{"id":"90a988f5-225e-5b0c-a60e-fe593e9fbebc","stable_key":"e37461ea-ea5d-5e2c-8091-138305f6dd70:l-aspartate-dars2-compartment","predicate":"recognizes","statement":"Human mitochondrial aspartyl-tRNA synthetase showed a broader catalytic groove and distinct tRNA-binding thermodynamics compared with its bacterial structural homologue.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"64864b34-31fc-50d8-a971-054d68fc74ce","mechanism_event_label":"Mitochondrial translation has its own aspartate-handling machinery.","subject":{"id":"6f1dcaad-d69c-5f46-974a-4a798777b5fb","slug":"dars2","display_name":"Human mitochondrial aspartyl-tRNA synthetase / DARS2","entity_type_key":"protein"},"object":{"id":"9964f811-1878-5e02-abb6-9d0240bb28ac","slug":"human-mitochondrial-trna-asp","display_name":"Human mitochondrial aspartate tRNA","entity_type_key":"rna"},"evidence_count":1,"mechanism_event":{"id":"64864b34-31fc-50d8-a971-054d68fc74ce","stable_key":"e37461ea-ea5d-5e2c-8091-138305f6dd70:l-aspartate-dars2-compartment-event","event_type":"observed_relationship","label":"Mitochondrial translation has its own aspartate-handling machinery.","description":"Human mitochondrial aspartyl-tRNA synthetase showed a broader catalytic groove and distinct tRNA-binding thermodynamics compared with its bacterial structural homologue.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"6f1dcaad-d69c-5f46-974a-4a798777b5fb","slug":"dars2","display_name":"Human mitochondrial aspartyl-tRNA synthetase / DARS2","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"9964f811-1878-5e02-abb6-9d0240bb28ac","slug":"human-mitochondrial-trna-asp","display_name":"Human mitochondrial aspartate tRNA","entity_type_key":"rna"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"0a0923d3-72b7-5d6a-bf3a-5a7a3071a09b","slug":"l-aspartate","display_name":"L-Aspartate","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 mitochondrial DARS2, crystallography and isothermal titration calorimetry.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Bacterial structural comparison is not a human aspartate-deficiency model or proof of supplement rescue.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Aspartate collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-aspartate","display_name":"L-Aspartate","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Mitochondrial translation has its own aspartate-handling machinery.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Thermodynamic properties distinguish human mitochondrial aspartyl-tRNA synthetase from bacterial homolog with same 3D architecture. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23275545/ · DOI 10.1093/nar/gks1322","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"2548a09d-2701-512e-aae7-3b4dd43f7a8d","evidence_kind":"source_excerpt","locator":"Lines 362-368","start_line":362,"end_line":368,"excerpt":"## l-aspartate-dars2-compartment\nMitochondrial translation has its own aspartate-handling machinery.\nHuman mitochondrial aspartyl-tRNA synthetase showed a broader catalytic groove and distinct tRNA-binding thermodynamics compared with its bacterial structural homologue.\nModel: Purified human mitochondrial DARS2, crystallography and isothermal titration calorimetry.\nLimitations: Bacterial structural comparison is not a human aspartate-deficiency model or proof of supplement rescue.\nEvidence access: Primary full text\nThermodynamic properties distinguish human mitochondrial aspartyl-tRNA synthetase from bacterial homolog with same 3D architecture. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23275545/ · DOI 10.1093/nar/gks1322","model_system":"Purified human mitochondrial DARS2, crystallography and isothermal titration calorimetry.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; 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