| http://purl.uniprot.org/citations/17226937 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17226937 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17226937 | http://www.w3.org/2000/01/rdf-schema#comment | "S-(Phenacyl)glutathione reductase (SPG-R) plays a significant role in the biotransformation of reactive alpha-haloketones to nontoxic acetophenones. Comparison of the apparent subunit size, amino acid composition, and catalysis of the reduction of S-(phenacyl)glutathiones indicated that a previously described rat SPG-R (Kitada, M., McLenithan, J. C., and Anders, M. W. (1985) J. Biol. Chem. 260, 11749-11754) is homologous to the omega-class glutathione transferase GSTO1-1. The available data show that the SPG-R reaction is catalyzed by GSTO1-1 and not by other GSTs, including the closely related GSTO2-2 isoenzyme. In the proposed reaction mechanism, the active-site cysteine residue of GSTO1-1 reacts with the S-(phenacyl)glutathione substrate to give an acetophenone and a mixed disulfide with the active-site cysteine; a second thiol substrate (e.g., glutathione or 2-mercaptoethanol) reacts with the active-site disulfide to regenerate the catalytically active enzyme and to form a mixed disulfide. A new spectrophotometric assay was developed that allows the rapid determination of SPG-R activity and specific measurement of GSTO1-1 in the presence of other GSTs. This is the first specific reaction attributed to GSTO1-1, and these results demonstrate the catalytic diversity of GSTO1-1, which, in addition to SPG-R activity, catalyzes the reduction of dehydroascorbate and monomethylarsonate(V) and also possesses thioltransferase and GST activity."xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://purl.org/dc/terms/identifier | "doi:10.1021/tx600305y"xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://purl.org/dc/terms/identifier | "doi:10.1021/tx600305y"xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://purl.uniprot.org/core/author | "Board P.G."xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://purl.uniprot.org/core/author | "Board P.G."xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://purl.uniprot.org/core/author | "Anders M.W."xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://purl.uniprot.org/core/author | "Anders M.W."xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17226937 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17226937 | http://purl.uniprot.org/core/name | "Chem. Res. Toxicol."xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://purl.uniprot.org/core/name | "Chem. Res. Toxicol."xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://purl.uniprot.org/core/pages | "149-154"xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://purl.uniprot.org/core/pages | "149-154"xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://purl.uniprot.org/core/title | "Glutathione transferase omega 1 catalyzes the reduction of S-(phenacyl)glutathiones to acetophenones."xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://purl.uniprot.org/core/title | "Glutathione transferase omega 1 catalyzes the reduction of S-(phenacyl)glutathiones to acetophenones."xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://purl.uniprot.org/core/volume | "20"xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://purl.uniprot.org/core/volume | "20"xsd:string |
| http://purl.uniprot.org/citations/17226937 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17226937 |
| http://purl.uniprot.org/citations/17226937 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17226937 |
| http://purl.uniprot.org/citations/17226937 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17226937 |
| http://purl.uniprot.org/citations/17226937 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17226937 |
| http://purl.uniprot.org/uniprot/P78417 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/17226937 |
| http://purl.uniprot.org/uniprot/P78417#attribution-0D76AC8560866294DC8B2CC0AD5D348C | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/17226937 |