{"id":"e535f745-3d4f-5dc9-bdbe-ea96fddda31f","stable_key":"6612c190-1948-5bcf-bbe3-a7f6c50fa3cf:l-proline-hypdh-specificity","predicate":"preferentially_oxidizes","statement":"Purified truncated human PRODH2/HYPDH contained one FAD and showed approximately twelvefold higher catalytic efficiency for hydroxyproline than proline.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"24ec0f96-4051-53a9-8939-4d274777bd55","mechanism_event_label":"Hydroxyproline uses a related but distinct breakdown enzyme.","subject":{"id":"4ef530a0-8fa3-54f7-b1f6-cb2cd53e2456","slug":"prodh2","display_name":"Human hydroxyproline dehydrogenase / PRODH2","entity_type_key":"protein"},"object":{"id":"6e07a914-e6e5-5f23-b0e4-36d9481191af","slug":"hydroxyproline","display_name":"4-Hydroxyproline","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"24ec0f96-4051-53a9-8939-4d274777bd55","stable_key":"6612c190-1948-5bcf-bbe3-a7f6c50fa3cf:l-proline-hypdh-specificity-event","event_type":"observed_relationship","label":"Hydroxyproline uses a related but distinct breakdown enzyme.","description":"Purified truncated human PRODH2/HYPDH contained one FAD and showed approximately twelvefold higher catalytic efficiency for hydroxyproline than proline.","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":"6e07a914-e6e5-5f23-b0e4-36d9481191af","slug":"hydroxyproline","display_name":"4-Hydroxyproline","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":"5e13a254-f92e-5317-abb5-2c683b178d39","slug":"prodh","display_name":"Human proline dehydrogenase / PRODH","entity_type_key":"protein"},"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":"Human recombinant catalytic core, residues 157–515; substrate kinetics.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"PRODH2 is not simply a second interchangeable proline oxidase.","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 uses a related but distinct breakdown enzyme.","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":"2c6f7cb2-0995-539b-82c8-647634af8288","evidence_kind":"source_excerpt","locator":"Lines 278-284","start_line":278,"end_line":284,"excerpt":"## l-proline-hypdh-specificity\nHydroxyproline uses a related but distinct breakdown enzyme.\nPurified truncated human PRODH2/HYPDH contained one FAD and showed approximately twelvefold higher catalytic efficiency for hydroxyproline than proline.\nModel: Human recombinant catalytic core, residues 157–515; substrate kinetics.\nLimitations: PRODH2 is not simply a second interchangeable proline oxidase.\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":"Human recombinant catalytic core, residues 157–515; substrate kinetics.","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. Not publisher full text.","file_path":"","sha256":"7b7f1981f9c7897fbb6baa19425bdc19dede78ad4d66fa554394b8337c7366fb","revision_id":"4971a925-fa70-59f8-8030-d3029a18a62f","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}