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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 | Populus trichocarpa |
| 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 | Lathyrus oleraceus |
| 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 | Avena sativa |
| 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 | Actinidia chinensis |
| 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 | Solanum tuberosum |
| 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 | Liriodendron chinense |
| 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 | Brassica napus |
| 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. 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 |
| 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 | Cenchrus americanus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 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 | 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 | 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 | 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 | 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, 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 | 0.07 | - |
dehydroascorbate | pH and temperature not specified in the publication, chloroplastic isozyme DHAR1 | Populus tomentosa | |
| 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, cytosolic isozyme DHAR2 | Populus tomentosa | |
| 1.8.5.1 | 0.23 | - |
dehydroascorbate | pH and temperature not specified in the publication, chloroplastic isozyme DHAR1 | Populus trichocarpa | |
| 1.8.5.1 | 0.35 | - |
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 | - |
Lathyrus oleraceus | 48046 | - |
| 1.8.5.1 | apoplast | - |
Hordeum vulgare | 48046 | - |
| 1.8.5.1 | apoplast | - |
Avena sativa | 48046 | - |
| 1.8.5.1 | chloroplast | - |
Spinacia oleracea | 9507 | - |
| 1.8.5.1 | chloroplast | isozyme DHAR2 | Actinidia chinensis | 9507 | - |
| 1.8.5.1 | chloroplast | - |
Populus tomentosa | 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 | cytosol | - |
Populus trichocarpa | 5829 | - |
| 1.8.5.1 | cytosol | - |
Hordeum vulgare | 5829 | - |
| 1.8.5.1 | cytosol | - |
Avena sativa | 5829 | - |
| 1.8.5.1 | cytosol | - |
Spinacia oleracea | 5829 | - |
| 1.8.5.1 | cytosol | isozyme DHAR1 | Actinidia chinensis | 5829 | - |
| 1.8.5.1 | cytosol | - |
Populus tomentosa | 5829 | - |
| 1.8.5.1 | cytosol | - |
Solanum tuberosum | 5829 | - |
| 1.8.5.1 | cytosol | - |
Ipomoea batatas | 5829 | - |
| 1.8.5.1 | cytosol | - |
Liriodendron chinense | 5829 | - |
| 1.8.5.1 | cytosol | - |
Pinus bungeana | 5829 | - |
| 1.8.5.1 | cytosol | - |
Brassica napus | 5829 | - |
| 1.8.5.1 | cytosol | - |
Acer saccharinum | 5829 | - |
| 1.8.5.1 | cytosol | - |
Arabidopsis thaliana | 5829 | - |
| 1.8.5.1 | cytosol | - |
Oryza sativa Japonica Group | 5829 | - |
| 1.8.5.1 | cytosol | - |
Cenchrus americanus | 5829 | - |
| 1.8.5.1 | mitochondrion | - |
Lathyrus oleraceus | 5739 | - |
| 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 | 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 | Lathyrus oleraceus | - |
- |
| 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 | 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 | 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 | 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 | 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 | 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 | Liriodendron chinense | - |
- |
| 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 | 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 | Acer saccharinum | - |
- |
| 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 | 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 | Cenchrus americanus | - |
- |
| 1.8.5.1 | peroxisome | - |
Lathyrus oleraceus | 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 | Populus trichocarpa | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Zea mays | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Lathyrus oleraceus | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Hordeum vulgare | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Avena sativa | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Spinacia oleracea | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Actinidia chinensis | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Populus tomentosa | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Solanum tuberosum | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Ipomoea batatas | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Liriodendron chinense | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Pinus bungeana | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Brassica napus | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Acer saccharinum | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Arabidopsis thaliana | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Oryza sativa Japonica Group | - |
glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | Cenchrus americanus | - |
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 | 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 | 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 | 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 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 | Lathyrus oleraceus | - |
- |
- |
| 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 | Populus tomentosa | J9WQY6 | - |
- |
| 1.8.5.1 | Populus tomentosa | J9WN12 | - |
- |
| 1.8.5.1 | Populus tomentosa | J9WNR5 | - |
- |
| 1.8.5.1 | Populus trichocarpa | - |
- |
- |
| 1.8.5.1 | Populus trichocarpa | D2WL75 | - |
- |
| 1.8.5.1 | Populus trichocarpa | D2WL74 | - |
- |
| 1.8.5.1 | Populus trichocarpa | D2WL73 | - |
- |
| 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 | 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 | 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 | Lathyrus oleraceus | |
| 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 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 | 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 | 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 | 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 | 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 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 | - |
Zea mays | - |
| 1.8.5.1 | leaf | - |
Lathyrus oleraceus | - |
| 1.8.5.1 | leaf | - |
Hordeum vulgare | - |
| 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 | 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 | leaf | - |
Oryza sativa Japonica Group | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Populus trichocarpa | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Zea mays | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Lathyrus oleraceus | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Hordeum vulgare | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Avena sativa | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Spinacia oleracea | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Actinidia chinensis | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Populus tomentosa | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Solanum tuberosum | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Ipomoea batatas | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Liriodendron chinense | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Pinus bungeana | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Brassica napus | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Acer saccharinum | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Arabidopsis thaliana | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Oryza sativa Japonica Group | glutathione disulfide + ascorbate | - |
? | |
| 1.8.5.1 | 2 glutathione + dehydroascorbate | - |
