| http://purl.uniprot.org/citations/23593192 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23593192 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/23593192 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0060324"xsd:string |
| http://purl.uniprot.org/citations/23593192 | http://purl.uniprot.org/core/author | "Board P.G."xsd:string |
| http://purl.uniprot.org/citations/23593192 | http://purl.uniprot.org/core/author | "Brock J."xsd:string |
| http://purl.uniprot.org/citations/23593192 | http://purl.uniprot.org/core/author | "Oakley A.J."xsd:string |
| http://purl.uniprot.org/citations/23593192 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23593192 | http://purl.uniprot.org/core/name | "PLoS One"xsd:string |
| http://purl.uniprot.org/citations/23593192 | http://purl.uniprot.org/core/pages | "e60324"xsd:string |
| http://purl.uniprot.org/citations/23593192 | http://purl.uniprot.org/core/title | "Structural insights into omega-class glutathione transferases: a snapshot of enzyme reduction and identification of a non-catalytic ligandin site."xsd:string |
| http://purl.uniprot.org/citations/23593192 | http://purl.uniprot.org/core/volume | "8"xsd:string |
| http://purl.uniprot.org/citations/23593192 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23593192 |
| http://purl.uniprot.org/citations/23593192 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/23593192 |
| http://purl.uniprot.org/uniprot/#_P78417-mappedCitation-23593192 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23593192 |
| http://purl.uniprot.org/uniprot/P78417 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/23593192 |