Literature summary for 1.8.5.1 extracted from

Ding, H.; Wang, B.; Han, Y.; Li, S.
The pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants (2020), J. Exp. Bot., 71, 3405-3416 .

Cloned(Commentary)

Cloned (Comment)	Organism
gene AtDHAR2, recombinant expression in tobacco leaves results in increased aluminum tolerance in roots	Arabidopsis thaliana
isozyme DHAR1, recombinant expression in Arabidopsis thaliana leaves resulting in increased salt and drought tolerance	Liriodendron chinense
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
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
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)

Crystallization (Comment)	Organism
isozyme AtDHAR2, X-ray diffraction structure determination and analysis	Arabidopsis thaliana
isozyme OsDHAR1, X-ray diffraction structure determination and analysis	Oryza sativa Japonica Group
isozyme PgDHAR1, X-ray diffraction structure determination and analysis	Cenchrus americanus

Protein Variants

Protein Variants	Comment	Organism
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Hordeum vulgare
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Pisum sativum
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Avena sativa
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Brassica napus
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Actinidia chinensis
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Acer saccharinum
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Populus trichocarpa
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Pinus bungeana
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Ipomoea batatas
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Populus tomentosa
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Cenchrus americanus
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Zea mays
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Spinacia oleracea
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Solanum tuberosum
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Liriodendron chinense
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Arabidopsis thaliana
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
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
additional information	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity. Transgenic expression of AtDHAR2 in tobacco maintains a higher ascorbate level and its oxidation status compared to wild-type plants, resulting in enhanced tolerance to various stresses including ozone, drought, salt, polyethylene glycol (PEG), and aluminium. In Arabidopsis, disruption of DHAR2 decreases the ascorbate redox state but not its pool size, and plants exhibit increased ozone sensitivity, and glutathione oxidation is inhibited in all three dhar single-mutants following photo-oxidative stress	Arabidopsis thaliana

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
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
additional information	-	additional information	chloroplastic DHAR displays similar values to the cytosolic isoform, despite having somewhat higher affinity for GSH	Spinacia oleracea
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
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
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
0.04	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme	Cenchrus americanus
0.05	-	dehydroascorbate	pH and temperature not specified in the publication, chloroplastic isozyme	Spinacia oleracea
0.07	-	dehydroascorbate	pH and temperature not specified in the publication, chloroplastic isozyme DHAR1	Populus tomentosa
0.07	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme	Spinacia oleracea
0.07	-	dehydroascorbate	pH and temperature not specified in the publication, plastidic isozyme DHAR2	Actinidia chinensis
0.08	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme	Pinus bungeana
0.09	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme DHAR2	Populus trichocarpa
0.11	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme DHAR1	Actinidia chinensis
0.13	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme	Cenchrus americanus
0.16	-	dehydroascorbate	pH and temperature not specified in the publication, chloroplastic isozyme DHAR3B	Populus trichocarpa
0.18	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme DHAR3A	Populus trichocarpa
0.19	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme	Ipomoea batatas
0.23	-	dehydroascorbate	pH and temperature not specified in the publication, chloroplastic isozyme DHAR1	Populus trichocarpa
0.23	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme DHAR2	Populus tomentosa
0.35	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme	Oryza sativa Japonica Group
0.39	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme	Solanum tuberosum
0.48	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme DHAR3	Populus tomentosa
0.81	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme	Liriodendron chinense
0.84	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme	Oryza sativa Japonica Group
1.03	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme	Pinus bungeana
1.1	-	glutathione	pH and temperature not specified in the publication, chloroplastic isozyme	Spinacia oleracea
1.27	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme DHAR1	Actinidia chinensis
1.41	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme	Liriodendron chinense
2.22	-	glutathione	pH and temperature not specified in the publication, plastidic isozyme DHAR2	Actinidia chinensis
2.28	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme DHAR2	Populus tomentosa
2.38	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme	Ipomoea batatas
2.47	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme DHAR3	Populus tomentosa
2.5	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme	Spinacia oleracea
3.7	5	glutathione	pH and temperature not specified in the publication, chloroplastic isozyme DHAR1	Populus tomentosa
4.35	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme	Solanum tuberosum

