{"id":"6e7d3bff-da35-59ae-b4dd-42c268c3b6a8","stable_key":"44eaeae5-557a-552b-8998-884f30462e2a:sulforaphane-gstp-conjugation","predicate":"catalyzes_formation_of","statement":"GSTP1-1 catalyzed sulforaphane conjugation with glutathione in the human enzyme comparison.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"fb6bbd3d-652f-5e06-9d98-3a539d6b793c","mechanism_event_label":"Glutathione attaches to sulforaphane during its handling.","subject":{"id":"3574cefe-a463-5a19-83f0-d8efc9b5c908","slug":"gstp1","display_name":"Human glutathione S-transferase P1 / GSTP1","entity_type_key":"protein"},"object":{"id":"e91e547a-a84c-5d7d-afbd-89e38a950c16","slug":"sulforaphane-glutathione","display_name":"Sulforaphane-glutathione conjugate / SFN-GSH","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"fb6bbd3d-652f-5e06-9d98-3a539d6b793c","stable_key":"44eaeae5-557a-552b-8998-884f30462e2a:sulforaphane-gstp-conjugation-event","event_type":"biochemical_relationship","label":"Glutathione attaches to sulforaphane during its handling.","description":"GSTP1-1 catalyzed sulforaphane conjugation with glutathione in the human enzyme comparison.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"b44c9e27-4bbb-52d3-a022-14cddded5073","slug":"glutathione","display_name":"GSH","entity_type_key":"small_molecule"},"role":"cosubstrate","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"67e70215-70c4-546a-84b4-0819fac0b326","slug":"sulforaphane","display_name":"Sulforaphane / SFN, stereochemistry specified per study","entity_type_key":"small_molecule"},"role":"electrophile","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"e91e547a-a84c-5d7d-afbd-89e38a950c16","slug":"sulforaphane-glutathione","display_name":"Sulforaphane-glutathione conjugate / SFN-GSH","entity_type_key":"small_molecule"},"role":"conjugate","stoichiometry":null,"state_label":"","sequence_order":2,"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":3,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/sulforaphane-research/7826396.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe\", \"start_char\": 0, \"end_char\": 989, \"text_sha256\": \"5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant human GST conjugation and reverse-reaction kinetics","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Four isothiocyanates and GSTP1-1, GSTM1-1, GSTA1-1 and GSTM2-2","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Relative enzyme rates are not whole-person clearance predictions; reverse reactions were slower and inhibited by high GSH.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Sulforaphane research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"sulforaphane","display_name":"Sulforaphane / SFN, stereochemistry specified per study","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Human GST isoenzymes","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Glutathione attaches to sulforaphane during its handling.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[sulforaphane-p7826396] Reversible conjugation of isothiocyanates with glutathione catalyzed by human glutathione transferases. (1995). https://pubmed.ncbi.nlm.nih.gov/7826396/ DOI: 10.1006/bbrc.1995.1106","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Isothiocyanate-glutathione chemistry","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"87829b8f-07f0-5f20-b12b-378619e33cf6","evidence_kind":"source_excerpt","locator":"Lines 255-266","start_line":255,"end_line":266,"excerpt":"### sulforaphane-gstp-conjugation\nGSTP1-1 catalyzed sulforaphane conjugation with glutathione in the human enzyme comparison.\nCondition category: normal\nnutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Glutathione attaches to sulforaphane during its handling.\norganism: Human GST isoenzymes\ntissue_or_cell_type: Isothiocyanate-glutathione chemistry\nexperimental_model: Recombinant human GST conjugation and reverse-reaction kinetics\nlimitations: Relative enzyme rates are not whole-person clearance predictions; reverse reactions were slower and inhibited by high GSH.\nexposure: Four isothiocyanates and GSTP1-1, GSTM1-1, GSTA1-1 and GSTM2-2\nevidence_span: {\"source_cache\": \"artifacts/sulforaphane-research/7826396.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe\", \"start_char\": 0, \"end_char\": 989, \"text_sha256\": \"5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe\"}\n[sulforaphane-p7826396] Reversible conjugation of isothiocyanates with glutathione catalyzed by human glutathione transferases. (1995). https://pubmed.ncbi.nlm.nih.gov/7826396/ DOI: 10.1006/bbrc.1995.1106","model_system":"Recombinant human GST conjugation and reverse-reaction kinetics","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [sulforaphane-p7826396] Reversible conjugation of isothiocyanates with glutathione catalyzed by human glutathione transferases. (1995). https://pubmed.ncbi.nlm.nih.gov/7826396/ DOI: 10.1006/bbrc.1995.1106","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"a4bafbf7-f117-53c9-a6d7-8fb25e4aca72","stable_key":"import-44eaeae5-557a-552b-8998-884f30462e2a","title":"Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. 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