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evolution
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DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
-
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
-
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
-
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
-
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
-
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
-
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
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malfunction
a mutant lacking all three DHAR isozymes (DELTAdhar), with negligible DHAR activity, is shown to be equivalent to wild-type plants in terms of growth and development, as well as ascorbate levels. Analysis of the DELTAdhar mutant shows that DHARs are required to couple hydrogen peroxide metabolism to glutathione oxidation and that this is functionally important for downstream activation of the salicylic acid pathway. Thus, the role of DHARs in ascorbate recycling remains controversial. DHAR activity is dispensable for growth and ascorbate homeostasis under low light. When subjected to high-light stress, both the wild-type plants and DELTAdhar mutants accumulate ascorbate to high levels, but minor differences are observed after a prolonged stress. The lower ascorbate accumulation of DELTAdhar relative to the wild-type is associated with a slight overaccumulation of threonate, an ascorbate degradation. A blockage of ascorbate accumulation in response to high light is also observed when glutathione deficiency is induced pharmacologically by buthionine sulfoximine treatment, providing extra evidence that, in high-light conditions, glutathione acts as a substitute for ascorbate reduction
malfunction
DHAR overexpression in maize leads to an increase in ascorbate and glutathione concentration, as well as a shift toward the reduced state for glutathione
malfunction
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DHAR-downregulated tobacco lines show reduced total ascorbate levels, lower dry weight, and diminished photosynthetic efficiency. DHAR overexpression in tobacco leads to an increase in ascorbate and glutathione concentration, as well as a shift toward the reduced state for glutathione
malfunction
multiple loss of DHAR functions markedly decreases glutathione oxidation triggered by catalase deficiency. No evidence is obtained that either GRs or MDHARs are upregulated in plants lacking DHAR function. 3-Aminotriazole (3-AT) decreases catalase to very low levels while inducing ascorbate peroxidase (APX) and DHAR activities. These effects are accompanied by extensive leaf bleaching, and glutathione oxidation is evident as marked accumulation of GSSG. No difference is observed in bleaching or glutathione contents between the wild-type control and any of the mutants. Loss-of-function mutants for DHAR suggest that ascorbate regeneration is the major route leading to GSSG accumulation in response to intracellular H2O2. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHAR isozymes (DHAR1-3) are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited. Similar effects are observed in dhar1/dhar2 and dhar1/dhar2/dhar3 mutants using 3-AT to inhibit catalase. The major contribution to both lesion formation and glutathione oxidation triggered by catalase deficiency appears to come from DHAR1 and DHAR2 with a minor but significant contribution from chloroplastic DHAR3
malfunction
multiple loss of DHAR functions markedly decreases glutathione oxidation triggered by catalase deficiency. No evidence is obtained that either GRs or MDHARs are upregulated in plants lacking DHAR function. 3-Aminotriazole (3-AT) decreases catalase to very low levels while inducing ascorbate peroxidase (APX) and DHAR activities. These effects are accompanied by extensive leaf bleaching, and glutathione oxidation is evident as marked accumulation of GSSG. No difference is observed in bleaching or glutathione contents between the wild-type control and any of the mutants. Loss-of-function mutants for DHAR suggest that ascorbate regeneration is the major route leading to GSSG accumulation in response to intracellular H2O2. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHAR isozymes (DHAR1-3) are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited. Similar effects were observed in dhar1/dhar2 and dhar1/dhar2/dhar3 mutants using 3-AT to inhibit catalase. The major contribution to both lesion formation and glutathione oxidation triggered by catalase deficiency appears to come from DHAR1 and DHAR2 with a minor but significant contribution from chloroplastic DHAR3
malfunction
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site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
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site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
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site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
-
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
-
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
-
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity. In Arabidopsis, disruption of DHAR2 decreases the ascorbate redox state but not its pool size, and plants exhibit increased ozone sensitivity, and glutathione oxidation is inhibited in all three dhar single-mutants following photo-oxidative stress
malfunction
the increase of AsA regeneration via enhanced DHAR activity modulates the ascorbate-glutathione cycle activity against photooxidative stress in Chlamydomonas reinhardtii
malfunction
