{"id":"36a0dfa6-8905-5069-82d3-53e4bd51e381","stable_key":"6612c190-1948-5bcf-bbe3-a7f6c50fa3cf:l-proline-eprs-charging","predicate":"charges","statement":"The prolyl-tRNA synthetase domain of human EPRS attaches proline to its cognate tRNA in an ATP-dependent aminoacylation reaction.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"1bdfb1e4-a26d-572e-b3c5-9bb4d869fcb1","mechanism_event_label":"A protein-building block must first be loaded onto the correct tRNA.","subject":{"id":"a0af759a-af37-5303-a1de-f90380b527c0","slug":"eprs1","display_name":"Human glutamyl-prolyl-tRNA synthetase / EPRS1","entity_type_key":"protein"},"object":{"id":"c1de32ab-9b92-509f-a5b0-08a39e67b8fa","slug":"human-trna-pro","display_name":"Human cytosolic tRNA(Pro)","entity_type_key":"rna"},"evidence_count":1,"mechanism_event":{"id":"1bdfb1e4-a26d-572e-b3c5-9bb4d869fcb1","stable_key":"6612c190-1948-5bcf-bbe3-a7f6c50fa3cf:l-proline-eprs-charging-event","event_type":"observed_relationship","label":"A protein-building block must first be loaded onto the correct tRNA.","description":"The prolyl-tRNA synthetase domain of human EPRS attaches proline to its cognate tRNA in an ATP-dependent aminoacylation reaction.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"a0af759a-af37-5303-a1de-f90380b527c0","slug":"eprs1","display_name":"Human glutamyl-prolyl-tRNA synthetase / EPRS1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"c1de32ab-9b92-509f-a5b0-08a39e67b8fa","slug":"human-trna-pro","display_name":"Human cytosolic tRNA(Pro)","entity_type_key":"rna"},"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":"58b974f1-d389-5bf6-81cd-889c44442c42","slug":"atp","display_name":"ATP","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","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified human EPRS/ProRS biochemical assays.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"tRNA charging and collagen hydroxylation are separate enzyme steps.","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":"A protein-building block must first be loaded onto the correct tRNA.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Halofuginone and other febrifugine derivatives inhibit prolyl-tRNA synthetase. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22327401/ · DOI 10.1038/nchembio.790","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"08d56ec0-dc7e-57d2-874d-c71e8ab4e644","evidence_kind":"source_excerpt","locator":"Lines 222-228","start_line":222,"end_line":228,"excerpt":"## l-proline-eprs-charging\nA protein-building block must first be loaded onto the correct tRNA.\nThe prolyl-tRNA synthetase domain of human EPRS attaches proline to its cognate tRNA in an ATP-dependent aminoacylation reaction.\nModel: Purified human EPRS/ProRS biochemical assays.\nLimitations: tRNA charging and collagen hydroxylation are separate enzyme steps.\nEvidence access: Primary full text\nHalofuginone and other febrifugine derivatives inhibit prolyl-tRNA synthetase. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22327401/ · DOI 10.1038/nchembio.790","model_system":"Purified human EPRS/ProRS biochemical assays.","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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