{"id":"1bc571ee-48a9-50df-9d1d-3fa9107c3ca0","stable_key":"e0ea2d6a-7429-5e9f-b774-41e5e3288da3:ve-transport-cyp4f2-k1-hydroxylation","predicate":"catalyzes_formation","statement":"Human CYP4F2-expressing microsomes hydroxylated phylloquinone, demonstrating substrate overlap with tocopherol catabolism.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"b38fe257-1d65-5ef7-9101-8d5c69347024","mechanism_event_label":"Vitamins E and K1 share an initial catabolic enzyme.","subject":{"id":"0510331f-d4bd-57ba-97a0-ce64171ec3e7","slug":"cyp4f2","display_name":"Human cytochrome P450 4F2","entity_type_key":"protein"},"object":{"id":"89bad4c7-8c79-50f8-ac00-19bf8b3f31db","slug":"omega-hydroxyphylloquinone","display_name":"Omega-hydroxyphylloquinone","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"b38fe257-1d65-5ef7-9101-8d5c69347024","stable_key":"e0ea2d6a-7429-5e9f-b774-41e5e3288da3:ve-transport-cyp4f2-k1-hydroxylation-event","event_type":"biochemical_relationship","label":"Vitamins E and K1 share an initial catabolic enzyme.","description":"Human CYP4F2-expressing microsomes hydroxylated phylloquinone, demonstrating substrate overlap with tocopherol catabolism.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"0510331f-d4bd-57ba-97a0-ce64171ec3e7","slug":"cyp4f2","display_name":"Human cytochrome P450 4F2","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"89bad4c7-8c79-50f8-ac00-19bf8b3f31db","slug":"omega-hydroxyphylloquinone","display_name":"Omega-hydroxyphylloquinone","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"5f9fd13b-5428-5024-a855-9db526855890","slug":"phylloquinone","display_name":"Phylloquinone","entity_type_key":"small_molecule"},"role":"vitamin_k_substrate","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"40a6525a-76b8-576e-b73d-1e11aecf5f8d","slug":"alpha-tocopherol","display_name":"Alpha-tocopherol","entity_type_key":"small_molecule"},"role":"shared_enzyme_substrate","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"4aba2a5e-8d06-5304-bb01-c0402b225a94","slug":"nadph","display_name":"NADPH","entity_type_key":"small_molecule"},"role":"reducing_cofactor","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"cross_nutrient","value_text":"true","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant CYP4F2 kinetic assay","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"25 pmol CYP4F2; labeled phylloquinone 1–100 µM; 1 mM NADPH; 30 min at 37 °C.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Shared substrate use alone does not imply vitamin E accelerates vitamin K depletion.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Vitamin E research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"vitamin-e","display_name":"Vitamin E","entity_type_key":"chemical_species"}},{"dimension":"organism","value_text":"Human protein in insect microsomes","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Vitamins E and K1 share an initial catabolic enzyme.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[farley2013] ω-Hydroxylation of phylloquinone by CYP4F2 is not increased by α-tocopherol. (2013). https://pubmed.ncbi.nlm.nih.gov/23650179/ DOI: 10.1002/mnfr.201200797","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Microsomal enzyme preparation","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"9f11e362-067d-52a3-a6d7-3f5d1d0ba5a9","evidence_kind":"source_excerpt","locator":"Lines 454-465","start_line":454,"end_line":465,"excerpt":"### ve-transport-cyp4f2-k1-hydroxylation\nHuman CYP4F2-expressing microsomes hydroxylated phylloquinone, demonstrating substrate overlap with tocopherol catabolism.\nCondition category: normal\nnutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Vitamins E and K1 share an initial catabolic enzyme.\norganism: Human protein in insect microsomes\ntissue_or_cell_type: Microsomal enzyme preparation\nexperimental_model: Recombinant CYP4F2 kinetic assay\nlimitations: Shared substrate use alone does not imply vitamin E accelerates vitamin K depletion.\nexposure: 25 pmol CYP4F2; labeled phylloquinone 1–100 µM; 1 mM NADPH; 30 min at 37 °C.\ncross_nutrient: true\n[farley2013] ω-Hydroxylation of phylloquinone by CYP4F2 is not increased by α-tocopherol. (2013). https://pubmed.ncbi.nlm.nih.gov/23650179/ DOI: 10.1002/mnfr.201200797","model_system":"Recombinant CYP4F2 kinetic assay","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [farley2013] ω-Hydroxylation of phylloquinone by CYP4F2 is not increased by α-tocopherol. (2013). https://pubmed.ncbi.nlm.nih.gov/23650179/ DOI: 10.1002/mnfr.201200797","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"3ac41dba-4727-5116-a556-ac3bbb0dc41c","stable_key":"import-e0ea2d6a-7429-5e9f-b774-41e5e3288da3","title":"Vitamin E: transport, membrane protection and nutrient interactions (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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