{"id":"e91e3945-d1e9-578a-8397-bca0ed14cfcd","stable_key":"5d8e27d8-6a74-5560-827f-3f90908bbc34:ala-lipt1-gcsh-transfer","predicate":"transfers_lipoyl_group_from","statement":"Reconstituted LIPT1 transfers the lipoyl group from GCSH to dehydrogenase E2 lipoyl domains.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"c5a94eaf-383a-55b2-ade6-8a61b5322f38","mechanism_event_label":"GCSH carries the cofactor before LIPT1 passes it to energy-processing enzymes.","subject":{"id":"a044660b-d63d-5adb-9b1f-ac9c2b8901bd","slug":"lipt1","display_name":"Human lipoyl amidotransferase / LIPT1","entity_type_key":"protein"},"object":{"id":"280f29ca-25cf-57bb-92b9-ffc43ca11373","slug":"gcsh-lipoyl","display_name":"Human lipoyl-GCSH","entity_type_key":"protein_state"},"evidence_count":1,"mechanism_event":{"id":"c5a94eaf-383a-55b2-ade6-8a61b5322f38","stable_key":"5d8e27d8-6a74-5560-827f-3f90908bbc34:ala-lipt1-gcsh-transfer-event","event_type":"biochemical_relationship","label":"GCSH carries the cofactor before LIPT1 passes it to energy-processing enzymes.","description":"Reconstituted LIPT1 transfers the lipoyl group from GCSH to dehydrogenase E2 lipoyl domains.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"78a93278-7e43-59c7-b097-31bbae21c771","slug":"gcsh","display_name":"Human glycine-cleavage H-protein / GCSH","entity_type_key":"protein"},"role":"donor_protein","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"12e22bc4-4bc8-5a45-87bc-9274656e9dab","slug":"dlat","display_name":"Dihydrolipoyl acetyltransferase / DLAT","entity_type_key":"protein"},"role":"acceptor","stoichiometry":null,"state_label":"","sequence_order":1,"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":2,"notes":""},{"entity":{"id":"280f29ca-25cf-57bb-92b9-ffc43ca11373","slug":"gcsh-lipoyl","display_name":"Human lipoyl-GCSH","entity_type_key":"protein_state"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/ala-research/29987032.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"3fc07be493a0d6e22ea55c9509cb2d727180f5921d588a52d2d9300a25aa49a2\", \"start_char\": 0, \"end_char\": 989, \"text_sha256\": \"3fc07be493a0d6e22ea55c9509cb2d727180f5921d588a52d2d9300a25aa49a2\"}","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":"Human and mouse constructs must not be conflated. Recombinant reconstruction establishes chemistry, not supplementation efficacy.","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":"GCSH carries the cofactor before LIPT1 passes it to energy-processing enzymes.","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":"f41ac7c7-6989-5408-b228-67062bdcf9ea","evidence_kind":"source_excerpt","locator":"Lines 208-219","start_line":208,"end_line":219,"excerpt":"### ala-lipt1-gcsh-transfer\nReconstituted LIPT1 transfers the lipoyl group from GCSH to dehydrogenase E2 lipoyl domains.\nCondition category: normal\nnutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: GCSH carries the cofactor before LIPT1 passes it to energy-processing enzymes.\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: Human and mouse constructs must not be conflated. Recombinant reconstruction establishes chemistry, not supplementation efficacy.\nexposure: Recombinant proteins and radiolabeled substrates\nevidence_span: {\"source_cache\": \"artifacts/ala-research/29987032.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"3fc07be493a0d6e22ea55c9509cb2d727180f5921d588a52d2d9300a25aa49a2\", \"start_char\": 0, \"end_char\": 989, \"text_sha256\": \"3fc07be493a0d6e22ea55c9509cb2d727180f5921d588a52d2d9300a25aa49a2\"}\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}