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Literature summary extracted from
- The pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants (2020), J. Exp. Bot., 71, 3405-3416 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.8.5.1 | gene AtDHAR2, recombinant expression in tobacco leaves results in increased aluminum tolerance in roots | Arabidopsis thaliana |
| 1.8.5.1 | isozyme DHAR1, recombinant expression in Arabidopsis thaliana leaves resulting in increased salt and drought tolerance | Liriodendron chinense |
| 1.8.5.1 | isozyme DHAR1, recombinant expression in Arabidopsis thaliana leaves resulting in increased salt tolerance. Recombinant expression in Zea mays kernels results in improved nutrition value of grain. Recombinant expression in tobacco leaves recults in decreased GSH/GSSG and increased salt and chilling tolerance. Recombinant overexpression in rice plants results in increased grain yield and biomass, as well as in increased paraquat and salt tolerance | Oryza sativa Japonica Group |
| 1.8.5.1 | isozyme DHAR1, recombinant overexpression in Arabidopsis thaliana leaves resulting in increased total glutathione content and GSH/GSSG, as well as in increased tolerance to paraquat, high light, and high temperature, Recombinant expression of AtDHAr1 in Solanum tuberosum results in increased tolerance to paraquat, drought, and salt of the potato plants | Arabidopsis thaliana |
| 1.8.5.1 | recombinant overexpression of DHAR isozymes in potato plants does not result in different phenotypes. Recombinant expression of the isozymes in Solanum lycopersicum results in no increase in ascorbate content in fruit expressing a chloroplast-localized DHAR, but increased paraquat and salt tolerance | Solanum tuberosum |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.8.5.1 | isozyme AtDHAR2, X-ray diffraction structure determination and analysis | Arabidopsis thaliana |
| 1.8.5.1 | isozyme OsDHAR1, X-ray diffraction structure determination and analysis | Oryza sativa Japonica Group |
| 1.8.5.1 | isozyme PgDHAR1, X-ray diffraction structure determination and analysis | Cenchrus americanus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Hordeum vulgare |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Pisum sativum |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Avena sativa |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Brassica napus |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Actinidia chinensis |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Acer saccharinum |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Populus trichocarpa |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Pinus bungeana |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Ipomoea batatas |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Populus tomentosa |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Cenchrus americanus |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Zea mays |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Spinacia oleracea |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Solanum tuberosum |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Liriodendron chinense |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Arabidopsis thaliana |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity. Despite only a small increase in ascorbate content, transgenic Arabidopsis thaliana expressing OsDHAR are more tolerant to salt stress than control plants. Even small changes in DHAR activity may improve tolerance to some environmental stresses | Oryza sativa Japonica Group |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity. Transgenic Arabidopsis thaliana overexpressing AtDHAR1 maintain higher levels of ascorbate and chlorophyll with reduced levels of membrane damage compared to control plants following exposure to high light, high temperature, or following MV treatment | Arabidopsis thaliana |
| 1.8.5.1 | additional information | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity. Transgenic expression of AtDHAR2 in tobacco maintains a higher ascorbate level and its oxidation status compared to wild-type plants, resulting in enhanced tolerance to various stresses including ozone, drought, salt, polyethylene glycol (PEG), and aluminium. 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 | Arabidopsis thaliana |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.8.5.1 | additional information | - |
additional information | AtDHAR2 is the first DHAR reported to behave as an allosteric enzyme, and its kcat/K0.5 for DHA is substantially higher than for GSH, suggesting that it has a considerably higher substrate specificity for DHA | Arabidopsis thaliana | |
| 1.8.5.1 | additional information | - |
additional information | chloroplastic DHAR displays similar values to the cytosolic isoform, despite having somewhat higher affinity for GSH | Spinacia oleracea | |
| 1.8.5.1 | additional information | - |
