{"id":"06fd4bd6-7ac7-5696-a132-b41baa612390","stable_key":"9a47f338-d127-5e4d-abf6-e99056833a69:d-aspartate-ddo-fad","predicate":"binds","statement":"Human D-aspartate oxidase structure and kinetics showed a FAD-containing enzyme with higher FAD affinity than human D-amino-acid oxidase.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"0f40f423-6bd0-5e91-a827-10bae82affe0","mechanism_event_label":"Two similarly named enzymes handle different D-amino-acid pathways and bind their cofactor differently.","subject":{"id":"e2cd7179-f218-54e8-9ce9-7a836ae35fac","slug":"fad","display_name":"FAD","entity_type_key":"small_molecule"},"object":{"id":"17871951-099f-5a48-832e-ff9cb1c65755","slug":"ddo","display_name":"Human D-aspartate oxidase / DDO","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"0f40f423-6bd0-5e91-a827-10bae82affe0","stable_key":"9a47f338-d127-5e4d-abf6-e99056833a69:d-aspartate-ddo-fad-event","event_type":"observed_relationship","label":"Two similarly named enzymes handle different D-amino-acid pathways and bind their cofactor differently.","description":"Human D-aspartate oxidase structure and kinetics showed a FAD-containing enzyme with higher FAD affinity than human D-amino-acid oxidase.","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":"17871951-099f-5a48-832e-ff9cb1c65755","slug":"ddo","display_name":"Human D-aspartate oxidase / DDO","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"b3404670-6db1-517f-b9a0-27ecfaac558b","slug":"d-aspartate","display_name":"D-Aspartate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified human DASPO/DDO structural and kinetic comparison with human DAO.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Does not show that dietary riboflavin limits DDO in vivo or that DAO inhibitors also inhibit DDO.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"D-Aspartate collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"d-aspartate","display_name":"D-Aspartate","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Two similarly named enzymes handle different D-amino-acid pathways and bind their cofactor differently.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Structure and kinetic properties of human d-aspartate oxidase, the enzyme-controlling d-aspartate levels in brain. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31914658/ · DOI 10.1096/fj.201901703R","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"46843398-d32b-5284-9766-38fa68a1f11e","evidence_kind":"source_excerpt","locator":"Lines 96-102","start_line":96,"end_line":102,"excerpt":"## d-aspartate-ddo-fad\nTwo similarly named enzymes handle different D-amino-acid pathways and bind their cofactor differently.\nHuman D-aspartate oxidase structure and kinetics showed a FAD-containing enzyme with higher FAD affinity than human D-amino-acid oxidase.\nModel: Purified human DASPO/DDO structural and kinetic comparison with human DAO.\nLimitations: Does not show that dietary riboflavin limits DDO in vivo or that DAO inhibitors also inhibit DDO.\nEvidence access: Primary abstract\nStructure and kinetic properties of human d-aspartate oxidase, the enzyme-controlling d-aspartate levels in brain. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31914658/ · DOI 10.1096/fj.201901703R","model_system":"Purified human DASPO/DDO structural and kinetic comparison with human DAO.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; evidence access and experimental limitations specified.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"3751103e-e256-5615-b24f-39cc76ccfb47","stable_key":"import-9a47f338-d127-5e4d-abf6-e99056833a69","title":"D-Aspartate: synthesis, clearance, neural and endocrine mechanisms (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. 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