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Information on EC 1.8.5.1 - glutathione dehydrogenase (ascorbate)
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1.8.5.1 glutathione dehydrogenase (ascorbate)Specify your search results
Word Map
- 1.8.5.1
- metallothioneins
- monodehydroascorbate
- dismutase
- catalase
- sod
- seedlings
- cadmium
-
ascorbate-glutathione
- chlorophyll
- malondialdehyde
- chloroplast
- zn
- s-transferase
- copper
- shoot
-
1.11.1.11
- drought
-
melanocortins
- guaiacol
- gssg
- glutathione-s-transferase
-
asa-gsh
- yam
- omega
-
metal-binding
-
1.6.4.2
- thioltransferase
- glyoxalase
- methylglyoxal
-
l-ascorbic
- dioscorea
-
hydroponic
-
cd-induced
- alpha-msh
-
foliar
-
gsh-dependent
- glutaredoxins
-
cadmium-induced
- batatas
- agriculture
- medicine
-
pradesh
- bothrops
-
xanthophyl
-
photoinhibition
-
beta-domains
- l-galactose
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
mt-ii, dehydroascorbate reductase, dhar, metallothionein-1, gsto1-1, dioscorin, metallothionein-2, dha reductase, dhar1, dhar2, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydroascorbate reductase
DHA reductase
DHAR
DHAR1
DHAR2
DHAR3
glutathione dehydroascorbate reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
catalytic mechanism
-
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
reduction
reduction
human GSTO1-1 has monomethylarsonate reductase activity and is considered to be the rate-limiting enzyme in the biomethylation pathway of inorganic arsenic metabolism
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
glutathione:dehydroascorbate oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9026-38-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-acetylcysteine + dehydroascorbate
N,N'-diacetyl-L-cystine + ascorbate
-
4% of the activity with GSH
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
vitamin C-conserving mechanism
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
the enzyme is critical for maintenance of an appropriate level of ascorbate in plant cells
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
regenerates ascorbate after it is oxidized during normal aerobic metabolism
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
specific for glutathione as hydrogen donor
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
L-threo-diastereomer is reduced faster than the L-erythro-dehydroascorbate and D-erythro-dehydroascorbate
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
specific for glutathione as hydrogen donor
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
L-threo-dehydroascorbate is the best and D-threo-dehydroascorbate is the worst substrate of the four dehydroascorbate stereoisomers
-
?
additional information
?
-
no substrates: 1-chloro-2,4-dinitrobenzene, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, nitrobutyl chloride, 4-nitrophenyl acetate, 1,2-dichloro-4-nitrobenzene
-
?
additional information
?
-
no substrates: 1-chloro-2,4-dinitrobenzene, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, nitrobutyl chloride, 4-nitrophenyl acetate, 1,2-dichloro-4-nitrobenzene
-
?
additional information
?
-
no substrates: 1-chloro-2,4-dinitrobenzene, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, nitrobutyl chloride, 4-nitrophenyl acetate, 1,2-dichloro-4-nitrobenzene
-
?
additional information
?
-
-
no substrates: 1-chloro-2,4-dinitrobenzene, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, nitrobutyl chloride, 4-nitrophenyl acetate, 1,2-dichloro-4-nitrobenzene
-
?
additional information
?
-
-
glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin)
-
?
additional information
?
-
-
L-Cys-L-Gly is not active as hydrogen donor
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
vitamin C-conserving mechanism
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
the enzyme is critical for maintenance of an appropriate level of ascorbate in plant cells
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
regenerates ascorbate after it is oxidized during normal aerobic metabolism
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
flavin
-
enzyme shows an unusual flavin peak, enzyme might form a flavin adduct
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iodoacetic acid
-
41% and 1% residual activity after treatment with 0.1 mM and 1 mM, respectively
additional information
-
heat treatment at 80°C for 10 min inhibits the enzyme leading to 1% residual activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hydrogen peroxide
-
the activity of DHAR significantly increases from 1 d after treatment with 0.1 mM and thereafter declines gradually to the control level
methyl jasmonate
-
0.2 mM, activity increases after methyl jasmonate exposure and remains higher till the 9 days compared to non-treated roots
methyl viologen
-
the activity of DHAR significantly increases from 1 d after treatment with 0.05 mM and thereafter declines gradually to the control level
additional information
-
hot air treatment at 50°C for 2 h maintains the enzyme activity for 2 days, whereas the activity in control florets decreases gradually
-
additional information
DHAR activity increases after infection with Fusarium graminearum
-
additional information
-
DHAR activity increases after infection with Fusarium graminearum
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
dehydroascorbate
pH not specified in the publication, temperature not specified in the publication
0.13
dehydroascorbate
mutant D72A, pH not specified in the publication, temperature not specified in the publication
0.23
dehydroascorbate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.32
dehydroascorbate
-
glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin)
0.43
dehydroascorbate
mutant containing six cysteine-to-serine mutations, with C-terminal residues FGLC deleted, pH 6.9, 30°C
0.48
dehydroascorbate
pH not specified in the publication, temperature not specified in the publication
0.51
dehydroascorbate
-
glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin), C25S mutant
0.52
dehydroascorbate
mutant containing six cysteine-to-serine mutations with the C-terminal cysteine residue deleted, pH 6.9, 30°C
0.53
dehydroascorbate
mutant with C-terminal residues FGLC deleted, pH 6.9, 30°C
0.7
dehydroascorbate
mutant S73A, pH not specified in the publication, temperature not specified in the publication
0.97
dehydroascorbate
mutant K8A, pH not specified in the publication, temperature not specified in the publication
1.71
glutathione
mutant D72A, pH not specified in the publication, temperature not specified in the publication
2.28
glutathione
wild-type, pH not specified in the publication, temperature not specified in the publication
2.47
glutathione
pH not specified in the publication, temperature not specified in the publication
3.01
glutathione
mutant K8A, pH not specified in the publication, temperature not specified in the publication
3.26
glutathione
mutant S73A, pH not specified in the publication, temperature not specified in the publication
3.7 - 5
glutathione
