberg, C.; Hansch, R.; Mendel, R.R.; Bittner, F.
Tandem orientation of duplicated xanthine dehydrogenase genes from Arabidopsis thaliana: differential gene expression and enzyme activities
J. Biol. Chem.
279
13547-13554
2004
Arabidopsis thaliana (Q8GUQ8), Arabidopsis thaliana
Yesbergenova, Z.; Yang, G.; Oron, E.; Soffer, D.; Fluhr, R.; Sagi, M.
The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have distinct reactive oxygen species signatures and are induced by drought and abscisic acid
Plant J.
42
862-876
2005
Arabidopsis thaliana, Solanum lycopersicum
Zarepour, M.; Kaspari, K.; Stagge, S.; Rethmeier, R.; Mendel, R.R.; Bittner, F.
Xanthine dehydrogenase AtXDH1 from Arabidopsis thaliana is a potent producer of superoxide anions via its NADH oxidase activity
Plant Mol. Biol.
72
301-310
2009
Arabidopsis thaliana, Arabidopsis thaliana (Q8GUQ8)
Wang, C.H.; Zhang, C.; Xing, X.H.
Xanthine dehydrogenase an old enzyme with new knowledge and prospects
Bioengineered
7
395-405
2016
Acinetobacter baumannii, Acinetobacter phage Ab105-3phi, Arabidopsis thaliana (Q8GUQ8), Arthrobacter luteolus, Bos taurus, Clostridium cylindrosporum, Drosophila melanogaster, Enterobacter cloacae, Escherichia coli (Q46799 AND Q46800), Gallus gallus, Homo sapiens, Micrococcus sp., Ovis aries, Pseudomonas putida, Rattus norvegicus, Rhodobacter capsulatus, Rhodobacter capsulatus B10XDHB, Streptomyces cyanogenus
Watanabe, S.; Kounosu, Y.; Shimada, H.; Sakamoto, A.
Arabidopsis xanthine dehydrogenase mutants defective in purine degradation show a compromised protective response to drought and oxidative stress
Plant Biotechnol.
31
173-178
2014
Arabidopsis thaliana (Q8GUQ8), Arabidopsis thaliana Col-0 (Q8GUQ8)
-
Hofmann, N.
Opposing functions for plant xanthine dehydrogenase in response to powdery mildew infection production and scavenging of reactive oxygen species
Plant Cell
28
1001
2016
Mammalia, Arabidopsis thaliana (Q8GUQ8), Arabidopsis thaliana Col-0 (Q8GUQ8)
Ma, X.; Wang, W.; Bittner, F.; Schmidt, N.; Berkey, R.; Zhang, L.; King, H.; Zhang, Y.; Feng, J.; Wen, Y.; Tan, L.; Li, Y.; Zhang, Q.; Deng, Z.; Xiong, X.; Xiao, S.
Dual and opposing roles of xanthine dehydrogenase in defense-associated reactive oxygen species metabolism in Arabidopsis
Plant Cell
28
1108-1126
2016
Arabidopsis thaliana (Q8GUQ8), Arabidopsis thaliana Col-0 (Q8GUQ8)
EXTERNAL LINKS (specific for EC-Number 1.17.1.4)
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