{"id":"90cfcad0-9e2a-58dc-9b7f-9c54117f4bb9","stable_key":"97957230-601f-5dec-8524-0812be8fadbf:l-threonine-trna-mark-substrates","predicate":"cooperates_with","statement":"Human YRDC and OSGEPL1 supported mitochondrial t6A37 formation using L-threonine, ATP and CO2/bicarbonate as substrates.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"a44698d1-c580-5da1-99ea-46a3f9a821f6","mechanism_event_label":"Threonine helps make a decoding mark on tRNA, separate from being loaded for protein synthesis.","subject":{"id":"3114b5d2-04d2-59d6-88c3-c04eb28aeeff","slug":"yrdc","display_name":"Human threonylcarbamoyladenylate synthase / YRDC","entity_type_key":"protein"},"object":{"id":"f28550d6-0143-5fe3-ae30-1e634dbd024d","slug":"osgepl1","display_name":"Human mitochondrial tRNA threonylcarbamoyltransferase / OSGEPL1","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"a44698d1-c580-5da1-99ea-46a3f9a821f6","stable_key":"97957230-601f-5dec-8524-0812be8fadbf:l-threonine-trna-mark-substrates-event","event_type":"observed_relationship","label":"Threonine helps make a decoding mark on tRNA, separate from being loaded for protein synthesis.","description":"Human YRDC and OSGEPL1 supported mitochondrial t6A37 formation using L-threonine, ATP and CO2/bicarbonate as substrates.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"3114b5d2-04d2-59d6-88c3-c04eb28aeeff","slug":"yrdc","display_name":"Human threonylcarbamoyladenylate synthase / YRDC","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"f28550d6-0143-5fe3-ae30-1e634dbd024d","slug":"osgepl1","display_name":"Human mitochondrial tRNA threonylcarbamoyltransferase / OSGEPL1","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"fcef4dc2-a7b6-5812-bc33-c8af3d83f4d0","slug":"l-threonine","display_name":"L-Threonine","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":""},{"entity":{"id":"edf44f6b-7b23-5b97-a86b-c940e5812b06","slug":"bicarbonate-ion","display_name":"Bicarbonate ion","entity_type_key":"ion"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"5c27b149-da7e-5a90-8bd3-d4b2a42bb2ef","slug":"trna-threonylcarbamoyladenosine","display_name":"tRNA-bound N6-threonylcarbamoyladenosine / t6A37","entity_type_key":"rna"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human mitochondrial tRNA-modification reconstitution and cellular experiments.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"The mark occurs on multiple tRNAs; it is not restricted to the tRNA that carries threonine.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-threonine","display_name":"L-Threonine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Threonine helps make a decoding mark on tRNA, separate from being loaded for protein synthesis.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"CO2-sensitive tRNA modification associated with human mitochondrial disease. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29760464/ · DOI 10.1038/s41467-018-04250-4","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"393c9ac3-bab0-5286-ac2f-1556e63885d7","evidence_kind":"source_excerpt","locator":"Lines 122-128","start_line":122,"end_line":128,"excerpt":"## l-threonine-trna-mark-substrates\nThreonine helps make a decoding mark on tRNA, separate from being loaded for protein synthesis.\nHuman YRDC and OSGEPL1 supported mitochondrial t6A37 formation using L-threonine, ATP and CO2/bicarbonate as substrates.\nModel: Human mitochondrial tRNA-modification reconstitution and cellular experiments.\nLimitations: The mark occurs on multiple tRNAs; it is not restricted to the tRNA that carries threonine.\nEvidence access: Primary abstract\nCO2-sensitive tRNA modification associated with human mitochondrial disease. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29760464/ · DOI 10.1038/s41467-018-04250-4","model_system":"Human mitochondrial tRNA-modification reconstitution and cellular experiments.","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":"35396730-235a-537e-8a05-c6ef2960c509","stable_key":"import-97957230-601f-5dec-8524-0812be8fadbf","title":"L-Threonine: translation, intestinal barrier, 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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