{"id":"d9232c7b-1bf6-5259-8717-1a8d683c6a5b","stable_key":"dc8975b1-95ff-5d9b-be17-a1c04610cca7:mo-aox-fad","predicate":"is_bound_cofactor_of","statement":"AOX1-bound FAD acted as the intrinsic fluorescence reporter in ThermoFAD unfolding assays.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"ced44140-b2a0-519f-8518-b62954c0911f","mechanism_event_label":"The molybdenum enzyme also contains a riboflavin-derived cofactor.","subject":{"id":"e2cd7179-f218-54e8-9ce9-7a836ae35fac","slug":"fad","display_name":"FAD","entity_type_key":"small_molecule"},"object":{"id":"dcc4b976-aeb9-5dbd-8916-6507714db779","slug":"aox1","display_name":"Human aldehyde oxidase 1 / AOX1","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"ced44140-b2a0-519f-8518-b62954c0911f","stable_key":"dc8975b1-95ff-5d9b-be17-a1c04610cca7:mo-aox-fad-event","event_type":"biochemical_relationship","label":"The molybdenum enzyme also contains a riboflavin-derived cofactor.","description":"AOX1-bound FAD acted as the intrinsic fluorescence reporter in ThermoFAD unfolding assays.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"e2cd7179-f218-54e8-9ce9-7a836ae35fac","slug":"fad","display_name":"FAD","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"dcc4b976-aeb9-5dbd-8916-6507714db779","slug":"aox1","display_name":"Human aldehyde oxidase 1 / AOX1","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/molybdenum-research/30985987.fulltext.txt\", \"locator\": \"Exact primary full-text span; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"d187787b0c042c674903c56275b485ee23c2b3545ed1c0ed02ca0cd2e3abb7c0\", \"start_char\": 11532, \"end_char\": 12101, \"text_sha256\": \"13ae767e495f8efc3a6c44005156563bc471d8aec37486330086d3fed343ef38\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human AOX1 variant crystallography and CD/ThermoFAD stability assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Wild type compared with SNP variants","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"In-vitro structures and thermal stability; not physiological temperature or diet thresholds.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Molybdenum research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"molybdenum","display_name":"Molybdenum","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Homo sapiens protein","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The molybdenum enzyme also contains a riboflavin-derived cofactor.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mo-p30985987] Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms. 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