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1-chloro-2,4-dinitrobenzene + NADH + H+
? + NAD+
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
enzyme also shows diaphorase activity, i.e. ferricyanide reductase
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
-
-
-
?
2 ferricyanide + NADPH + H+
2 ferrocyanide + NADP+
-
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2,4,6-trinitrotoluene + NADH + H+
? + NAD+
-
-
-
?
CO2 + H2O
HCO3- + H+
bifunctional enzyme showing monodehydroascorbate reductase and carbonic anhydrase, EC 4.2.1.1, activities
-
-
?
ferricyanide + NADPH + H+
ferrocyanide + NADP+
ferricyanide + reduced 2,6-dichlorophenolindophenol
ferrocyanide + 2,6-dichlorophenolindophenol
-
enzyme also shows diaphorase activity, i.e. ferricyanide reductase
-
-
?
monodehydroascorbate + NADH
ascorbate + NAD+
-
-
-
-
?
monodehydroascorbate + NADH + H+
ascorbate + NAD+
monodehydroascorbate + NADPH + H+
ascorbate + NADP+
-
-
-
?
NAD(P)H + monodehydroascorbate
NAD(P)+ + ascorbate
-
reduction of the radical monodehydroascorbate, via FAD as intermediary electron acceptor, FAD reduction by NADH producing a charge-transfer complex
-
-
?
NADH + 1,4-benzoquinone
NAD+ + ?
-
-
-
-
?
NADH + 2,6-dichlorophenol indophenol
NAD+ + ?
NADH + H+ + 2 monodehydroascorbate
NAD+ + 2 ascorbate
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
NADH + monodehydroascorbate
NAD+ + ascorbate
NADH + monodehydroisoascorbate
NAD+ + ?
-
-
-
-
?
NADH + monodehydroisoascorbate
NAD+ + isoascorbate
-
-
-
-
?
NADH + p-benzoquinone
NAD+ + ?
-
-
-
-
?
NADPH + H+ + 2 monodehydroascorbate
NADP+ + 2 ascorbate
NADPH + monodehydroascorbate
NADP+ + ascorbate
additional information
?
-
ferricyanide + NADPH + H+
ferrocyanide + NADP+
-
-
-
-
r
ferricyanide + NADPH + H+
ferrocyanide + NADP+
-
-
-
-
r
monodehydroascorbate + NADH + H+
ascorbate + NAD+
-
-
-
?
monodehydroascorbate + NADH + H+
ascorbate + NAD+
-
-
-
?
monodehydroascorbate + NADH + H+
ascorbate + NAD+
-
-
-
?
monodehydroascorbate + NADH + H+
ascorbate + NAD+
-
-
-
?
NADH + 2,6-dichlorophenol indophenol
NAD+ + ?
-
-
-
-
?
NADH + 2,6-dichlorophenol indophenol
NAD+ + ?
-
about 10% of the activity with monodehydroascorbate radical
-
-
?
NADH + 2,6-dichlorophenol indophenol
NAD+ + ?
-
-
-
-
?
NADH + 2,6-dichlorophenol indophenol
NAD+ + ?
-
-
-
-
?
NADH + 2,6-dichlorophenol indophenol
NAD+ + ?
-
-
-
-
?
NADH + H+ + 2 monodehydroascorbate
NAD+ + 2 ascorbate
-
-
-
-
?
NADH + H+ + 2 monodehydroascorbate
NAD+ + 2 ascorbate
-
-
-
-
?
NADH + H+ + 2 monodehydroascorbate
NAD+ + 2 ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the enzyme is involved in maintaining the ascorbic acid system in the reduced state
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the enzyme is involved in maintaining the ascorbic acid system in the reduced state
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
enzyme is involved in the ascorbate-glutathione cycle together with EC 1.8.5.1, and EC 1.6.4.2
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the monodehydroascorbate radical reacts with the fully reduced form of the enzyme with a diffusion-controlled rate
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
key enzyme for maintaining the ascorbic acid system in the reduced state
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the enzyme is involved in maintaining the ascorbic acid system in the reduced state
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
enzyme of the ascorbate-glutathione cycle
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the enzyme is involved in maintaining the ascorbic acid system in the reduced state
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the enzyme is involved in maintaining the ascorbic acid system in the reduced state
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
enzyme may constitute part of cellular mechanisms which protect against and repair oxidant injury to biomolecules
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
r
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the enzyme is involved in maintaining the ascorbic acid system in the reduced state
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the enzyme is involved in maintaining the ascorbic acid system in the reduced state
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
enzyme is responsible for maintaining ascorbate concentrations in nectar
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
key enzyme in maintaining reduced pools of ascorbate
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the enzyme is involved in maintaining the ascorbic acid system in the reduced state
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
Pterocladia sp.