additional information | in Arabidopsis, the cytosolic DHAR1 exhibits higher affinity for DHA than the chloroplastic DHAR3, while their affinities for GSH are approximately the same | Arabidopsis thaliana | |
| 1.8.5.1 | additional information | - |
additional information | the chloroplastic DHAR of kiwifruit shows higher affinity for DHA than the cytosolic DHAR, while the affinity for GSH of the cytosolic isoform is higher than that of the chloroplastic isoform | Actinidia chinensis | |
| 1.8.5.1 | additional information | - |
additional information | the chloroplastic DHAR of kiwifruit shows higher affinity for DHA than the cytosolic DHAR, while the affinity for GSH of the cytosolic isoform is higher than that of the chloroplastic isoform | Populus tomentosa | |
| 1.8.5.1 | 0.04 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme | Cenchrus americanus |  |
| 1.8.5.1 | 0.05 | - |
dehydroascorbate | pH and temperature not specified in the publication, chloroplastic isozyme | Spinacia oleracea | |
| 1.8.5.1 | 0.07 | - |
dehydroascorbate | pH and temperature not specified in the publication, chloroplastic isozyme DHAR1 | Populus tomentosa | |
| 1.8.5.1 | 0.07 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme | Spinacia oleracea | |
| 1.8.5.1 | 0.07 | - |
dehydroascorbate | pH and temperature not specified in the publication, plastidic isozyme DHAR2 | Actinidia chinensis | |
| 1.8.5.1 | 0.08 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme | Pinus bungeana | |
| 1.8.5.1 | 0.09 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme DHAR2 | Populus trichocarpa | |
| 1.8.5.1 | 0.11 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme DHAR1 | Actinidia chinensis | |
| 1.8.5.1 | 0.13 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme | Cenchrus americanus | |
| 1.8.5.1 | 0.16 | - |
dehydroascorbate | pH and temperature not specified in the publication, chloroplastic isozyme DHAR3B | Populus trichocarpa | |
| 1.8.5.1 | 0.18 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme DHAR3A | Populus trichocarpa | |
| 1.8.5.1 | 0.19 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme | Ipomoea batatas | |
| 1.8.5.1 | 0.23 | - |
dehydroascorbate | pH and temperature not specified in the publication, chloroplastic isozyme DHAR1 | Populus trichocarpa | |
| 1.8.5.1 | 0.23 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme DHAR2 | Populus tomentosa | |
| 1.8.5.1 | 0.35 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme | Oryza sativa Japonica Group | |
| 1.8.5.1 | 0.39 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme | Solanum tuberosum | |
| 1.8.5.1 | 0.48 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme DHAR3 | Populus tomentosa | |
| 1.8.5.1 | 0.81 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme | Liriodendron chinense | |
| 1.8.5.1 | 0.84 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme | Oryza sativa Japonica Group | |
| 1.8.5.1 | 1.03 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme | Pinus bungeana | |
| 1.8.5.1 | 1.1 | - |
glutathione | pH and temperature not specified in the publication, chloroplastic isozyme | Spinacia oleracea | |
| 1.8.5.1 | 1.27 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme DHAR1 | Actinidia chinensis | |
| 1.8.5.1 | 1.41 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme | Liriodendron chinense | |
| 1.8.5.1 | 2.22 | - |
glutathione | pH and temperature not specified in the publication, plastidic isozyme DHAR2 | Actinidia chinensis | |
| 1.8.5.1 | 2.28 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme DHAR2 | Populus tomentosa | |
| 1.8.5.1 | 2.38 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme | Ipomoea batatas | |
| 1.8.5.1 | 2.47 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme DHAR3 | Populus tomentosa | |
| 1.8.5.1 | 2.5 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme | Spinacia oleracea | |
| 1.8.5.1 | 3.7 | 5 | glutathione | pH and temperature not specified in the publication, chloroplastic isozyme DHAR1 | Populus tomentosa | |
| 1.8.5.1 | 4.35 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme | Solanum tuberosum | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.8.5.1 | apoplast | - |
Hordeum vulgare | 48046 | - |
| 1.8.5.1 | apoplast | - |
Pisum sativum | 48046 | - |
| 1.8.5.1 | apoplast | - |
Avena sativa | 48046 | - |
| 1.8.5.1 | chloroplast | - |
Populus tomentosa | 9507 | - |
| 1.8.5.1 | chloroplast | - |
Spinacia oleracea | 9507 | - |
| 1.8.5.1 | chloroplast | AtDHAR3 contains an N-terminal extension and is chloroplastic, with no evidence for mitochondrial localization | Arabidopsis thaliana | 9507 | - |
| 1.8.5.1 | chloroplast | isozyme DHAR2 | Actinidia chinensis | 9507 | - |
| 1.8.5.1 | cytosol | - |
Hordeum vulgare | 5829 | - |
| 1.8.5.1 | cytosol | - |
Avena sativa | 5829 | - |
| 1.8.5.1 | cytosol | - |
Brassica napus | 5829 | - |
| 1.8.5.1 | cytosol | - |
Acer saccharinum | 5829 | - |
| 1.8.5.1 | cytosol | - |
Populus trichocarpa | 5829 | - |
| 1.8.5.1 | cytosol | - |
Pinus bungeana | 5829 | - |