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
apoplast	-	Hordeum vulgare	48046	-
apoplast	-	Pisum sativum	48046	-
apoplast	-	Avena sativa	48046	-
chloroplast	-	Populus tomentosa	9507	-
chloroplast	-	Spinacia oleracea	9507	-
chloroplast	AtDHAR3 contains an N-terminal extension and is chloroplastic, with no evidence for mitochondrial localization	Arabidopsis thaliana	9507	-
chloroplast	isozyme DHAR2	Actinidia chinensis	9507	-
cytosol	-	Hordeum vulgare	5829	-
cytosol	-	Avena sativa	5829	-
cytosol	-	Brassica napus	5829	-
cytosol	-	Acer saccharinum	5829	-
cytosol	-	Populus trichocarpa	5829	-
cytosol	-	Pinus bungeana	5829	-
cytosol	-	Ipomoea batatas	5829	-
cytosol	-	Populus tomentosa	5829	-
cytosol	-	Cenchrus americanus	5829	-
cytosol	-	Oryza sativa Japonica Group	5829	-
cytosol	-	Arabidopsis thaliana	5829	-
cytosol	-	Spinacia oleracea	5829	-
cytosol	-	Solanum tuberosum	5829	-
cytosol	-	Liriodendron chinense	5829	-
cytosol	isozyme DHAR1	Actinidia chinensis	5829	-
mitochondrion	-	Pisum sativum	5739	-
additional information	DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers	Hordeum vulgare	-	-
additional information	DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers	Avena sativa	-	-
additional information	DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers	Zea mays	-	-
additional information	in Pisum sativum, DHAR isozymes are reported to localize in peroxisomes, mitochondria, and the apoplast. DHA generated in cellular compartments lacking DHAR may be transported to the cytosol for re-reduction through plasma membrane carriers	Pisum sativum	-	-
additional information	isozyme AtDHAR1 contains no clear targeting signal sequence	Arabidopsis thaliana	-	-
additional information	isozyme AtDHAR2 contains no clear targeting signal sequence	Arabidopsis thaliana	-	-
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	-	-
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	-	-
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	-	-
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	-	-
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	-	-
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	-	-
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	-	-
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	-	-
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	-	-
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	-	-
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	-	-
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	-	-
peroxisome	-	Pisum sativum	5777	-
peroxisome	-	Arabidopsis thaliana	5777	-
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)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
2 glutathione + dehydroascorbate	Hordeum vulgare	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Pisum sativum	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Avena sativa	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Brassica napus	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Actinidia chinensis	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Acer saccharinum	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Populus trichocarpa	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Pinus bungeana	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Ipomoea batatas	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Populus tomentosa	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Cenchrus americanus	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Oryza sativa Japonica Group	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Arabidopsis thaliana	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Zea mays	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Spinacia oleracea	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Solanum tuberosum	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Liriodendron chinense	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Arabidopsis thaliana Col-0	-	glutathione disulfide + ascorbate	-	?

Organism

Organism	UniProt	Comment	Textmining
Acer saccharinum	-	-	-
Actinidia chinensis	-	-	-
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	-
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	-
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	-
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	-
Avena sativa	-	-	-
Brassica napus	-	-	-
Cenchrus americanus	U5XYA0	Pennisetum glaucum	-
Hordeum vulgare	-	-	-
Ipomoea batatas	D2CGD4	-	-
Liriodendron chinense	A0A6C0W973	-	-
Oryza sativa Japonica Group	Q65XA0	-	-
Pinus bungeana	B2ZHM6	-	-
Pisum sativum	-	-	-
Populus tomentosa	J9WN12	-	-
Populus tomentosa	J9WNR5	-	-
Populus tomentosa	J9WQY6	-	-
Populus trichocarpa	-	-	-
Populus trichocarpa	D2WL73	-	-
Populus trichocarpa	D2WL74	-	-
Populus trichocarpa	D2WL75	-	-
Solanum tuberosum	M1BA41	-	-
Spinacia oleracea	Q9T2H6	-	-
Zea mays	C0P9V2	the Zea mays genome contains four DHAR isozymes	-

Reaction

Reaction	Comment	Organism	Reaction ID
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	a
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate	the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism	Pisum sativum	a
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	a
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	a
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	a
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	a
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	a
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	a
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	a
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	a
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	a
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	a
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	a
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	a
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	a
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	a
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	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Hordeum vulgare	-
leaf	-	Pisum sativum	-
leaf	-	Avena sativa	-
leaf	-	Brassica napus	-
leaf	-	Acer saccharinum	-
leaf	-	Oryza sativa Japonica Group	-
leaf	-	Zea mays	-
leaf	cytosolic DHAR1 and chloroplastic DHAR3 contribute approximately equally and constitute almost all the leaf DHAR activity, while DHAR2 makes a minor contribution	Arabidopsis thaliana	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2 glutathione + dehydroascorbate	-	Hordeum vulgare	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Pisum sativum	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Avena sativa	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Brassica napus	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Actinidia chinensis	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Acer saccharinum	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Populus trichocarpa	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Pinus bungeana	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Ipomoea batatas	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Populus tomentosa	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Cenchrus americanus	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Oryza sativa Japonica Group	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Arabidopsis thaliana	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Zea mays	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Spinacia oleracea	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Solanum tuberosum	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Liriodendron chinense	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Arabidopsis thaliana Col-0	glutathione disulfide + ascorbate	-	?
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	?	-	-
additional information	while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant	Pisum sativum	?	-	-
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	?	-	-
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	?	-	-
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	?	-	-
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	?	-	-
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	?	-	-
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	?	-	-
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	?	-	-
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	?	-	-
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	?	-	-
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	?	-	-
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	?	-	-
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	?	-	-
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	?	-	-
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	?	-	-
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	?	-	-
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

