{"id":"86900a63-8c5d-5e96-beb9-90e8dbcece8f","stable_key":"9a47f338-d127-5e4d-abf6-e99056833a69:d-aspartate-ddo-peroxide","predicate":"produces","statement":"Reoxidation of reduced FAD by oxygen during porcine DDO turnover produced hydrogen peroxide.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"5f89da19-d020-53f5-9a1f-f09054bc80c4","mechanism_event_label":"Clearing D-aspartate also generates a peroxide-handling requirement.","subject":{"id":"99492fdd-f4b3-5466-bfff-b45e80d71cbc","slug":"porcine-ddo","display_name":"Porcine D-aspartate oxidase / DDO","entity_type_key":"protein"},"object":{"id":"da9d64bc-69d4-5d97-90a4-8f0ed03e0ac8","slug":"hydrogen-peroxide","display_name":"Hydrogen peroxide","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"5f89da19-d020-53f5-9a1f-f09054bc80c4","stable_key":"9a47f338-d127-5e4d-abf6-e99056833a69:d-aspartate-ddo-peroxide-event","event_type":"observed_relationship","label":"Clearing D-aspartate also generates a peroxide-handling requirement.","description":"Reoxidation of reduced FAD by oxygen during porcine DDO turnover produced hydrogen peroxide.","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":"da9d64bc-69d4-5d97-90a4-8f0ed03e0ac8","slug":"hydrogen-peroxide","display_name":"Hydrogen peroxide","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":""},{"entity":{"id":"899c7ab0-6f81-5b38-a6bd-fbb33d66ac8d","slug":"oxygen","display_name":"Molecular oxygen","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"16f7d93a-3ba6-5767-a059-39acd97c6fca","slug":"iminoaspartate","display_name":"Iminoaspartate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified porcine enzyme oxidative half-reaction.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"This chemistry alone does not demonstrate oxidative injury after human oral supplementation.","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":"Clearing D-aspartate also generates a peroxide-handling requirement.","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":"96ba9a6a-8550-5896-83b9-b4e9d00c1cb8","evidence_kind":"source_excerpt","locator":"Lines 112-118","start_line":112,"end_line":118,"excerpt":"## d-aspartate-ddo-peroxide\nClearing D-aspartate also generates a peroxide-handling requirement.\nReoxidation of reduced FAD by oxygen during porcine DDO turnover produced hydrogen peroxide.\nModel: Purified porcine enzyme oxidative half-reaction.\nLimitations: This chemistry alone does not demonstrate oxidative injury after human oral supplementation.\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 porcine enzyme oxidative half-reaction.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; 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