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
Pterocladia sp.
-
the enzyme is involved in maintaining the ascorbic acid system in the reduced state
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
392732, 392734, 392736, 392738, 392740, 392741, 392742, 392743, 392745, 392752, 392753 -
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the enzyme is involved in part of the transplasmamembrane redox system
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the enzyme supports cholesterol side chain cleavage, the enzyme functions to provide cytoplasmic reducing equivalents to intramitochondrial cytochrome P-450SCC
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the only physiologically important system for the regeneration of ascorbate
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
involvement of semidehydroascorbate reductase in the oxidation of NADH by lipid peroxide in mitochondria and microsomes
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the enzyme sustains glyoxysomal NAD+ during beta-oxidation, the glyoxylate cycle and gluconeogenesis in the endosperm during germination
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the enzyme is involved in maintaining the ascorbic acid system in the reduced state
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
enzyme participates in the regeneration of ascorbate for scavenging toxic oxygen species in potato tuber mitochondria
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the enzyme is an effective scavenger of the monodehydroascorbate radical
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
-
-
-
?
NADH + monodehydroascorbate
NAD+ + ascorbate
-
the enzyme is involved in maintaining the ascorbic acid system in the reduced state
-
-
?
NADPH + H+ + 2 monodehydroascorbate
NADP+ + 2 ascorbate
-
-
-
-
?
NADPH + H+ + 2 monodehydroascorbate
NADP+ + 2 ascorbate
-
-
-
-
?
NADPH + monodehydroascorbate
NADP+ + ascorbate
-
-
-
-
?
NADPH + monodehydroascorbate
NADP+ + ascorbate
NADH is the preferred electron donor
-
-
?
NADPH + monodehydroascorbate
NADP+ + ascorbate
-
-
-
-
?
additional information
?
-
-
enzyme is also capable of reducing phenoxyl radicals which are generated by horseradish peroxidase with H2O2
-
-
?
additional information
?
-
metallothionein-lke protein MT1K shows both dehydroascorbate reductase EC 1.8.5.1, and monodehydroascorbate reductase activity
-
-
?
additional information
?
-
metallothionein-lke protein MT1K shows both dehydroascorbate reductase EC 1.8.5.1, and monodehydroascorbate reductase activity
-
-
?
additional information
?
-
-
metallothionein-lke protein MT1K shows both dehydroascorbate reductase EC 1.8.5.1, and monodehydroascorbate reductase activity
-
-
?
additional information
?
-
metallothionein-lke protein MT1K shows both dehydroascorbate reductase EC 1.8.5.1, and monodehydroascorbate reductase activity
-
-
?
additional information
?
-
metallothionein-lke protein MT1K shows both dehydroascorbate reductase EC 1.8.5.1, and monodehydroascorbate reductase activity
-
-
?
additional information
?
-
-
no activity with NADPH
-
-
?
additional information
?
-
reaction scheme, the enzyme is involved in nectary production in floral organs, multiple molecular mechanism responsible for expression in the nectary gland
-
-
?
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Schulze, H.U.; Schott, H.H.; Staudinger, H.
The isolation and characterization of a NADH: semidehydroascorbic acid oxidoreductase from Neurospora crassa
Hoppe-Seyler's Z. Physiol. Chem.
353
1931-1942
1972
Neurospora crassa
brenda
Dalton, D.A.; Post, C.J.; Langeberg, L.
Effects of ambient oxygen and of fixed nitrogen on concentrations of glutathione, ascorbate, and associated enzymes in soybean root nodules
Plant Physiol.