Subunits	Comment	Organism
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
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
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
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
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
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
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
More	the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)	Hordeum vulgare
More	the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)	Pisum sativum
More	the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)	Avena sativa
More	the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)	Actinidia chinensis
More	the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)	Ipomoea batatas
More	the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)	Populus tomentosa
More	the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)	Arabidopsis thaliana
More	the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)	Zea mays
More	the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)	Spinacia oleracea
More	the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)	Solanum tuberosum
More	the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)	Liriodendron chinense

Synonyms

Synonyms	Comment	Organism
AtDHAR	-	Arabidopsis thaliana
AtDHAR1	-	Arabidopsis thaliana
AtDHAR2	-	Arabidopsis thaliana
AtDHAR3	-	Arabidopsis thaliana
dehydroascorbate reductase	-	Hordeum vulgare
dehydroascorbate reductase	-	Pisum sativum
dehydroascorbate reductase	-	Avena sativa
dehydroascorbate reductase	-	Brassica napus
dehydroascorbate reductase	-	Actinidia chinensis
dehydroascorbate reductase	-	Acer saccharinum
dehydroascorbate reductase	-	Populus trichocarpa
dehydroascorbate reductase	-	Pinus bungeana
dehydroascorbate reductase	-	Ipomoea batatas
dehydroascorbate reductase	-	Populus tomentosa
dehydroascorbate reductase	-	Cenchrus americanus
dehydroascorbate reductase	-	Oryza sativa Japonica Group
dehydroascorbate reductase	-	Arabidopsis thaliana
dehydroascorbate reductase	-	Zea mays
dehydroascorbate reductase	-	Spinacia oleracea
dehydroascorbate reductase	-	Solanum tuberosum
dehydroascorbate reductase	-	Liriodendron chinense
DHA reductase	-	Hordeum vulgare
DHA reductase	-	Pisum sativum
DHA reductase	-	Avena sativa
DHA reductase	-	Brassica napus
DHA reductase	-	Actinidia chinensis
DHA reductase	-	Acer saccharinum
DHA reductase	-	Populus trichocarpa
DHA reductase	-	Pinus bungeana
DHA reductase	-	Ipomoea batatas
DHA reductase	-	Populus tomentosa
DHA reductase	-	Cenchrus americanus
DHA reductase	-	Oryza sativa Japonica Group
DHA reductase	-	Arabidopsis thaliana
DHA reductase	-	Zea mays
DHA reductase	-	Spinacia oleracea
DHA reductase	-	Solanum tuberosum
DHA reductase	-	Liriodendron chinense
DHAR	-	Hordeum vulgare
DHAR	-	Pisum sativum
DHAR	-	Avena sativa
DHAR	-	Brassica napus
DHAR	-	Actinidia chinensis
DHAR	-	Acer saccharinum
DHAR	-	Populus trichocarpa
DHAR	-	Pinus bungeana
DHAR	-	Ipomoea batatas
DHAR	-	Populus tomentosa
DHAR	-	Cenchrus americanus
DHAR	-	Oryza sativa Japonica Group
DHAR	-	Arabidopsis thaliana
DHAR	-	Zea mays
DHAR	-	Spinacia oleracea
DHAR	-	Solanum tuberosum
DHAR	-	Liriodendron chinense
DHAR1	-	Actinidia chinensis
DHAR1	-	Populus tomentosa
DHAR1	-	Liriodendron chinense
DHAR2	-	Actinidia chinensis
DHAR2	-	Populus tomentosa
DHAR3	-	Populus tomentosa
DHAR4	-	Zea mays
LcDHAR	-	Liriodendron chinense
OsDHAR	-	Oryza sativa Japonica Group
OsDHAR1	-	Oryza sativa Japonica Group
PgDHAR1	-	Cenchrus americanus
PtrDHAR1	-	Populus trichocarpa
PtrDHAR2	-	Populus trichocarpa
PtrDHAR3A	-	Populus trichocarpa
PtrDHAR3B	-	Populus trichocarpa

