Molecular cloning and characterization of a rice dehydroascorbate reductase [PDF]
FEBS Letters, 2000 Plant dehydroascorbate reductase (DHAR), which re‐reduces oxidized ascorbate to maintain an appropriate level of ascorbate, is very important, but no gene or cDNA for plant DHAR has been cloned yet. Here, we describe a cDNA for a rice glutathione‐dependent DHAR (designated DHAR1). A recombinant Dhar1p produced in Escherichia coli was functional.
Urano, Jun’ichi +6 more
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Over-expression of dehydroascorbate reductase enhances oxidative stress tolerance in tobacco
Electronic Journal of Biotechnology, 2017 Background: Ascorbic acid (Asc) is one of the most abundant antioxidants and it serves as a major contributor to protect plants against oxidative damage. Plants use two enzymes that participate in the metabolic recycling of Asc.
Lingmo Chang +6 more
doaj +2 more sources
Proteomic analysis of dehydroascorbate reductase transgenic potato plants
Journal of Plant Biotechnology, 2016 Ascorbic acid (AsA) is a strong antioxidant/reducing agent that can be converted to dehydroascorbate (DHA) by oxidation in plants. DHA, a very short-lived chemical, is recycled to AsA by dehydroascorbate reductase (DHAR). Previously, DHAR cDNA was isolated from the hairy roots of the sesame plant, and DHAR-overexpressing transgenic potato plants were ...
Eun-Heui Han +3 more
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Purification and Characterization of Chloroplast Dehydroascorbate Reductase from Spinach Leaves [PDF]
Plant and Cell Physiology, 2000 Green leaves of plants require the high-level activity that can regenerate ascorbate during photosynthesis. One of such enzyme is dehydroascorbate reductase (DHAR), but the molecular and enzymological properties of the enzyme remain to be fully characterized. In this study, we showed that two major DHAR existed in spinach leaves. The two DHARs occupied
T, Shimaoka, A, Yokota, C, Miyake
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Purification and Characterization of Dehydroascorbate Reductase from Rice [PDF]
Plant and Cell Physiology, 1997 Dehydroascorbate reductase (DHAR; EC 1.8.5.1) is an enzyme that is critical for maintenance of an appropriate level of ascorbate in plant cells. This report describes the purification and characterization of a GSH-dependent DHAR from rice (Oryza sativa) bran and is the first, to our knowledge, of such an analysis of DHAR from a monocot.
Y. Kato, J. Urano, Y. Maki, T. Ushimaru
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The pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants [PDF]
Journal of Experimental Botany, 2020 Abstract Under natural conditions, plants are exposed to various abiotic and biotic stresses that trigger rapid changes in the production and removal of reactive oxygen species (ROS) such as hydrogen peroxide (H2O2). The ascorbate-glutathione pathway has been recognized to be a key player in H2O2 metabolism, in which reduced glutathione (
Shengchun Li +3 more
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Reduction of Dehydroascorbate to Ascorbate by the Selenoenzyme Thioredoxin Reductase [PDF]
Journal of Biological Chemistry, 1997 Recycling of ascorbate from its oxidized forms is essential to maintain stores of the vitamin in human cells. Whereas reduction of dehydroascorbate to ascorbate is thought to be largely GSH-dependent, we reconsidered the possibility that the selenium-dependent thioredoxin system might contribute to ascorbate regeneration.
J M, May +3 more
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Dehydroascorbate Reductase Affects Non-photochemical Quenching and Photosynthetic Performance [PDF]
Journal of Biological Chemistry, 2008 Ascorbic acid (Asc) is a major antioxidant involved in photoprotection and photosynthetic function in plants. Dehydroascorbate reductase (DHAR) catalyzes the regeneration of Asc from its oxidized state and serves as an important regulator of Asc recycling.
Zhong, Chen, Daniel R, Gallie
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A Novel and Potentially MultifacetedDehydroascorbate Reductase Increasing theAntioxidant Systems Is Induced by Beauvericinin Tomato. [PDF]
Antioxidants (Basel), 2020 Loi M +4 more
europepmc +3 more sources
Purification and characterization of glutathione-dependent dehydroascorbate reductase from rat liver [PDF]
Biochemical Journal, 1994 GSH-dependent enzymic reduction of dehydroascorbic acid to ascorbic acid has been studied in rat liver cytosol. After gel filtration of cytosol on Sephadex G-100 SF, dehydroascorbate reductase activity was recovered in two distinct peaks, one corresponding to glutaredoxin (an enzyme already known for its dehydroascorbate reductase activity) and another,
Maellaro, E. +5 more
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