ArticlePloS one2013
Structural insights into omega-class glutathione transferases: a snapshot of enzyme reduction and identification of a non-catalytic ligandin site.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.
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Who cites it
14 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Glutathione Transferases Omega-1 and -2 Polymorphisms in Cancer: Drivers or Silent Bystanders?International journal of molecular sciences · 2025Pooled it
- Editorial: The expanding functional network of glutathione transferases.Frontiers in molecular biosciences · 2023Article
- Biochemical and Structural Insights on the Poplar Tau Glutathione Transferase GSTU19 and 20 Paralogs Binding Flavonoids.Frontiers in molecular biosciences · 2022Article
- Molecular recognition of wood polyphenols by phase II detoxification enzymes of the white rot Trametes versicolor.Scientific reports · 2018Article
- Structure-Guided Mechanisms Behind the Metabolism of 2,4,6-Trinitrotoluene by Glutathione Transferases U25 and U24 That Lead to Alternate Product Distribution.Frontiers in plant science · 2018Article
- Structural evidence forFEBS open bio · 2017Article
- Omega Class Glutathione S-Transferase: Antioxidant Enzyme in Pathogenesis of Neurodegenerative Diseases.Oxidative medicine and cellular longevity · 2017Review
- Energetics of Glutathione Binding to Human Eukaryotic Elongation Factor 1 Gamma: Isothermal Titration Calorimetry and Molecular Dynamics Studies.The protein journal · 2016Article
- Mechanistic evaluation and transcriptional signature of a glutathione S-transferase omega 1 inhibitor.Nature communications · 2016Article
- Clonorchis sinensis omega-class glutathione transferases play major roles in the protection of the reproductive system during maturation and the response to oxidative stress.Parasites & vectors · 2016Article
- Structural understanding of the recycling of oxidized ascorbate by dehydroascorbate reductase (OsDHAR) from Oryza sativa L. japonica.Scientific reports · 2016Article
- Genomic Analysis of Detoxification Supergene Families in the Mosquito Anopheles sinensis.PloS one · 2015Article
- The still mysterious roles of cysteine-containing glutathione transferases in plants.Frontiers in pharmacology · 2014Review
- Diversification of fungal specific class a glutathione transferases in saprotrophic fungi.PloS one · 2013Article
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3 authors.
Funding
Abstract
Glutathione transferases (GSTs) are dimeric enzymes containing one active-site per monomer. The omega-class GSTs (hGSTO1-1 and hGSTO2-2 in humans) are homodimeric and carry out a range of reactions including the glutathione-dependant reduction of a range of compounds and the reduction of S-(phenacyl)glutathiones to acetophenones. Both types of reaction result in the formation of a mixed-disulfide of the enzyme with glutathione through the catalytic cysteine (C32). Recycling of the enzyme utilizes a second glutathione molecule and results in oxidized glutathione (GSSG) release. The crystal structure of an active-site mutant (C32A) of the hGSTO1-1 isozyme in complex with GSSG provides a snapshot of the enzyme in the process of regeneration. GSSG occupies both the G (GSH-binding) and H (hydrophobic-binding) sites and causes re-arrangement of some H-site residues. In the same structure we demonstrate the existence of a novel "ligandin" binding site deep within in the dimer interface of this enzyme, containing S-(4-nitrophenacyl)glutathione, an isozyme-specific substrate for hGSTO1-1. The ligandin site, conserved in Omega class GSTs from a range of species, is hydrophobic in nature and may represent the binding location for tocopherol esters that are uncompetitive hGSTO1-1 inhibitors.
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