ArticleThe Biochemical journal2007
Novel class of glutathione transferases from cyanobacteria exhibit high catalytic activities towards naturally occurring isothiocyanates.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 63 citations in OpenAlex.
- Versatility of Glutathione Transferase Proteins.Biomolecules · 2023Article
- Article
- The Glutathione System: A Journey from Cyanobacteria to Higher Eukaryotes.Antioxidants (Basel, Switzerland) · 2023Review
- Biochemical and Structural Characterization of Chi-Class Glutathione Transferases: A Snapshot on the Glutathione Transferase Encoded byBiomolecules · 2022Article
- Functional and Structural Diversity of Insect Glutathione S-transferases in Xenobiotic Adaptation.International journal of biological sciences · 2022Review
- Genetic, Genomics, and Responses to Stresses in Cyanobacteria: Biotechnological Implications.Genes · 2021Review
- Diversity of Glutathione S-Transferases (GSTs) in Cyanobacteria with Reference to Their Structures, Substrate Recognition and Catalytic Functions.Microorganisms · 2020Article
- FirstFrontiers in microbiology · 2019Article
- Roles of Two Glutathione-Dependent 3,6-Dichlorogentisate Dehalogenases in Rhizorhabdus dicambivorans Ndbn-20 in the Catabolism of the Herbicide Dicamba.Applied and environmental microbiology · 2018Article
- Arabidopsis mutants impaired in glutathione biosynthesis exhibit higher sensitivity towards the glucosinolate hydrolysis product allyl-isothiocyanate.Scientific reports · 2018Article
- SaxA-Mediated Isothiocyanate Metabolism in Phytopathogenic Pectobacteria.Applied and environmental microbiology · 2016Article
- Structural Basis of Stereospecificity in the Bacterial Enzymatic Cleavage of β-Aryl Ether Bonds in Lignin.The Journal of biological chemistry · 2016Article
- Insecticides induced biochemical changes in freshwater microalga Chlamydomonas mexicana.Environmental science and pollution research international · 2016Article
- Phi Class of Glutathione S-transferase Gene Superfamily Widely Exists in Nonplant Taxonomic Groups.Evolutionary bioinformatics online · 2016Article
- Assessing the antibiotic susceptibility of freshwater Cyanobacteria spp.Frontiers in microbiology · 2015Article
- Characterization of a Highly pH Stable Chi-Class Glutathione S-Transferase from Synechocystis PCC 6803.PloS one · 2015Article
- Functional classification and biochemical characterization of a novel rho class glutathione S-transferase in Synechocystis PCC 6803.FEBS open bio · 2015Article
- Evolution in an ancient detoxification pathway is coupled with a transition to herbivory in the drosophilidae.Molecular biology and evolution · 2014Article
- Characterization of affinity-purified isoforms of Acinetobacter calcoaceticus Y1 glutathione transferases.TheScientificWorldJournal · 2014Article
- Insights into the mode of action of benzyl isothiocyanate on Campylobacter jejuni.Applied and environmental microbiology · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the present paper, we report a novel class of GSTs (glutathione transferases), called the Chi class, originating from cyanobacteria and with properties not observed previously in prokaryotic enzymes. GSTs constitute a widespread multifunctional group of proteins, of which mammalian enzymes are the best characterized. Although GSTs have their origin in prokaryotes, few bacterial representatives have been characterized in detail, and the catalytic activities and substrate specificities observed have generally been very modest. The few well-studied bacterial GSTs have largely unknown physiological functions. Genome databases reveal that cyanobacteria have an extensive arsenal of glutathione-associated proteins. We have studied two cyanobacterial GSTs which are the first examples of bacterial enzymes that are as catalytically efficient as the best mammalian enzymes. GSTs from the thermophile Thermosynechococcus elongatus BP-1 and from Synechococcus elongatus PCC 6301 were found to catalyse the conjugation of naturally occurring plant-derived isothiocyanates to glutathione at high rates. The cyanobacterial GSTs studied are smaller than previously described members of this enzyme family, but display many of the typical structural features that are characteristics of GSTs. They are also active towards several classical substrates, but at the same moderate rates that have been observed for other GSTs derived from prokaryotes. The cloning, expression and characterization of two cyanobacterial GSTs are described. The possible significance of the observed catalytic properties is discussed in the context of physiological relevance and GST evolution.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.