| 1.8.5.1 | cytosol | - |
Ipomoea batatas | 5829 | - |
| 1.8.5.1 | cytosol | - |
Populus tomentosa | 5829 | - |
| 1.8.5.1 | cytosol | - |
Cenchrus americanus | 5829 | - |
| 1.8.5.1 | cytosol | - |
Oryza sativa Japonica Group | 5829 | - |
| 1.8.5.1 | cytosol | - |
Arabidopsis thaliana | 5829 | - |
| 1.8.5.1 | cytosol | - |
Spinacia oleracea | 5829 | - |
| 1.8.5.1 | cytosol | - |
Solanum tuberosum | 5829 | - |
| 1.8.5.1 | cytosol | - |
Liriodendron chinense | 5829 | - |
| 1.8.5.1 | cytosol | isozyme DHAR1 | Actinidia chinensis | 5829 | - |
| 1.8.5.1 | mitochondrion | - |
Pisum sativum | 5739 | - |
| 1.8.5.1 | additional information | DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Hordeum vulgare | - |
- |
| 1.8.5.1 | additional information | DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Avena sativa | - |
- |
| 1.8.5.1 | additional information | DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Zea mays | - |
- |
| 1.8.5.1 | additional information | in Pisum sativum, DHAR isozymes are reported to localize in peroxisomes, mitochondria, and the apoplast. DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Pisum sativum | - |
- |
| 1.8.5.1 | additional information | isozyme AtDHAR1 contains no clear targeting signal sequence | Arabidopsis thaliana | - |
- |
| 1.8.5.1 | additional information | isozyme AtDHAR2 contains no clear targeting signal sequence | Arabidopsis thaliana | - |
- |
| 1.8.5.1 | additional information | isozymes can occur in chloroplast, mitochondrion, cytosol, and peroxisome. DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Brassica napus | - |
- |
| 1.8.5.1 | additional information | isozymes can occur in chloroplast, mitochondrion, cytosol, and peroxisome. DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Actinidia chinensis | - |
- |
| 1.8.5.1 | additional information | isozymes can occur in chloroplast, mitochondrion, cytosol, and peroxisome. DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Acer saccharinum | - |
- |
| 1.8.5.1 | additional information | isozymes can occur in chloroplast, mitochondrion, cytosol, and peroxisome. DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Populus trichocarpa | - |
- |
| 1.8.5.1 | additional information | isozymes can occur in chloroplast, mitochondrion, cytosol, and peroxisome. DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Pinus bungeana | - |
- |
| 1.8.5.1 | additional information | isozymes can occur in chloroplast, mitochondrion, cytosol, and peroxisome. DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Ipomoea batatas | - |
- |
| 1.8.5.1 | additional information | isozymes can occur in chloroplast, mitochondrion, cytosol, and peroxisome. DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Populus tomentosa | - |
- |
| 1.8.5.1 | additional information | isozymes can occur in chloroplast, mitochondrion, cytosol, and peroxisome. DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Cenchrus americanus | - |
- |
| 1.8.5.1 | additional information | isozymes can occur in chloroplast, mitochondrion, cytosol, and peroxisome. DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Oryza sativa Japonica Group | - |
- |
| 1.8.5.1 | additional information | isozymes can occur in chloroplast, mitochondrion, cytosol, and peroxisome. DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Spinacia oleracea | - |
- |
| 1.8.5.1 | additional information | isozymes can occur in chloroplast, mitochondrion, cytosol, and peroxisome. DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Solanum tuberosum | - |
- |
| 1.8.5.1 | additional information | isozymes can occur in chloroplast, mitochondrion, cytosol, and peroxisome. DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers | Liriodendron chinense | - |
- |
| 1.8.5.1 | peroxisome | - |
Pisum sativum | 5777 | - |
| 1.8.5.1 | peroxisome | - |
Arabidopsis thaliana | 5777 | - |
| 1.8.5.1 | vacuole | the Zea mays genome contains four DHAR isozymes, of which ZmDHAR4 is identified as a vacuolar DHAR | Zea mays | 5773 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Hordeum vulgare | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Pisum sativum | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Avena sativa | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Brassica napus | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Actinidia chinensis | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Acer saccharinum | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Populus trichocarpa | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Pinus bungeana | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Ipomoea batatas | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Populus tomentosa | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Cenchrus americanus | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Oryza sativa Japonica Group | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Arabidopsis thaliana | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Zea mays | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Spinacia oleracea | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Solanum tuberosum | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Liriodendron chinense | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Arabidopsis thaliana Col-0 | - |