96
812-818
1991
Glycine max
brenda
Tanaka, K.; Masuda, R.; Sugimoto, T.; Kawamura, Y.; Kuboi, T.
An H2O2-decomposing system in cultured tobaco cells
Agric. Biol. Chem.
54
2003-2008
1990
Nicotiana tabacum
-
brenda
Bowditch, M.I.; Donaldson, R.P.
Ascorbate free-radical reduction by glyoxysomal membranes
Plant Physiol.
94
531-537
1990
Ricinus communis
brenda
Tommasi, F.; De Gara, L.; Liso, R.; Arrigoni, O.
The ascorbic acid system in Cuscuta reflexa Roxb.
J. Plant Physiol.
135
766-768
1990
Cuscuta reflexa
-
brenda
Borraccino, G.; Dipierro, S.; Arrigoni, O.
Interaction of ascorbate free radical reductase with sulphhydryl reagents
Phytochemistry
28
715-717
1989
Solanum tuberosum
-
brenda
Navas, P.; Estevez, A.; Villalba, J.M.; Buron, M.I.; Crane, F.L.
Cell surface glycoconjugates control the activity of the NADH-ascorbate free radical reductase of rat liver plasma membrane
Biochem. Biophys. Res. Commun.
154
1029-1033
1988
Rattus norvegicus
brenda
Hossain, M.A.; Asada, K.
Monodehydroascorbate reductase from cucumber is a flavin adenine dinucleotide enzyme
J. Biol. Chem.
260
12920-12926
1985
Cucumis sativus
brenda
Nishino, H.; Ito, A.
Subcellular distribution of OM cytochrome b-mediated NADH-semidehydroascorbate reductase activity in rat liver
J. Biochem.
100
1523-1531
1986
Rattus norvegicus
brenda
Borraccino, G.; Dipierro, S.; Arrigoni, O.
Purification and properties of ascorbate free-radical reductase from potato tubers
Planta
167
521-526
1986
Solanum tuberosum
brenda
Goldenberg, H.
Insulin inhibits NADH-semidehydroascorbate reductase in rat liver plasma membrane
Biochem. Biophys. Res. Commun.
94
721-726
1980
Rattus norvegicus
brenda
Stankova, L.; Bigley, R.; Wyss, S.R.; Aebi, H.
Catalase and dehydroascorbate reductase in human polymorphonuclear leukocytes (PMN): possible functional relationship
Experientia
35
852-853
1979
Homo sapiens
brenda
Gei, D.; Schulze, H.U.
Isolation and chemical composition of the NADH: semidehydroascorbate oxidoreductase rich membranes from rat liver
FEBS Lett.
60
374-379
1975
Rattus norvegicus
brenda
Weber, H.; Weis, W.; Wolf, B.
Monodehydro-L(plus)-ascorbate reducing systems in differently prepared pig liver microsomes
Hoppe-Seyler's Z. Physiol. Chem.
355
595-599
1974
Sus scrofa
brenda
Schulze, H.U.; Gallenkamp, H.; Staudinger, H.
Effect of membrane lipids on the activity of NADH:semidehydroascorbic acid oxidoreductase (EC 1.6.5.4) of rat liver microsomes
Hoppe-Seyler's Z. Physiol. Chem.
354
391-406
1973
Rattus norvegicus
brenda
Green, R.C.; O'Brien, P.J.
The involvement of semidehydroascorbate reductase in the oxidation of NADH by lipid peroxide in mitochondria and microsomes
Biochim. Biophys. Acta
293
334-342
1973
Rattus norvegicus
brenda
Schulze, H.U.; Gallenkamp, H.; Staudinger, H.
Microsomal NADH-dependent electron transport
Hoppe-Seyler's Z. Physiol. Chem.
351
809-817
1970
Rattus norvegicus
brenda
Oehler, G.; Weis, W.; Staudinger, H.
Semidehydro-D(-)-ascorbic acid as a substrate of microsomal NADH: semidehydroascorbate oxidoreductase (EC 1.6.5.4)
Hoppe-Seyler's Z. Physiol. Chem.
353
495-496
1972
Rattus norvegicus
brenda
Arrigoni, O.; Dipierro, S.; Borraccino, G.
Ascorbate free radical reductase, a key enzyme of the ascorbic acid system
FEBS Lett.
