{"id":"5df2ad4f-f27e-5bca-8339-7b5ec68309ea","stable_key":"dff9f743-3766-5f20-a71e-d6d2bd5bfb6f:va-rdh10-retinol-oxidation","predicate":"converts","statement":"Recombinant human RDH10 oxidized all-trans-retinol with NAD+ in microsomal assays.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"ea94bd22-46be-565f-a1fa-640b0eff0987","mechanism_event_label":"RDH10 uses the oxidized nicotinamide cofactor to make retinal.","subject":{"id":"89b4b04a-7637-56f4-ac55-501ad31d1f61","slug":"rdh10","display_name":"Retinol dehydrogenase 10 / RDH10","entity_type_key":"protein"},"object":{"id":"194eccf2-c7a5-52a6-a0c6-1c1f6d0f3a3e","slug":"all-trans-retinal","display_name":"All-trans-retinal","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"ea94bd22-46be-565f-a1fa-640b0eff0987","stable_key":"dff9f743-3766-5f20-a71e-d6d2bd5bfb6f:va-rdh10-retinol-oxidation-event","event_type":"biochemical_relationship","label":"RDH10 uses the oxidized nicotinamide cofactor to make retinal.","description":"Recombinant human RDH10 oxidized all-trans-retinol with NAD+ in microsomal assays.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"148c57d8-c658-5769-89e8-1194cef2a782","slug":"retinol","display_name":"All-trans-retinol","entity_type_key":"small_molecule"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"283ed24b-06a1-50aa-9281-df3bac6ce37e","slug":"nad-plus","display_name":"NAD+","entity_type_key":"small_molecule"},"role":"oxidizing-cofactor","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"9fbf2e03-16a9-5ca7-965c-0bfc07ca24da","slug":"nadh","display_name":"NADH","entity_type_key":"small_molecule"},"role":"reduced-cofactor-product","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"89b4b04a-7637-56f4-ac55-501ad31d1f61","slug":"rdh10","display_name":"Retinol dehydrogenase 10 / RDH10","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"194eccf2-c7a5-52a6-a0c6-1c1f6d0f3a3e","slug":"all-trans-retinal","display_name":"All-trans-retinal","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"cross_nutrient","value_text":"NAD-dependent retinol oxidation connects vitamin A metabolism to nicotinamide redox-cofactor availability.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"evidence_location","value_text":"Results: cofactor preference","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human RDH10 in Sf9 microsomes and siRNA perturbation in human cells.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"1 micromolar retinol and 1 millimolar NAD+ versus NADP+.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Cofactor specificity does not establish an effect of dietary niacin deficiency.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Vitamin A research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"vitamin-a","display_name":"Vitamin A","entity_type_key":"chemical_species"}},{"dimension":"organism","value_text":"Homo sapiens protein in Spodoptera frugiperda Sf9 cells","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"outcome","value_text":"Recombinant human RDH10 oxidized all-trans-retinol with NAD+ in microsomal assays.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"RDH10 uses the oxidized nicotinamide cofactor to make retinal.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[va-belyaeva-2008] Kinetic Analysis of Human Enzyme RDH10 Defines the Characteristics of a Physiologically Relevant Retinol Dehydrogenase (2008). https://pmc.ncbi.nlm.nih.gov/articles/PMC2459273/ DOI: 10.1074/jbc.M800019200","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Microsomes","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"dc36c7b9-6598-5efe-92d7-ce601e17d98d","evidence_kind":"source_excerpt","locator":"Lines 487-500","start_line":487,"end_line":500,"excerpt":"### va-rdh10-retinol-oxidation\nRecombinant human RDH10 oxidized all-trans-retinol with NAD+ in microsomal assays.\nCondition category: normal\nnutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: RDH10 uses the oxidized nicotinamide cofactor to make retinal.\norganism: Homo sapiens protein in Spodoptera frugiperda Sf9 cells\ntissue_or_cell_type: Microsomes\nexperimental_model: Human RDH10 in Sf9 microsomes and siRNA perturbation in human cells.\nlimitations: Cofactor specificity does not establish an effect of dietary niacin deficiency.\nexposure: 1 micromolar retinol and 1 millimolar NAD+ versus NADP+.\noutcome: Recombinant human RDH10 oxidized all-trans-retinol with NAD+ in microsomal assays.\nevidence_location: Results: cofactor preference\ncross_nutrient: NAD-dependent retinol oxidation connects vitamin A metabolism to nicotinamide redox-cofactor availability.\n[va-belyaeva-2008] Kinetic Analysis of Human Enzyme RDH10 Defines the Characteristics of a Physiologically Relevant Retinol Dehydrogenase (2008). https://pmc.ncbi.nlm.nih.gov/articles/PMC2459273/ DOI: 10.1074/jbc.M800019200","model_system":"Human RDH10 in Sf9 microsomes and siRNA perturbation in human cells.","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [va-belyaeva-2008] Kinetic Analysis of Human Enzyme RDH10 Defines the Characteristics of a Physiologically Relevant Retinol Dehydrogenase (2008). https://pmc.ncbi.nlm.nih.gov/articles/PMC2459273/ DOI: 10.1074/jbc.M800019200","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"0c5474e2-be48-547b-b287-9c07a59c9ff1","stable_key":"import-dff9f743-3766-5f20-a71e-d6d2bd5bfb6f","title":"Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text.","file_path":"","sha256":"b217224b262abbd77d6a0c8c9beefff9c022fae4d31e2a5273915d769b9a6546","revision_id":"61008909-871f-575c-b5e2-21542689ea3c","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}