glutathione disulfide + ascorbate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.5.1 | Acer saccharinum | - |
- |
- |
| 1.8.5.1 | Actinidia chinensis | - |
- |
- |
| 1.8.5.1 | Arabidopsis thaliana | Q8LE52 | although five DHAR-like genes have been reported in Arabidopsis, three are annotated to encode functional proteins, namely DHAR1, DHAR2 , and DHAR3. DHAR4 appears to be a pseudogene. DHAR1 has also been described as DHAR5 | - |
| 1.8.5.1 | Arabidopsis thaliana | Q9FRL8 | although five DHAR-like genes have been reported in Arabidopsis, three are annotated to encode functional proteins, namely DHAR1, DHAR2, and DHAR3. DHAR4 appears to be a pseudogene. DHAR1 has also been described as DHAR5 | - |
| 1.8.5.1 | Arabidopsis thaliana | Q9FWR4 | although five DHAR-like genes have been reported in Arabidopsis, three are annotated to encode functional proteins, namely DHAR1, DHAR2, and DHAR3. DHAR4 appears to be a pseudogene. DHAR1 has also been described as DHAR5 | - |
| 1.8.5.1 | Arabidopsis thaliana Col-0 | Q9FWR4 | although five DHAR-like genes have been reported in Arabidopsis, three are annotated to encode functional proteins, namely DHAR1, DHAR2, and DHAR3. DHAR4 appears to be a pseudogene. DHAR1 has also been described as DHAR5 | - |
| 1.8.5.1 | Avena sativa | - |
- |
- |
| 1.8.5.1 | Brassica napus | - |
- |
- |
| 1.8.5.1 | Cenchrus americanus | U5XYA0 | Pennisetum glaucum | - |
| 1.8.5.1 | Hordeum vulgare | - |
- |
- |
| 1.8.5.1 | Ipomoea batatas | D2CGD4 | - |
- |
| 1.8.5.1 | Liriodendron chinense | A0A6C0W973 | - |
- |
| 1.8.5.1 | Oryza sativa Japonica Group | Q65XA0 | - |
- |
| 1.8.5.1 | Pinus bungeana | B2ZHM6 | - |
- |
| 1.8.5.1 | Pisum sativum | - |
- |
- |
| 1.8.5.1 | Populus tomentosa | J9WN12 | - |
- |
| 1.8.5.1 | Populus tomentosa | J9WNR5 | - |
- |
| 1.8.5.1 | Populus tomentosa | J9WQY6 | - |
- |
| 1.8.5.1 | Populus trichocarpa | - |
- |
- |
| 1.8.5.1 | Populus trichocarpa | D2WL73 | - |
- |
| 1.8.5.1 | Populus trichocarpa | D2WL74 | - |
- |
| 1.8.5.1 | Populus trichocarpa | D2WL75 | - |
- |
| 1.8.5.1 | Solanum tuberosum | M1BA41 | - |
- |
| 1.8.5.1 | Spinacia oleracea | Q9T2H6 | - |
- |
| 1.8.5.1 | Zea mays | C0P9V2 | the Zea mays genome contains four DHAR isozymes | - |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Hordeum vulgare | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Pisum sativum | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Avena sativa | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Brassica napus | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Actinidia chinensis | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Acer saccharinum | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Populus trichocarpa | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Pinus bungeana | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Ipomoea batatas | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Populus tomentosa | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Oryza sativa Japonica Group | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Arabidopsis thaliana | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Zea mays | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Spinacia oleracea | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Solanum tuberosum | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Liriodendron chinense | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate | the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be deprotonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). 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 | Cenchrus americanus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.8.5.1 | leaf | - |
Hordeum vulgare | - |
| 1.8.5.1 | leaf | - |
Pisum sativum | - |
| 1.8.5.1 | leaf | - |
Avena sativa | - |
| 1.8.5.1 | leaf | - |
Brassica napus | - |
| 1.8.5.1 | leaf | - |
Acer saccharinum | - |
| 1.8.5.1 | leaf | - |
Oryza sativa Japonica Group | - |
| 1.8.5.1 | leaf | - |
Zea mays | - |
