{"id":"3be41a03-4430-5658-bad3-575133cb3a9d","stable_key":"6612c190-1948-5bcf-bbe3-a7f6c50fa3cf:l-proline-pycr1-reduction","predicate":"reduces_p5c_to","statement":"Recombinant human PYCR1 reduced P5C to proline with NADH or NADPH; in the tested conditions its specific activity was higher with NADH.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"79507252-e7d3-5b4a-bbcb-868d0e49eab6","mechanism_event_label":"One mitochondrial enzyme finishes the synthesis of proline.","subject":{"id":"6a5e6627-f4fd-5a02-b74b-371b629b076b","slug":"pycr1","display_name":"Human pyrroline-5-carboxylate reductase 1 / PYCR1","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":"79507252-e7d3-5b4a-bbcb-868d0e49eab6","stable_key":"6612c190-1948-5bcf-bbe3-a7f6c50fa3cf:l-proline-pycr1-reduction-event","event_type":"observed_relationship","label":"One mitochondrial enzyme finishes the synthesis of proline.","description":"Recombinant human PYCR1 reduced P5C to proline with NADH or NADPH; 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comparison with 0.1 mM P5C and 0.1 mM reduced cofactor, 37 degrees C.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Cofactor preference depends on assay conditions and does not make the alternative cofactor unusable.","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":"One mitochondrial enzyme finishes the synthesis of proline.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Functional specialization in proline biosynthesis of melanoma. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23024808/ · DOI 10.1371/journal.pone.0045190","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"5e1e8842-6a2e-5512-99f3-c1e2ed9f86b6","evidence_kind":"source_excerpt","locator":"Lines 14-20","start_line":14,"end_line":20,"excerpt":"## l-proline-pycr1-reduction\nOne mitochondrial enzyme finishes the synthesis of proline.\nRecombinant human PYCR1 reduced P5C to proline with NADH or NADPH; in the tested conditions its specific activity was higher with NADH.\nModel: Purified human enzyme; comparison with 0.1 mM P5C and 0.1 mM reduced cofactor, 37 degrees C.\nLimitations: Cofactor preference depends on assay conditions and does not make the alternative cofactor unusable.\nEvidence access: Primary full text\nFunctional specialization in proline biosynthesis of melanoma. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23024808/ · DOI 10.1371/journal.pone.0045190","model_system":"Purified human enzyme; comparison with 0.1 mM P5C and 0.1 mM reduced cofactor, 37 degrees C.","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; 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