pH not specified in the publication, temperature not specified in the publication
4.18
glutathione
mutant with C-terminal residues FGLC deleted, pH 6.9, 30°C
5.97
glutathione
mutant containing six cysteine-to-serine mutations, with C-terminal residues FGLC deleted, pH 6.9, 30°C
7.8
glutathione
mutant containing six cysteine-to-serine mutations with the C-terminal cysteine residue deleted, pH 6.9, 30°C
3.7
GSH
-
glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin)
5.2
GSH
-
glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin), C25S mutant
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0047
dehydroascorbate
mutant with C-terminal residues FGLC deleted, pH 6.9, 30°C
0.008
dehydroascorbate
mutant containing six cysteine-to-serine mutations, with C-terminal residues FGLC deleted, pH 6.9, 30°C
0.0135
dehydroascorbate
mutant containing six cysteine-to-serine mutations with the C-terminal cysteine residue deleted, pH 6.9, 30°C
570
dehydroascorbate
mutant K8A, pH not specified in the publication, temperature not specified in the publication
3988
dehydroascorbate
mutant S73A, pH not specified in the publication, temperature not specified in the publication
5737
dehydroascorbate
mutant D72A, pH not specified in the publication, temperature not specified in the publication
13130
dehydroascorbate
pH not specified in the publication, temperature not specified in the publication
17730
dehydroascorbate
wild-type, pH not specified in the publication, temperature not specified in the publication
21150
dehydroascorbate
pH not specified in the publication, temperature not specified in the publication
0.0058
glutathione
mutant with C-terminal residues FGLC deleted, pH 6.9, 30°C
0.0138
glutathione
mutant containing six cysteine-to-serine mutations, with C-terminal residues FGLC deleted, pH 6.9, 30°C
0.0293
glutathione
mutant containing six cysteine-to-serine mutations with the C-terminal cysteine residue deleted, pH 6.9, 30°C
745
glutathione
mutant K8A, pH not specified in the publication, temperature not specified in the publication
6705
glutathione
mutant S73A, pH not specified in the publication, temperature not specified in the publication
15960
glutathione
mutant D72A, pH not specified in the publication, temperature not specified in the publication
40850
glutathione
pH not specified in the publication, temperature not specified in the publication
53880
glutathione
wild-type, pH not specified in the publication, temperature not specified in the publication
99830
glutathione
pH not specified in the publication, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
588
dehydroascorbate
mutant K8A, pH not specified in the publication, temperature not specified in the publication
5697
dehydroascorbate
mutant S73A, pH not specified in the publication, temperature not specified in the publication
7708
dehydroascorbate
wild-type, pH not specified in the publication, temperature not specified in the publication
18760
dehydroascorbate
pH not specified in the publication, temperature not specified in the publication
44050
dehydroascorbate
pH not specified in the publication, temperature not specified in the publication
44130
dehydroascorbate
mutant D72A, pH not specified in the publication, temperature not specified in the publication
247
glutathione
mutant K8A, pH not specified in the publication, temperature not specified in the publication
2056
glutathione
mutant S73A, pH not specified in the publication, temperature not specified in the publication
9332
glutathione
mutant D72A, pH not specified in the publication, temperature not specified in the publication
16540
glutathione
pH not specified in the publication, temperature not specified in the publication
23630
glutathione
wild-type, pH not specified in the publication, temperature not specified in the publication
26620
glutathione
pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.13
allelic variant A140/E155/E208 of GSTO1-1, dehydroascorbate as substrate, at 30°C
0.14
0.21
allelic variant D140/DELTAE155/K208 of GSTO1-1, dehydroascorbate as substrate, at 30°C
0.25
allelic variant A140/DELTAE155/E208 of GSTO1-1, dehydroascorbate as substrate, at 30°C
11.6
allelic variant D142 of GSTO2-2, dehydroascorbate as substrate, at 30°C
13.8
allelic variant N142 of GSTO2-2, dehydroascorbate as substrate, at 30°C
49.1
53
pH not specified in the publication, temperature not specified in the publication
965
recombinant enzyme, at pH 8.0, temperature not specified in the publication
additional information
0.14
allelic variant A140/E155/K208 of GSTO1-1, dehydroascorbate as substrate, at 30°C
0.14
allelic variant D140/E155/E208 of GSTO1-1, dehydroascorbate as substrate, at 30°C
additional information
-
hemoglobin downregulating lines have significantly higher DHAR than wild type lines, which, in turn, are significantly higher than hemoglobin overexpressing lines, regardless of oxygen pressures
additional information
activity of dehydroascorbate reductase is significantly higher at 30°C, as compared with 20°C in tobacco mosaic virus-inoculated Xanthi-nc tobacco induced for hypersensitive response-type necroses
additional information
-
activity of dehydroascorbate reductase is significantly higher at 30°C, as compared with 20°C in tobacco mosaic virus-inoculated Xanthi-nc tobacco induced for hypersensitive response-type necroses
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7
pH 5.0: about 25% of maximal activity, pH 7.0: about 65% of maximal activity
5.5 - 10
6 - 10
6.5 - 8.5
5.5 - 10
the enzyme almost completely loses its activity below pH 5.5 or above pH 10.0
5.5 - 10
-
the enzyme almost completely loses its activity below pH 5.5 or above pH 10.0
5.5 - 10
-
the enzyme almost completely loses its activity below pH 5.5 or above pH 10.0
5.5 - 10
-
the enzyme almost completely loses its activity below pH 5.5 or above pH 10.0
5.5 - 10
-
the enzyme almost completely loses its activity below pH 5.5 or above pH 10.0
5.5 - 10
-
the enzyme almost completely loses its activity below pH 5.5 or above pH 10.0
5.5 - 10
-
the enzyme almost completely loses its activity below pH 5.5 or above pH 10.0
6 - 10
-
isoforms DHAR1 and DHAR2 retain more than 80% of their maximum enzymatic activities at pH values between 6.0 and 10.0, respectively
6.5 - 8.5
-
pH 6.5: about 25% of maximal activity, pH 8.5: about 60% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
20°C: about 60% of maximal activity, 70°C: about 35% of maximal activity
25 - 50
25 - 50
the enzyme retains more than 45% of its maximum enzymatic activity between 25 and 50°C
25 - 50
-
the enzyme retains more than 45% of its maximum enzymatic activity between 25 and 50°C
25 - 50
-
the enzyme retains more than 45% of its maximum enzymatic activity between 25 and 50°C
25 - 50
-
the enzyme retains more than 45% of its maximum enzymatic activity between 25 and 50°C
25 - 50
-
the enzyme retains more than 45% of its maximum enzymatic activity between 25 and 50°C
25 - 50
-
the enzyme retains more than 45% of its maximum enzymatic activity between 25 and 50°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Prunus sp.
