{"id":"5d7c2b43-3558-5fed-bdd2-e61141bb457a","stable_key":"9a47f338-d127-5e4d-abf6-e99056833a69:d-aspartate-ddo-imino","predicate":"converts_to","statement":"Porcine kidney DDO oxidized D-aspartate to iminoaspartate while reducing enzyme-bound FAD.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"f7bde59d-8a7a-52df-8dbb-1c1b9b8d064f","mechanism_event_label":"The first chemical step removes reducing equivalents from D-aspartate.","subject":{"id":"99492fdd-f4b3-5466-bfff-b45e80d71cbc","slug":"porcine-ddo","display_name":"Porcine D-aspartate oxidase / DDO","entity_type_key":"protein"},"object":{"id":"16f7d93a-3ba6-5767-a059-39acd97c6fca","slug":"iminoaspartate","display_name":"Iminoaspartate","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"f7bde59d-8a7a-52df-8dbb-1c1b9b8d064f","stable_key":"9a47f338-d127-5e4d-abf6-e99056833a69:d-aspartate-ddo-imino-event","event_type":"observed_relationship","label":"The first chemical step removes reducing equivalents from D-aspartate.","description":"Porcine kidney DDO oxidized D-aspartate to iminoaspartate while reducing enzyme-bound FAD.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"99492fdd-f4b3-5466-bfff-b45e80d71cbc","slug":"porcine-ddo","display_name":"Porcine D-aspartate oxidase / DDO","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"16f7d93a-3ba6-5767-a059-39acd97c6fca","slug":"iminoaspartate","display_name":"Iminoaspartate","entity_type_key":"small_molecule"},"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":""},{"entity":{"id":"e2cd7179-f218-54e8-9ce9-7a836ae35fac","slug":"fad","display_name":"FAD","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified native and recombinant porcine kidney enzyme.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Species-specific enzyme evidence; FAD is recycled rather than consumed once per substrate molecule.","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":"The first chemical step removes reducing equivalents from D-aspartate.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Functional and structural characterization of D-aspartate oxidase from porcine kidney: non-Michaelis kinetics due to substrate activation. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17234685/ · DOI 10.1093/jb/mvm041","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"9130b77e-9753-553e-a20f-db8095edda4d","evidence_kind":"source_excerpt","locator":"Lines 104-110","start_line":104,"end_line":110,"excerpt":"## d-aspartate-ddo-imino\nThe first chemical step removes reducing equivalents from D-aspartate.\nPorcine kidney DDO oxidized D-aspartate to iminoaspartate while reducing enzyme-bound FAD.\nModel: Purified native and recombinant porcine kidney enzyme.\nLimitations: Species-specific enzyme evidence; FAD is recycled rather than consumed once per substrate molecule.\nEvidence access: Primary abstract\nFunctional and structural characterization of D-aspartate oxidase from porcine kidney: non-Michaelis kinetics due to substrate activation. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17234685/ · DOI 10.1093/jb/mvm041","model_system":"Purified native and recombinant porcine kidney enzyme.","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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