{"id":"04c9ac57-645f-5d9a-b1d7-74917d8afc43","stable_key":"5d8e27d8-6a74-5560-827f-3f90908bbc34:ala-lipt1-glycine-spared","predicate":"loss_can_spare","statement":"Despite LIPT1 deficiency, H-protein lipoylation, glycine-cleavage activity and glycine concentrations were normal in this case.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"9314f854-b392-5e67-9fa8-a8cf2e2de4e2","mechanism_event_label":"The glycine pathway can keep working when a later transfer step fails.","subject":{"id":"a044660b-d63d-5adb-9b1f-ac9c2b8901bd","slug":"lipt1","display_name":"Human lipoyl amidotransferase / LIPT1","entity_type_key":"protein"},"object":{"id":"206d41a9-3025-5cd2-8fa0-ccf9563d501a","slug":"glycine-cleavage-flux","display_name":"Glycine cleavage flux","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"9314f854-b392-5e67-9fa8-a8cf2e2de4e2","stable_key":"5d8e27d8-6a74-5560-827f-3f90908bbc34:ala-lipt1-glycine-spared-event","event_type":"biochemical_relationship","label":"The glycine pathway can keep working when a later transfer step fails.","description":"Despite LIPT1 deficiency, H-protein lipoylation, glycine-cleavage activity and glycine concentrations were normal in this case.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"280f29ca-25cf-57bb-92b9-ffc43ca11373","slug":"gcsh-lipoyl","display_name":"Human lipoyl-GCSH","entity_type_key":"protein_state"},"role":"preserved_state","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"a044660b-d63d-5adb-9b1f-ac9c2b8901bd","slug":"lipt1","display_name":"Human lipoyl amidotransferase / LIPT1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"206d41a9-3025-5cd2-8fa0-ccf9563d501a","slug":"glycine-cleavage-flux","display_name":"Glycine cleavage flux","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"availability_state","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null},{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/ala-research/24256811.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"57599dd35c58b21d16f2a5955ea667ec8211ab129ee7d0b639b31f18f0976eb2\", \"start_char\": 0, \"end_char\": 1749, \"text_sha256\": \"57599dd35c58b21d16f2a5955ea667ec8211ab129ee7d0b639b31f18f0976eb2\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Affected patient, biochemical testing and complementation","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Compound-heterozygous LIPT1 variants","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Single rare inherited case; enzyme deficits are not interchangeable with nutritional deficiency.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"lipoic-acid","display_name":"Lipoic acid","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Human","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The glycine pathway can keep working when a later transfer step fails.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[ala-p24256811] Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes. (2014). https://pubmed.ncbi.nlm.nih.gov/24256811/ DOI: 10.1093/hmg/ddt585","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Patient-derived cells","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":"ce5b8ac7-54c4-59f3-984c-05274ae279bd","evidence_kind":"source_excerpt","locator":"Lines 468-479","start_line":468,"end_line":479,"excerpt":"### ala-lipt1-glycine-spared\nDespite LIPT1 deficiency, H-protein lipoylation, glycine-cleavage activity and glycine concentrations were normal in this case.\nCondition category: machinery_impairment\nnutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The glycine pathway can keep working when a later transfer step fails.\norganism: Human\ntissue_or_cell_type: Patient-derived cells\nexperimental_model: Affected patient, biochemical testing and complementation\nlimitations: Single rare inherited case; enzyme deficits are not interchangeable with nutritional deficiency.\nexposure: Compound-heterozygous LIPT1 variants\nevidence_span: {\"source_cache\": \"artifacts/ala-research/24256811.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"57599dd35c58b21d16f2a5955ea667ec8211ab129ee7d0b639b31f18f0976eb2\", \"start_char\": 0, \"end_char\": 1749, \"text_sha256\": \"57599dd35c58b21d16f2a5955ea667ec8211ab129ee7d0b639b31f18f0976eb2\"}\n[ala-p24256811] Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes. (2014). https://pubmed.ncbi.nlm.nih.gov/24256811/ DOI: 10.1093/hmg/ddt585","model_system":"Affected patient, biochemical testing and complementation","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [ala-p24256811] Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes. (2014). https://pubmed.ncbi.nlm.nih.gov/24256811/ DOI: 10.1093/hmg/ddt585","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"d8afa8c2-ced9-5b28-90ca-2ac120ec7202","stable_key":"import-5d8e27d8-6a74-5560-827f-3f90908bbc34","title":"Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. 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