ArticleThe Journal of biological chemistry2011
Glutathione transferases of Phanerochaete chrysosporium: S-glutathionyl-p-hydroquinone reductase belongs to a new structural class.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 40 citations in OpenAlex.
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- Testing the Capability of Embedding-Based Alignments on the GST Superfamily Classification: The Role of Protein Length.Molecules (Basel, Switzerland) · 2024Article
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- Biochemical and Structural Characterization of Chi-Class Glutathione Transferases: A Snapshot on the Glutathione Transferase Encoded byBiomolecules · 2022Article
- Interactive Gene Expression BetweenFrontiers in physiology · 2021Article
- Redox and Thiols in Archaea.Antioxidants (Basel, Switzerland) · 2020Review
- Characterization of Xi-class mycothiol S-transferase from Corynebacterium glutamicum and its protective effects in oxidative stress.Microbial cell factories · 2019Article
- Structural Characterization of the Xi Class Glutathione Transferase From the Haloalkaliphilic ArchaeonFrontiers in microbiology · 2019Article
- Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases.Frontiers in plant science · 2019Review
- Delineation of the functional and structural properties of the glutathione transferase family from the plant pathogen Erwinia carotovora.Functional & integrative genomics · 2019Article
- Crystal Structure of Saccharomyces cerevisiae ECM4, a Xi-Class Glutathione Transferase that Reacts with Glutathionyl-(hydro)quinones.PloS one · 2016Article
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- Changes in protein thiols in response to salt stress in embryogenic suspension cultures ofBiotechnology, biotechnological equipment · 2014Article
- Large-scale determination of sequence, structure, and function relationships in cytosolic glutathione transferases across the biosphere.PLoS biology · 2014Article
- The still mysterious roles of cysteine-containing glutathione transferases in plants.Frontiers in pharmacology · 2014Review
- Xenomic networks variability and adaptation traits in wood decaying fungi.Microbial biotechnology · 2013Review
- Diversification of fungal specific class a glutathione transferases in saprotrophic fungi.PloS one · 2013Article
- Article
- Characterization of a Phanerochaete chrysosporium glutathione transferase reveals a novel structural and functional class with ligandin properties.The Journal of biological chemistry · 2012Article
- Structural understanding of the glutathione-dependent reduction mechanism of glutathionyl-hydroquinone reductases.The Journal of biological chemistry · 2012Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The white rot fungus Phanerochaete chrysosporium, a saprophytic basidiomycete, possesses a large number of cytosolic glutathione transferases, eight of them showing similarity to the Omega class. PcGSTO1 (subclass I, the bacterial homologs of which were recently proposed, based on their enzymatic function, to constitute a new class of glutathione transferase named S-glutathionyl-(chloro)hydroquinone reductases) and PcGSTO3 (subclass II related to mammalian homologs) have been investigated in this study. Biochemical investigations demonstrate that both enzymes are able to catalyze deglutathionylation reactions thanks to the presence of a catalytic cysteinyl residue. This reaction leads to the formation of a disulfide bridge between the conserved cysteine and the removed glutathione from their substrate. The substrate specificity of each isoform differs. In particular PcGSTO1, in contrast to PcGSTO3, was found to catalyze deglutathionylation of S-glutathionyl-p-hydroquinone substrates. The three-dimensional structure of PcGSTO1 presented here confirms the hypothesis that it belongs not only to a new biological class but also to a new structural class that we propose to name GST xi. Indeed, it shows specific features, the most striking ones being a new dimerization mode and a catalytic site that is buried due to the presence of long loops and that contains the catalytic cysteine.
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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.