{"id":"989a0547-13f9-5efe-9c45-d4ecda43568f","stable_key":"research:gpx1-peroxide-reduction","predicate":"reduces_peroxide","statement":"Classical GPX1 couples hydrogen-peroxide reduction to oxidation of reduced glutathione; water and glutathione disulfide are products.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"literature_reviewed:supported_interpretation","direction":"positive","is_public":true,"mechanism_event_id":"c4582ce0-6ab8-5cc4-9d6e-9861657fc9d2","mechanism_event_label":"GPX1 uses glutathione to remove hydrogen peroxide.","subject":{"id":"e79d035c-0c02-5c0e-ac8f-d7fdeb663fbd","slug":"gpx1","display_name":"GPX1","entity_type_key":"protein"},"object":{"id":"da9d64bc-69d4-5d97-90a4-8f0ed03e0ac8","slug":"hydrogen-peroxide","display_name":"Hydrogen peroxide","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"c4582ce0-6ab8-5cc4-9d6e-9861657fc9d2","stable_key":"research:gpx1-peroxide-reduction","event_type":"experimentally_scoped_interaction","label":"GPX1 uses glutathione to remove hydrogen peroxide.","description":"Classical GPX1 couples hydrogen-peroxide reduction to oxidation of reduced glutathione; water and glutathione disulfide are products.","status":"active","compartment":null,"participants":[{"entity":{"id":"e79d035c-0c02-5c0e-ac8f-d7fdeb663fbd","slug":"gpx1","display_name":"GPX1","entity_type_key":"protein"},"role":"catalyst","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"da9d64bc-69d4-5d97-90a4-8f0ed03e0ac8","slug":"hydrogen-peroxide","display_name":"Hydrogen peroxide","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"b44c9e27-4bbb-52d3-a022-14cddded5073","slug":"glutathione","display_name":"GSH","entity_type_key":"small_molecule"},"role":"reducing_substrate","stoichiometry":null,"state_label":"reduced","sequence_order":2,"notes":""},{"entity":{"id":"1d9b9d7b-3fdf-57af-b9dd-00194fa1de9e","slug":"oxidized-glutathione","display_name":"GSSG","entity_type_key":"small_molecule"},"role":"product","stoichiometry":null,"state_label":"oxidized","sequence_order":3,"notes":""},{"entity":{"id":"d31225b7-8e94-5857-9ea1-67ac794b1f15","slug":"water","display_name":"H2O","entity_type_key":"small_molecule"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"experimental_model","value_text":"Animal selenium status and erythrocyte glutathione-peroxidase biochemistry.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"This experiment-specific relationship does not establish a human dietary-deficiency threshold or supplementation benefit.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"organism","value_text":"Rat","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"b3d226b3-dda8-5e76-b7ba-4318fddd31b3","evidence_kind":"curated_literature_summary","locator":"lines 954-963","start_line":954,"end_line":963,"excerpt":"## gpx1-peroxide-reduction\n\nGPX1 uses glutathione to remove hydrogen peroxide.\n\nClassical GPX1 couples hydrogen-peroxide reduction to oxidation of reduced glutathione; water and glutathione disulfide are products.\n\nExperimental model: Animal selenium status and erythrocyte glutathione-peroxidase biochemistry.\nOrganism: Rat\nLimitations: This experiment-specific relationship does not establish a human dietary-deficiency threshold or supplementation benefit.\nPrimary reference: [Selenium: biochemical role as a component of glutathione peroxidase](https://pubmed.ncbi.nlm.nih.gov/4686466/)","model_system":"Animal selenium status and erythrocyte glutathione-peroxidase biochemistry.","directness":"author_interpretation","verification_status":"secondary_verified","notes":"Curated summary; inspect the linked primary papers for original methods and results.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"4f892f13-06ea-5199-a33c-a703f35c80ae","stable_key":"selenium-research-2026-09-17","title":"Selenium: literature corrections and mechanism additions","document_type":"curated_literature_review","citation_label":"Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually","file_path":"","sha256":"0b818b10c1c7120e5caf7f4d4019d7bd025d745692e424f515d3ef903c9ab7f3","revision_id":"80984e03-5f0f-5877-8094-afef7637444e","review_status":"secondary_verified","notes":"Secondary curated summaries of primary experiments, with explicit models and limitations. Not archived primary full text."}}],"relations":[],"conflicts":[],"corrections":[],"research":{"topic":"Peroxide control","plain_language":"GPX1 uses glutathione to remove hydrogen peroxide.","evidence_scope":"supported_interpretation","papers":[{"key":"catalog-gpx-1973","title":"Selenium: biochemical role as a component of glutathione peroxidase","url":"https://pubmed.ncbi.nlm.nih.gov/4686466/","doi":null,"year":1973,"model":"Animal selenium status and erythrocyte glutathione-peroxidase biochemistry.","summary":"Links selenium to classical glutathione-peroxidase activity and erythrocyte peroxide handling."}]}}