{"id":"054912d8-85fe-5b27-a152-f2f424d713eb","stable_key":"6612c190-1948-5bcf-bbe3-a7f6c50fa3cf:l-proline-pepd-recycling","predicate":"releases","statement":"Human prolidase hydrolyzes dipeptides with C-terminal proline or hydroxyproline; substrate- and product-bound structures explain its terminal peptide-cleavage reaction.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"1c284ca6-2229-5884-8076-67615eeee3d1","mechanism_event_label":"Recycling a proline-containing peptide requires a suitable peptidase.","subject":{"id":"fe1bbc6f-5c7d-5ae9-829c-e911804c23f7","slug":"pepd","display_name":"Human prolidase / PEPD","entity_type_key":"protein"},"object":{"id":"70ccd53c-83ad-5251-a4f5-6370973bc40a","slug":"l-proline","display_name":"L-Proline","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"1c284ca6-2229-5884-8076-67615eeee3d1","stable_key":"6612c190-1948-5bcf-bbe3-a7f6c50fa3cf:l-proline-pepd-recycling-event","event_type":"observed_relationship","label":"Recycling a proline-containing peptide requires a suitable peptidase.","description":"Human prolidase hydrolyzes dipeptides with C-terminal proline or hydroxyproline; substrate- and product-bound structures explain its terminal peptide-cleavage reaction.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"fe1bbc6f-5c7d-5ae9-829c-e911804c23f7","slug":"pepd","display_name":"Human prolidase / PEPD","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"70ccd53c-83ad-5251-a4f5-6370973bc40a","slug":"l-proline","display_name":"L-Proline","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"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":2,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant human wild-type prolidase, high-resolution substrate/product complexes.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"This does not mean prolidase by itself cleaves an intact collagen triple helix.","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":"Recycling a proline-containing peptide requires a suitable peptidase.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Substrate specificity and reaction mechanism of human prolidase. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28677335/ · DOI 10.1111/febs.14158","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"9d26add1-6f68-5675-8976-d538d84c35db","evidence_kind":"source_excerpt","locator":"Lines 262-268","start_line":262,"end_line":268,"excerpt":"## l-proline-pepd-recycling\nRecycling a proline-containing peptide requires a suitable peptidase.\nHuman prolidase hydrolyzes dipeptides with C-terminal proline or hydroxyproline; substrate- and product-bound structures explain its terminal peptide-cleavage reaction.\nModel: Recombinant human wild-type prolidase, high-resolution substrate/product complexes.\nLimitations: This does not mean prolidase by itself cleaves an intact collagen triple helix.\nEvidence access: Primary abstract\nSubstrate specificity and reaction mechanism of human prolidase. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28677335/ · DOI 10.1111/febs.14158","model_system":"Recombinant human wild-type prolidase, high-resolution substrate/product complexes.","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}