dc.contributor.author | Chronopoulou, E | en |
dc.contributor.author | Axarli, I | en |
dc.contributor.author | Nianiou-Obeidat, I | en |
dc.contributor.author | Madesis, P | en |
dc.contributor.author | Tsaftaris, A | en |
dc.contributor.author | Labrou, NE | en |
dc.date.accessioned | 2014-06-06T06:51:02Z | |
dc.date.available | 2014-06-06T06:51:02Z | |
dc.date.issued | 2011 | en |
dc.identifier.issn | 18723136 | en |
dc.identifier.uri | http://dx.doi.org/10.2174/187231311793564306 | en |
dc.identifier.uri | http://62.217.125.90/xmlui/handle/123456789/5286 | |
dc.subject | Abiotic stress | en |
dc.subject | Biotic stress | en |
dc.subject | Glutathione transferase | en |
dc.subject | Herbicide detoxification | en |
dc.subject.other | glutathione transferase | en |
dc.subject.other | ligand | en |
dc.subject.other | vegetable protein | en |
dc.subject.other | antioxidant activity | en |
dc.subject.other | article | en |
dc.subject.other | binding site | en |
dc.subject.other | catalysis | en |
dc.subject.other | electrophilicity | en |
dc.subject.other | enzyme structure | en |
dc.subject.other | ligand binding | en |
dc.subject.other | nonhuman | en |
dc.subject.other | nucleotide sequence | en |
dc.subject.other | plant | en |
dc.subject.other | priority journal | en |
dc.subject.other | protein function | en |
dc.subject.other | protein interaction | en |
dc.subject.other | structure analysis | en |
dc.title | Structure and antioxidant catalytic function of plant glutathione transferases | en |
heal.type | journalArticle | en |
heal.identifier.primary | 10.2174/187231311793564306 | en |
heal.publicationDate | 2011 | en |
heal.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. © 2011 Bentham Science Publishers Ltd. | en |
heal.journalName | Current Chemical Biology | en |
dc.identifier.issue | 1 | en |
dc.identifier.volume | 5 | en |
dc.identifier.doi | 10.2174/187231311793564306 | en |
dc.identifier.spage | 64 | en |
dc.identifier.epage | 74 | en |
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