| 1.8.5.1 | leaf | cytosolic DHAR1 and chloroplastic DHAR3 contribute approximately equally and constitute almost all the leaf DHAR activity, while DHAR2 makes a minor contribution | Arabidopsis thaliana | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Hordeum vulgare | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Pisum sativum | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Avena sativa | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Brassica napus | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Actinidia chinensis | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Acer saccharinum | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Populus trichocarpa | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Pinus bungeana | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Ipomoea batatas | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Populus tomentosa | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Cenchrus americanus | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Oryza sativa Japonica Group | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Arabidopsis thaliana | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Zea mays | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Spinacia oleracea | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Solanum tuberosum | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Liriodendron chinense | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Arabidopsis thaliana Col-0 | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Hordeum vulgare | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Pisum sativum | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Avena sativa | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Brassica napus | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Actinidia chinensis | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Acer saccharinum | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Populus trichocarpa | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Pinus bungeana | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Ipomoea batatas | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Populus tomentosa | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Cenchrus americanus | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Oryza sativa Japonica Group | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Arabidopsis thaliana | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Zea mays | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Spinacia oleracea | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Solanum tuberosum | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Liriodendron chinense | ? | - |
- |
|
| 1.8.5.1 | additional information | while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant | Arabidopsis thaliana Col-0 | ? | - |
- |
|
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.8.5.1 | monomer | DHARs have a monomeric state that is unlike most GSTs. The enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Brassica napus |
| 1.8.5.1 | monomer | DHARs have a monomeric state that is unlike most GSTs. The enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Acer saccharinum |
| 1.8.5.1 | monomer | DHARs have a monomeric state that is unlike most GSTs. The enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Populus trichocarpa |
| 1.8.5.1 | monomer | DHARs have a monomeric state that is unlike most GSTs. The enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Pinus bungeana |
| 1.8.5.1 | monomer | DHARs have a monomeric state that is unlike most GSTs. The enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Cenchrus americanus |
| 1.8.5.1 | monomer | DHARs have a monomeric state that is unlike most GSTs. The enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Oryza sativa Japonica Group |
| 1.8.5.1 | monomer | DHARs have a monomeric state that is unlike most GSTs. The enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Arabidopsis thaliana |
| 1.8.5.1 | More | the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Hordeum vulgare |
| 1.8.5.1 | More | the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Pisum sativum |
| 1.8.5.1 | More | the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Avena sativa |
| 1.8.5.1 | More | the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Actinidia chinensis |
| 1.8.5.1 | More | the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Ipomoea batatas |
| 1.8.5.1 | More | the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Populus tomentosa |
| 1.8.5.1 | More | the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Arabidopsis thaliana |
| 1.8.5.1 | More | the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Zea mays |
| 1.8.5.1 | More | the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Spinacia oleracea |
| 1.8.5.1 | More | the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Solanum tuberosum |
| 1.8.5.1 | More | the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site) | Liriodendron chinense |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.8.5.1 | AtDHAR | - |
Arabidopsis thaliana |
| 1.8.5.1 | AtDHAR1 | - |
Arabidopsis thaliana |
| 1.8.5.1 | AtDHAR2 | - |
Arabidopsis thaliana |
| 1.8.5.1 | AtDHAR3 | - |
Arabidopsis thaliana |
| 1.8.5.1 | dehydroascorbate reductase | - |
Hordeum vulgare |
| 1.8.5.1 | dehydroascorbate reductase | - |
Pisum sativum |
| 1.8.5.1 | dehydroascorbate reductase | - |
Avena sativa |
| 1.8.5.1 | dehydroascorbate reductase | - |
Brassica napus |
| 1.8.5.1 | dehydroascorbate reductase | - |
Actinidia chinensis |
| 1.8.5.1 | dehydroascorbate reductase | - |
Acer saccharinum |
| 1.8.5.1 | dehydroascorbate reductase | - |