Cenchrus americanus | 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 | 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 | 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 | Lathyrus oleraceus | ? | - |
? | |
| 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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) | 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) | 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) | Arabidopsis thaliana |
| 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) | Cenchrus americanus |
| 1.8.5.1 | additional information | 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 | additional information | 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) | Lathyrus oleraceus |
| 1.8.5.1 | additional information | 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 | additional information | 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 | additional information | 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 | additional information | 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 | additional information | 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 | additional information | 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 | additional information | 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 | additional information | 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 |
| 1.8.5.1 | additional information | 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 |
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 | - |
Populus trichocarpa |
| 1.8.5.1 | dehydroascorbate reductase | - |
Zea mays |
| 1.8.5.1 | dehydroascorbate reductase | - |
Lathyrus oleraceus |
| 1.8.5.1 | dehydroascorbate reductase | - |
Hordeum vulgare |
| 1.8.5.1 | dehydroascorbate reductase | - |
Avena sativa |
| 1.8.5.1 | dehydroascorbate reductase | - |
Spinacia oleracea |
| 1.8.5.1 | dehydroascorbate reductase | - |
Actinidia chinensis |
| 1.8.5.1 | dehydroascorbate reductase | - |
Populus tomentosa |
| 1.8.5.1 | dehydroascorbate reductase | - |
Solanum tuberosum |
| 1.8.5.1 | dehydroascorbate reductase | - |
Ipomoea batatas |
| 1.8.5.1 | dehydroascorbate reductase | - |
Liriodendron chinense |
| 1.8.5.1 | dehydroascorbate reductase | - |
Pinus bungeana |
| 1.8.5.1 | dehydroascorbate reductase | - |
Brassica napus |
| 1.8.5.1 | dehydroascorbate reductase | - |
Acer saccharinum |
| 1.8.5.1 | dehydroascorbate reductase | - |
Arabidopsis thaliana |
| 1.8.5.1 | dehydroascorbate reductase | - |
Oryza sativa Japonica Group |
| 1.8.5.1 | dehydroascorbate reductase | - |
Cenchrus americanus |
| 1.8.5.1 | DHA reductase | - |
Populus trichocarpa |
| 1.8.5.1 | DHA reductase | - |
Zea mays |
| 1.8.5.1 | DHA reductase | - |
Lathyrus oleraceus |
| 1.8.5.1 | DHA reductase | - |
Hordeum vulgare |
| 1.8.5.1 | DHA reductase | - |
Avena sativa |
| 1.8.5.1 | DHA reductase | - |
Spinacia oleracea |
| 1.8.5.1 | DHA reductase | - |
Actinidia chinensis |
| 1.8.5.1 | DHA reductase | - |
Populus tomentosa |
| 1.8.5.1 | DHA reductase | - |
Solanum tuberosum |
| 1.8.5.1 | DHA reductase | - |
Ipomoea batatas |
| 1.8.5.1 | DHA reductase | - |
Liriodendron chinense |
| 1.8.5.1 | DHA reductase | - |
Pinus bungeana |
| 1.8.5.1 | DHA reductase | - |
Brassica napus |
| 1.8.5.1 | DHA reductase | - |
Acer saccharinum |
| 1.8.5.1 | DHA reductase | - |
Arabidopsis thaliana |
| 1.8.5.1 | DHA reductase | - |
Oryza sativa Japonica Group |
| 1.8.5.1 | DHA reductase | - |
Cenchrus americanus |
| 1.8.5.1 | DHAR | - |
Populus trichocarpa |
| 1.8.5.1 | DHAR | - |
Zea mays |
| 1.8.5.1 | DHAR | - |
Lathyrus oleraceus |
| 1.8.5.1 | DHAR | - |
Hordeum vulgare |
| 1.8.5.1 | DHAR | - |
Avena sativa |
| 1.8.5.1 | DHAR | - |
Spinacia oleracea |
| 1.8.5.1 | DHAR | - |
Actinidia chinensis |
| 1.8.5.1 | DHAR | - |
Populus tomentosa |
| 1.8.5.1 | DHAR | - |
Solanum tuberosum |
| 1.8.5.1 | DHAR | - |
Ipomoea batatas |
| 1.8.5.1 | DHAR | - |
Liriodendron chinense |
| 1.8.5.1 | DHAR | - |
Pinus bungeana |
| 1.8.5.1 | DHAR | - |
Brassica napus |
| 1.8.5.1 | DHAR | - |
Acer saccharinum |
| 1.8.5.1 | DHAR | - |
Arabidopsis thaliana |
| 1.8.5.1 | DHAR | - |
Oryza sativa Japonica Group |
| 1.8.5.1 | DHAR | - |
Cenchrus americanus |
| 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 | - |
dehydroascorbate | pH and temperature not specified in the publication, cytosolic isozyme | Ipomoea batatas | |
| 1.8.5.1 | 0.00004 | - |
glutathione | pH and temperature not specified in the publication, cytosolic isozyme | Pinus bungeana | |
| 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 | 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 | 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 | Lathyrus oleraceus |
| 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 | 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 | 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 | 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 | 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 | 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 | 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 | Liriodendron chinense |
| 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 | 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 | 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 | 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 | 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 | Cenchrus americanus |
| 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 | Zea mays |
| 1.8.5.1 | malfunction | site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity | Lathyrus oleraceus |
| 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 | Avena sativa |
| 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 | Actinidia chinensis |
| 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 | Solanum tuberosum |
| 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 | Liriodendron chinense |
| 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 | Brassica napus |
| 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 | Arabidopsis thaliana |
| 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 | 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 | 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 | 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 | 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 | Lathyrus oleraceus |
| 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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. 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 | 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 | 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 | Cenchrus americanus |
| 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 | 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 | 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 | 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 | 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 | 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 | Lathyrus oleraceus |
| 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 | 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 | 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 | 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 | 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 | 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 | 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 | Liriodendron chinense |
| 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 | 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 | 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 | 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 | 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 | Cenchrus americanus |
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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