125
242-244
1981
Allium cepa, Brassica oleracea, Cucumis sativus, Gigartina sp., Gracilaria sp., Helianthus tuberosus, Hypnea sp., Mus musculus, Pisum sativum, Pterocladia sp., Solanum tuberosum, Vicia faba
-
brenda
Natarajan, R.D.; Harding, B.W.
Cholesterol side chain cleavage in rat adrenal supported by outer mitochondrial membrane NADH-semidehydroascorbate reductase
J. Biol. Chem.
260
3902-3905
1985
Rattus norvegicus
brenda
Baier, M.; Noctor, G.; Foyer, C.H.; Dietz, K.J.
Antisense suppression of 2-cysteine peroxiredoxin in Arabidopsis specifically enhances the activities and expression of enzymes associated with ascorbate metabolism but not glutathione metabolism
Plant Physiol.
124
823-832
2000
Arabidopsis sp.
brenda
De Leonardis, S.; De Lorenzo, G.; Borraccino, G.; Dipierro, S.
A specific ascorbate free radical reductase isoenzyme participates in the regeneration of ascorbate for scavenging toxic oxygen species in potato tuber mitochondria
Plant Physiol.
109
847-851
1995
Solanum tuberosum
brenda
Kobayashi, K.; Tagawa, S.; Sano, S.; Asada, K.
A direct demonstration of the catalytic action of monodehydroascorbate reductase by pulse radiolysis
J. Biol. Chem.
270
27551-27554
1995
Cucumis sativus
brenda
Sano, S.; Miyake, C.; Mikami, B.; Asada, K.
Molecular characterization of monodehydroascorbate radical reductase from cucumber highly expressed in Escherichia coli
J. Biol. Chem.
270
21354-21361
1995
Cucumis sativus
brenda
Murthy, S.S.; Zilinskas, B.A.
Molecular cloning and characterization of a cDNA encoding pea monodehydroascorbate reductase
J. Biol. Chem.
269
31129-31133
1994
Pisum sativum
brenda
Yu, S.W.; Kim, Y.R.; Kang, S.O.
Spectral characterization and chemical modification of FMN-containing ascorbyl free-radical reductase from Pleurotus ostreatus
Biochem. J.
341
755-763
1999
Pleurotus ostreatus
-
brenda
Matsukura, S.; Bando, M.; Obazawa, H.; Oka, M.; Takehana, M.
Ascorbate free radical reductase activity in vertebrate lenses of certain species
Jpn. J. Ophthalmol.
45
233-239
2001
Bos taurus, Cavia porcellus, Oryctolagus cuniculus, Lithobates catesbeianus, Rattus norvegicus, Sus scrofa
brenda
Villalba, J.M.; Canalejo, A.; Buron, M.I.; Cordoba, F.; Navas, P.
Thiol groups are involved in NADH-ascorbate free radical reductase activity of rat liver plasma membrane
Biochem. Biophys. Res. Commun.
192
707-713
1993
Rattus norvegicus
brenda
Sakihama, Y.; Mano, J.; Sano, S.; Asada, K.; Yamasaki, H.
Reduction of phenoxyl radicals mediated by monodehydroascorbate reductase
Biochem. Biophys. Res. Commun.
279
949-954
2000
Cuscuta reflexa
brenda
Sano, S.; Kang, Y.N.; Shigemizu, H.; Morishita, N.; Yoon, H.J.; Saito, K.; Asada, K.; Mikami, B.
Crystallization and preliminary crystallographic analysis of monodehydroascorbate radical reductase from cucumber
Acta Crystallogr. Sect. D
60
1498-1499
2004
Cucumis sativus
brenda
Yoon, H.S.; Lee, H.; Lee, I.A.; Kim, K.Y.; Jo, J.
Molecular cloning of the monodehydroascorbate reductase gene from Brassica campestris and analysis of its mRNA level in response to oxidative stress
Biochim. Biophys. Acta
1658
181-186
2004
Brassica rapa subsp. pekinensis (Q93X74)
brenda
Bando, M.; Inoue, T.; Oka, M.; Nakamura, K.; Kawai, K.; Obazawa, H.; Kobayashi, S.; Takehana, M.