Populus trichocarpa |
| 1.8.5.1 | dehydroascorbate reductase | - |
Pinus bungeana |
| 1.8.5.1 | dehydroascorbate reductase | - |
Ipomoea batatas |
| 1.8.5.1 | dehydroascorbate reductase | - |
Populus tomentosa |
| 1.8.5.1 | dehydroascorbate reductase | - |
Cenchrus americanus |
| 1.8.5.1 | dehydroascorbate reductase | - |
Oryza sativa Japonica Group |
| 1.8.5.1 | dehydroascorbate reductase | - |
Arabidopsis thaliana |
| 1.8.5.1 | dehydroascorbate reductase | - |
Zea mays |
| 1.8.5.1 | dehydroascorbate reductase | - |
Spinacia oleracea |
| 1.8.5.1 | dehydroascorbate reductase | - |
Solanum tuberosum |
| 1.8.5.1 | dehydroascorbate reductase | - |
Liriodendron chinense |
| 1.8.5.1 | DHA reductase | - |
Hordeum vulgare |
| 1.8.5.1 | DHA reductase | - |
Pisum sativum |
| 1.8.5.1 | DHA reductase | - |
Avena sativa |
| 1.8.5.1 | DHA reductase | - |
Brassica napus |
| 1.8.5.1 | DHA reductase | - |
Actinidia chinensis |
| 1.8.5.1 | DHA reductase | - |
Acer saccharinum |
| 1.8.5.1 | DHA reductase | - |
Populus trichocarpa |
| 1.8.5.1 | DHA reductase | - |
Pinus bungeana |
| 1.8.5.1 | DHA reductase | - |
Ipomoea batatas |
| 1.8.5.1 | DHA reductase | - |
Populus tomentosa |
| 1.8.5.1 | DHA reductase | - |
Cenchrus americanus |
| 1.8.5.1 | DHA reductase | - |
Oryza sativa Japonica Group |
| 1.8.5.1 | DHA reductase | - |
Arabidopsis thaliana |
| 1.8.5.1 | DHA reductase | - |
Zea mays |
| 1.8.5.1 | DHA reductase | - |
Spinacia oleracea |
| 1.8.5.1 | DHA reductase | - |
Solanum tuberosum |
| 1.8.5.1 | DHA reductase | - |
Liriodendron chinense |
| 1.8.5.1 | DHAR | - |
Hordeum vulgare |
| 1.8.5.1 | DHAR | - |
Pisum sativum |
| 1.8.5.1 | DHAR | - |
Avena sativa |
| 1.8.5.1 | DHAR | - |
Brassica napus |
| 1.8.5.1 | DHAR | - |
Actinidia chinensis |
| 1.8.5.1 | DHAR | - |
Acer saccharinum |
| 1.8.5.1 | DHAR | - |
Populus trichocarpa |
| 1.8.5.1 | DHAR | - |
Pinus bungeana |
| 1.8.5.1 | DHAR | - |
Ipomoea batatas |
| 1.8.5.1 | DHAR | - |
Populus tomentosa |
| 1.8.5.1 | DHAR | - |
Cenchrus americanus |
| 1.8.5.1 | DHAR | - |
Oryza sativa Japonica Group |
| 1.8.5.1 | DHAR | - |
Arabidopsis thaliana |
| 1.8.5.1 | DHAR | - |
Zea mays |
| 1.8.5.1 | DHAR | - |
Spinacia oleracea |
| 1.8.5.1 | DHAR | - |
Solanum tuberosum |
| 1.8.5.1 | DHAR | - |
Liriodendron chinense |
| 1.8.5.1 | DHAR1 | - |
Actinidia chinensis |
| 1.8.5.1 | DHAR1 | - |
Populus tomentosa |
| 1.8.5.1 | DHAR1 | - |
Liriodendron chinense |
| 1.8.5.1 | DHAR2 | - |
Actinidia chinensis |
| 1.8.5.1 | DHAR2 | - |
Populus tomentosa |
| 1.8.5.1 | DHAR3 | - |
Populus tomentosa |
| 1.8.5.1 | DHAR4 | - |
Zea mays |
| 1.8.5.1 | LcDHAR | - |
Liriodendron chinense |
| 1.8.5.1 | OsDHAR | - |
Oryza sativa Japonica Group |
| 1.8.5.1 | OsDHAR1 | - |
Oryza sativa Japonica Group |
| 1.8.5.1 | PgDHAR1 | - |
Cenchrus americanus |
| 1.8.5.1 | PtrDHAR1 | - |
Populus trichocarpa |
| 1.8.5.1 | PtrDHAR2 | - |
Populus trichocarpa |
| 1.8.5.1 | PtrDHAR3A | - |
Populus trichocarpa |
| 1.8.5.1 | PtrDHAR3B | - |
Populus trichocarpa |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.8.5.1 | 0.000001 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme | Liriodendron chinense | |
| 1.8.5.1 | 0.000003 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme | Liriodendron chinense | |
| 1.8.5.1 | 0.00001 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme | Pinus bungeana | |
| 1.8.5.1 | 0.00002 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme DHAR1 | Actinidia chinensis | |
| 1.8.5.1 | 0.00002 | - |
dehydroascorbate | pH and temperature not specified in the publication, plastidic isozyme DHAR2 | Actinidia chinensis | |
| 1.8.5.1 | 0.00003 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme DHAR1 | Actinidia chinensis | |
| 1.8.5.1 | 0.00003 | - |
glutathione | pH and temperature not specified in the publication, plastidic isozyme DHAR2 | Actinidia chinensis | |
| 1.8.5.1 | 0.00004 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme | Pinus bungeana | |
| 1.8.5.1 | 0.00004 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme | Ipomoea batatas | |
| 1.8.5.1 | 0.0001 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme | Ipomoea batatas | |
| 1.8.5.1 | 0.00041 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme DHAR3A | Populus trichocarpa | |
| 1.8.5.1 | 0.00046 | - |
dehydroascorbate | pH and temperature not specified in the publication, chloroplastic isozyme DHAR1 | Populus trichocarpa | |
| 1.8.5.1 | 0.00046 | - |
dehydroascorbate | pH and temperature not specified in the publication, chloroplastic isozyme DHAR3B | Populus trichocarpa | |
| 1.8.5.1 | 0.00047 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme DHAR2 | Populus trichocarpa | |
| 1.8.5.1 | 0.0131 | - |
dehydroascorbate | pH and temperature not specified in the publication, chloroplastic isozyme DHAR1 | Populus tomentosa | |
| 1.8.5.1 | 0.0177 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme DHAR2 | Populus tomentosa | |
| 1.8.5.1 | 0.0211 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme DHAR3 | Populus tomentosa | |
