{"id":"2cfaaccf-87c8-58f2-a356-da9ea0d6351a","stable_key":"0f17db03-207f-5910-ac8e-13dfc2f378ce:mg-ogdh-independent-adp-model","predicate":"independently-co-activates","statement":"A 2011 kinetic reanalysis favored independent Mg and ADP effects rather than requiring MgADP as the activating species.","claim_class":"hypothesis_link","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"f76be3eb-f447-5a92-9347-af4600d718ab","mechanism_event_label":"One model explains activation using two separate regulators.","subject":{"id":"bff427ab-35f9-59c2-bb24-fd5953bbaec2","slug":"magnesium-ion","display_name":"Mg2+","entity_type_key":"ion"},"object":{"id":"8d8cf36b-d1f4-57eb-8ce2-798d6f3c30b9","slug":"oxoglutarate-dehydrogenase-complex","display_name":"2-Oxoglutarate dehydrogenase complex","entity_type_key":"protein_complex"},"evidence_count":1,"mechanism_event":{"id":"f76be3eb-f447-5a92-9347-af4600d718ab","stable_key":"0f17db03-207f-5910-ac8e-13dfc2f378ce:mg-ogdh-independent-adp-model-event","event_type":"biochemical_relationship","label":"One model explains activation using two separate regulators.","description":"A 2011 kinetic reanalysis favored independent Mg and ADP effects rather than requiring MgADP as the activating species.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"136c3764-1b93-5f79-8673-9001cab9bc3d","slug":"adp","display_name":"Adenosine diphosphate","entity_type_key":"small_molecule"},"role":"parallel activator","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"55da4e38-e280-584e-a524-91ae4812c592","slug":"mg-adp","display_name":"Magnesium-ADP complex","entity_type_key":"chemical_species"},"role":"alternative interpretation","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"bff427ab-35f9-59c2-bb24-fd5953bbaec2","slug":"magnesium-ion","display_name":"Mg2+","entity_type_key":"ion"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"8d8cf36b-d1f4-57eb-8ce2-798d6f3c30b9","slug":"oxoglutarate-dehydrogenase-complex","display_name":"2-Oxoglutarate dehydrogenase complex","entity_type_key":"protein_complex"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"cross_nutrient","value_text":"Magnesium and thiamine-derived ThDP intersect at mitochondrial carbon metabolism; purified-enzyme responses do not measure whole-body energy supply.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Primary kinetic modeling and reanalysis of published mammalian OGDHC datasets.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Computational inference, not a new binding measurement; more complex alternatives were not excluded.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Magnesium research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"magnesium","display_name":"Magnesium","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Mammalian datasets including Sus scrofa","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"One model explains activation using two separate regulators.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[qi-2011-ogdh] Detailed kinetics and regulation of mammalian 2-oxoglutarate dehydrogenase (2011). https://link.springer.com/article/10.1186/1471-2091-12-53 DOI: 10.1186/1471-2091-12-53","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Published isolated-enzyme datasets","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"1574a002-c9cd-5bc0-b9c9-0dfa2e76d4fc","evidence_kind":"source_excerpt","locator":"Lines 723-733","start_line":723,"end_line":733,"excerpt":"### mg-ogdh-independent-adp-model\nA 2011 kinetic reanalysis favored independent Mg and ADP effects rather than requiring MgADP as the activating species.\nCondition category: normal\nnutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: One model explains activation using two separate regulators.\norganism: Mammalian datasets including Sus scrofa\ntissue_or_cell_type: Published isolated-enzyme datasets\nexperimental_model: Primary kinetic modeling and reanalysis of published mammalian OGDHC datasets.\nlimitations: Computational inference, not a new binding measurement; more complex alternatives were not excluded.\ncross_nutrient: Magnesium and thiamine-derived ThDP intersect at mitochondrial carbon metabolism; purified-enzyme responses do not measure whole-body energy supply.