{"id":"63643502-a93d-5552-9b8d-7e1bc589add9","stable_key":"6612c190-1948-5bcf-bbe3-a7f6c50fa3cf:l-proline-prodh-oxidation","predicate":"oxidizes_proline_to","statement":"Mitochondrial PRODH catalyzes the FAD-dependent oxidation of proline to P5C, linking proline breakdown to mitochondrial electron transfer.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"8c8dae79-a499-500c-a0fa-57b3c3737a28","mechanism_event_label":"Breaking proline down starts with a flavin-dependent mitochondrial enzyme.","subject":{"id":"5e13a254-f92e-5317-abb5-2c683b178d39","slug":"prodh","display_name":"Human proline dehydrogenase / PRODH","entity_type_key":"protein"},"object":{"id":"cbf8b66e-3d66-53f0-9c21-bc9c014131e7","slug":"pyrroline-5-carboxylate","display_name":"Delta-1-pyrroline-5-carboxylate / P5C","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"8c8dae79-a499-500c-a0fa-57b3c3737a28","stable_key":"6612c190-1948-5bcf-bbe3-a7f6c50fa3cf:l-proline-prodh-oxidation-event","event_type":"observed_relationship","label":"Breaking proline down starts with a flavin-dependent mitochondrial enzyme.","description":"Mitochondrial PRODH catalyzes the FAD-dependent oxidation of proline to P5C, linking proline breakdown to mitochondrial electron transfer.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"5e13a254-f92e-5317-abb5-2c683b178d39","slug":"prodh","display_name":"Human proline dehydrogenase / PRODH","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"cbf8b66e-3d66-53f0-9c21-bc9c014131e7","slug":"pyrroline-5-carboxylate","display_name":"Delta-1-pyrroline-5-carboxylate / P5C","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"70ccd53c-83ad-5251-a4f5-6370973bc40a","slug":"l-proline","display_name":"L-Proline","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 full text; background reaction distinguished from new experiments","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Established reaction described in a primary mitochondrial proline-oxidation study.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"The reaction description is biochemical background, distinct from the paper-specific ROS-site experiments.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-proline","display_name":"L-Proline","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Breaking proline down starts with a flavin-dependent mitochondrial enzyme.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Sources of superoxide/H2O2 during mitochondrial proline oxidation. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25184115/ · DOI 10.1016/j.redox.2014.07.003","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"f70cb87f-ee68-568e-8cb0-29838e49f46a","evidence_kind":"source_excerpt","locator":"Lines 94-100","start_line":94,"end_line":100,"excerpt":"## l-proline-prodh-oxidation\nBreaking proline down starts with a flavin-dependent mitochondrial enzyme.\nMitochondrial PRODH catalyzes the FAD-dependent oxidation of proline to P5C, linking proline breakdown to mitochondrial electron transfer.\nModel: Established reaction described in a primary mitochondrial proline-oxidation study.\nLimitations: The reaction description is biochemical background, distinct from the paper-specific ROS-site experiments.\nEvidence access: Primary full text; background reaction distinguished from new experiments\nSources of superoxide/H2O2 during mitochondrial proline oxidation. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25184115/ · DOI 10.1016/j.redox.2014.07.003","model_system":"Established reaction described in a primary mitochondrial proline-oxidation study.","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":"e5aa7fc5-ee52-5376-8169-416082a89fd1","stable_key":"import-6612c190-1948-5bcf-bbe3-a7f6c50fa3cf","title":"L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient 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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