| 1.8.5.1 | 0.0409 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme DHAR3 | Populus tomentosa | |
| 1.8.5.1 | 0.0539 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme DHAR2 | Populus tomentosa | |
| 1.8.5.1 | 0.0998 | - |
glutathione | pH and temperature not specified in the publication, chloroplastic isozyme DHAR1 | Populus tomentosa | |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 1.8.5.1 | Brassica napus | after priming seeds of Brassica napus with PEG, the DHAR protein abundance is upregulated during subsequent germination | up |
| 1.8.5.1 | Acer saccharinum | treating seeds of silver maple (Acer saccharinum) with 2.5 mM GSH results in slower dehydration and a higher germination capacity compared to control seeds soaked with water, and a strong positive correlation between DHAR activity and germination capacity is detected in the GSH-treated seeds | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.8.5.1 | 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 | Hordeum vulgare |
| 1.8.5.1 | 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 | Pisum sativum |
| 1.8.5.1 | 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 | Avena sativa |
| 1.8.5.1 | 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 | Brassica napus |
| 1.8.5.1 | 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 | Actinidia chinensis |
| 1.8.5.1 | 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 | Acer saccharinum |
| 1.8.5.1 | 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 | Populus trichocarpa |
| 1.8.5.1 | 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 | Pinus bungeana |
| 1.8.5.1 | 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 | Ipomoea batatas |
| 1.8.5.1 | 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 | Populus tomentosa |
| 1.8.5.1 | 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 | Cenchrus americanus |
| 1.8.5.1 | 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 | Oryza sativa Japonica Group |
| 1.8.5.1 | 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 | Arabidopsis thaliana |
| 1.8.5.1 | 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 | Zea mays |
| 1.8.5.1 | 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 | Spinacia oleracea |
| 1.8.5.1 | 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 | Solanum tuberosum |
| 1.8.5.1 | 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 | Liriodendron chinense |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Hordeum vulgare |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Pisum sativum |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Avena sativa |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Brassica napus |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Actinidia chinensis |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Acer saccharinum |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Populus trichocarpa |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Pinus bungeana |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Ipomoea batatas |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Populus tomentosa |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Cenchrus americanus |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Oryza sativa Japonica Group |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Arabidopsis thaliana |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Zea mays |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Spinacia oleracea |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Solanum tuberosum |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Liriodendron chinense |
| 1.8.5.1 | 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 | Arabidopsis thaliana |
| 1.8.5.1 | 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 | Populus trichocarpa |
| 1.8.5.1 | 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 | Hordeum vulgare |
| 1.8.5.1 | 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 | Pisum sativum |
| 1.8.5.1 | 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 | Avena sativa |
| 1.8.5.1 | 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 | Brassica napus |
| 1.8.5.1 | 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 | Actinidia chinensis |
| 1.8.5.1 | 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 | Acer saccharinum |
| 1.8.5.1 | 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 | Populus trichocarpa |
| 1.8.5.1 | 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 | Pinus bungeana |
| 1.8.5.1 | 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 | Ipomoea batatas |
| 1.8.5.1 | 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 | Populus tomentosa |
| 1.8.5.1 | 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 | Cenchrus americanus |
| 1.8.5.1 | 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 | Oryza sativa Japonica Group |
| 1.8.5.1 | 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 | Zea mays |
