{"id":"06c7112d-8123-5e62-87d1-4b29e01d05d5","stable_key":"09b23d0d-35e2-51ff-b1aa-b4f9227e4fa2:isoleucine-acat1-potassium","predicate":"activates_tested","statement":"Increasing KCl from 0 to 40 mM increased purified human T2 turnover approximately threefold for both acetoacetyl-CoA and 2-methylacetoacetyl-CoA.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"5895d444-fbc0-579a-8cc3-5ba5205338e8","mechanism_event_label":"Potassium changed the activity of an enzyme shared by isoleucine and ketone processing.","subject":{"id":"5dd31e52-f51e-51f3-880e-240abcc0ab1d","slug":"potassium-ion","display_name":"Potassium ion","entity_type_key":"ion"},"object":{"id":"4e3ca267-b01e-550b-aa8e-4db62e54102d","slug":"acat1","display_name":"Mitochondrial acetyl-CoA acetyltransferase / ACAT1","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"5895d444-fbc0-579a-8cc3-5ba5205338e8","stable_key":"09b23d0d-35e2-51ff-b1aa-b4f9227e4fa2:isoleucine-acat1-potassium-event","event_type":"observed_relationship","label":"Potassium changed the activity of an enzyme shared by isoleucine and ketone processing.","description":"Increasing KCl from 0 to 40 mM increased purified human T2 turnover approximately threefold for both acetoacetyl-CoA and 2-methylacetoacetyl-CoA.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"5dd31e52-f51e-51f3-880e-240abcc0ab1d","slug":"potassium-ion","display_name":"Potassium ion","entity_type_key":"ion"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"4e3ca267-b01e-550b-aa8e-4db62e54102d","slug":"acat1","display_name":"Mitochondrial acetyl-CoA acetyltransferase / ACAT1","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"c85b327e-f132-5d9a-8e4b-c2976fcc0373","slug":"isoleucine","display_name":"L-Isoleucine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"2c795364-e2ff-5782-8270-81e153e92c9d","slug":"2-methylacetoacetyl-coa","display_name":"2-Methylacetoacetyl-CoA","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"4faa6456-aff8-59eb-9e3f-3326a436e401","slug":"coenzyme-a","display_name":"Coenzyme A","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified human enzyme and potassium-bound structures.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Assay activation is not proof that extra potassium accelerates isoleucine breakdown in a potassium-replete person.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Isoleucine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"isoleucine","display_name":"L-Isoleucine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Potassium changed the activity of an enzyme shared by isoleucine and ketone processing.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17371050/ · DOI 10.1021/bi6026192","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"ae4af10d-ec5c-51c7-b6dd-22100dc2df85","evidence_kind":"source_excerpt","locator":"Lines 234-240","start_line":234,"end_line":240,"excerpt":"## isoleucine-acat1-potassium\nPotassium changed the activity of an enzyme shared by isoleucine and ketone processing.\nIncreasing KCl from 0 to 40 mM increased purified human T2 turnover approximately threefold for both acetoacetyl-CoA and 2-methylacetoacetyl-CoA.\nModel: Purified human enzyme and potassium-bound structures.\nLimitations: Assay activation is not proof that extra potassium accelerates isoleucine breakdown in a potassium-replete person.\nEvidence access: Primary abstract\nCrystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17371050/ · DOI 10.1021/bi6026192","model_system":"Purified human enzyme and potassium-bound structures.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; 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