Isolation of ascorbate free radical reductase from rabbit lens soluble fraction
Exp. Eye Res.
79
869-873
2004
Oryctolagus cuniculus
brenda
Obara, K.; Sumi, K.; Fukuda, H.
The use of multiple transcription starts causes the dual targeting of Arabidopsis putative monodehydroascorbate reductase to both mitochondria and chloroplasts
Plant Cell Physiol.
43
697-705
2002
Arabidopsis thaliana (P92947)
brenda
Carter, C.J.; Thornburg, R.W.
Tobacco Nectarin III is a bifunctional enzyme with monodehydroascorbate reductase and carbonic anhydrase activities
Plant Mol. Biol.
54
415-425
2004
Nicotiana langsdorffii x Nicotiana sanderae (Q84UV8)
brenda
Sano, S.; Tao, S.; Endo, Y.; Inaba, T.; Hossain, M.A.; Miyake, C.; Matsuo, M.; Aoki, H.; Asada, K.; Saito, K.
Purification and cDNA cloning of chloroplastic monodehydroascorbate reductase from spinach
Biosci. Biotechnol. Biochem.
69
762-772
2005
Spinacia oleracea
brenda
Lisenbee, C.S.; Lingard, M.J.; Trelease, R.N.
Arabidopsis peroxisomes possess functionally redundant membrane and matrix isoforms of monodehydroascorbate reductase
Plant J.
43
900-914
2005
Arabidopsis thaliana
brenda
Lunde, C.; Baumann, U.; Shirley, N.J.; Drew, D.P.; Fincher, G.B.
Gene structure and expression pattern analysis of three monodehydroascorbate reductase (Mdhar) genes in Physcomitrella patens: implications for the evolution of the MDHAR family in plants
Plant Mol. Biol.
60
259-275
2006
Physcomitrium patens
brenda
Leterrier, M.; Corpas, F.J.; Barroso, J.B.; Sandalio, L.M.; del Rio, L.A.
Peroxisomal monodehydroascorbate reductase. Genomic clone characterization and functional analysis under environmental stress conditions
Plant Physiol.
138
2111-2123
2005
Pisum sativum (Q66PF9), Pisum sativum
brenda
Igamberdiev, A.U.; Bykova, N.V.; Hill, R.D.
Nitric oxide scavenging by barley hemoglobin is facilitated by a monodehydroascorbate reductase-mediated ascorbate reduction of methemoglobin
Planta
223
1033-1040
2006
Hordeum vulgare
brenda
Eltayeb, A.E.; Kawano, N.; Badawi, G.H.; Kaminaka, H.; Sanekata, T.; Shibahara, T.; Inanaga, S.; Tanaka, K.
Overexpression of monodehydroascorbate reductase in transgenic tobacco confers enhanced tolerance to ozone, salt and polyethylene glycol stresses
Planta
225
1255-1264
2007
Arabidopsis thaliana, Arabidopsis thaliana (Q9SR59)
brenda
Huang, G.; Chen, H.; Chang, Y.; Lu, T.; Lin, Y.
Sweet potato storage root thioredoxin h2 with both dehydroascorbate reductase and monodehydroascorbate reductase activities
Bot. Stud.
49
1-7
2008
Ipomoea batatas (Q6VBI6)
-
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
Stevens, R.; Page, D.; Gouble, B.; Garchery, C.; Zamir, D.; Causse, M.
Tomato fruit ascorbic acid content is linked with monodehydroascorbate reductase activity and tolerance to chilling stress
Plant Cell Environ.
31
1086-1096
2008
Solanum pennellii
brenda
Drew, D.P.; Lunde, C.; Lahnstein, J.; Fincher, G.B.
Heterologous expression of cDNAs encoding monodehydroascorbate reductases from the moss, Physcomitrella patens and characterization of the expressed enzymes
Planta
225
945-954
2007
Physcomitrium patens (Q2I826), Physcomitrium patens (Q2I827), Physcomitrium patens (Q2I828), Physcomitrium patens
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 (Q9LK94)
brenda
Kavitha, K.; George, S.; Venkataraman, G.; Parida, A.