hybrids P3605 (Prunus amygdalus L. 'Garfi' x Prunus persica L. 'Nemared'), 8-9 (P. cerasifera L. 'P2980' x 'P3605'), 7-7 (Prunus cerasifera L. 'P2175' x Prunus davidiana L.) and 6-5 (Prunus cerasifera L. 'P2175' x Prunus amygdalus L. 'Garfi')
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
ripening, expression analysis, transcript level of DHAR is highest at the intermediate stage of fruit ripening, overview
brenda
the highest activity of the sesame DHAR is detected in the 4 week cultures of the hairy roots, after which its activity is rapidly decreased to approximately 80%
brenda
-
activity is significantly increased by paraquat treatment and with the increasing of paraquat concentration, particularly in the modified plants (chimeric gene P(SAGI2)-IPT transformed)
brenda
-
DHAR5 mRNA levels are upregulated in Arabidopsis roots and shoots colonized by the beneficial endophyticfungus Piriformospora indica
brenda
additional information
-
widespread in the gray matter, not found in the white matter
brenda
-
DHAR5 mRNA levels are upregulated in Arabidopsis roots and shoots colonized by the beneficial endophyticfungus Piriformospora indica
brenda
the expression level of PbDHAR mRNA in Pinus bungeana seedlings do not show significant change under high temperature stress
brenda
additional information
under dark conditions, there is a sharp and significant decline in the total and reduced ascorbate contents, accompanied by a decrease in the level of transcripts and enzyme activities of the two genes in acerola leaves
brenda
additional information
-
under dark conditions, there is a sharp and significant decline in the total and reduced ascorbate contents, accompanied by a decrease in the level of transcripts and enzyme activities of the two genes in acerola leaves
brenda
additional information
RT-PCR reveals that the PbDHAR is a constitutive expression gene in Pinus bungeana
brenda
additional information
-
RT-PCR reveals that the PbDHAR is a constitutive expression gene in Pinus bungeana
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
two major dehydroascorbate reductases exist in spinach leaves. One form, DHAR-1, originates in chloroplast, the other, DHAR-b, occurs in a subcellular compartment other than chloroplast
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
isoform DHAR3 contributes, at least to some extent, to ascorbate recycling
physiological function
additional information
physiological function
chemical compounds that generate reactive oxygen species or directly applied hydrogen peroxide (H2O2) are able to induce hypersensitive response-type necroses in tobacco mosaic virus-inoculated Xanthi-nc tobacco even at high temperatures (e.g. 30°C). Activity of dehydroascorbate reductase is significantly higher at 30°C, as compared with 20°C, suggesting that DHAR might contribute to the inhibition of hypersensitive response-type necroses at 30°C
physiological function
-
monodehydroascorbate reductase 2 and DHAR5 (At1g19570) mRNA levels are upregulated in Arabidopsis roots colonized by the beneficial endophyticfungus Piriformospora indica. Insertional inactivation of the two genes show that they are crucial for maintaining the interaction between Piriformospora indica and Arabidopsis in a mutualistic state, and under drought stress in particular
physiological function
-
OsDHAR transformed Escherichia coli BL21 cells show significantly higher DHAR activity and a lower level of reactive oxygen species than the Escherichia coli cells transformed by an empty vector. The DHAR-overexpressing Escherichia coli strain is more tolerant to oxidant- and heavy metalmediated stress conditions than the control Escherichia coli strain, suggesting that the overexpressed rice DHAR gene effectively functions in a prokaryotic system and provides protection to various oxidative stresses
physiological function
monodehydroascorbate reductase and dehydroascorbate reductase are key enzymes of the ascorbate-glutathione cycle that maintain reduced pools of ascorbic acid and serve as important antioxidants
physiological function
enzyme overexpression AsA pool size, AsA:DHA ratio and the tolerance to moderate light-, high light-, methyl viologen- or H2O2-induced oxidative stress
physiological function
enzyme-expressing transgenic rice plants enhanced the redox state by reducing both hydroperoxide and malondialdehyde levels under salt and methyl viologen stress conditions, which lead to better plant growth, ion leakage and quantum yield
physiological function
expression of the enzyme can effectively enhance the tolerance to oxidative stress by decreasing the accumulation of reactive oxygen species
physiological function
-
isoform DHAR3 is required for high-light stress tolerance
physiological function
-
the enzyme is important for stress tolerance via induction of antioxidant proteins and can improve stress tolerance in transgenic potato plants
physiological function
-
the enzyme plays a pivotal role in the modulation of cellular redox states under photooxidative stress
physiological function
the enzyme plays a protective role under oxidative and other abiotic stress conditions
physiological function
the increased level of antioxidants generated by the enzyme protects rice from oxidative damage and increases the yield of rice grains
additional information
-
a high ascorbate level is required for aluminium tolerance
Show AA Sequence and Transmembrane Helices (741 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Aquifex aeolicus (strain VF5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15000
-
SDS-PAGE and electrospray ionization quadrupole-time-of-flight (ESI Q-TOF), His-tagged fusion protein
25000
26000
27000
29690
molecular mass of the recombinant protein including a 6xHis tag determined by SDS-PAGE and MALDI-TOF/MS
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
-
electrospray ionization quadrupole-time-of-flight (ESI Q-TOF), 1 * 15000 Da (His-tagged fusion protein)
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoform DHAr2 bound to glutathione, hanging drop vapor diffusion method, using 2.0 M ammonium sulfate, 0.1 M sodium acetate, pH 4.8
-
crystal structures of isoform GSTO1 in complex with ascoric acid, to 1.7 A resolution. Ascorbic acid binds in the glutathione site, where the glutamyl moiety of GSH binds and stacks against a conserved aromatic residue, F34
crystal structures of isoform GSTO2-2, stabilized through site-directed mutagenesis of cysteine residues to serines and determined at 1.9 A resolution in the presence and absence of glutathione
native, ascorbate-bound, and glutathione-bound enzyme forms, hanging drop vapor diffusion method, using 0.15 M potassium bromide and 30% (w/v) PEG MME 2000
sitting drop vapor diffusion method, using 0.15 M potassium bromide, 30% (w/v) PEG MME 2000
modeling of structure. Protein has a typical glutathione S-transferase structure containing a smaller thioredoxin-like N-terminal domain and a larger helical C-terminal domain
recombinant enzyme produced in Escherichia coli, crystallized by hanging-drop vapour-diffusion method
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q114H
-
the mutant shows reduced activity compared to the wild type enzyme
