{"id":"3543405f-2396-5fdc-ba6d-470790986872","stable_key":"c3df3634-4c3a-5099-a5d9-e4f6344c1084:lysyl-trna-formation","predicate":"converted_to","statement":"After pyrophosphate release, KARS1 transfers activated lysine to the tRNA-Lys 3-prime end, forming lysyl-tRNA and AMP.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"46d5cd1b-e34f-5846-b236-78e48f352609","mechanism_event_label":"Charged tRNA supplies lysine for protein synthesis.","subject":{"id":"a812ec0c-6962-580b-bf08-5e7c74b7b5ba","slug":"lysyl-adenylate","display_name":"Lysyl-adenylate","entity_type_key":"small_molecule"},"object":{"id":"165668b6-4ca7-5558-aabb-506ae43314e7","slug":"lysyl-trna-lys","display_name":"Lysyl-tRNA-Lys","entity_type_key":"rna"},"evidence_count":1,"mechanism_event":{"id":"46d5cd1b-e34f-5846-b236-78e48f352609","stable_key":"c3df3634-4c3a-5099-a5d9-e4f6344c1084:lysyl-trna-formation-event","event_type":"biochemical_relationship","label":"Charged tRNA supplies lysine for protein synthesis.","description":"After pyrophosphate release, KARS1 transfers activated lysine to the tRNA-Lys 3-prime end, forming lysyl-tRNA and AMP.","status":"provisional","compartment":{"slug":"cytosol","display_name":"Cytosol"},"participants":[{"entity":{"id":"5764a3e5-0715-5aa3-8c20-c0efb52123b5","slug":"kars1","display_name":"Lysyl-tRNA synthetase / KARS1","entity_type_key":"protein"},"role":"catalyst","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"109c934b-2a17-5f29-9712-6538ac8c2396","slug":"trna-lys","display_name":"Uncharged tRNA-Lys","entity_type_key":"rna"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"a812ec0c-6962-580b-bf08-5e7c74b7b5ba","slug":"lysyl-adenylate","display_name":"Lysyl-adenylate","entity_type_key":"small_molecule"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"165668b6-4ca7-5558-aabb-506ae43314e7","slug":"lysyl-trna-lys","display_name":"Lysyl-tRNA-Lys","entity_type_key":"rna"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"d47321ac-44bb-5a88-afdb-6435b57a91b9","slug":"amp","display_name":"AMP","entity_type_key":"small_molecule"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"experimental_model","value_text":"Human LysRS-tRNA-Lys3 structural and enzyme assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"This is tRNA charging; subsequent ribosomal peptide-bond formation is a distinct step.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"organism","value_text":"Homo sapiens","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Charged tRNA supplies lysine for protein synthesis.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[devarkar2025] Structural basis for aminoacylation of cellular modified tRNALys3 by human lysyl-tRNA synthetase (2025). https://pubmed.ncbi.nlm.nih.gov/40036503/ DOI: 10.1093/nar/gkaf114","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Cytosolic translation machinery","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"14463fb7-1077-534d-88de-7b94d6fa29ca","evidence_kind":"source_excerpt","locator":"Lines 64-72","start_line":64,"end_line":72,"excerpt":"### lysyl-trna-formation\nAfter pyrophosphate release, KARS1 transfers activated lysine to the tRNA-Lys 3-prime end, forming lysyl-tRNA and AMP.\nPlain language: Charged tRNA supplies lysine for protein synthesis.\nCondition category: normal\norganism: Homo sapiens\ntissue_or_cell_type: Cytosolic translation machinery\nexperimental_model: Human LysRS-tRNA-Lys3 structural and enzyme assays\nlimitations: This is tRNA charging; subsequent ribosomal peptide-bond formation is a distinct step.\n[devarkar2025] Structural basis for aminoacylation of cellular modified tRNALys3 by human lysyl-tRNA synthetase (2025). https://pubmed.ncbi.nlm.nih.gov/40036503/ DOI: 10.1093/nar/gkaf114","model_system":"Human LysRS-tRNA-Lys3 structural and enzyme assays","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact quote from the accompanying curation document, not from publisher text. Original study references: [devarkar2025] Structural basis for aminoacylation of cellular modified tRNALys3 by human lysyl-tRNA synthetase (2025). https://pubmed.ncbi.nlm.nih.gov/40036503/ DOI: 10.1093/nar/gkaf114","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"7633bde7-dcc9-5086-91c6-a45eb96857f3","stable_key":"import-c3df3634-4c3a-5099-a5d9-e4f6344c1084","title":"L-Lysine: mechanism-first literature curation (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text.","file_path":"","sha256":"93998d47c21525409ba82f1c82ededf2893dff15fbe61c7deffc175b0e298e97","revision_id":"3897e31f-6624-59e1-a053-8a81b7361632","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}