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multiple loss of DHAR functions markedly decreases glutathione oxidation triggered by catalase deficiency. No evidence is obtained that either GRs or MDHARs are upregulated in plants lacking DHAR function. 3-Aminotriazole (3-AT) decreases catalase to very low levels while inducing ascorbate peroxidase (APX) and DHAR activities. These effects are accompanied by extensive leaf bleaching, and glutathione oxidation is evident as marked accumulation of GSSG. No difference is observed in bleaching or glutathione contents between the wild-type control and any of the mutants. Loss-of-function mutants for DHAR suggest that ascorbate regeneration is the major route leading to GSSG accumulation in response to intracellular H2O2. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHAR isozymes (DHAR1-3) are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited. Similar effects were observed in dhar1/dhar2 and dhar1/dhar2/dhar3 mutants using 3-AT to inhibit catalase. The major contribution to both lesion formation and glutathione oxidation triggered by catalase deficiency appears to come from DHAR1 and DHAR2 with a minor but significant contribution from chloroplastic DHAR3
-
malfunction
-
multiple loss of DHAR functions markedly decreases glutathione oxidation triggered by catalase deficiency. No evidence is obtained that either GRs or MDHARs are upregulated in plants lacking DHAR function. 3-Aminotriazole (3-AT) decreases catalase to very low levels while inducing ascorbate peroxidase (APX) and DHAR activities. These effects are accompanied by extensive leaf bleaching, and glutathione oxidation is evident as marked accumulation of GSSG. No difference is observed in bleaching or glutathione contents between the wild-type control and any of the mutants. Loss-of-function mutants for DHAR suggest that ascorbate regeneration is the major route leading to GSSG accumulation in response to intracellular H2O2. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHAR isozymes (DHAR1-3) are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited. Similar effects are observed in dhar1/dhar2 and dhar1/dhar2/dhar3 mutants using 3-AT to inhibit catalase. The major contribution to both lesion formation and glutathione oxidation triggered by catalase deficiency appears to come from DHAR1 and DHAR2 with a minor but significant contribution from chloroplastic DHAR3
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malfunction
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site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
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metabolism
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isoform DHAR3 contributes, at least to some extent, to ascorbate recycling
metabolism
glutathione is a pivotal molecule in oxidative stress, during which it is potentially oxidized by several pathways linked to H2O2 detoxification. Response and functional importance of 3 potential routes for glutathione oxidation pathways mediated by glutathione S-transferases (GST), glutaredoxin-dependent peroxiredoxins (PRXII), and dehydroascorbate reductases (DHAR) in Arabidopsis during oxidative stress, overview. Interplay between different DHARs appears to be necessary to couple ascorbate and glutathione pools and to allow glutathione-related signaling during enhanced H2O2 metabolism
metabolism
nlGSTO exhibits DHA reductase and thiol transferase, which are responsible for antioxidant reactions. GSH is known to be a redox regulator. Thiol transferase is involved in GSH homeostasis, which is important for antioxidant defense. DHA reductase is responsible for maintaining the balance of ascorbate, which functions in scavenging reactive oxygen species
metabolism
the ascorbate glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
-
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
-
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
-
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
-
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
-
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
-
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress. Cytosolic DHAR1 and chloroplastic DHAR3 contribute approximately equally and constitute almost all the leaf DHAR activity, while DHAR2 makes a minor contribution
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress. Isozyme DHAR1 also appears to be capable of transmembrane ion conductance. Cytosolic DHAR1 and chloroplastic DHAR3 contribute approximately equally and constitute almost all the leaf DHAR activity, while DHAR2 makes a minor contribution
metabolism
the enzyme is part of the ascorbate recycling pathways, overview
metabolism
the enzyme is part of the ascorbate-glutathione pathway, overview. This defense system is composed by enzymes such as the ascorbate peroxidase (APX, EC 1.11.1.11), the monodehydroascorbate reductase (MDHAR, EC 1.6.5.4), the dehydroascorbate reductase (DHAR, EC 1.8.5.1), and the glutathione reductase (GR, EC 1.6.4.2), and compounds, such as ascorbate (ASC), dehydroascorbate (DHA), reduced (GSH) and oxidized (GSSG) glutathione
metabolism
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glutathione is a pivotal molecule in oxidative stress, during which it is potentially oxidized by several pathways linked to H2O2 detoxification. Response and functional importance of 3 potential routes for glutathione oxidation pathways mediated by glutathione S-transferases (GST), glutaredoxin-dependent peroxiredoxins (PRXII), and dehydroascorbate reductases (DHAR) in Arabidopsis during oxidative stress, overview. Interplay between different DHARs appears to be necessary to couple ascorbate and glutathione pools and to allow glutathione-related signaling during enhanced H2O2 metabolism
-
metabolism
-
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress. Isozyme DHAR1 also appears to be capable of transmembrane ion conductance. Cytosolic DHAR1 and chloroplastic DHAR3 contribute approximately equally and constitute almost all the leaf DHAR activity, while DHAR2 makes a minor contribution