\n[qi-2011-ogdh] Detailed kinetics and regulation of mammalian 2-oxoglutarate dehydrogenase (2011). https://link.springer.com/article/10.1186/1471-2091-12-53 DOI: 10.1186/1471-2091-12-53","model_system":"Primary kinetic modeling and reanalysis of published mammalian OGDHC datasets.","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [qi-2011-ogdh] Detailed kinetics and regulation of mammalian 2-oxoglutarate dehydrogenase (2011). https://link.springer.com/article/10.1186/1471-2091-12-53 DOI: 10.1186/1471-2091-12-53","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"dd101e28-1a2e-5a48-9d1e-809c77514866","stable_key":"import-0f17db03-207f-5910-ac8e-13dfc2f378ce","title":"Magnesium: cross-nutrient mechanisms and deficiency (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":"e111c412f57143a17e8e65e74e8f7888b5bb9a61099873f4767f527fac19bb07","revision_id":"6b7f04f2-66ed-5859-955f-c2b50d4bf041","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[{"id":"da012e0a-f8d6-510f-9c7e-be5aa996fd5f","title":"Does MgADP activate OGDHC, or do Mg and ADP act independently?","kind":"contradiction","status":"open","why":"The 2000 speciation interpretation assigns enhanced activation to MgADP; the 2011 reanalysis argues that separate Mg and ADP effects explain the same data more parsimoniously.","resolution":"Unresolved molecular assignment. Preserve both interpretations; discriminate with binding or kinetic experiments that constrain species independently. Neither interpretation establishes a universal Mg gate.","created_at":"2026-09-17 08:30:08","record_type":"conflict","display_label":"Recorded conflict","record_url":"/conflicts/da012e0a-f8d6-510f-9c7e-be5aa996fd5f","sides":[{"conflict_id":"da012e0a-f8d6-510f-9c7e-be5aa996fd5f","ordinal":0,"label":"MgADP as stronger activator","revision_id":"6b7f04f2-66ed-5859-955f-c2b50d4bf041","start_line":699,"end_line":709,"quote":"### mg-ogdh-mgadp-interpretation\nThe 2000 experiments interpreted MgADP as a more potent OGDHC activator than free ADP.\nCondition category: normal\nnutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The authors assigned enhanced activity to magnesium-bound ADP.\norganism: Sus scrofa\ntissue_or_cell_type: Isolated heart enzyme; additional mitochondrial-extract source not resolved\nexperimental_model: Isolated pig-heart enzyme complex plus mitochondrial extracts; extract source not resolved in this curation; nucleotide/phosphate/Mg speciation experiments.\nlimitations: Speciation-based interpretation; later modeling offered independent Mg/ADP effects.\ncross_nutrient: Magnesium and thiamine-derived ThDP intersect at mitochondrial carbon metabolism; purified-enzyme responses do not measure whole-body energy supply.\n[rodriguez-2000-ogdh] Modulation of 2-oxoglutarate dehydrogenase complex by inorganic phosphate, Mg(2+), and other effectors (2000). https://pubmed.ncbi.nlm.nih.gov/10864444/ DOI: 10.1006/abbi.2000.1856","source_key":"import-0f17db03-207f-5910-ac8e-13dfc2f378ce","source_title":"Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17)","claim_ids":["65eeae05-fbe9-560f-9875-a4e31107cb67"]},{"conflict_id":"da012e0a-f8d6-510f-9c7e-be5aa996fd5f","ordinal":1,"label":"Independent Mg and ADP effects","revision_id":"6b7f04f2-66ed-5859-955f-c2b50d4bf041","start_line":723,"end_line":733,"quote":"### mg-ogdh-independent-adp-model\nA 2011 kinetic reanalysis favored independent Mg and ADP effects rather than requiring MgADP as the activating species.\nCondition category: normal\nnutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: One model explains activation using two separate regulators.\norganism: Mammalian datasets including Sus scrofa\ntissue_or_cell_type: Published isolated-enzyme datasets\nexperimental_model: Primary kinetic modeling and reanalysis of published mammalian OGDHC datasets.\nlimitations: Computational inference, not a new binding measurement; more complex alternatives were not excluded.\ncross_nutrient: Magnesium and thiamine-derived ThDP intersect at mitochondrial carbon metabolism; purified-enzyme responses do not measure whole-body energy supply.\n[qi-2011-ogdh] Detailed kinetics and regulation of mammalian 2-oxoglutarate dehydrogenase (2011). https://link.springer.com/article/10.1186/1471-2091-12-53 DOI: 10.1186/1471-2091-12-53","source_key":"import-0f17db03-207f-5910-ac8e-13dfc2f378ce","source_title":"Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17)","claim_ids":["2cfaaccf-87c8-58f2-a356-da9ea0d6351a"]}]}],"corrections":[],"research":null}