A salt-inducible chloroplastic monodehydroascorbate reductase from halophyte Avicennia marina confers salt stress tolerance on transgenic plants
Biochimie
92
1321-1329
2010
Avicennia marina (C3VPH7), Avicennia marina
brenda
Li, F.; Wu, Q.Y.; Sun, Y.L.; Ma, N.N.; Wang, X.Y.; Meng, Q.W.
Evidence that the amino acid residue Cys117 of chloroplastic monodehydroascorbate reductase is involved in its activity and structural stability
Int. J. Biol. Macromol.
46
350-355
2010
Solanum lycopersicum
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 (E2RWY5), Malpighia glabra
brenda
Li, F.; Wu, Q.Y.; Sun, Y.L.; Wang, L.Y.; Yang, X.H.; Meng, Q.W.
Overexpression of chloroplastic monodehydroascorbate reductase enhanced tolerance to temperature and methyl viologen-mediated oxidative stresses
Physiol. Plant.
139
421-434
2010
Solanum lycopersicum (B3EYD3), Solanum lycopersicum
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
Sultana, S.; Khew, C.Y.; Morshed, M.M.; Namasivayam, P.; Napis, S.; Ho, C.L.
Overexpression of monodehydroascorbate reductase from a mangrove plant (AeMDHAR) confers salt tolerance on rice
J. Plant Physiol.
169
311-318
2012
Acanthus ebracteatus
brenda
Li, F.; Wu, Q.; Duan, M.; Dong, X.; Li, B.; Meng, Q.
Transgenic tomato plants overexpressing chloroplastic monodehydroascorbate reductase are resistant to salt- and PEG-induced osmotic stress
Photosynthetica
50
120-128
2012
Solanum lycopersicum, Solanum lycopersicum Zhongshu 4
-
brenda
Gest, N.; Garchery, C.; Gautier, H.; Jimenez, A.; Stevens, R.
Light-dependent regulation of ascorbate in tomato by a monodehydroascorbate reductase localized in peroxisomes and the cytosol
Plant Biotechnol. J.
11
344-354
2013
Solanum lycopersicum, Solanum lycopersicum West Virginia 106
brenda
Do, H.; Kim, I.; Kim, Y.; Shin, S.; Kim, J.; Mok, J.; Park, S.; Wi, A.; Park, H.; Lee, J.; Yoon, H.; Kim, H.
Purification, characterization and preliminary X-ray crystallographic studies of monodehydroascorbate reductase from Oryza sativa L. japonica
Acta Crystallogr. Sect. F
70
1244-1248
2014
Oryza sativa Japonica Group (Q652L6)
-
brenda
Feng, H.; Wang, X.; Zhang, Q.; Fu, Y.; Feng, C.; Wang, B.; Huang, L.; Kang, Z.
Monodehydroascorbate reductase gene, regulated by the wheat PN-2013 miRNA, contributes to adult wheat plant resistance to stripe rust through ROS metabolism
Biochim. Biophys. Acta
1839
1-12
2014
Triticum aestivum (K4HRS2), Triticum aestivum
brenda
Huang, G.; Deng, J.; Chen, H.; Huang, S.; Shih, C.; Lin, Y.
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
007
2013
Ipomoea batatas (B6VJL9), Ipomoea batatas (Q9ZSC6), Ipomoea batatas, Ipomoea batatas Lam. Tainong 57 (B6VJL9), Ipomoea batatas Lam. Tainong 57 (Q9ZSC6)
brenda
Begara-Morales, J.C.; Sanchez-Calvo, B.; Chaki, M.; Mata-Perez, C.; Valderrama, R.; Padilla, M.N.; Lopez-Jaramillo, J.; Luque, F.; Corpas, F.J.; Barroso, J.B.
Differential molecular response of monodehydroascorbate reductase and glutathione reductase by nitration and S-nitrosylation
J. Exp. Bot.
66
5983-5996
2015
Pisum sativum (Q66PF9), Pisum sativum
brenda
Sudan, J.; Negi, B.; Arora, S.
Oxidative stress induced expression of monodehydroascorbate reductase gene in Eleusine coracana
Physiol. Mol. Biol. Plants
21
551-558
2015
Eleusine coracana (A0A0A7R8U8), Eleusine coracana
brenda
Gest, N.; Garchery, C.; Gautier, H.; Jimenez, A.; Stevens, R.
