{"id":"afe5b5a2-f24e-5ce3-9aa4-8a4036d0b06f","stable_key":"5d8e27d8-6a74-5560-827f-3f90908bbc34:ala-human-lipt2-complementation","predicate":"supports","statement":"Full-length human LIPT2 complemented the E. coli lipB/lplA deletion strain, supporting its octanoyltransferase assignment.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"4e4cc444-af12-5a47-b9c6-329f76e91c8e","mechanism_event_label":"Human LIPT2 restored the missing pathway function in a bacterial test.","subject":{"id":"1bd56cad-1080-5586-bcd3-3c9d626443eb","slug":"lipt2","display_name":"Human octanoyltransferase / LIPT2","entity_type_key":"protein"},"object":{"id":"a545cda4-692b-5513-a8f3-71c0afb0736c","slug":"mitochondrial-protein-lipoylation","display_name":"Mitochondrial protein lipoylation","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"4e4cc444-af12-5a47-b9c6-329f76e91c8e","stable_key":"5d8e27d8-6a74-5560-827f-3f90908bbc34:ala-human-lipt2-complementation-event","event_type":"biochemical_relationship","label":"Human LIPT2 restored the missing pathway function in a bacterial test.","description":"Full-length human LIPT2 complemented the E. coli lipB/lplA deletion strain, supporting its octanoyltransferase assignment.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"1bd56cad-1080-5586-bcd3-3c9d626443eb","slug":"lipt2","display_name":"Human octanoyltransferase / LIPT2","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"a545cda4-692b-5513-a8f3-71c0afb0736c","slug":"mitochondrial-protein-lipoylation","display_name":"Mitochondrial protein lipoylation","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/ala-research/29987032.fulltext.txt\", \"locator\": \"Exact primary full-text span; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"d0569075b59128ea021be6077596127d1c7aae1f9ac6b0acfd2ebcb268b650d3\", \"start_char\": 31198, \"end_char\": 31564, \"text_sha256\": \"967fbdc21edbac2bfd27e7c9c92a2ffe8a0b167c96d55f1095e429241be9463f\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified enzymes and bacterial pathway reconstruction","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Recombinant proteins and radiolabeled substrates","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Bacterial complementation; the purified donor-transfer assay used mouse Lipt2. This is not direct flux measurement in a human mitochondrion.","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 proteins; mouse Lipt2 in purified transfer assays; E. coli host","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Human LIPT2 restored the missing pathway function in a bacterial test.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[ala-p29987032] Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes. (2018). https://pubmed.ncbi.nlm.nih.gov/29987032/ DOI: 10.1073/pnas.1805862115","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Lipoyl assembly pathway","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"5f09e480-5c45-51b0-861c-bc6cc173f2df","evidence_kind":"source_excerpt","locator":"Lines 234-245","start_line":234,"end_line":245,"excerpt":"### ala-human-lipt2-complementation\nFull-length human LIPT2 complemented the E. coli lipB/lplA deletion strain, supporting its octanoyltransferase assignment.\nCondition category: normal\nnutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Human LIPT2 restored the missing pathway function in a bacterial test.\norganism: Human proteins; mouse Lipt2 in purified transfer assays; E. coli host\ntissue_or_cell_type: Lipoyl assembly pathway\nexperimental_model: Purified enzymes and bacterial pathway reconstruction\nlimitations: Bacterial complementation; the purified donor-transfer assay used mouse Lipt2. This is not direct flux measurement in a human mitochondrion.\nexposure: Recombinant proteins and radiolabeled substrates\nevidence_span: {\"source_cache\": \"artifacts/ala-research/29987032.fulltext.txt\", \"locator\": \"Exact primary full-text span; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"d0569075b59128ea021be6077596127d1c7aae1f9ac6b0acfd2ebcb268b650d3\", \"start_char\": 31198, \"end_char\": 31564, \"text_sha256\": \"967fbdc21edbac2bfd27e7c9c92a2ffe8a0b167c96d55f1095e429241be9463f\"}\n[ala-p29987032] Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes. (2018). https://pubmed.ncbi.nlm.nih.gov/29987032/ DOI: 10.1073/pnas.1805862115","model_system":"Purified enzymes and bacterial pathway reconstruction","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [ala-p29987032] Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes. (2018). https://pubmed.ncbi.nlm.nih.gov/29987032/ DOI: 10.1073/pnas.1805862115","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. Not publisher full text.","file_path":"","sha256":"611da198ab85a272eb26b64ee330ef6d1a762853a8481f3191c4acfca9f3cf3d","revision_id":"618b4ce6-3157-5222-8325-408064be5ea5","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}