Structure and Antioxidant Catalytic Function of Plant Glutathione Transferases

Author(s): Evangelia Chronopoulou, Irene Axarli, Irini Nianiou-Obeidat, Panagiotis Madesis, Athanasios Tsaftaris, Nikolaos E. Labrou.

Journal Name: Current Chemical Biology

Volume 5 , Issue 1 , 2011

Become EABM
Become Reviewer

Abstract:

Plant cytosolic glutathione transferases (GSTs) are an ancient enzyme superfamily with multiple and diverse functions which are important in counteracting biotic and abiotic stresses. GSTs play an important role in catalyzing the conjugation of xenobiotics and endogenous electrophilic compounds with glutathione (GSH), such as pesticides, chemical carcinogens, environmental pollutants, which leads 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 formed during oxidative stress, biosynthesis of sulfur-containing secondary metabolites, and exhibit thioltransferase and dehydroascorbate reductase activity. This review focuses on plant GSTs, and attempts to give an overview of the new insights into the catalytic function and structural biology of these enzymes.

Keywords: Glutathione transferase, herbicide detoxification, biotic stress, abiotic stress, Antioxidant, Catalytic Function, enzymes, cytosolic, mitochondrial, microsomal proteins, electrophilic centers, endogenous, xenobiotic, metabolites, nucleotide sequence, organic hydroperoxides, epoxides, arene oxides, unsaturated carbonyls, organic nitrate esters, organic thiocyanates, isomerization reactions, sulfur, volatiles, phenolics, flavonoids, oxylipins, toxins, oxygen toxicity, isoenzymes, cell proliferation, metabolic pathways, cell death, non-catalytically, anticancer drugs, ligand-binding, catabolite repression, non-controlled oxidation, DNA, cellular structure destruction, peroxidase activity, pathogen attack, herbicide treatment, selenium-dependent, catalytic site, chloroplasts, peroxisome, apoplast, Alopecurus myosuroides, Arabidopsis thaliana, ascorbic acid, monomeric, hydrophilic, dimerization, thiol grou, thiolate, hydrogen bonds, Electrophilic Binding Site, Ligand Binding Site

Rights & PermissionsPrintExport Cite as

Article Details

VOLUME: 5
ISSUE: 1
Year: 2011
Page: [64 - 74]
Pages: 11
DOI: 10.2174/2212796811105010064

Article Metrics

PDF: 11