{"id":"f3c22d5b-562b-5282-9d81-671add80201a","stable_key":"6612c190-1948-5bcf-bbe3-a7f6c50fa3cf:l-proline-hypdh-electrons","predicate":"transfers_electrons_to","statement":"Quinone acceptors including CoQ1 reacted more efficiently than oxygen during purified human HYPDH turnover, supporting a dehydrogenase mechanism.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"7b3dab5f-e37b-5665-8dce-03d23b10752c","mechanism_event_label":"Hydroxyproline breakdown can feed a quinone electron-transfer route.","subject":{"id":"4ef530a0-8fa3-54f7-b1f6-cb2cd53e2456","slug":"prodh2","display_name":"Human hydroxyproline dehydrogenase / PRODH2","entity_type_key":"protein"},"object":{"id":"41633de0-0bf7-5c19-913c-754af183598f","slug":"coenzyme-q1","display_name":"Coenzyme Q1, experimental ubiquinone analogue","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"7b3dab5f-e37b-5665-8dce-03d23b10752c","stable_key":"6612c190-1948-5bcf-bbe3-a7f6c50fa3cf:l-proline-hypdh-electrons-event","event_type":"observed_relationship","label":"Hydroxyproline breakdown can feed a quinone electron-transfer route.","description":"Quinone acceptors including CoQ1 reacted more efficiently than oxygen during purified human HYPDH turnover, supporting a dehydrogenase mechanism.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"4ef530a0-8fa3-54f7-b1f6-cb2cd53e2456","slug":"prodh2","display_name":"Human hydroxyproline dehydrogenase / PRODH2","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"41633de0-0bf7-5c19-913c-754af183598f","slug":"coenzyme-q1","display_name":"Coenzyme Q1, experimental ubiquinone analogue","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":""},{"entity":{"id":"6e07a914-e6e5-5f23-b0e4-36d9481191af","slug":"hydroxyproline","display_name":"4-Hydroxyproline","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Truncated purified human HYPDH; quinone analogue and oxygen comparisons.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"CoQ10 as the physiological acceptor is inferred, not directly measured in intact human tissues; this does not demonstrate benefit from CoQ10 supplements.","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":"Hydroxyproline breakdown can feed a quinone electron-transfer route.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25697095/ · DOI 10.1042/BJ20141159","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"53ad7757-68ca-5030-92f6-00b981569d4f","evidence_kind":"source_excerpt","locator":"Lines 286-292","start_line":286,"end_line":292,"excerpt":"## l-proline-hypdh-electrons\nHydroxyproline breakdown can feed a quinone electron-transfer route.\nQuinone acceptors including CoQ1 reacted more efficiently than oxygen during purified human HYPDH turnover, supporting a dehydrogenase mechanism.\nModel: Truncated purified human HYPDH; quinone analogue and oxygen comparisons.\nLimitations: CoQ10 as the physiological acceptor is inferred, not directly measured in intact human tissues; this does not demonstrate benefit from CoQ10 supplements.\nEvidence access: Primary abstract\nProline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25697095/ · DOI 10.1042/BJ20141159","model_system":"Truncated purified human HYPDH; quinone analogue and oxygen comparisons.","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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