Light-dependent regulation of ascorbate in tomato by a monodehydroascorbate reductase localized in peroxisomes and the cytosol
Plant Biotechnol. J.
11
344-354
2013
Solanum lycopersicum (Q49B52)
-
brenda
Feng, H.; Liu, W.; Zhang, Q.; Wang, X.; Wang, X.; Duan, X.; Li, F.; Huang, L.; Kang, Z.
TaMDHAR4, a monodehydroascorbate reductase gene participates in the interactions between wheat and Puccinia striiformis f. sp. tritici
Plant Physiol. Biochem.
76
7-16
2014
Triticum aestivum (K4HRS2), Triticum aestivum
brenda
Kim, I.S.; Kim, Y.S.; Kim, Y.H.; Park, A.K.; Kim, H.W.; Lee, J.H.; Yoon, H.S.
Potential Application of the Oryza sativa monodehydroascorbate reductase gene (OsMDHAR) to improve the stress tolerance and fermentative capacity of Saccharomyces cerevisiae
PLoS ONE
11
e0158841
2016
Oryza sativa
brenda
El Airaj, H.; Gest, N.; Truffault, V.; Garchery, C.; Riqueau, G.; Gouble, B.; Page, D.; Stevens, R.
Decreased monodehydroascorbate reductase activity reduces tolerance to cold storage in tomato and affects fruit antioxidant levels
Postharvest Biol. Technol.
86
502-510
2013
Solanum lycopersicum (Q49B52)
-
brenda
Park, A.; Kim, I.; Do, H.; Jeon, B.; Lee, C.; Roh, S.; Shin, S.; Park, H.; Kim, Y.; Kim, Y.; Yoon, H.; Lee, J.; Kim, H.
Structure and catalytic mechanism of monodehydroascorbate reductase, MDHAR, from Oryza sativa L. japonica
Sci. Rep.
6
33903
2016
Oryza sativa Japonica Group (Q652L6)
brenda
Johnston, E.; Rylott, E.; Beynon, E.; Lorenz, A.; Chechik, V.; Bruce, N.
Monodehydroascorbate reductase mediates TNT toxicity in plants
Science
349
1072-1075
2015
Arabidopsis thaliana (P92947)
-
brenda
Vanacker, H.; Guichard, M.; Bohrer, A.S.; Issakidis-Bourguet, E.
Redox regulation of monodehydroascorbate reductase by thioredoxin y in plastids revealed in the context of water stress
Antioxidants (Basel)
7
183
2018
Arabidopsis thaliana (P92947)
brenda
Truffault, V.; Riqueau, G.; Garchery, C.; Gautier, H.; Stevens, R.G.
Is monodehydroascorbate reductase activity in leaf tissue critical for the maintenance of yield in tomato?
J. Plant Physiol.
222
1-8
2018
Solanum lycopersicum (Q43497), Solanum lycopersicum
brenda
Yeh, H.L.; Lin, T.H.; Chen, C.C.; Cheng, T.X.; Chang, H.Y.; Lee, T.M.
Monodehydroascorbate reductase plays a role in the tolerance of Chlamydomonas reinhardtii to photooxidative stress
Plant Cell Physiol.
60
2167-2179
2019
Chlamydomonas reinhardtii (A8JDG4), Chlamydomonas reinhardtii
brenda
Maynard, D.; Kumar, V.; Sproi, J.; Dietz, K.J.
12-Oxophytodienoic acid reductase 3 (OPR3) functions as NADPH-dependent alpha,beta-ketoalkene reductase in detoxification and monodehydroascorbate reductase in redox homeostasis
Plant Cell Physiol.
61
584-595
2020
Arabidopsis thaliana (Q9FUP0)
brenda
Negi, B.; Salvi, P.; Bhatt, D.; Majee, M.; Arora, S.
Molecular cloning, in-silico characterization and functional validation of monodehydroascorbate reductase gene in Eleusine coracana
PLoS ONE
12
e0187793
2017
Eleusine coracana (A0A0U2UAN2), Eleusine coracana
brenda