A140D
no alteration in specific activity compared to the wild type enzyme
E155
the deletion causes a 2-3fold increase in the specific activity with each substrate and a significant decrease in the enzyme's heat stability, it is also linked to abnormal arsenic excretion patterns
E208K
no alteration in specific activity compared to the wild type enzyme
N142D
no effect on the specific activity of the enzyme with any substrate
K8A
the mutation significantly reduces the enzymatic activity
D72A
reduction in catalytic efficincy. D72 is a glutathione-site residue
K8A
severe reduction in catalytic efficincy. K8 is a glutathione-site residue
S73A
reduction in catalytic efficincy. S73 is a glutathione-site residue
C26S
-
turnover number is 57% of the wild-type value, KM-value for dehydroascorbate is 2fold lower than the wild-type value, KM-value for GSH is 1.6old lower than the wild-type value
C9S
-
turnover number is 86% of the wild-type value, KM-value for dehydroascorbate is 2.8fold lower than the wild-type value, KM-value for GSH is 2fold lower than the wild-type value
C9S/C26S
-
turnover number is 43% of the wild-type value, KM-value for dehydroascorbate is 1.1fold higher than the wild-type value, KM-value for GSH is identical to the wild-type value
C25S
-
has equivalent specificity constants for dehydroascorbate and GSH, but may have a different catalytic mechanism
additional information
additional information
-
mutant dhar or T-DNA tag line SALK_026089, the expression level of dhar is only one-quarter that in the wild-type, the mutant completely lacks DHAR activity and is highly ozone sensitive
additional information
-
overexpression in transgenic Nicotiana tabacum plants, the Arabidopsis enzyme confers resistance to aluminium induced oxidative damage and growth inhibition. Transgenic Nicotiana tabacum plants overexpressing the Arabidosis thaliana DHAR show lower hydrogen peroxide content, less lipid peroxidation and lower level of oxidative DNA damage than wild-type SR-1 plants, overview
additional information
construcution of different mutants with containing cysteine-to-serine mutations and/or C-terminal residues deleted, kinetic analysis
additional information
construcution of different mutants with containing cysteine-to-serine mutations and/or C-terminal residues deleted, kinetic analysis
additional information
-
construcution of different mutants with containing cysteine-to-serine mutations and/or C-terminal residues deleted, kinetic analysis
additional information
-
construction of overexpressing potato plants overexpressing both the cytosolic and the plastidic isozyme. the trangenic plants overexpressing the cytosolic isozyme show highly increased DHAR activities and ascorbate contents in leaves and tubers, while the plants overexpressing the plastidic isozyme show highly increased DHAR activities and ascorbate contents only in leaves, not in tubers
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
highest stability at, unstable under acidic and highly alkaline conditions
394028
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
-
the half-life of deactivation of the enzyme at 100°C is 8.5 min, and its thermal inactivation rate constant Kd is 0.0652/min
30 - 60
the enzyme retains more than 80% activity between 30 and 60°C for 20 min
35 - 55
-
when preincubated at 35°C for 15 min, the enzyme activity is almost unaffected but begins to decrease when the temperature sets above 40°C. Isoform DHAR1 and DHAR2 still retain 61 and 73% of their initial activity when pre-incubated at 55°C for 15 min
40
-
the activity of DHAR significantly increases from 1 d after incubation at 40°C and thereafter declines gradually to the control level
50
55
the recombinant PbDHAR is a thermostable enzyme, retaining 77% of its initial activity at 55°C
70
80
80
-
heat treatment at 80°C for 10 min inhibits the enzyme leading to 1% residual activity
80
-
10 min, 81% loss of activity of enzyme form DHAR-a, 97% loss of activity of enzyme form DHAR-b
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
resistant to digestion by trypsin and chymotrypsin even at a high enzyme/substrate (w/w) ratio of 1:10
slight decrease in activity with increasing concentration of imidazole to 0.8 M
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
functional TcGrx is purified by Ni2+-nitrilotriacetic acid sepharose
-
Ni Sepharose column chromatography
Ni-NTA column chromatography
Ni-NTA column chromatography and Superdex 200 gel filtration
recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells, Arabidopsis thaliana, and Nicotiana benthamiana
-
expressed in Escherichia coli C41(DE3) cells
expression in Escherichia coli
gene encoding DHAr, DNA and amino acid sequence determination and analysis, phylogenetic tree
overexpressed in Escherichia coli BL21 (DE3) strain using the pET-28a(+) expression vector
-
overexpression of cytosolic and plastidic isozymes in transgenic potato plants
-
the coding region is expressed as a His-tagged fusion protein in Escherichia coli
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
DHAR transcript and enzyme activity are significantly up-regulated in the leaves of acerola under cold and salt stress conditions
the enzyme expression is down-regulated under salinity stress (250 mM NaCl)
the enzyme expression is up-regulated in response to high temperature (45°C)
under dark conditions, there is a sharp and significant decline in the total and reduced ascorbate contents, accompanied by a decrease in the level of transcripts and enzyme activities of the two genes in acerola leaves
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
medicine
significant association with the age-at-onset of Alzheimer's disease and Parkinson's disease
agriculture
-
development of overexpressing rice plants under the regulation of a maize ubiquitin promoter. Enzyme overexpression in seven independent homologous transgenic plants, as compared to wild-type plants, increases photosynthetic capacity and antioxidant enzyme activities under paddy field conditions, which leads to an improved ascorbate pool and redox homeostasis. Overexpression significantly improves grain yield and biomass due to the increase of culm and root weights and enhance panicles and spikelet numbers
agriculture
-
study on single chromosome substitution lines of cv. Chinese Spring carrying separate chromosomes from the donor Synthetic 6x, an artificial hexaploid combining the genomes of the two wild species, Triticum dicoccoides, AABB, and Aegilops tauschii, DD. The lines carrying a synthetic hexaploid homologous pair of chromosomes 1B, 1D, 2D, 3D or 4D all express a low constitutive level of dehydroascorbate reductase and the lines carrying chromosomes 3B, 1D, 2D and 3D a low constitutive level of catalyse. All are able to increase this level by fourfold for dehydroascorbate reductase and by 1.5-fold for catalyase in response to stress caused by water deficit. When challenged by drought stress, these lines tend to be the most effective in retaining the water status of the leaves and preventing the grain yield components from being compromised
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Redman, D.G.
