ArticlePlanta2012
Catalytic and structural diversity of the fluazifop-inducible glutathione transferases from Phaseolus vulgaris.
Article in Planta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 38 citations in OpenAlex.
- Genome-wide analysis of the glutathione S-transferase family inFrontiers in plant science · 2026Article
- Genome-Wide Identification and Drought-Responsive Functional Analysis of theAntioxidants (Basel, Switzerland) · 2025Article
- Genome-wide identification and characterization of Glutathione S-Transferases (GSTs) and their expression profile under abiotic stresses in tobacco (Nicotiana tabacum L.).BMC genomics · 2023Article
- Directed Evolution of Phi Class Glutathione Transferases Involved in Multiple-Herbicide Resistance of Grass Weeds and Crops.International journal of molecular sciences · 2022Article
- Genome-Wide Identification, Evolution and Expression Analysis of the Glutathione S-Transferase Supergene Family in Euphorbiaceae.Frontiers in plant science · 2022Article
- Biochemical and Structural Insights on the Poplar Tau Glutathione Transferase GSTU19 and 20 Paralogs Binding Flavonoids.Frontiers in molecular biosciences · 2022Article
- A Novel GlutathioneToxins · 2021Article
- Overexpression of A Biotic Stress-InducibleInternational journal of molecular sciences · 2021Article
- Expanding the Plant GSTome Through Directed Evolution: DNA Shuffling for the Generation of New Synthetic Enzymes With Engineered Catalytic and Binding Properties.Frontiers in plant science · 2018Article
- Tolerance of Transplastomic Tobacco Plants Overexpressing a Theta Class Glutathione Transferase to Abiotic and Oxidative Stresses.Frontiers in plant science · 2018Article
- Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics.Biochimie · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plant glutathione transferases (GSTs) comprise a large family of inducible enzymes that play important roles in stress tolerance and herbicide detoxification. Treatment of Phaseolus vulgaris leaves with the aryloxyphenoxypropionic herbicide fluazifop-p-butyl resulted in induction of GST activities. Three inducible GST isoenzymes were identified and separated by affinity chromatography. Their full-length cDNAs with complete open reading frame were isolated using RACE-RT and information from N-terminal amino acid sequences. Analysis of the cDNA clones showed that the deduced amino acid sequences share high homology with GSTs that belong to phi and tau classes. The three isoenzymes were expressed in E. coli and their substrate specificity was determined towards 20 different substrates. The results showed that the fluazifop-inducible glutathione transferases from P. vulgaris (PvGSTs) catalyze a broad range of reactions and exhibit quite varied substrate specificity. Molecular modeling and structural analysis was used to identify key structural characteristics and to provide insights into the substrate specificity and the catalytic mechanism of these enzymes. These results provide new insights into catalytic and structural diversity of GSTs and the detoxifying mechanism used by P. vulgaris.
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