{"id":"8ed3ea78-b69e-528c-88c9-afc2d0d059e5","stable_key":"e37461ea-ea5d-5e2c-8091-138305f6dd70:l-aspartate-human-nat8l-loss","predicate":"impairs","statement":"A homozygous 19-base-pair NAT8L deletion in a patient with absent brain NAA produced a frameshift and failure to produce a functional enzyme.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"1992cff2-0aac-552c-803a-e48d18527e37","mechanism_event_label":"Lack of the derived metabolite can reflect faulty synthesis machinery.","subject":{"id":"a7cc6a39-7db3-5525-b74e-eb856f68697a","slug":"human-nat8l-frameshift","display_name":"Human NAT8L 19-base-pair deletion","entity_type_key":"cellular_process"},"object":{"id":"5413d2d0-823f-5cf2-94c7-c23b57597808","slug":"nat8l","display_name":"Human aspartate N-acetyltransferase / NAT8L","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"1992cff2-0aac-552c-803a-e48d18527e37","stable_key":"e37461ea-ea5d-5e2c-8091-138305f6dd70:l-aspartate-human-nat8l-loss-event","event_type":"observed_relationship","label":"Lack of the derived metabolite can reflect faulty synthesis machinery.","description":"A homozygous 19-base-pair NAT8L deletion in a patient with absent brain NAA produced a frameshift and failure to produce a functional enzyme.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"a7cc6a39-7db3-5525-b74e-eb856f68697a","slug":"human-nat8l-frameshift","display_name":"Human NAT8L 19-base-pair deletion","entity_type_key":"cellular_process"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"5413d2d0-823f-5cf2-94c7-c23b57597808","slug":"nat8l","display_name":"Human aspartate N-acetyltransferase / NAT8L","entity_type_key":"protein"},"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":"eec6e0e7-9355-5d6d-af44-39441c048ae8","slug":"n-acetylaspartate","display_name":"N-Acetyl-L-aspartate / NAA","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"b7ed6e4c-e560-5cee-b68f-895f21862e6f","slug":"acetyl-coa","display_name":"Acetyl-CoA","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"availability_state","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null},{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human patient genetic study with functional expression characterization.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"A single rare disorder is not evidence of dietary aspartate deficiency or that supplying aspartate fixes the defect.","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":"Lack of the derived metabolite can reflect faulty synthesis machinery.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Molecular identification of aspartate N-acetyltransferase and its mutation in hypoacetylaspartia. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19807691/ · DOI 10.1042/BJ20091024","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"trigger_kind","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null}],"evidence":[{"id":"c096e21c-4077-5bb4-af91-6a4b154a3dc5","evidence_kind":"source_excerpt","locator":"Lines 386-392","start_line":386,"end_line":392,"excerpt":"## l-aspartate-human-nat8l-loss\nLack of the derived metabolite can reflect faulty synthesis machinery.\nA homozygous 19-base-pair NAT8L deletion in a patient with absent brain NAA produced a frameshift and failure to produce a functional enzyme.\nModel: Human patient genetic study with functional expression characterization.\nLimitations: A single rare disorder is not evidence of dietary aspartate deficiency or that supplying aspartate fixes the defect.\nEvidence access: Primary abstract\nMolecular identification of aspartate N-acetyltransferase and its mutation in hypoacetylaspartia. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19807691/ · DOI 10.1042/BJ20091024","model_system":"Human patient genetic study with functional expression characterization.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; 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