{"id":"2907aee7-be79-583c-be15-ad4de26d3f91","stable_key":"548ab9d6-3a9b-5bed-879c-17d03813b636:transport-flad1-adenylylation","predicate":"converts","statement":"Human FAD synthase isoform 2 adenylylates FMN with ATP to form FAD and pyrophosphate.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"10fe8108-edb4-5959-8ea6-9ace4c21df16","mechanism_event_label":"FLAD1 performs the second activation step, making FAD from FMN.","subject":{"id":"992093d2-2665-50b6-8681-95705f09322b","slug":"flad1-isoform-2","display_name":"Human FAD synthetase isoform 2","entity_type_key":"protein"},"object":{"id":"d3eacf85-1a35-546d-bd30-161474dd9691","slug":"fmn","display_name":"Flavin mononucleotide","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"10fe8108-edb4-5959-8ea6-9ace4c21df16","stable_key":"548ab9d6-3a9b-5bed-879c-17d03813b636:transport-flad1-adenylylation-event","event_type":"biochemical_relationship","label":"FLAD1 performs the second activation step, making FAD from FMN.","description":"Human FAD synthase isoform 2 adenylylates FMN with ATP to form FAD and pyrophosphate.","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":"enzyme","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"d3eacf85-1a35-546d-bd30-161474dd9691","slug":"fmn","display_name":"Flavin mononucleotide","entity_type_key":"small_molecule"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"58b974f1-d389-5bf6-81cd-889c44442c42","slug":"atp","display_name":"ATP","entity_type_key":"small_molecule"},"role":"adenylyl-donor","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"e2cd7179-f218-54e8-9ce9-7a836ae35fac","slug":"fad","display_name":"FAD","entity_type_key":"small_molecule"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"cd026fef-529f-5e03-b6b5-37ede8ce9127","slug":"pyrophosphate","display_name":"Inorganic pyrophosphate","entity_type_key":"small_molecule"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_location","value_text":"FAD synthesis and reverse pyrophosphorolysis assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified recombinant human FADS2 catalytic assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"ATP and FMN in FAD-synthesis assays.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Adenylylation is distinct from RFK phosphorylation; reaction products should not be conflated.","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":"FLAD1 performs the second activation step, making FAD from FMN.","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 protein","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"04b84142-92f7-556b-940c-5b2c7d112773","evidence_kind":"source_excerpt","locator":"Lines 320-331","start_line":320,"end_line":331,"excerpt":"### transport-flad1-adenylylation\nHuman FAD synthase isoform 2 adenylylates FMN with ATP to form FAD and pyrophosphate.\nCondition category: normal\nnutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: FLAD1 performs the second activation step, making FAD from FMN.\norganism: Homo sapiens\ntissue_or_cell_type: Purified protein\nexperimental_model: Purified recombinant human FADS2 catalytic assays\nlimitations: Adenylylation is distinct from RFK phosphorylation; reaction products should not be conflated.\nexposure: ATP and FMN in FAD-synthesis assays.\nevidence_location: FAD synthesis and reverse pyrophosphorolysis assays\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 recombinant human FADS2 catalytic 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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