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
0.000001	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme	Liriodendron chinense
0.000003	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme	Liriodendron chinense
0.00001	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme	Pinus bungeana
0.00002	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme DHAR1	Actinidia chinensis
0.00002	-	dehydroascorbate	pH and temperature not specified in the publication, plastidic isozyme DHAR2	Actinidia chinensis
0.00003	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme DHAR1	Actinidia chinensis
0.00003	-	glutathione	pH and temperature not specified in the publication, plastidic isozyme DHAR2	Actinidia chinensis
0.00004	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme	Pinus bungeana
0.00004	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme	Ipomoea batatas
0.0001	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme	Ipomoea batatas
0.00041	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme DHAR3A	Populus trichocarpa
0.00046	-	dehydroascorbate	pH and temperature not specified in the publication, chloroplastic isozyme DHAR1	Populus trichocarpa
0.00046	-	dehydroascorbate	pH and temperature not specified in the publication, chloroplastic isozyme DHAR3B	Populus trichocarpa
0.00047	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme DHAR2	Populus trichocarpa
0.0131	-	dehydroascorbate	pH and temperature not specified in the publication, chloroplastic isozyme DHAR1	Populus tomentosa
0.0177	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme DHAR2	Populus tomentosa
0.0211	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme DHAR3	Populus tomentosa
0.0409	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme DHAR3	Populus tomentosa
0.0539	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme DHAR2	Populus tomentosa
0.0998	-	glutathione	pH and temperature not specified in the publication, chloroplastic isozyme DHAR1	Populus tomentosa

Expression

Organism	Comment	Expression
Brassica napus	after priming seeds of Brassica napus with PEG, the DHAR protein abundance is upregulated during subsequent germination	up
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

General Information	Comment	Organism
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
evolution	DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism	Pisum sativum
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Hordeum vulgare
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Pisum sativum
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Avena sativa
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Brassica napus
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Actinidia chinensis
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Acer saccharinum
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Populus trichocarpa
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Pinus bungeana
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Ipomoea batatas
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Populus tomentosa
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Cenchrus americanus
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Oryza sativa Japonica Group
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Arabidopsis thaliana
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Zea mays
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Spinacia oleracea
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Solanum tuberosum
malfunction	site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity	Liriodendron chinense
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
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
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
metabolism	the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress	Pisum sativum
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
additional information	DHARs have a monomeric state that is unlike most GSTs	Brassica napus
additional information	DHARs have a monomeric state that is unlike most GSTs	Acer saccharinum
additional information	DHARs have a monomeric state that is unlike most GSTs	Populus trichocarpa
additional information	DHARs have a monomeric state that is unlike most GSTs	Pinus bungeana
additional information	three-dimensional structure analysis of isozyme AtDHAR2, DHARs have a monomeric state that is unlike most GSTs	Arabidopsis thaliana
additional information	three-dimensional structure analysis of isozyme OsDHAR1. DHARs have a monomeric state that is unlike most GSTs	Oryza sativa Japonica Group
additional information	three-dimensional structure analysis of isozyme PgDHAR1. DHARs have a monomeric state that is unlike most GSTs	Cenchrus americanus
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
physiological function	pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism	Pisum sativum
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
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
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
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
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
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
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
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
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
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
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
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
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
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
physiological function	pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism	Liriodendron chinense

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism
0.00000071	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme	Liriodendron chinense
0.0000037	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme	Liriodendron chinense
0.000039	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme	Pinus bungeana
0.000042	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme	Ipomoea batatas
0.000125	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme	Pinus bungeana
0.002	-	dehydroascorbate	pH and temperature not specified in the publication, chloroplastic isozyme DHAR1	Populus trichocarpa
0.0021	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme	Ipomoea batatas
0.0023	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme DHAR3A	Populus trichocarpa
0.0029	-	dehydroascorbate	pH and temperature not specified in the publication, chloroplastic isozyme DHAR3B	Populus trichocarpa
0.0052	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme DHAR2	Populus trichocarpa
0.0166	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme DHAR3	Populus tomentosa
0.024	-	glutathione	pH and temperature not specified in the publication, cytosolic isozyme DHAR2	Populus tomentosa
0.027	-	glutathione	pH and temperature not specified in the publication, chloroplastic isozyme DHAR1	Populus tomentosa
0.077	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme DHAR2	Populus tomentosa
0.187	-	dehydroascorbate	pH and temperature not specified in the publication, chloroplastic isozyme DHAR1	Populus tomentosa
0.44	-	dehydroascorbate	pH and temperature not specified in the publication, cytosolic isozyme DHAR3	Populus tomentosa