Plant Peroxidases: Biomarkers of Environmental Stresses and Signaling in Plants

Jha, Saket; Singh, Rachana; Jha, Gunja; Singh, Parul; Aggarwal, Divya; Shukla, Mohee; Dikshit, Anupam

doi:10.1007/978-981-16-7981-0_7

Cited by 3 publications

(3 citation statements)

References 104 publications

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“…The various defense-related enzymes like PO, PPO, and PAL are induced, which provides strong protection for the host plant against biotic and abiotic stress [ [128] , [129] , [130] ]. Peroxidases are glycoproteins that are synthesized by the endoplasmic reticulum and play a number of physiological functions in plant resistance via wound healing and plant cell elongation [ [131] , [132] , [133] ]. Polyphenol oxidase is a ubiquitous copper-containing enzyme that oxidize phenolics to highly toxic quinones and has a potential role in disease resistance [ 134 , 135 ].…”

Section: Discussionmentioning

confidence: 99%

Microbial consortium mediated acceleration of the defense response in potato against Alternaria solani through prodigious inflation in phenylpropanoid derivatives and redox homeostasis

Kumar,

Chandra,

Behera

et al. 2023

Heliyon

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Section: Discussionmentioning

confidence: 99%

Microbial consortium mediated acceleration of the defense response in potato against Alternaria solani through prodigious inflation in phenylpropanoid derivatives and redox homeostasis

Kumar,

Chandra,

Behera

et al. 2023

Heliyon

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“…They include cytochrome c peroxidases (EC 1.11.1.5; CcPs), catalase (EC 1.11.1.6; CAT), and ascorbate peroxidases (EC 1.11.1.11; APX), which have the primary function of the cell is to scavenge excess H 2 O 2 . The Class II Prxs include manganese peroxidases (EC 1.11.1.13; MnPs) and lignin peroxidases (EC 1.11.1.14; LiPs), which play a key role in the degradation of lignin-containing detritus in the soil, as none of the other peroxidases are capable of degrading lignin (Cosio and Dunand, 2009; Jha et al, 2022) . The Class III Prxs (EC 1.11.1.7), plant-specific heme oxidoreductases, are secreted into the extracellular space or vacuole, which are typically localized in the cytoplasm and cell wall, are highly thermally stable and naturally glycoproteins with a wide range of substrates and marked substrate specificity for phenols (Cosio and Dunand, 2009; Shigeto and Tsutsumi, 2016) .…”

Section: Introductionmentioning

confidence: 99%

The Class III peroxidase OsPrx20 is a key regulator of stress response and growth in rice

Shen,

Wang,

Chen

et al. 2024

Preprint

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In plants, reactive oxygen species maintain strictly low intracellular levels that is prerequisite for their function as second messengers. However, abiotic and biotic stresses are also long-term processes, requiring rapid scavenging of excess intracellular ROS. Plant Class III peroxidases, as multifunctional enzymes, are core enzymes in regulating intracellular ROS homeostasis and are key to regulating the complicated signaling network. Here, we found a rice Class III peroxidase OsPrx20 maintains intracellular ROS homeostasis in different conditions. OsPrx20 is a target of Ca2+/calmodulin-dependent protein kinase (OsDMI3) and phosphorylates its Thr-244 site by OsDMI3. Overexpression of OsPrx20 enhances osmotic stress tolerance but reduces blast resistance, while lack of OsPrx20 is opposite, suggesting OsPrx20 positively regulates osmotic stress tolerance but negatively regulates blast resistance in rice. Meanwhile, overexpression of OsPrx20 enlarges spike size and grain fullness, whereas lack of OsPrx20 leads to dwarfism and smaller spike. In ABA signaling, OsPrx20 Thr-244 phosphorylation is specifically dependent on OsDMI3 to reduce the sensitivity of ABA to seed germination and root growth and to enhance osmotic stress tolerance without affecting spike and grain development. Our study reveals an essential regulatory mechanism that directly activates OsPrx20 in ABA signaling, highlighting the multi-functionality of OsPrx20 in different biological processes.

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“…Peroxidases (PODs) are ubiquitous enzymes belonging to the class of oxidoreductases, capable of catalysing a wide variety of oxygen-transfer reactions between hydrogen peroxide or other peroxides as electron acceptors and many kinds of substrates (xenobiotic, lignin and other phenolic compounds), resulting in oxygen (O 2 ) liberation from H 2 O 2 1 . The non-animal heme superfamily is one of the most studied groups of peroxidases, which includes enzymes from plant, fungi and bacteria, and it is further divided into three classes based on the origin, amino acid homology and metal-binding capability 2 , 3 . Within this group, enzymes from plant sources have been proposed for a wide range of industrial applications within areas such as health sciences, food industry and ecology.…”

Section: Introductionmentioning

confidence: 99%

A new versatile peroxidase with extremophilic traits over-produced in MicroTom cell cultures

Gogliettino,

Cocca,

Apone

et al. 2023

Sci Rep

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Peroxidases are widespread key antioxidant enzymes that catalyse the oxidation of electron donor substrates in parallel with the decomposition of H2O2. In this work, a novel tomato peroxidase, named SAAP2, was isolated from MicroTom cell cultures, purified, and characterised. The enzyme was identified with 64% sequence coverage as the leprx21 gene product (suberization-associated anionic peroxidase 2-like) from Solanum lycopersicum, 334 amino acids long. Compared to other plant peroxidases, SAAP2 was more active at elevated temperatures, with the optimal temperature and pH at 90 °C and 5.0, respectively. Furthermore, the enzyme retained more than 80% of its maximal activity over the range of 70–80 °C and the presence of NaCl (1.0–4.5 M). It also exhibited broad pH versatility (65% relative activity over the pH range 2.0–7.0), acid-tolerance (80% residual activity after 22 h at pH 2.0–7.0), high thermostability (50% residual activity after 2 h at 80 °C) and proteolytic resistance. SAAP2 exhibited exceptional resistance under thermo-acidic conditions compared to the horseradish peroxidase benchmark, suggesting that it may find potential applications as a supplement or anti-pollution agent in the food industry.

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Plant Peroxidases: Biomarkers of Environmental Stresses and Signaling in Plants

Cited by 3 publications

References 104 publications

Microbial consortium mediated acceleration of the defense response in potato against Alternaria solani through prodigious inflation in phenylpropanoid derivatives and redox homeostasis

Microbial consortium mediated acceleration of the defense response in potato against Alternaria solani through prodigious inflation in phenylpropanoid derivatives and redox homeostasis

The Class III peroxidase OsPrx20 is a key regulator of stress response and growth in rice

A new versatile peroxidase with extremophilic traits over-produced in MicroTom cell cultures

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