{"id":"0f792080-2a54-5282-b7d1-3266fdc52db1","stable_key":"548ab9d6-3a9b-5bed-879c-17d03813b636:transport-flad1-fad-binding","predicate":"binds","statement":"Purified human FADS2 retained approximately one FAD per enzyme noncovalently; complete release required extensive denaturation.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"e45e8816-3a34-588d-b981-7569d6101be2","mechanism_event_label":"FAD can remain tightly associated with the enzyme that makes it.","subject":{"id":"992093d2-2665-50b6-8681-95705f09322b","slug":"flad1-isoform-2","display_name":"Human FAD synthetase isoform 2","entity_type_key":"protein"},"object":{"id":"e2cd7179-f218-54e8-9ce9-7a836ae35fac","slug":"fad","display_name":"FAD","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"e45e8816-3a34-588d-b981-7569d6101be2","stable_key":"548ab9d6-3a9b-5bed-879c-17d03813b636:transport-flad1-fad-binding-event","event_type":"biochemical_relationship","label":"FAD can remain tightly associated with the enzyme that makes it.","description":"Purified human FADS2 retained approximately one FAD per enzyme noncovalently; complete release required extensive denaturation.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"992093d2-2665-50b6-8681-95705f09322b","slug":"flad1-isoform-2","display_name":"Human FAD synthetase isoform 2","entity_type_key":"protein"},"role":"binding-protein","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"e2cd7179-f218-54e8-9ce9-7a836ae35fac","slug":"fad","display_name":"FAD","entity_type_key":"small_molecule"},"role":"bound-product","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"evidence_location","value_text":"Abstract; bound-FAD measurements","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified His-tagged human FADS2 binding and denaturation assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Isolated enzyme, chaotrope treatment and denaturation.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Product retention alone does not prove direct delivery to every cellular flavoprotein.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Riboflavin research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"riboflavin","display_name":"Riboflavin (vitamin B2)","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Homo sapiens","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"FAD can remain tightly associated with the enzyme that makes it.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[transport-fads2-2011] Human FAD synthase (isoform 2): a component of the machinery that delivers FAD to apo-flavoproteins. (2011). https://pubmed.ncbi.nlm.nih.gov/21951714/ DOI: 10.1111/j.1742-4658.2011.08368.x","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified enzyme","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"0527fa29-3c75-5d31-b81d-a8ac72361a70","evidence_kind":"source_excerpt","locator":"Lines 373-384","start_line":373,"end_line":384,"excerpt":"### transport-flad1-fad-binding\nPurified human FADS2 retained approximately one FAD per enzyme noncovalently; complete release required extensive denaturation.\nCondition category: normal\nnutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: FAD can remain tightly associated with the enzyme that makes it.\norganism: Homo sapiens\ntissue_or_cell_type: Purified enzyme\nexperimental_model: Purified His-tagged human FADS2 binding and denaturation assays\nlimitations: Product retention alone does not prove direct delivery to every cellular flavoprotein.\nexposure: Isolated enzyme, chaotrope treatment and denaturation.\nevidence_location: Abstract; bound-FAD measurements\n[transport-fads2-2011] Human FAD synthase (isoform 2): a component of the machinery that delivers FAD to apo-flavoproteins. (2011). https://pubmed.ncbi.nlm.nih.gov/21951714/ DOI: 10.1111/j.1742-4658.2011.08368.x","model_system":"Purified His-tagged human FADS2 binding and denaturation assays","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [transport-fads2-2011] Human FAD synthase (isoform 2): a component of the machinery that delivers FAD to apo-flavoproteins. (2011). https://pubmed.ncbi.nlm.nih.gov/21951714/ DOI: 10.1111/j.1742-4658.2011.08368.x","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"4f7c9578-82bf-5e2d-b5c4-72a79fb4f6af","stable_key":"import-548ab9d6-3a9b-5bed-879c-17d03813b636","title":"Riboflavin: mechanisms, deficiency 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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