Plant Glutathione Transferases: Structure, Antioxidant Catalytic Function and in planta Protective Role in Biotic and Abiotic Stress

Author(s): Evangelia Chronopoulou, Kassiani Kontouri, Marianna Chantzikonstantinou, Fotini Pouliou, Fereniki Perperopoulou, Georgia Voulgari, Eirini Bosmali, Irene Axarli, Irini Nianiou-Obeidat, Panagiotis Madesis, Athanasios Tsaftaris, Nikolaos E. Labrou

Journal Name: Current Chemical Biology

Volume 8 , Issue 2 , 2014

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Graphical Abstract:


Plant cytosolic glutathione transferases (GSTs) belong to an ancient enzyme superfamily with multiple and diverse functions which are important in counteracting biotic and abiotic stress. GSTs catalyze the conjugation of xenobiotics and endogenous electrophilic compounds with glutathione (GSH), leading to their detoxification. GSTs not only catalyze detoxification reactions but they are also involved in GSH-dependent isomerization reactions, in GSH-dependent reduction of organic hydroperoxides, biosynthesis of secondary metabolites, and exhibit thioltransferase and dehydroascorbate reductase activity. The applications of ‘omics’ technologies have allowed the classification of GSTs and the study of their evolution and sequence diversity, while enzymology has provided powerful insights into their catalytic role. This review focuses on plant GSTs, and attempts to give an overview of the new insights into their catalytic function and biological role in biotic and abiotic stress tolerance mechanisms in plants.

Keywords: Abiotic stress, biotic stress, glutathione transferase, herbicide detoxification.

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Article Details

Year: 2014
Published on: 02 March, 2015
Page: [58 - 75]
Pages: 18
DOI: 10.2174/2212796809666150302213733
Price: $25

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