{"id":"020580f3-0a9d-5843-8743-4ce0366a4717","stable_key":"db0fc92e-b5ef-5667-a4c5-3ef257edbc9b:glutathione-prdx6-gstp","predicate":"supports_reactivation_of","statement":"PRDX6 heterodimerization with piGST supports glutathionylation needed in the peroxidatic cycle.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"25b06f97-9f02-5802-bc40-b2709c756216","mechanism_event_label":"A glutathione transferase helps reactivate another peroxide-handling enzyme.","subject":{"id":"3574cefe-a463-5a19-83f0-d8efc9b5c908","slug":"gstp1","display_name":"Human glutathione S-transferase P1 / GSTP1","entity_type_key":"protein"},"object":{"id":"84991dbd-89b3-5e75-beaa-3253443bcc84","slug":"prdx6","display_name":"Human peroxiredoxin 6 / PRDX6","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"25b06f97-9f02-5802-bc40-b2709c756216","stable_key":"db0fc92e-b5ef-5667-a4c5-3ef257edbc9b:glutathione-prdx6-gstp-event","event_type":"biochemical_relationship","label":"A glutathione transferase helps reactivate another peroxide-handling enzyme.","description":"PRDX6 heterodimerization with piGST supports glutathionylation needed in the peroxidatic cycle.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"b44c9e27-4bbb-52d3-a022-14cddded5073","slug":"glutathione","display_name":"GSH","entity_type_key":"small_molecule"},"role":"reducing_system_component","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"3574cefe-a463-5a19-83f0-d8efc9b5c908","slug":"gstp1","display_name":"Human glutathione S-transferase P1 / GSTP1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"84991dbd-89b3-5e75-beaa-3253443bcc84","slug":"prdx6","display_name":"Human peroxiredoxin 6 / PRDX6","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/glutathione-research/26891882.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"919a342fc31314fef155eba006fd5a61b2a0a2d93a02c4de5e122c3d25d690fc\", \"start_char\": 0, \"end_char\": 1661, \"text_sha256\": \"919a342fc31314fef155eba006fd5a61b2a0a2d93a02c4de5e122c3d25d690fc\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human PRDX6 structures, dimerization and mutagenesis","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Leu145/Leu148 substitutions","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"PRDX6 peroxidase and phospholipase activities are distinct; this is not a clinical GSTP1-variant study.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Glutathione research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"glutathione","display_name":"GSH","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Human","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"A glutathione transferase helps reactivate another peroxide-handling enzyme.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[glutathione-p26891882] Peroxiredoxin 6 homodimerization and heterodimerization with glutathione S-transferase pi are required for its peroxidase but not phospholipase A2 activity. (2016). https://pubmed.ncbi.nlm.nih.gov/26891882/ DOI: 10.1016/j.freeradbiomed.2016.02.012","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified protein and proximity assays","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"1542943c-adbd-5204-81a7-6fbc198d5d81","evidence_kind":"source_excerpt","locator":"Lines 957-968","start_line":957,"end_line":968,"excerpt":"### glutathione-prdx6-gstp\nPRDX6 heterodimerization with piGST supports glutathionylation needed in the peroxidatic cycle.\nCondition category: normal\nnutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: A glutathione transferase helps reactivate another peroxide-handling enzyme.\norganism: Human\ntissue_or_cell_type: Purified protein and proximity assays\nexperimental_model: Human PRDX6 structures, dimerization and mutagenesis\nlimitations: PRDX6 peroxidase and phospholipase activities are distinct; this is not a clinical GSTP1-variant study.\nexposure: Leu145/Leu148 substitutions\nevidence_span: {\"source_cache\": \"artifacts/glutathione-research/26891882.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"919a342fc31314fef155eba006fd5a61b2a0a2d93a02c4de5e122c3d25d690fc\", \"start_char\": 0, \"end_char\": 1661, \"text_sha256\": \"919a342fc31314fef155eba006fd5a61b2a0a2d93a02c4de5e122c3d25d690fc\"}\n[glutathione-p26891882] Peroxiredoxin 6 homodimerization and heterodimerization with glutathione S-transferase pi are required for its peroxidase but not phospholipase A2 activity. 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