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
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uric
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1.2.1.37
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1.1.1.204
- allopurinol
- environmental protection
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ureide
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1.1.3.22
- medicine
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1.2.3.1
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xanthinuria
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oxypurines
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butyrophilins
- synthesis
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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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General Information
General Information on EC 1.17.1.4 - xanthine dehydrogenase
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evolution
malfunction
metabolism
physiological function
additional information
evolution
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XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
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XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
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XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
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XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
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XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
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XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
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XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
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XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
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XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
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XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
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XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
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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
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XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
evolution
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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
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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
Rhodobacter capsulatus B10XDHB
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XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
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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
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the retinoic acid deficiency in breast tumour epithelial cells has been ascribed to an insufficient expression of either the enzyme(s) involved in its biosynthesis or the cellular retinol binding protein or both, overview
malfunction
disruption of XDH by allopurinol or XDH1 by RNA interference significantly affect mosquito survival, causing a disruption in blood digestion, excretion, oviposition, and reproduction. XDH1-deficient mosquitoes show a persistence of serine proteases in the midgut at 48 h after blood feeding and a reduction in the uptake of vitellogenin by the ovaries. Analysis of the fat body from dsRNA-XDH1-injected mosquitoes fall into 2 groups: one group is characterized by a reduction of the XDH1 transcript, whereas the other group is characterized by an upregulation of several transcripts, including XDH1, glutamine synthetase, alanine aminotransferase, catalase, superoxide dismutase, ornithine decarboxylase, glutamate receptor, and ammonia transporter. Depletion of XDH1 activity is lethal to bloodfed mosquitoes. Silencing of XDH1 reduces protein expression and delays synthesis and excretion of nitrogen waste, XDH1 deficiency slows digestion, vitellogenesis, and oviposition, and reduces fecundity
malfunction
dysfunction of purine degradation is a result of knocking down the key enzyme xanthine dehydrogenase, leading to severely reduced survival of Arabidopsis thaliana under progressive drought conditions and to significantly decreased tolerance to superoxide-mediated oxidative stress. The enhanced stress sensitivity of the knockdown mutants likely results from defective stress responses, because the drought-induced accumulation of the cellular protectant proline is compromised in the knockdown plants, which also show lower mRNA levels of P5CS1, the gene encoding the rate-limiting enzyme for proline biosynthesis, DELTA1-pyrroline-5-carboxylate synthase 1
malfunction
RNAi silencing of XDH1 in ecotype Col-0 results in autofluorescent object formation and infiltration of allopurinol, an inhibitor of XDH. drf1 Mutants contain missense mutations in XDH1, whole-cell and haustorial complex-confined H2O2 is significantly reduced in the mutants compared with the parental line
malfunction
the powdery mildew fungus Golovinomyces cichoracearum triggers defense responses in Arabidopsis mediated by the R gene RPW8.2. In a screen for mutants defective in RPW8.2-related resistance to powdery mildew, three plants with point mutations in xanthine dehydrogenase 1 (XDH1), including two that alter residues strictly conserved among xanthine dehydrogenases. The mutants show impaired resistance to powdery mildew and accumulate less H2O2 in the haustorial complex in epidermal cells invaded by the fungus. These point mutations decrease the activity of recombinant XDH1 proteins, in terms of both dehydrogenase activity and ROS production. Xanthine accumulation in the mutants is further induced by pathogen inoculation due to increased purine catabolism (mediated at least in part by XDH1) upon infection. Feeding uric acid suppressed the H2O2 accumulation normally observed in mesophyll cells of infected xdh1 mutant plants
malfunction
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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
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malfunction
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the powdery mildew fungus Golovinomyces cichoracearum triggers defense responses in Arabidopsis mediated by the R gene RPW8.2. In a screen for mutants defective in RPW8.2-related resistance to powdery mildew, three plants with point mutations in xanthine dehydrogenase 1 (XDH1), including two that alter residues strictly conserved among xanthine dehydrogenases. The mutants show impaired resistance to powdery mildew and accumulate less H2O2 in the haustorial complex in epidermal cells invaded by the fungus. These point mutations decrease the activity of recombinant XDH1 proteins, in terms of both dehydrogenase activity and ROS production. 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
