Results 11 to 20 of about 6,098 (242)
Measurement of Ascorbate Peroxidase Activity in Sorghum
Bio-Protocol, 2022 The ascorbate peroxidase (APX) is a widely distributed antioxidant enzyme. It differs from catalase and other peroxidases in that it scavenges/reduces reactive oxygen species (ROS) such as hydrogen peroxide (H2O2) to water using reduced ascorbate as the ...
Praveen Kumar
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Ascorbate Peroxidase cDNA from Maize [PDF]
Plant Physiology, 1995 APx (EC 1.11.1.11) is a heme-containing, nonglycosylated enzyme that destroys harmful hydrogen peroxide via the ascorbate-glutathione pathway in plants. This pathway provides protection against oxidative stress by a series of coupled redox reactions, particularly in photosynthetic tissues (Foyer and Halliwell, 1976).
van Breusegem, Frank +3 more
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Molecular Plant-Microbe Interactions, 2022 Chloroplasts serve as cold priming hubs modulating the transcriptional response of Arabidopsis thaliana to a second cold stimulus for several days by postcold accumulation of thylakoid ascorbate peroxidases (tAPX).
Thomas Griebel +4 more
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Ascorbate Peroxidase from Soybean Root Nodules [PDF]
Plant Physiology, 1993 AP is involved in the destruction of harmful H202. In soybean (Glycine max [L] Merr.) root nodules, AP initiates a sequence of coupled redox reactions (ascorbate-GSH pathway) that results in peroxide scavenging (Dalton et al., 1986). The ascorbate-GSH pathway occurs in other plant tissues and has been extensively studied in chloroplasts where ...
M, Chatfield, D A, Dalton
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Engineering Ascorbate Peroxidase Activity into Cytochrome c Peroxidase [PDF]
Biochemistry, 2008 Cytochrome c peroxidase (CCP) and ascorbate peroxidase (APX) have very similar structures, and yet neither CCP nor APX exhibits each other's activities with respect to reducing substrates. APX has a unique substrate binding site near the heme propionates where ascorbate H-bonds with a surface Arg and one heme propionate (Sharp et al. (2003) Nat. Struct.
Yergalem T, Meharenna +3 more
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Triazine Probes Target Ascorbate Peroxidases in Plants [PDF]
Plant Physiology, 2019 Though they are rare in nature, anthropogenic 1,3,5-triazines have been used in herbicides as chemically stable scaffolds. Here, we show that small 1,3,5-triazines selectively target ascorbate peroxidases (APXs) in Arabidopsis (Arabidopsis thaliana), tomato (Solanum lycopersicum), rice (Oryza sativa), maize (Zea mays), liverwort (Marchantia polymorpha),
Kyoko Morimoto +13 more
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Arabidopsis APx-R Is a Plastidial Ascorbate-Independent Peroxidase Regulated by Photomorphogenesis
Antioxidants, 2021 Peroxidases are enzymes that catalyze the reduction of hydrogen peroxide, thus minimizing cell injury and modulating signaling pathways as response to this reactive oxygen species.
Fernanda Lazzarotto +5 more
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Catalase and Ascorbate Peroxidase in Euglenozoan Protists [PDF]
Pathogens, 2020 In this work, we studied the biochemical properties and evolutionary histories of catalase (CAT) and ascorbate peroxidase (APX), two central enzymes of reactive oxygen species detoxification, across the highly diverse clade Eugenozoa. This clade encompasses free-living phototrophic and heterotrophic flagellates, as well as obligate parasites of insects,
Ingrid Škodová-Sveráková +5 more
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Engineering the active site of ascorbate peroxidase [PDF]
European Journal of Biochemistry, 2001 The oxidation of a number of thioethers, namely methyl phenyl sulphide (1), ethyl phenyl sulphide (2), isopropyl phenyl sulphide (3), n‐propyl phenyl sulphide (4), p‐chlorophenyl methyl sulphide (5), p‐nitrophenyl methyl sulphide (6) and methyl naphthalene sulphide (7), by recombinant pea cytosolic ascorbate peroxidase (rAPX) and a site‐directed ...
Çelik, A +4 more
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OsAPX1 Positively Contributes to Rice Blast Resistance
Frontiers in Plant Science, 2022 Ascorbate peroxidases (APXs) maintain cellular reactive oxygen species (ROS) homeostasis through their peroxidase activity. Here, we report that OsAPX1 also promotes ROS production such that a delicate cellular ROS homeostasis is achieved temporally ...
Cong Sheng +17 more
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