{"id":"8df223ed-55ad-54d0-8f3a-fbf4984d03ce","stable_key":"dc8975b1-95ff-5d9b-be17-a1c04610cca7:mo-aox-retinal","predicate":"contributes_to","statement":"A separable aldehyde-oxidase fraction accounted for some NAD-independent retinaldehyde metabolism in human liver and kidney extracts.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"6c57cd18-3484-52f7-a69c-02d40c9a8e9f","mechanism_event_label":"AOX1 intersects vitamin A chemistry, alongside other enzymes.","subject":{"id":"dcc4b976-aeb9-5dbd-8916-6507714db779","slug":"aox1","display_name":"Human aldehyde oxidase 1 / AOX1","entity_type_key":"protein"},"object":{"id":"dcd9aada-258d-5855-a5fb-591a177eb5a5","slug":"hepatic-retinal-oxidase-activity","display_name":"Hepatic retinal oxidase activity","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"6c57cd18-3484-52f7-a69c-02d40c9a8e9f","stable_key":"dc8975b1-95ff-5d9b-be17-a1c04610cca7:mo-aox-retinal-event","event_type":"biochemical_relationship","label":"AOX1 intersects vitamin A chemistry, alongside other enzymes.","description":"A separable aldehyde-oxidase fraction accounted for some NAD-independent retinaldehyde metabolism in human liver and kidney extracts.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"283ed24b-06a1-50aa-9281-df3bac6ce37e","slug":"nad-plus","display_name":"NAD+","entity_type_key":"small_molecule"},"role":"comparison cofactor","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"63693dbb-fe50-5a5d-ba37-7f78dab3f6ea","slug":"aldh1a1","display_name":"Aldehyde dehydrogenase 1A1 / ALDH1A1","entity_type_key":"protein"},"role":"major NAD-dependent pathway","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"dcc4b976-aeb9-5dbd-8916-6507714db779","slug":"aox1","display_name":"Human aldehyde oxidase 1 / AOX1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"dcd9aada-258d-5855-a5fb-591a177eb5a5","slug":"hepatic-retinal-oxidase-activity","display_name":"Hepatic retinal oxidase activity","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/molybdenum-research/10559215.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"a0a70e022e9499ca5d0608c1da80afadfad2215ac6cf1219c8ce8da3280a5238\", \"start_char\": 0, \"end_char\": 1879, \"text_sha256\": \"a0a70e022e9499ca5d0608c1da80afadfad2215ac6cf1219c8ce8da3280a5238\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Biochemical fractionation of four human livers and three kidneys","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Retinaldehyde and other aldehyde substrate assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Biochemical enzyme-fraction identification predates modern isoform assays; does not establish AOX1 as the dominant human retinoic-acid source or mineral-responsive route.","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","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"AOX1 intersects vitamin A chemistry, alongside other enzymes.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mo-p10559215] Metabolism of retinaldehyde and other aldehydes in soluble extracts of human liver and kidney. (1999). https://pubmed.ncbi.nlm.nih.gov/10559215/ DOI: 10.1074/jbc.274.47.33366","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Liver and kidney soluble extracts","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"420c5e92-1697-5d43-a2d4-854761293ee5","evidence_kind":"source_excerpt","locator":"Lines 885-896","start_line":885,"end_line":896,"excerpt":"### mo-aox-retinal\nA separable aldehyde-oxidase fraction accounted for some NAD-independent retinaldehyde metabolism in human liver and kidney extracts.\nCondition category: normal\nnutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: AOX1 intersects vitamin A chemistry, alongside other enzymes.\norganism: Homo sapiens\ntissue_or_cell_type: Liver and kidney soluble extracts\nexperimental_model: Biochemical fractionation of four human livers and three kidneys\nlimitations: Biochemical enzyme-fraction identification predates modern isoform assays; does not establish AOX1 as the dominant human retinoic-acid source or mineral-responsive route.\nexposure: Retinaldehyde and other aldehyde substrate assays\nevidence_span: {\"source_cache\": \"artifacts/molybdenum-research/10559215.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"a0a70e022e9499ca5d0608c1da80afadfad2215ac6cf1219c8ce8da3280a5238\", \"start_char\": 0, \"end_char\": 1879, \"text_sha256\": \"a0a70e022e9499ca5d0608c1da80afadfad2215ac6cf1219c8ce8da3280a5238\"}\n[mo-p10559215] Metabolism of retinaldehyde and other aldehydes in soluble extracts of human liver and kidney. 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