Dehydroascorbic acid reductase activity in germinating wheat grains
Chem. Ind.
10
414-415
1974
Triticum aestivum
-
brenda
Grimble, R.F.; Hughes, R.E.
The glutathione: dehydroascorbate oxidoreductase activity of guinea-pigs from two different age groups
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1968
Cavia porcellus
brenda
Kahnt, W.D.; Mundy, V.; Grosch, W.
Determination of GSH-DH activity (E.C.1.8.5.1) presence of the enzyme in different wheat varieties
Z. Lebensm. Unters. Forsch.
158
77-82
1975
Triticum aestivum
brenda
Walther, C.; Grosch, W.
Substrate specificity of the glutathione dehydrogenase (dehydroascorbate reductase) from wheat flour
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5
299-305
1987
Triticum aestivum
-
brenda
Shigeoka, S.; Yasumoto, R.; Onishi, T.; Nakano, Y.; Kitaoka, S.
Properties of monodehydroascorbate reductase and dehydroascorbate reductase and their participation in the regeneration of ascorbate in Euglena gracilis
J. Gen. Microbiol.
133
227-232
1987
Euglena gracilis
-
brenda
Foyer, C.H.; Halliwell, B.
Purification and properties of dehydroascorbate reductase from spinach leaves
Phytochemistry
16
1347-1350
1977
Spinacia oleracea
-
brenda
Bigley, R.; Riddle, M.; Layman, D.; Stankova, L.
Human cell dehydroascorbate reductase. Kinetic and functional properties
Biochim. Biophys. Acta
659
15-22
1981
Homo sapiens
brenda
Stahl, R.L.; Liebes, L.F.; Silber, R.
Glutathione dehydrogenase (ascorbate)
Methods Enzymol.
122
10-12
1986
Spinacia oleracea
brenda
Mizohata, E.; Kumei, M.; Matsumura, H.; Shimaoka, T.; Miyake, C.; Inoue, T.; Yokota, A.; Kai, Y.
Crystallization and preliminary X-ray diffraction analysis of glutathione-dependent dehydroascorbate reductase from spinach chloroplasts
Acta Crystallogr. Sect. D
57
1726-1728
2001
Spinacia oleracea
brenda
Boeck, D.; Grosch, W.
Glutathatione-dehydrogenase of wheat flour. Purification and properties
Z. Lebensm. Unters. Forsch.
162
243-251
1976
Triticum aestivum
brenda
Basu, S.; Som, S.; Deb, S.; Mukherjee, D.; Chatterjee, I.B.
Dehydroascorbic acid reduction in human erythrocytes
Biochem. Biophys. Res. Commun.
90
1335-1340
1979
Homo sapiens
brenda
Stahl, R.L.; Liebes, L.F.; Farber, C.M.; Silber, R.
A spectrophotometric assay for dehydroascorbate reductase
Anal. Biochem.
131
341-344
1983
Spinacia oleracea
brenda
Dipierro, S.; Borraccino, G.
Dehydroascorbate reductase from potato tubers
Phytochemistry
30
427-429
1991
Solanum tuberosum
-
brenda
Fornai, F.; Piaggi, S.; Gesi, M.; Saviozzi, M.; Lenzi, P.; Paparelli, A.; Casini, A.F.
Subcellular localization of a glutathione-dependent dehydroascorbate reductase within specific rat brain regions
Neuroscience
104
15-31
2001
Rattus norvegicus
brenda
Fornai, F.; Saviozzi, M.; Piaggi, S.; Gesi, M.; Corsini, G.U.; Malvaldi, G.; Casini, A.F.
Localization of a glutathione-dependent dehydroascorbate reductase within the central nervous system of the rat
Neuroscience
94
937-948
1999
Rattus norvegicus
brenda
Kim, Y.R.; Kang, S.O.
Purification and characterization of dehydroascorbate reductase from Pleurotus ostreatus
J. Microbiol.
36
164-170
1998
Pleurotus ostreatus
-
brenda
Xu, D.P.; Washburn, M.P.; Sun, G.P.; Wells, W.W.
Purification and characterization of a glutathione dependent dehydroascorbate reductase from human erythrocytes
Biochem. Biophys. Res. Commun.
221
117-121
1996
Homo sapiens
brenda
Shimaoka, T.; Yokota, A.; Miyake, C.
Purification and characterization of chloroplast dehydroascorbate reductase from spinach leaves
Plant Cell Physiol.
41
1110-1118
2000
Spinacia oleracea
brenda
Kato, Y.; Urano, J.i.; Maki, Y.; Ushimaru, T.
Purification and characterization of dehydroascorbate reductase from rice
Plant Cell Physiol.
38
173-178
1997
Oryza sativa
-
brenda
Washburn, M.P.; Wells, W.W.
The catalytic mechanism of the glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin)
Biochemistry
38
268-274
1999
Sus scrofa
brenda
Paolicchi, A.; Pezzini, A.; Saviozzi, M.; Piaggi, S.; Andreuccetti, M.; Chieli, E.; Malvaldi, G.; Casini, A.F.
Localization of a GSH-dependent dehydroascorbate reductase in rat tissues and subcellular fractions
Arch. Biochem. Biophys.