| 1.8.5.1 | 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 | Spinacia oleracea |
| 1.8.5.1 | 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 | Solanum tuberosum |
| 1.8.5.1 | 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 | Liriodendron chinense |
| 1.8.5.1 | 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 | Arabidopsis thaliana |
| 1.8.5.1 | 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 | Arabidopsis thaliana |
| 1.8.5.1 | additional information | determination and analysis of the NMR solution structure of isozyme PtrDHAR3A. DHARs have a monomeric state that is unlike most GSTs | Populus trichocarpa |
| 1.8.5.1 | additional information | DHARs have a monomeric state that is unlike most GSTs | Brassica napus |
| 1.8.5.1 | additional information | DHARs have a monomeric state that is unlike most GSTs | Acer saccharinum |
| 1.8.5.1 | additional information | DHARs have a monomeric state that is unlike most GSTs | Populus trichocarpa |
| 1.8.5.1 | additional information | DHARs have a monomeric state that is unlike most GSTs | Pinus bungeana |
| 1.8.5.1 | additional information | three-dimensional structure analysis of isozyme AtDHAR2, DHARs have a monomeric state that is unlike most GSTs | Arabidopsis thaliana |
| 1.8.5.1 | additional information | three-dimensional structure analysis of isozyme OsDHAR1. DHARs have a monomeric state that is unlike most GSTs | Oryza sativa Japonica Group |
| 1.8.5.1 | additional information | three-dimensional structure analysis of isozyme PgDHAR1. DHARs have a monomeric state that is unlike most GSTs | Cenchrus americanus |
| 1.8.5.1 | 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 | Hordeum vulgare |
| 1.8.5.1 | 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 | Pisum sativum |
| 1.8.5.1 | 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 | Avena sativa |
| 1.8.5.1 | 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 | Brassica napus |
| 1.8.5.1 | 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 | Actinidia chinensis |
| 1.8.5.1 | 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 | Acer saccharinum |
| 1.8.5.1 | 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 | Populus trichocarpa |
| 1.8.5.1 | 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 | Pinus bungeana |
| 1.8.5.1 | 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 | Ipomoea batatas |
| 1.8.5.1 | 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 | Populus tomentosa |
| 1.8.5.1 | 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 | Cenchrus americanus |
| 1.8.5.1 | 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 | Oryza sativa Japonica Group |
| 1.8.5.1 | 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 | Arabidopsis thaliana |
| 1.8.5.1 | 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 | Zea mays |
| 1.8.5.1 | 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 | Spinacia oleracea |
| 1.8.5.1 | 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 | Solanum tuberosum |
| 1.8.5.1 | 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 | Liriodendron chinense |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.8.5.1 | 0.00000071 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme | Liriodendron chinense | |
| 1.8.5.1 | 0.0000037 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme | Liriodendron chinense | |
| 1.8.5.1 | 0.000039 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme | Pinus bungeana | |
| 1.8.5.1 | 0.000042 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme | Ipomoea batatas | |
| 1.8.5.1 | 0.000125 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme | Pinus bungeana | |
| 1.8.5.1 | 0.002 | - |
dehydroascorbate | pH and temperature not specified in the publication, chloroplastic isozyme DHAR1 | Populus trichocarpa | |
| 1.8.5.1 | 0.0021 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme | Ipomoea batatas | |
| 1.8.5.1 | 0.0023 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme DHAR3A | Populus trichocarpa | |
| 1.8.5.1 | 0.0029 | - |
dehydroascorbate | pH and temperature not specified in the publication, chloroplastic isozyme DHAR3B | Populus trichocarpa | |
| 1.8.5.1 | 0.0052 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme DHAR2 | Populus trichocarpa | |
| 1.8.5.1 | 0.0166 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme DHAR3 | Populus tomentosa | |
| 1.8.5.1 | 0.024 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme DHAR2 | Populus tomentosa | |
| 1.8.5.1 | 0.027 | - |
glutathione | pH and temperature not specified in the publication, chloroplastic isozyme DHAR1 | Populus tomentosa | |
| 1.8.5.1 | 0.077 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme DHAR2 | Populus tomentosa | |
| 1.8.5.1 | 0.187 | - |
dehydroascorbate | pH and temperature not specified in the publication, chloroplastic isozyme DHAR1 | Populus tomentosa | |
| 1.8.5.1 | 0.44 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme DHAR3 | Populus tomentosa | |
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