{"id":"591796c1-d170-58da-8626-9f2707189bd8","stable_key":"be889add-cec8-500b-be89-676431432a70:mn-enz-sod2-yeast-apo","predicate":"undergoes","statement":"At 30 °C, more than half of human SOD2 purified from expressing yeast mitochondria was apoprotein, and that apoprotein could be fully activated by reconstitution.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"e74e3c5d-dd2f-5e16-b07d-06846a8a72cf","mechanism_event_label":"Making SOD2 protein does not guarantee that it has loaded its metal.","subject":{"id":"d06f7f30-672e-5d63-9818-652210fd425e","slug":"sod2-apo","display_name":"Metal-free human SOD2","entity_type_key":"protein_state"},"object":{"id":"68204766-fef3-5610-93c6-de6f7557c6ea","slug":"human-sod2-metallation","display_name":"Human SOD2 metallation","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"e74e3c5d-dd2f-5e16-b07d-06846a8a72cf","stable_key":"be889add-cec8-500b-be89-676431432a70:mn-enz-sod2-yeast-apo-event","event_type":"biochemical_relationship","label":"Making SOD2 protein does not guarantee that it has loaded its metal.","description":"At 30 °C, more than half of human SOD2 purified from expressing yeast mitochondria was apoprotein, and that apoprotein could be fully activated by reconstitution.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"d06f7f30-672e-5d63-9818-652210fd425e","slug":"sod2-apo","display_name":"Metal-free human SOD2","entity_type_key":"protein_state"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"68204766-fef3-5610-93c6-de6f7557c6ea","slug":"human-sod2-metallation","display_name":"Human SOD2 metallation","entity_type_key":"cellular_process"},"role":"object","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"eda566c2-d338-54b2-a872-0dd39daffcdf","slug":"sod2","display_name":"Human mitochondrial manganese superoxide dismutase / SOD2","entity_type_key":"protein"},"role":"protein","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"a8082b11-c484-5792-bb81-48e8e699cbe4","slug":"manganese-ion","display_name":"Mn2+","entity_type_key":"ion"},"role":"cofactor","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"experimental_model","value_text":"Human SOD2 expressed in Saccharomyces cerevisiae and purified from yeast mitochondria","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Heterologous expression; metallation and reconstitution","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Heterologous yeast expression, not endogenous human tissue. The indexed abstract does not specify a reconstitution dose.","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":"Human protein in Saccharomyces cerevisiae","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Making SOD2 protein does not guarantee that it has loaded its metal.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mn-enz-22561997] Metallation state of human manganese superoxide dismutase expressed in Saccharomyces cerevisiae. (2012). https://pubmed.ncbi.nlm.nih.gov/22561997/ DOI: 10.1016/j.abb.2012.04.016","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Yeast mitochondria","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"360f4890-5920-57c1-adf9-5ec64e5ab167","evidence_kind":"source_excerpt","locator":"Lines 471-481","start_line":471,"end_line":481,"excerpt":"### mn-enz-sod2-yeast-apo\nAt 30 °C, more than half of human SOD2 purified from expressing yeast mitochondria was apoprotein, and that apoprotein could be fully activated by reconstitution.\nCondition category: normal\nnutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Making SOD2 protein does not guarantee that it has loaded its metal.\norganism: Human protein in Saccharomyces cerevisiae\ntissue_or_cell_type: Yeast mitochondria\nexperimental_model: Human SOD2 expressed in Saccharomyces cerevisiae and purified from yeast mitochondria\nlimitations: Heterologous yeast expression, not endogenous human tissue. The indexed abstract does not specify a reconstitution dose.\nexposure: Heterologous expression; metallation and reconstitution\n[mn-enz-22561997] Metallation state of human manganese superoxide dismutase expressed in Saccharomyces cerevisiae. (2012). https://pubmed.ncbi.nlm.nih.gov/22561997/ DOI: 10.1016/j.abb.2012.04.016","model_system":"Human SOD2 expressed in Saccharomyces cerevisiae and purified from yeast mitochondria","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [mn-enz-22561997] Metallation state of human manganese superoxide dismutase expressed in Saccharomyces cerevisiae. 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