333
489-495
1996
Rattus norvegicus
brenda
Maellaro, E.; Del Bello, B.; Sugherini, L.; Comporti, M.; Casini, A.F.
Purification and characterization of glutathione-dependent dehydroascorbate reductase from rat liver
Methods Enzymol.
279
30-35
1997
Rattus norvegicus
brenda
Shimaoka, T.; Miyake, C.; Yokota, A.
Mechanism of the reaction catalyzed by dehydroascorbate reductase from spinach chloroplasts
Eur. J. Biochem.
270
921-928
2003
Spinacia oleracea
brenda
Ananieva, E.A.; Christov, K.N.; Popova, L.P.
Exogenous treatment with salicylic acid leads to increased antioxidant capacity in leaves of barley plants exposed to paraquat
J. Plant Physiol.
161
319-328
2004
Hordeum vulgare
brenda
Zhou, W.; Kolb, F.L.; Riechers, D.E.
Identification of proteins induced or upregulated by Fusarium head blight infection in the spikes of hexaploid wheat (Triticum aestivum)
Genome
48
770-780
2005
Triticum aestivum (Q84UH6), Triticum aestivum
brenda
Amako, K.; Ushimaru, T.; Ishikawa, A.; Ogishi, Y.; Kishimoto, R.; Goda, K.
Heterologous expression of dehydroascorbate reductase from rice and its application to determination of dehydroascorbate concentrations
J. Nutr. Sci. Vitaminol.
52
89-95
2006
Oryza sativa
brenda
Chun, J.A.; Seo, J.Y.; Han, M.O.; Lee, J.W.; Yi, Y.B.; Park, G.Y.; Lee, S.W.; Bae, S.C.; Cho, K.J.; Chung, C.H.
Comparative expression and characterization of dehydroascorbate reductase cDNA from transformed sesame hairy roots using real-time RT-PCR
J. Plant Biol.
49
507-512
2006
Sesamum indicum
-
brenda
Ushimaru, T.; Nakagawa, T.; Fujioka, Y.; Daicho, K.; Naito, M.; Yamauchi, Y.; Nonaka, H.; Amako, K.; Yamawaki, K.; Murata, N.
Transgenic Arabidopsis plants expressing the rice dehydroascorbate reductase gene are resistant to salt stress
J. Plant Physiol.
163
1179-1184
2006
Oryza sativa
brenda
Schmuck, E.M.; Board, P.G.; Whitbread, A.K.; Tetlow, N.; Cavanaugh, J.A.; Blackburn, A.C.; Masoumi, A.
Characterization of the monomethylarsonate reductase and dehydroascorbate reductase activities of Omega class glutathione transferase variants: implications for arsenic metabolism and the age-at-onset of Alzheimers and Parkinsons diseases
Pharmacogenet. Genomics
15
493-501
2005
Homo sapiens (P78417), Homo sapiens
brenda
Yoshida, S.; Tamaoki, M.; Shikano, T.; Nakajima, N.; Ogawa, D.; Ioki, M.; Aono, M.; Kubo, A.; Kamada, H.; Inoue, Y.; Saji, H.
Cytosolic dehydroascorbate reductase is important for ozone tolerance in Arabidopsis thaliana
Plant Cell Physiol.
47
304-308
2006
Arabidopsis thaliana
brenda
Chen, Z.; Gallie, D.R.
Dehydroascorbate reductase affects leaf growth, development, and function
Plant Physiol.
142
775-787
2006
Nicotiana tabacum
brenda
Song, X.S.; Hu, W.H.; Mao, W.H.; Ogweno, J.O.; Zhou, Y.H.; Yu, J.Q.
Response of ascorbate peroxidase isoenzymes and ascorbate regeneration system to abiotic stresses in Cucumis sativus L
Plant Physiol. Biochem.
43
1082-1088
2005
Cucumis sativus
brenda
Garnczarska, M.
Response of the ascorbate-glutathione cycle to re-aeration following hypoxia in lupine roots
Plant Physiol. Biochem.
43
583-590
2005
Lupinus luteus
brenda
Sofo, A.; Tuzio, A.C.; Dichio, B.; Xiloyannis, C.
Influence of water deficit and rewatering on the components of the ascorbate-glutathione cycle in four interspecific Prunus hybrids
Plant Sci.
169
403-412
2005
Prunus sp.
brenda
Ali, M.B.; Yu, K.; Hahn, E.; Paek, K.
Differential responses of anti-oxidants enzymes, lipoxygenase activity, ascorbate content and the production of saponins in tissue cultured root of mountain Panax ginseng C.A. Mayer and Panax quinquefolium L. in bioreactor subjected to methyl jasmonate stress.
Plant Sci.
169
83-92
2005
Panax ginseng, Panax quinquefolius
brenda
Zou, L.; Li, H.; Ouyang, B.; Zhang, J.; Ye, Z.
Cloning and mapping of genes involved in tomato ascorbic acid biosynthesis and metabolism
Plant Sci.
170
120-127
2006
Solanum lycopersicum (Q4VDN7), Solanum lycopersicum (Q4VDN8)
brenda
Igamberdiev, A.U.; Stoimenova, M.; Seregelyes, C.; Hill, R.D.
Class-1 hemoglobin and antioxidant metabolism in alfalfa roots
Planta
223
1041-1046
2006
Medicago sativa
brenda
Shigenaga, T.; Yamauchi, N.; Funamoto, Y.; Shigyo, M.
Effects of heat treatment on an ascorbate-glutathione cycle in stored broccoli (Brassica oleracea L.) florets
Postharvest Biol. Technol.
38
152-159
2005
Brassica oleracea
-
brenda
Lai, Q.; Bao, Z.; Zhu, Z.; Mao, B.; Qian, Q.
Paraquat resistance in leaf discs of PSAG12-IPT modified gerbera is related to the activities of superoxide dismutase, catalase, and dehydroascorbate reductase
Agric. Sci. China
6
446-451
2007
Gerbera jamesonii
-
brenda
Chun, J.A.; Lee, W.H.; Han, M.O.; Lee, J.W.; Yi, Y.B.; Goo, Y.M.; Lee, S.W.; Bae, S.C.; Cho, K.J.; Chung, C.H.
