{"id":"d417083e-1850-58dd-b400-aad44f8f959a","stable_key":"182336c6-ed36-5ec6-8a09-25c31096262e:dim-cyp1a2-heme","predicate":"contains_catalytic","statement":"The CYP1A2 structure places its ligand above the heme prosthetic group.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"4f21b0b2-93e1-564b-9127-ff3817235a28","mechanism_event_label":"The induced enzyme still needs its iron-containing catalytic machinery.","subject":{"id":"9b15c13c-a369-5d10-a76a-525e8b19221d","slug":"cyp1a2","display_name":"Human cytochrome P450 1A2","entity_type_key":"protein"},"object":{"id":"2e1f7e0a-8b54-5ea3-9d34-01e7167f9097","slug":"heme","display_name":"Heme","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"4f21b0b2-93e1-564b-9127-ff3817235a28","stable_key":"182336c6-ed36-5ec6-8a09-25c31096262e:dim-cyp1a2-heme-event","event_type":"biochemical_relationship","label":"The induced enzyme still needs its iron-containing catalytic machinery.","description":"The CYP1A2 structure places its ligand above the heme prosthetic group.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"9b15c13c-a369-5d10-a76a-525e8b19221d","slug":"cyp1a2","display_name":"Human cytochrome P450 1A2","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"2e1f7e0a-8b54-5ea3-9d34-01e7167f9097","slug":"heme","display_name":"Heme","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/dim-research/17311915.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"4c3f047d0ee4583ca15aae2c7059d2237b02105371fda21bf32639cbaad2d318\", \"start_char\": 0, \"end_char\": 1400, \"text_sha256\": \"4c3f047d0ee4583ca15aae2c7059d2237b02105371fda21bf32639cbaad2d318\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"X-ray crystallography","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Alpha-naphthoflavone-bound structure at 1.95 angstrom resolution","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Structural enzyme requirement; not proof that DIM depletes iron or that iron supplementation changes DIM response.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"dim","display_name":"3,3'-Diindolylmethane / DIM","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Purified human CYP1A2","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The induced enzyme still needs its iron-containing catalytic machinery.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[dim-p17311915] Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2. (2007). https://pubmed.ncbi.nlm.nih.gov/17311915/ DOI: 10.1074/jbc.m611692200","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Catalytic pocket","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"87132e8d-0ec2-5f03-a7d0-0865340c101c","evidence_kind":"source_excerpt","locator":"Lines 259-270","start_line":259,"end_line":270,"excerpt":"### dim-cyp1a2-heme\nThe CYP1A2 structure places its ligand above the heme prosthetic group.\nCondition category: normal\nnutrient_topic: Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The induced enzyme still needs its iron-containing catalytic machinery.\norganism: Purified human CYP1A2\ntissue_or_cell_type: Catalytic pocket\nexperimental_model: X-ray crystallography\nlimitations: Structural enzyme requirement; not proof that DIM depletes iron or that iron supplementation changes DIM response.\nexposure: Alpha-naphthoflavone-bound structure at 1.95 angstrom resolution\nevidence_span: {\"source_cache\": \"artifacts/dim-research/17311915.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"4c3f047d0ee4583ca15aae2c7059d2237b02105371fda21bf32639cbaad2d318\", \"start_char\": 0, \"end_char\": 1400, \"text_sha256\": \"4c3f047d0ee4583ca15aae2c7059d2237b02105371fda21bf32639cbaad2d318\"}\n[dim-p17311915] Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2. (2007). https://pubmed.ncbi.nlm.nih.gov/17311915/ DOI: 10.1074/jbc.m611692200","model_system":"X-ray crystallography","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [dim-p17311915] Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2. (2007). https://pubmed.ncbi.nlm.nih.gov/17311915/ DOI: 10.1074/jbc.m611692200","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"b6d70682-97f9-5893-a03c-f9f88836033c","stable_key":"import-182336c6-ed36-5ec6-8a09-25c31096262e","title":"Diindolylmethane (DIM): formation, receptor signaling, metabolism and drug 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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