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physiological function
chemical compounds that generate reactive oxygen species or directly applied hydrogen peroxide (H2O2) are able to induce hypersensitive response-type necroses in tobacco mosaic virus-inoculated Xanthi-nc tobacco even at high temperatures (e.g. 30°C). Activity of dehydroascorbate reductase is significantly higher at 30°C, as compared with 20°C, suggesting that DHAR might contribute to the inhibition of hypersensitive response-type necroses at 30°C
physiological function
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monodehydroascorbate reductase 2 and DHAR5 (At1g19570) mRNA levels are upregulated in Arabidopsis roots colonized by the beneficial endophyticfungus Piriformospora indica. Insertional inactivation of the two genes show that they are crucial for maintaining the interaction between Piriformospora indica and Arabidopsis in a mutualistic state, and under drought stress in particular
physiological function
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OsDHAR transformed Escherichia coli BL21 cells show significantly higher DHAR activity and a lower level of reactive oxygen species than the Escherichia coli cells transformed by an empty vector. The DHAR-overexpressing Escherichia coli strain is more tolerant to oxidant- and heavy metalmediated stress conditions than the control Escherichia coli strain, suggesting that the overexpressed rice DHAR gene effectively functions in a prokaryotic system and provides protection to various oxidative stresses
physiological function
monodehydroascorbate reductase and dehydroascorbate reductase are key enzymes of the ascorbate-glutathione cycle that maintain reduced pools of ascorbic acid and serve as important antioxidants
physiological function
enzyme overexpression AsA pool size, AsA:DHA ratio and the tolerance to moderate light-, high light-, methyl viologen- or H2O2-induced oxidative stress
physiological function
enzyme-expressing transgenic rice plants enhanced the redox state by reducing both hydroperoxide and malondialdehyde levels under salt and methyl viologen stress conditions, which lead to better plant growth, ion leakage and quantum yield
physiological function
expression of the enzyme can effectively enhance the tolerance to oxidative stress by decreasing the accumulation of reactive oxygen species
physiological function
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isoform DHAR3 is required for high-light stress tolerance
physiological function
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the enzyme is important for stress tolerance via induction of antioxidant proteins and can improve stress tolerance in transgenic potato plants
physiological function
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the enzyme plays a pivotal role in the modulation of cellular redox states under photooxidative stress
physiological function
the enzyme plays a protective role under oxidative and other abiotic stress conditions
physiological function
the increased level of antioxidants generated by the enzyme protects rice from oxidative damage and increases the yield of rice grains
physiological function
dehydroascorbate reductase (DHAR) is a key enzyme for glutathione (GSH)-dependent reduction of dehydroascorbate (DHA) to recycled ascorbate (AsA) in plants, and plays a major role against the toxicity of reactive oxygen species (ROS)
physiological function
DHARs are required to couple hydrogen peroxide metabolism to glutathione oxidation and that this is functionally important for downstream activation of the salicylic acid pathway. DHAR activity is dispensable for growth and ascorbate homeostasis under low light
physiological function
in addition to these secondary metabolites, antioxidant enzymes play a fundamental role in regulating both biotic and abiotic stress responses in plants. One of the important antioxidant enzymes in plants is dehydroascorbate reductase (DHAR), which is crucial in maintaining the cellular levels of ascorbate through the ascorbate-glutathione cycle. DHAR converts dehydroascorbate (DHA) to ascorbate using reducing equivalents from GSH, whereby GSH is converted to oxidized glutathione (GSSG) and ascorbate is recycled. DHAR plays an important role in regulating H2O2-induced OS through the ascorbate-glutathione cycle. Thus, DHAR is a key player in detoxification of ROS to effectively regulate the cellular redox homeostasis
physiological function
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pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
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pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
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pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
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pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
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pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
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pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
the DHA reductases (DHARs) that catalyze the GSH-dependent DHA reduction allows plants to rapidly recycle ascorbate from DHA. Cooperation of DHARs and GSH is required for ascorbate accumulation under high-light stress in Arabidopsis thaliana
physiological function
the enzyme is part of the ascorbate-glutathione pathway. This defense system is composed by enzymes such as the ascorbate peroxidase (APX, EC 1.11.1.11), the monodehydroascorbate reductase (MDHAR, EC 1.6.5.4), the dehydroascorbate reductase (DHAR, EC 1.8.5.1), and the glutathione reductase (GR, EC 1.6.4.2), and compounds, such as ascorbate (ASC), dehydroascorbate (DHA), reduced (GSH) and oxidized (GSSG) glutathione. In this pathway, DHAR uses GSH to reduce DHA generated from the oxidation of ASC, thereby regenerating it. The enzyme plays a critical role in the ASC-GSH recycling reaction in higher plants