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malfunction
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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
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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
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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
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dual and opposing roles of XDH1 in reactive oxygen species metabolism, detailed overview
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xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation
physiological function
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xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation
physiological function
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xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation
physiological function
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xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation
physiological function
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xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation
physiological function
xanthine oxidoreductase is a ubiquitous molybdenum-iron-flavo enzyme with a central role in purine catabolism where it catalyzes the oxidation of hypoxanthine to xanthine and of xanthine to uric acid
physiological function
AtXDH1 is a key enzyme in purine degradation where it oxidizes hypoxanthine to xanthine and xanthine to uric acid
physiological function
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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
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dual and opposing roles of XDH1 in reactive oxygen species metabolism, detailed overview. The enzyme's basic function is in purine catabolism, catalyzing the conversion of hypoxanthine to xanthine and xanthine to uric acid. In mammals, xanthine dehydrogenases, which use NAD+ as electron acceptor to produce uric acid, can be posttranslationally modified to become xanthine oxidases, which use O2 as electron acceptor to produce reactive oxygen species (ROS). Because uric acid is a scavenger of ROS, the resulting influence of xanthine dehydrogenase on ROS status is likely responsible for its importance in a remarkably wide range of processes in mammals, including immunity
physiological function
in leaf mesophyll cells, XDH1 carries out xanthine dehydrogenase activity to produce uric acid in local and systemic tissues to scavenge H2O2 from stressed chloroplasts, thereby protecting plants from stress-induced oxidative damage. XDH1-derived uric acid is essential for removing H2O2 from stressed chloroplasts in leaf mesophyll cells. XDH1 plays spatially specified dual and opposing roles in modulation of ROS metabolism during defense responses in Arabidopsis thaliana as xanthine dehydrogenase and as xanthine oxidase, EC 1.17.3.2. XDH1 is required for scavenging age-dependent and pathogen-induced H2O2 in chloroplasts. XDH1 plays opposing roles in H2O2 metabolism in Golovinomyces cichoracearum GcUCSC1 haustorium-affected epidermal and mesophyll cells. XDH1-derived H2O2 is also required for RPW8-dependent and -independent basal resistance
physiological function
isozyme XDH1 plays an essential role in Aedes aegypti vector control
physiological function
mammalian xanthine oxidoreductase can exist in both dehydrogenase and oxidase forms. The C-terminal peptide plays a role in the formation of an intermediate form during the transition between xanthine dehydrogenase and xanthine oxidase. Conversion between the two is implicated in such diverse processes as lactation, anti-bacterial activity, reperfusion injury and a growing number of diseases. The dehydrogenase-oxidase transformation occurs rather readily and the insertion of the C-terminal peptide into the active site cavity of its subunit stabilizes the dehydrogenase form. The intermediate form can be generated (e.g. in endothelial cells) upon interaction of the C-terminal peptide portion of the enzyme with other proteins or the cell membrane. Residues Cys535 and Cys992 are involved in the rapid phase and Cys1316 and Cys1324 in the slow phase of the modification reaction. The irreversible conversion of XDH to XOR by trypsin involves limited proteolysis at the same linker peptide. Triggering events, such as the formation of a disulfide bond between Cys535 and Cys992 or proteolysis of the linker, reorient Phe549 (also a part of the long linker), resulting in disruption of a four amino acid cluster. Arg426 is then released from the cluster and moves the A-loop that blocks the approach of NAD+ to the flavin ring of the FAD moiety, as well as changing the electrostatic environment
physiological function
plant xanthine dehydrogenases do not undergo a posttranslational modification, las in mammals becoming xanthine oxidases, which use O2 as electron acceptor to produce reactive oxygen species. Plant enzymes appear capable of using both O2 and NAD+ as electron acceptors, as well as of producing high levels of ROS. In leaf mesophyll cells, XDH1 carries out xanthine dehydrogenase activity to produce uric acid in local and systemic tissues to scavenge H2O2 from stressed chloroplasts, thereby protecting plants from stress-induced oxidative damage. XDH1-derived uric acid is essential for removing H2O2 from stressed chloroplasts in leaf mesophyll cells. XDH1 plays spatially specified dual and opposing roles in modulation of ROS metabolism during defense responses in Arabidopsis thaliana as xanthine dehydrogenase and as xanthine oxidase, EC 1.17.3.2. XDH1 is required for scavenging age-dependent and pathogen-induced H2O2 in chloroplasts. XDH1 activity appears to be important for RPW8.2-mediated powdery mildew resistance. XDH1 appears to be an important tool allowing plants to harness and direct the power of ROS
physiological function
role for purine metabolites in stress responses, supporting the possible contribution of purine degradation to plant acclimation to changing environments, overview
physiological function
xanthine dehydrogenase plays an important role in purine catabolism catalyzing the oxidative hydroxylation of hypoxanthine to xanthine and of xanthine to uric acid, it plays a role in recycling and remobilization of nitrogen, and XDH is implicated in plant stress responses and acclimation. Explicit function of VvXDH in conferring salt stress by increasing allantoin accumulation and activating abscisic acid signaling pathway, enhancing ROS scavenging in transgenic Arabidopsis thaliana. VvXDH application results in increased tolerance to abiotic stresses by elevating allantoin accumulation
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
physiological function
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
physiological function
XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
physiological function
Rhodobacter capsulatus B10XDHB
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XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview
