{"id":"0a37ccbe-aacc-5b15-9994-24b80043c12e","stable_key":"be889add-cec8-500b-be89-676431432a70:mn-enz-sod1-distinct-metals","predicate":"requires","statement":"Human SOD1 maturation involves copper and zinc insertion and a Cys57–Cys146 disulfide; this is a different metalloprotein system from manganese SOD2.","claim_class":"identity","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"bb639524-707c-5160-b6dc-8c832923aa05","mechanism_event_label":"SOD1 and SOD2 use different metals.","subject":{"id":"19f2bdc0-4888-57d5-860f-119d5d478eb4","slug":"sod1","display_name":"Human copper-zinc superoxide dismutase / SOD1","entity_type_key":"protein"},"object":{"id":"0c41cbf9-2e5f-541b-b7a3-6359bcefa4a6","slug":"sod1-maturation","display_name":"SOD1 maturation","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"bb639524-707c-5160-b6dc-8c832923aa05","stable_key":"be889add-cec8-500b-be89-676431432a70:mn-enz-sod1-distinct-metals-event","event_type":"biochemical_relationship","label":"SOD1 and SOD2 use different metals.","description":"Human SOD1 maturation involves copper and zinc insertion and a Cys57–Cys146 disulfide; this is a different metalloprotein system from manganese SOD2.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"19f2bdc0-4888-57d5-860f-119d5d478eb4","slug":"sod1","display_name":"Human copper-zinc superoxide dismutase / SOD1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"0c41cbf9-2e5f-541b-b7a3-6359bcefa4a6","slug":"sod1-maturation","display_name":"SOD1 maturation","entity_type_key":"cellular_process"},"role":"object","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"9f0afdde-1ec1-5c8a-bb5e-f3b2b75f67f6","slug":"copper","display_name":"Copper","entity_type_key":"nutrient_element"},"role":"catalytic metal identity","stoichiometry":null,"state_label":"","sequence_order":2,"notes":"Copper identity in SOD1; this abstract does not assign a fixed catalytic oxidation state."},{"entity":{"id":"49c806c2-7041-5020-8b3b-fa04ffa122ac","slug":"zinc-ion","display_name":"Zinc(II) ion","entity_type_key":"ion"},"role":"structural metal","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"eda566c2-d338-54b2-a872-0dd39daffcdf","slug":"sod2","display_name":"Human mitochondrial manganese superoxide dismutase / SOD2","entity_type_key":"protein"},"role":"distinct protein","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"cross_nutrient","value_text":"Copper and zinc cofactor identity in SOD1 is distinguished from Mn-dependent SOD2.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"NMR of copper-depleted human SOD1 C6A/C111S preparation","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Copper-depleted zinc-containing disulfide-reduced preparation","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"The study structurally examined the C6A/C111S copper-depleted, zinc-containing preparation. This identity statement does not assert Mn can replace either SOD1 metal.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Manganese research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"manganese","display_name":"Manganese","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Homo sapiens protein","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"SOD1 and SOD2 use different metals.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mn-enz-16291742] Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form. (2006). https://pubmed.ncbi.nlm.nih.gov/16291742/ DOI: 10.1074/jbc.m506497200","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified SOD1","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"2be04ce0-f55f-55bd-afa7-813aaae765bd","evidence_kind":"source_excerpt","locator":"Lines 458-469","start_line":458,"end_line":469,"excerpt":"### mn-enz-sod1-distinct-metals\nHuman SOD1 maturation involves copper and zinc insertion and a Cys57–Cys146 disulfide; this is a different metalloprotein system from manganese SOD2.\nCondition category: normal\nnutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: SOD1 and SOD2 use different metals.\norganism: Homo sapiens protein\ntissue_or_cell_type: Purified SOD1\nexperimental_model: NMR of copper-depleted human SOD1 C6A/C111S preparation\nlimitations: The study structurally examined the C6A/C111S copper-depleted, zinc-containing preparation. This identity statement does not assert Mn can replace either SOD1 metal.\nexposure: Copper-depleted zinc-containing disulfide-reduced preparation\ncross_nutrient: Copper and zinc cofactor identity in SOD1 is distinguished from Mn-dependent SOD2.\n[mn-enz-16291742] Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form. (2006). https://pubmed.ncbi.nlm.nih.gov/16291742/ DOI: 10.1074/jbc.m506497200","model_system":"NMR of copper-depleted human SOD1 C6A/C111S preparation","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [mn-enz-16291742] Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form. (2006). https://pubmed.ncbi.nlm.nih.gov/16291742/ DOI: 10.1074/jbc.m506497200","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"03224387-8a73-5b4f-906d-9f0be6625b7f","stable_key":"import-be889add-cec8-500b-be89-676431432a70","title":"Manganese: enzyme cofactors, glycosylation, transport 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":"f029ee5a1133a4f296047f06a6f0178deb9fd02e8d9707bc285bbe0f4e08fcb5","revision_id":"a77068c1-5a13-5aa9-bbac-d1cff6d34f15","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}