Molecular and biochemical characterizations of dehydroascorbate reductase from sesame (Sesamum indicum L.) hairy root cultures
J. Agric. Food Chem.
55
6067-6073
2007
Sesamum indicum (A0S5Z5), Sesamum indicum
brenda
Huang, G.J.; Lai, H.C.; Chang, Y.S.; Sheu, M.J.; Lu, T.L.; Huang, S.S.; Lin, Y.H.
Antimicrobial, dehydroascorbate reductase, and monodehydroascorbate reductase activities of defensin from sweet potato [Ipomoea batatas (L.) Lam. Tainong 57] storage roots
J. Agric. Food Chem.
56
2989-2995
2008
Ipomoea batatas (Q6Q8S2), Ipomoea batatas
brenda
Jiang, Y.C.; Huang, C.Y.; Wen, L.; Lin, C.T.
Dehydroascorbate reductase cDNA from sweet potato (Ipomoea batatas [L.] Lam): expression, enzyme properties, and kinetic studies
J. Agric. Food Chem.
56
3623-3627
2008
Ipomoea batatas (D2CGD4), Ipomoea batatas
brenda
Ken, C.F.; Lin, C.Y.; Jiang, Y.C.; Wen, L.; Lin, C.T.
Cloning, expression, and characterization of an enzyme possessing both glutaredoxin and dehydroascorbate reductase activity from Taiwanofungus camphorata
J. Agric. Food Chem.
57
10357-10362
2009
Taiwanofungus camphoratus
brenda
Kiraly, L.; Hafez, Y.M.; Fodor, J.; Kiraly, Z.
Suppression of tobacco mosaic virus-induced hypersensitive-type necrotization in tobacco at high temperature is associated with downregulation of NADPH oxidase and superoxide and stimulation of dehydroascorbate reductase
J. Gen. Virol.
89
799-808
2008
Nicotiana tabacum (Q84UH4), Nicotiana tabacum
brenda
Yang, H.L.; Zhao, Y.R.; Wang, C.L.; Yang, Z.L.; Zeng, Q.Y.; Lu, H.
Molecular characterization of a dehydroascorbate reductase from Pinus bungeana
J. Integr. Plant Biol.
51
993-1001
2009
Pinus bungeana (B2ZHM6), Pinus bungeana
brenda
Vadassery, J.; Tripathi, S.; Prasad, R.; Varma, A.; Oelmueller, R.
Monodehydroascorbate reductase 2 and dehydroascorbate reductase 5 are crucial for a mutualistic interaction between Piriformospora indica and Arabidopsis
J. Plant Physiol.
166
1263-1274
2009
Arabidopsis thaliana
brenda
Shin, S.Y.; Kim, I.S.; Kim, Y.H.; Park, H.M.; Lee, J.Y.; Kang, H.G.; Yoon, H.S.
Scavenging reactive oxygen species by rice dehydroascorbate reductase alleviates oxidative stresses in Escherichia coli
Mol. Cells
26
616-620
2008
Oryza sativa
brenda
Eltelib, H.A.; Badejo, A.A.; Fujikawa, Y.; Esaka, M.
Gene expression of monodehydroascorbate reductase and dehydroascorbate reductase during fruit ripening and in response to environmental stresses in acerola (Malpighia glabra)
J. Plant Physiol.
168
619-627
2011
Malpighia glabra (E2RWY6), Malpighia glabra
brenda
Qin, A.; Shi, Q.; Yu, X.
Ascorbic acid contents in transgenic potato plants overexpressing two dehydroascorbate reductase genes
Mol. Biol. Rep.
38
1557-1566
2010
Solanum tuberosum
brenda
Yin, L.; Wang, S.; Eltayeb, A.E.; Uddin, M.I.; Yamamoto, Y.; Tsuji, W.; Takeuchi, Y.; Tanaka, K.
Overexpression of dehydroascorbate reductase, but not monodehydroascorbate reductase, confers tolerance to aluminum stress in transgenic tobacco
Planta
231
609-621
2010
Arabidopsis thaliana
brenda
Osipova, S.; Permyakov, A.; Permyakova, M.; Pshenichnikova, T.; Börner, A.
Leaf dehydroascorbate reductase and catalase activity is associated with soil drought tolerance in bread wheat
Acta Physiol. Plant.
33
2169-2177
2011
Triticum aestivum
-
brenda
Zhou, H.; Brock, J.; Liu, D.; Board, P.G.; Oakley, A.J.
Structural insights into the dehydroascorbate reductase activity of human omega-class glutathione transferases
J. Mol. Biol.
420
190-203
2012
Homo sapiens (P78417), Homo sapiens (Q9H4Y5), Homo sapiens
brenda
Tang, Z.X.; Yang, H.L.
Functional divergence and catalytic properties of dehydroascorbate reductase family proteins from Populus tomentosa
Mol. Biol. Rep.
40
5105-5114
2013
Populus tomentosa (J9WN12), Populus tomentosa (J9WNR5), Populus tomentosa (J9WQY6), Populus tomentosa
brenda
Kim, Y.S.; Kim, I.S.; Bae, M.J.; Choe, Y.H.; Kim, Y.H.; Park, H.M.; Kang, H.G.; Yoon, H.S.
Homologous expression of cytosolic dehydroascorbate reductase increases grain yield and biomass under paddy field conditions in transgenic rice (Oryza sativa L. japonica)
Planta
237
1613-1625
2013
Oryza sativa
brenda
Do, H.; Kim, I.S.; Kim, Y.S.; Shin, S.Y.; Kim, J.J.; Mok, J.E.; Park, S.I.; Wi, A.R.; Park, H.; Kim, H.W.; Yoon, H.S.; Lee, J.H.
Crystallization and preliminary X-ray crystallographic studies of dehydroascorbate reductase (DHAR) from Oryza sativa L. japonica
Acta Crystallogr. Sect. F
70
781-785
2014
Oryza sativa Japonica Group (Q65XA0)
brenda
Krishna Das, B.; Kumar, A.; Maindola, P.; Mahanty, S.; Jain, S.K.; Reddy, M.K.; Arockiasamy, A.
Non-native ligands define the active site of Pennisetum glaucum (L.) R. Br dehydroascorbate reductase
Biochem. Biophys. Res. Commun.