physiological function
the omega-class glutathione S-transferase (GST), nlGSTO, of the brown planthopper, Nilaparvata lugens, catalyzes the biotransformation of glutathione with 1-chloro-2,4-dinitrobenzene, a general substrate for GST, as well as with dehydroascorbate to synthesize ascorbate. As ascorbate is a reducing agent, nlGSTO may participate in antioxidant resistance
physiological function
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the DHA reductases (DHARs) that catalyze the GSH-dependent DHA reduction allows plants to rapidly recycle ascorbate from DHA. Cooperation of DHARs and GSH is required for ascorbate accumulation under high-light stress in Arabidopsis thaliana
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physiological function
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pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
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additional information
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a high ascorbate level is required for aluminium tolerance
additional information
transcriptional regulation of DHAR, overview
additional information
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transcriptional regulation of DHAR, overview
additional information
computational modeling analysis is performed to understand the potential of five plant metabolites including ascorbic acid (AA), reduced glutathione (GSH), serotonin, jasmonic acid (JA), and salicylic acid (SA) in ameliorating metal/metalloid stress in rice, using dehydroascorbate reductase (DHAR) as a model. Six metal/metalloid ions (As3+, As5+, Cd2+, Cu2+, Pb2+, Zn2+) are used in the study, and the relative affinity, binding geometry and electrostatic surfaces of secondary metabolites and ions with the active site of DHAR are predicted. The results reveal that all the metabolites and ions may potentially interact with the active catalytic site of DHAR. The free energies of binding (docking score) of the metabolites are manyfolds higher than those of the ions. On comparison, the docking score of As3+ is found to be 28.29% of that of AA. Further, compared to AA, SA has lower score, and GSH, JA and serotonin show 1.42, 1.30 and 1.18fold higher score than AA. Further analysis reveals that the electrostatic surfaces of the metabolites and ions overlap with one another. Statistical analysis is performed to determine the properties of the ligands which are crucial in facilitating interaction of the ligands. Molecular docking, ligand-receptor interactions analysis, detailed overview
additional information
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determination and analysis of the NMR solution structure of isozyme PtrDHAR3A. DHARs have a monomeric state that is unlike most GSTs
additional information
determination and analysis of the NMR solution structure of isozyme PtrDHAR3A. DHARs have a monomeric state that is unlike most GSTs
additional information
determination and analysis of the NMR solution structure of isozyme PtrDHAR3A. DHARs have a monomeric state that is unlike most GSTs
additional information
determination and analysis of the NMR solution structure of isozyme PtrDHAR3A. DHARs have a monomeric state that is unlike most GSTs
additional information
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DHARs have a monomeric state that is unlike most GSTs
additional information
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DHARs have a monomeric state that is unlike most GSTs
additional information
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DHARs have a monomeric state that is unlike most GSTs
additional information
DHARs have a monomeric state that is unlike most GSTs
additional information
DHARs have a monomeric state that is unlike most GSTs
additional information
DHARs have a monomeric state that is unlike most GSTs
additional information
DHARs have a monomeric state that is unlike most GSTs
additional information
putative substrate-binding sites, including Phe28, Cys29, Phe30, Arg176, and Lue225, are important for glutathione transferase and dehydroascorbate reductase activities
additional information
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putative substrate-binding sites, including Phe28, Cys29, Phe30, Arg176, and Lue225, are important for glutathione transferase and dehydroascorbate reductase activities
additional information
the crystal structure of apo CrDHAR1 provides insights into the proposed mechanism centering on the strictly conserved Cys22, which is suggested to initiate the redox reactions of DHA and GSH, crucial roles of Asp21 and Cys22 in substrate binding and catalysis
additional information
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the crystal structure of apo CrDHAR1 provides insights into the proposed mechanism centering on the strictly conserved Cys22, which is suggested to initiate the redox reactions of DHA and GSH, crucial roles of Asp21 and Cys22 in substrate binding and catalysis
additional information
three-dimensional structure analysis of isozyme AtDHAR2, DHARs have a monomeric state that is unlike most GSTs
additional information
three-dimensional structure analysis of isozyme AtDHAR2, DHARs have a monomeric state that is unlike most GSTs
additional information
three-dimensional structure analysis of isozyme AtDHAR2, DHARs have a monomeric state that is unlike most GSTs
additional information
three-dimensional structure analysis of isozyme OsDHAR1. DHARs have a monomeric state that is unlike most GSTs
additional information
three-dimensional structure analysis of isozyme PgDHAR1. DHARs have a monomeric state that is unlike most GSTs