{"id":"c697d1d4-5ff8-53c4-af3a-d91794314084","stable_key":"5d8e27d8-6a74-5560-827f-3f90908bbc34:ala-lias-sulfur-installation","predicate":"catalyzes","statement":"LIAS installs sulfur at carbon 6 and carbon 8 of an octanoyl-lysyl residue on GCSH.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"698bd9ec-d856-53fc-8062-be45e3382bb2","mechanism_event_label":"LIAS turns the attached precursor into a sulfur-bearing working cofactor.","subject":{"id":"f9fc9417-ca4f-5e0c-b01d-60b337493d34","slug":"lias","display_name":"Lipoic acid synthetase / LIAS","entity_type_key":"protein"},"object":{"id":"e614f093-4ccf-59eb-96df-8d35b1c6f311","slug":"lias-sulfur-insertion","display_name":"LIAS sulfur insertion into octanoyl-GCSH","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"698bd9ec-d856-53fc-8062-be45e3382bb2","stable_key":"5d8e27d8-6a74-5560-827f-3f90908bbc34:ala-lias-sulfur-installation-event","event_type":"biochemical_relationship","label":"LIAS turns the attached precursor into a sulfur-bearing working cofactor.","description":"LIAS installs sulfur at carbon 6 and carbon 8 of an octanoyl-lysyl residue on GCSH.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"05891ff0-fe54-5c5d-9ca2-5fe3c39bf603","slug":"gcsh-octanoyl","display_name":"Human octanoyl-GCSH","entity_type_key":"protein_state"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"280f29ca-25cf-57bb-92b9-ffc43ca11373","slug":"gcsh-lipoyl","display_name":"Human lipoyl-GCSH","entity_type_key":"protein_state"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"f9fc9417-ca4f-5e0c-b01d-60b337493d34","slug":"lias","display_name":"Lipoic acid synthetase / LIAS","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"e614f093-4ccf-59eb-96df-8d35b1c6f311","slug":"lias-sulfur-insertion","display_name":"LIAS sulfur insertion into octanoyl-GCSH","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/ala-research/40640146.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"292f83149906d0c3be473ce3b23be4ee13d1c662b2665993808021098523cd23\", \"start_char\": 0, \"end_char\": 953, \"text_sha256\": \"292f83149906d0c3be473ce3b23be4ee13d1c662b2665993808021098523cd23\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"X-ray structures of catalytic stages with human lipoyl synthase","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Structural trapping of sulfur-insertion intermediates","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Structural snapshots establish reaction intermediates, not clinical nutrient requirements.","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 recombinant proteins","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"LIAS turns the attached precursor into a sulfur-bearing working cofactor.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[ala-p40640146] Structural basis for catalysis by human lipoyl synthase. (2025). https://pubmed.ncbi.nlm.nih.gov/40640146/ DOI: 10.1038/s41467-025-61393-x","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"LIAS and H-protein substrate","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"715d3383-80d9-57b3-a9b1-ce1b30992d56","evidence_kind":"source_excerpt","locator":"Lines 260-271","start_line":260,"end_line":271,"excerpt":"### ala-lias-sulfur-installation\nLIAS installs sulfur at carbon 6 and carbon 8 of an octanoyl-lysyl residue on GCSH.\nCondition category: normal\nnutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: LIAS turns the attached precursor into a sulfur-bearing working cofactor.\norganism: Human recombinant proteins\ntissue_or_cell_type: LIAS and H-protein substrate\nexperimental_model: X-ray structures of catalytic stages with human lipoyl synthase\nlimitations: Structural snapshots establish reaction intermediates, not clinical nutrient requirements.\nexposure: Structural trapping of sulfur-insertion intermediates\nevidence_span: {\"source_cache\": \"artifacts/ala-research/40640146.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"292f83149906d0c3be473ce3b23be4ee13d1c662b2665993808021098523cd23\", \"start_char\": 0, \"end_char\": 953, \"text_sha256\": \"292f83149906d0c3be473ce3b23be4ee13d1c662b2665993808021098523cd23\"}\n[ala-p40640146] Structural basis for catalysis by human lipoyl synthase. 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