{"id":"7859b78c-336b-58d3-b1a7-f967d8c7c87d","stable_key":"4fef8d72-f107-5eb5-b2fb-483ca85465e0:k2-cyp4f2-acid","predicate":"supports_sequential_formation_of","statement":"CYP4F2, but not CYP4F11, supported sequential MK-4 oxidation to the omega-acid without apparent release of the aldehyde intermediate.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"ce54e9a4-7354-5f76-a544-3dec24e5894d","mechanism_event_label":"The two enzymes did not perform every later breakdown step equally.","subject":{"id":"0510331f-d4bd-57ba-97a0-ce64171ec3e7","slug":"cyp4f2","display_name":"Human cytochrome P450 4F2","entity_type_key":"protein"},"object":{"id":"a065424f-ac9b-507f-93d6-9fcffb38fb0c","slug":"mk4-omega-acid","display_name":"Menaquinone-4 omega-carboxylic acid","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"ce54e9a4-7354-5f76-a544-3dec24e5894d","stable_key":"4fef8d72-f107-5eb5-b2fb-483ca85465e0:k2-cyp4f2-acid-event","event_type":"biochemical_relationship","label":"The two enzymes did not perform every later breakdown step equally.","description":"CYP4F2, but not CYP4F11, supported sequential MK-4 oxidation to the omega-acid without apparent release of the aldehyde intermediate.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"5155b9d1-e835-54b4-9f61-4cf35b3e5227","slug":"menaquinone-4","display_name":"Menaquinone-4 / MK-4 / menatetrenone","entity_type_key":"small_molecule"},"role":"starting_substrate","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"cb906f08-58f9-573f-8828-3da93477b1ef","slug":"cyp4f11","display_name":"Human cytochrome P450 4F11","entity_type_key":"protein"},"role":"comparison_enzyme","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"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":2,"notes":""},{"entity":{"id":"a065424f-ac9b-507f-93d6-9fcffb38fb0c","slug":"mk4-omega-acid","display_name":"Menaquinone-4 omega-carboxylic acid","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/k2-research/24138531.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"bcb3784026ddabfeb55257cddc84ffd1001d6eb4fb04ba2e9daf8ade8de770fb\", \"start_char\": 0, \"end_char\": 1608, \"text_sha256\": \"bcb3784026ddabfeb55257cddc84ffd1001d6eb4fb04ba2e9daf8ade8de770fb\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified enzymes, liver microsomes and genotyping","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"MK-4 oxidation and common enzyme variants","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Catabolism assay; no assumption that all long-chain menaquinones have identical kinetics.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"k2","display_name":"Vitamin K2 / menaquinone family","entity_type_key":"chemical_species"}},{"dimension":"organism","value_text":"Human CYP4F2/CYP4F11 and human liver microsomes","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The two enzymes did not perform every later breakdown step equally.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[k2-p24138531] Cytochrome P450-dependent catabolism of vitamin K: ω-hydroxylation catalyzed by human CYP4F2 and CYP4F11. (2013). https://pubmed.ncbi.nlm.nih.gov/24138531/ DOI: 10.1021/bi401208m","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"MK-4 catabolism","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"043f43ad-87a0-5b56-87e3-a3a3e31c5497","evidence_kind":"source_excerpt","locator":"Lines 344-355","start_line":344,"end_line":355,"excerpt":"### k2-cyp4f2-acid\nCYP4F2, but not CYP4F11, supported sequential MK-4 oxidation to the omega-acid without apparent release of the aldehyde intermediate.\nCondition category: normal\nnutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The two enzymes did not perform every later breakdown step equally.\norganism: Human CYP4F2/CYP4F11 and human liver microsomes\ntissue_or_cell_type: MK-4 catabolism\nexperimental_model: Purified enzymes, liver microsomes and genotyping\nlimitations: Catabolism assay; no assumption that all long-chain menaquinones have identical kinetics.\nexposure: MK-4 oxidation and common enzyme variants\nevidence_span: {\"source_cache\": \"artifacts/k2-research/24138531.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"bcb3784026ddabfeb55257cddc84ffd1001d6eb4fb04ba2e9daf8ade8de770fb\", \"start_char\": 0, \"end_char\": 1608, \"text_sha256\": \"bcb3784026ddabfeb55257cddc84ffd1001d6eb4fb04ba2e9daf8ade8de770fb\"}\n[k2-p24138531] Cytochrome P450-dependent catabolism of vitamin K: ω-hydroxylation catalyzed by human CYP4F2 and CYP4F11. 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