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physiological function
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role for purine metabolites in stress responses, supporting the possible contribution of purine degradation to plant acclimation to changing environments, overview
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physiological function
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plant xanthine dehydrogenases do not undergo a posttranslational modification, las in mammals becoming xanthine oxidases, which use O2 as electron acceptor to produce reactive oxygen species. Plant enzymes appear capable of using both O2 and NAD+ as electron acceptors, as well as of producing high levels of ROS. In leaf mesophyll cells, XDH1 carries out xanthine dehydrogenase activity to produce uric acid in local and systemic tissues to scavenge H2O2 from stressed chloroplasts, thereby protecting plants from stress-induced oxidative damage. XDH1-derived uric acid is essential for removing H2O2 from stressed chloroplasts in leaf mesophyll cells. XDH1 plays spatially specified dual and opposing roles in modulation of ROS metabolism during defense responses in Arabidopsis thaliana as xanthine dehydrogenase and as xanthine oxidase, EC 1.17.3.2. XDH1 is required for scavenging age-dependent and pathogen-induced H2O2 in chloroplasts. XDH1 activity appears to be important for RPW8.2-mediated powdery mildew resistance. XDH1 appears to be an important tool allowing plants to harness and direct the power of ROS
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physiological function
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in leaf mesophyll cells, XDH1 carries out xanthine dehydrogenase activity to produce uric acid in local and systemic tissues to scavenge H2O2 from stressed chloroplasts, thereby protecting plants from stress-induced oxidative damage. XDH1-derived uric acid is essential for removing H2O2 from stressed chloroplasts in leaf mesophyll cells. XDH1 plays spatially specified dual and opposing roles in modulation of ROS metabolism during defense responses in Arabidopsis thaliana as xanthine dehydrogenase and as xanthine oxidase, EC 1.17.3.2. XDH1 is required for scavenging age-dependent and pathogen-induced H2O2 in chloroplasts. XDH1 plays opposing roles in H2O2 metabolism in Golovinomyces cichoracearum GcUCSC1 haustorium-affected epidermal and mesophyll cells. XDH1-derived H2O2 is also required for RPW8-dependent and -independent basal resistance
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additional information
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biofilm formation is stimulated in the presence of uric acid, Se, and Mo and inhibited by auranofin or tungstate
additional information
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mammalian XOR exists in two interconvertible forms, the xanthine dehydrogenase, XDH, form and the xanthine oxidase, XO, form. The primary gene product is XDH, which can be converted into XO
additional information
mammalian XOR exists in two interconvertible forms, the xanthine dehydrogenase, XDH, form and the xanthine oxidase, XO, form. The primary gene product is XDH, which can be converted into XO
additional information
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XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4
additional information
XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4
additional information
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analysis of the mechanism of transfer of an oxygen atom to the substrate
additional information
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Glu802 binds the substrate and stabilizes the transition state, Glu1261 is the catalytic base, Arg880 and Thr1010 bind the substrate and decrease the reaction activation energy, Phe914 and Phe1009 orientate the substrate via pi-pi stacking, Val1011 is the key residue channeling the substrate, and Gln758 is responsible for releasing the product. There is an obvious variation of key residues channeling the substrate and binding pocket, which affect the substrate entry and product release, resulting in different catalytic activity and enzymatic properties. Surprisingly, the 2 pairs of cysteines, C535 and C992, and C1316 and C1324 numbering in bovine XDH, which are proposed to control the reversible post-translational conversion from XDH to XOD, EC 1.17.3.2, by forming 2 cysteine disulfide bonds, are totally absent in other XDHs. Bovine milk XDH can be converted reversibly into active XOD form by forming disulfide bond or irreversibly by limited proteolysis, overview
additional information
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rat liver XDH can be converted reversibly into active XOD form by forming disulfide bond or irreversibly by limited proteolysis, overview
additional information
the Arabidopsis thaliana XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
additional information
the biosynthesis of functionally active XDH is a multi-step process requiring a series of helper proteins to aid the formation of cofactors and apoproteins and their ordered assembly, in vivo biosynthetic mechanism of active xanthine dehydrogenase in schematic overview. NifS is a cysteine desulfurase, which catalyzes the sulfur transfer from L-cysteine to Moco to form Mo-S bond. Chaperone XDHC binds stoichiometric amount of Moco as a scaffold protein, interacts with NifS for the sulfuration of Moco, protects sulfurated Moco from oxidation, and further transfers to XDH
additional information
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the chicken XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
additional information
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the Rhodobacter capsulatus XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
additional information
XDH active site structure with conserved Glu232 and Arg310 residues. Analysis of crystal structure of xanthine dehydrogenase, PDB ID 2W3S, where an ionized glutamate 802/232 acts as a hydrogen bonding acceptor from the substrate N3 nitrogen
additional information
Rhodobacter capsulatus B10XDHB
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the Rhodobacter capsulatus XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
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additional information
Rhodobacter capsulatus CGMCC 1.3366
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the biosynthesis of functionally active XDH is a multi-step process requiring a series of helper proteins to aid the formation of cofactors and apoproteins and their ordered assembly, in vivo biosynthetic mechanism of active xanthine dehydrogenase in schematic overview. NifS is a cysteine desulfurase, which catalyzes the sulfur transfer from L-cysteine to Moco to form Mo-S bond. Chaperone XDHC binds stoichiometric amount of Moco as a scaffold protein, interacts with NifS for the sulfuration of Moco, protects sulfurated Moco from oxidation, and further transfers to XDH
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