{"id":"311a4424-7e7d-5e91-9db8-a50f5ff2507f","stable_key":"dff9f743-3766-5f20-a71e-d6d2bd5bfb6f:va-aldh1a1-retinal-oxidation","predicate":"converts","statement":"Human ALDH1A1 oxidized all-trans-retinaldehyde to retinoic acid in comparative enzyme assays.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"8b5751e2-fcf7-529b-8fba-c2f98f922472","mechanism_event_label":"This independently identified enzyme supplies the acid form used for signaling.","subject":{"id":"63693dbb-fe50-5a5d-ba37-7f78dab3f6ea","slug":"aldh1a1","display_name":"Aldehyde dehydrogenase 1A1 / ALDH1A1","entity_type_key":"protein"},"object":{"id":"05487b29-8c59-5af8-83cf-cf9c79c5ecb8","slug":"all-trans-retinoic-acid","display_name":"All-trans-retinoic acid","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"8b5751e2-fcf7-529b-8fba-c2f98f922472","stable_key":"dff9f743-3766-5f20-a71e-d6d2bd5bfb6f:va-aldh1a1-retinal-oxidation-event","event_type":"biochemical_relationship","label":"This independently identified enzyme supplies the acid form used for signaling.","description":"Human ALDH1A1 oxidized all-trans-retinaldehyde to retinoic acid in comparative enzyme assays.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"194eccf2-c7a5-52a6-a0c6-1c1f6d0f3a3e","slug":"all-trans-retinal","display_name":"All-trans-retinal","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":"63693dbb-fe50-5a5d-ba37-7f78dab3f6ea","slug":"aldh1a1","display_name":"Aldehyde dehydrogenase 1A1 / ALDH1A1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"05487b29-8c59-5af8-83cf-cf9c79c5ecb8","slug":"all-trans-retinoic-acid","display_name":"All-trans-retinoic acid","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_location","value_text":"Abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Side-by-side recombinant human ALDH1A1, ALDH1A2 and ALDH1A3 kinetic assays.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Side-by-side retinaldehyde kinetic measurements by HPLC.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"In vitro catalytic efficiency does not specify its contribution in a particular tissue.","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 recombinant protein","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"outcome","value_text":"Human ALDH1A1 oxidized all-trans-retinaldehyde to retinoic acid in comparative enzyme assays.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"This independently identified enzyme supplies the acid form used for signaling.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[va-pequerul-2020] Structural and kinetic features of aldehyde dehydrogenase 1A (ALDH1A) subfamily members, cancer stem cell markers active in retinoic acid biosynthesis (2020). https://pubmed.ncbi.nlm.nih.gov/31923393/ DOI: 10.1016/j.abb.2020.108256","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Cell-free enzyme","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"632ff93f-a7f1-577c-bad8-6bf794148729","evidence_kind":"source_excerpt","locator":"Lines 559-571","start_line":559,"end_line":571,"excerpt":"### va-aldh1a1-retinal-oxidation\nHuman ALDH1A1 oxidized all-trans-retinaldehyde to retinoic acid in comparative enzyme assays.\nCondition category: normal\nnutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: This independently identified enzyme supplies the acid form used for signaling.\norganism: Homo sapiens recombinant protein\ntissue_or_cell_type: Cell-free enzyme\nexperimental_model: Side-by-side recombinant human ALDH1A1, ALDH1A2 and ALDH1A3 kinetic assays.\nlimitations: In vitro catalytic efficiency does not specify its contribution in a particular tissue.\nexposure: Side-by-side retinaldehyde kinetic measurements by HPLC.\noutcome: Human ALDH1A1 oxidized all-trans-retinaldehyde to retinoic acid in comparative enzyme assays.\nevidence_location: Abstract\n[va-pequerul-2020] Structural and kinetic features of aldehyde dehydrogenase 1A (ALDH1A) subfamily members, cancer stem cell markers active in retinoic acid biosynthesis (2020). https://pubmed.ncbi.nlm.nih.gov/31923393/ DOI: 10.1016/j.abb.2020.108256","model_system":"Side-by-side recombinant human ALDH1A1, ALDH1A2 and ALDH1A3 kinetic assays.","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [va-pequerul-2020] Structural and kinetic features of aldehyde dehydrogenase 1A (ALDH1A) subfamily members, cancer stem cell markers active in retinoic acid biosynthesis (2020). https://pubmed.ncbi.nlm.nih.gov/31923393/ DOI: 10.1016/j.abb.2020.108256","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}