{"id":"568e3e74-8d0d-54ae-990e-03d2b1f22998","stable_key":"5d8e27d8-6a74-5560-827f-3f90908bbc34:ala-aux-cluster-consumed","predicate":"limits","statement":"Without auxiliary-cluster restoration, sulfur extraction degrades the LIAS auxiliary cluster and limits turnover.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"c083672d-1b8e-5b61-9e84-3e8d4089d5a4","mechanism_event_label":"The sulfur-supplying part must be rebuilt for continued work.","subject":{"id":"65497586-1f6a-5981-a0b1-784ecb5e849f","slug":"lias-auxiliary-cluster-state","display_name":"LIAS auxiliary [4Fe-4S] site","entity_type_key":"protein_state"},"object":{"id":"be60e286-b472-584a-8f13-7050d0c3ad4f","slug":"lias-catalytic-turnover","display_name":"LIAS catalytic turnover","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"c083672d-1b8e-5b61-9e84-3e8d4089d5a4","stable_key":"5d8e27d8-6a74-5560-827f-3f90908bbc34:ala-aux-cluster-consumed-event","event_type":"biochemical_relationship","label":"The sulfur-supplying part must be rebuilt for continued work.","description":"Without auxiliary-cluster restoration, sulfur extraction degrades the LIAS auxiliary cluster and limits turnover.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"65497586-1f6a-5981-a0b1-784ecb5e849f","slug":"lias-auxiliary-cluster-state","display_name":"LIAS auxiliary [4Fe-4S] site","entity_type_key":"protein_state"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"be60e286-b472-584a-8f13-7050d0c3ad4f","slug":"lias-catalytic-turnover","display_name":"LIAS catalytic turnover","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"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/36281303.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"29a716d2027786ee1eefa5380aca1ddc035ec330409162f3d4e61db20015780f\", \"start_char\": 0, \"end_char\": 1732, \"text_sha256\": \"29a716d2027786ee1eefa5380aca1ddc035ec330409162f3d4e61db20015780f\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified human LIAS turnover and cluster-transfer assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"LIAS with candidate iron-sulfur cluster donors","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Cell-free transfer distinguishes direct donor activity from upstream functions in intact cells.","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":"The sulfur-supplying part must be rebuilt for continued work.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[ala-p36281303] In Vitro Demonstration of Human Lipoyl Synthase Catalytic Activity in the Presence of NFU1. (2022). https://pubmed.ncbi.nlm.nih.gov/36281303/ DOI: 10.1021/acsbiomedchemau.2c00020","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Mitochondrial lipoyl synthesis machinery","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":"718993cd-6e8d-512e-9011-48ce244d191d","evidence_kind":"source_excerpt","locator":"Lines 312-323","start_line":312,"end_line":323,"excerpt":"### ala-aux-cluster-consumed\nWithout auxiliary-cluster restoration, sulfur extraction degrades the LIAS auxiliary cluster and limits turnover.\nCondition category: machinery_impairment\nnutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The sulfur-supplying part must be rebuilt for continued work.\norganism: Human recombinant proteins\ntissue_or_cell_type: Mitochondrial lipoyl synthesis machinery\nexperimental_model: Purified human LIAS turnover and cluster-transfer assays\nlimitations: Cell-free transfer distinguishes direct donor activity from upstream functions in intact cells.\nexposure: LIAS with candidate iron-sulfur cluster donors\nevidence_span: {\"source_cache\": \"artifacts/ala-research/36281303.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"29a716d2027786ee1eefa5380aca1ddc035ec330409162f3d4e61db20015780f\", \"start_char\": 0, \"end_char\": 1732, \"text_sha256\": \"29a716d2027786ee1eefa5380aca1ddc035ec330409162f3d4e61db20015780f\"}\n[ala-p36281303] In Vitro Demonstration of Human Lipoyl Synthase Catalytic Activity in the Presence of NFU1. 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