473
1152-1157
2016
Cenchrus americanus
brenda
Lallement, P.A.; Roret, T.; Tsan, P.; Gualberto, J.M.; Girardet, J.M.; Didierjean, C.; Rouhier, N.; Hecker, A.
Insights into ascorbate regeneration in plants investigating the redox and structural properties of dehydroascorbate reductases from Populus trichocarpa
Biochem. J.
473
717-731
2016
Populus trichocarpa
brenda
Noshi, M.; Hatanaka, R.; Tanabe, N.; Terai, Y.; Maruta, T.; Shigeoka, S.
Redox regulation of ascorbate and glutathione by a chloroplastic dehydroascorbate reductase is required for high-light stress tolerance in Arabidopsis
Biosci. Biotechnol. Biochem.
80
870-877
2016
Arabidopsis thaliana
brenda
Noshi, M.; Yamada, H.; Hatanaka, R.; Tanabe, N.; Tamoi, M.; Shigeoka, S.
Arabidopsis dehydroascorbate reductase 1 and 2 modulate redox states of ascorbate-glutathione cycle in the cytosol in response to photooxidative stress
Biosci. Biotechnol. Biochem.
81
523-533
2017
Arabidopsis thaliana
brenda
Huang, G.J.; Deng, J.S.; Chen, H.J.; Huang, S.S.; Shih, C.C.; Lin, Y.H.
Dehydroascorbate reductase and monodehydroascorbate reductase activities of two metallothionein-like proteins from sweet potato (Ipomoea batatas [L.] Lam. Tainong 57) storage roots
Bot. Stud.
54
7-7
2013
Ipomoea batatas
brenda
Chang, L.; Sun, H.; Yang, H.; Wang, X.; Su, Z.; Chen, F.; Wei, W.
Over-expression of dehydroascorbate reductase enhances oxidative stress tolerance in tobacco
Electron. J. Biotechnol.
25
1-8
2017
Jatropha curcas (R9QAK3)
-
brenda
Kim, Y.; Kim, I.; Shin, S.; Park, T.; Park, H.; Kim, Y.; Lee, G.; Kang, H.; Lee, S.; Yoon, H.
Overexpression of dehydroascorbate reductase confers enhanced tolerance to salt stress in rice plants (Oryza sativa L. japonica)
J. Agron. Crop Sci.
200
444-456
2014
Oryza sativa Japonica Group (Q65XA0)
-
brenda
Han, E.; Goo, Y.; Kim, Y.; Lee, S.
Proteomic analysis of dehydroascorbate reductase transgenic potato plants
J. Plant Biotechnol.
43
223-230
2016
Sesamum indicum
-
brenda
Shin, S.Y.; Kim, M.H.; Kim, Y.H.; Park, H.M.; Yoon, H.S.
Co-expression of monodehydroascorbate reductase and dehydroascorbate reductase from Brassica rapa effectively confers tolerance to freezing-induced oxidative stress
Mol. Cells
36
304-315
2013
Brassica rapa
brenda
Xue, Y.; Miyakawa, T.; Nakamura, A.; Hatano, K.; Sawano, Y.; Tanokura, M.
Yam tuber storage protein reduces plant oxidants using the coupled reactions as carbonic anhydrase and dehydroascorbate reductase
Mol. Plant
8
1115-1118
2015
Dioscorea japonica
brenda
Lin, S.T.; Chiou, C.W.; Chu, Y.L.; Hsiao, Y.; Tseng, Y.F.; Chen, Y.C.; Chen, H.J.; Chang, H.Y.; Lee, T.M.
Enhanced ascorbate regeneration via dehydroascorbate reductase confers tolerance to photo-oxidative stress in Chlamydomonas reinhardtii
Plant Cell Physiol.
57
2104-2121
2016
Chlamydomonas reinhardtii (A8I0K9), Chlamydomonas reinhardtii
brenda
Pandey, P.; Achary, V.M.; Kalasamudramu, V.; Mahanty, S.; Reddy, G.M.; Reddy, M.K.
Molecular and biochemical characterization of dehydroascorbate reductase from a stress adapted C4 plant, pearl millet [Pennisetum glaucum (L.) R. Br]
Plant Cell Rep.
33
435-445
2014
Cenchrus americanus (U5XYA0), Cenchrus americanus
brenda
Liu, F.; Guo, X.; Yao, Y.; Tang, W.; Zhang, W.; Cao, S.; Han, Y.; Liu, Y.
Cloning and function characterization of two dehydroascorbate reductases from kiwifruit (Actinidia chinensis L.)
Plant Mol. Biol. Rep.
34
815-826
2016
Actinidia chinensis
-
brenda
Zhang, Y.J.; Wang, W.; Yang, H.L.; Li, Y.; Kang, X.Y.; Wang, X.R.; Yang, Z.L.
Molecular Properties and functional divergence of the dehydroascorbate reductase gene family in lower and higher plants
PLoS ONE
10
e0145038
2015
Picea abies, Pinus taeda, Populus trichocarpa, Zea mays, Selaginella moellendorffii, Brachypodium distachyon, Arabidopsis thaliana (Q9FWR4)
brenda
Do, H.; Kim, I.S.; Jeon, B.W.; Lee, C.W.; Park, A.K.; Wi, A.R.; Shin, S.C.; Park, H.; Kim, Y.S.; Yoon, H.S.; Kim, H.W.; Lee, J.H.
Structural understanding of the recycling of oxidized ascorbate by dehydroascorbate reductase (OsDHAR) from Oryza sativa L. japonica
Sci. Rep.
6
19498
2016
Oryza sativa Japonica Group (Q65XA0)
brenda
Bodra, N.; Young, D.; Astolfi Rosado, L.; Pallo, A.; Wahni, K.; De Proft, F.; Huang, J.; Van Breusegem, F.; Messens, J.
Arabidopsis thaliana dehydroascorbate reductase 2 Conformational flexibility during catalysis
Sci. Rep.
7
42494
2017
Arabidopsis thaliana
brenda
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EXTERNAL LINKS (specific for EC-Number 1.8.5.1)
Transporter Classification Database (TCDB): 1.A.12.2.1
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