{"id":"fb2d9243-04b4-5e63-9332-e62fba630100","stable_key":"220adaab-10d8-5c4e-a3f5-a48700ea794d:agmatine-sulfate-yeast-rescue","predicate":"supports_in_heterologous_model","statement":"Human AGMAT expression supported growth of polyamine-biosynthesis-deficient yeast in the presence of agmatine despite absent directly measured in vitro agmatinase activity.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"09c267d0-9542-5606-94da-f5e3804aece5","mechanism_event_label":"Growth complementation and direct enzyme catalysis answer different questions.","subject":{"id":"bba88813-506c-5bbf-b85e-fc33beefc748","slug":"agmat","display_name":"Human AGMAT, guanidino acid hydrolase candidate / historically annotated agmatinase","entity_type_key":"protein"},"object":{"id":"f5e95ea3-9d69-5d08-aa5c-a9b9b40bb0e3","slug":"yeast-human-agmat-polyamine-growth-rescue","display_name":"Yeast polyamine-deficient growth rescue by human AGMAT expression","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"09c267d0-9542-5606-94da-f5e3804aece5","stable_key":"220adaab-10d8-5c4e-a3f5-a48700ea794d:agmatine-sulfate-yeast-rescue-event","event_type":"observed_relationship","label":"Growth complementation and direct enzyme catalysis answer different questions.","description":"Human AGMAT expression supported growth of polyamine-biosynthesis-deficient yeast in the presence of agmatine despite absent directly measured in vitro agmatinase activity.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"bba88813-506c-5bbf-b85e-fc33beefc748","slug":"agmat","display_name":"Human AGMAT, guanidino acid hydrolase candidate / historically annotated agmatinase","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"f5e95ea3-9d69-5d08-aa5c-a9b9b40bb0e3","slug":"yeast-human-agmat-polyamine-growth-rescue","display_name":"Yeast polyamine-deficient growth rescue by human AGMAT expression","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"ae2dddf4-ce04-57e3-8a06-7ed9fdc24554","slug":"agmatine-sulfate","display_name":"Agmatine Sulfate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"e2f83eb4-99ed-5050-87d3-3e4701d05c1a","slug":"agmatine","display_name":"Agmatine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"c71bf622-f14b-5314-b1a5-dfa002d2d8ff","slug":"putrescine","display_name":"Putrescine","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":"Saccharomyces cerevisiae TRY104Δspe1 complementation plus enzyme assays.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Indirect yeast rescue is retained as reported; it is not sufficient to override later direct human substrate-specificity experiments.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"agmatine-sulfate","display_name":"Agmatine Sulfate","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Growth complementation and direct enzyme catalysis answer different questions.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Mammalian agmatinases constitute unusual members in the family of Mn2+-dependent ureahydrolases. · 2017 · https://pubmed.ncbi.nlm.nih.gov/27846445/ · DOI 10.1016/j.jinorgbio.2016.11.015","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"b02574b8-2848-51c2-8f09-55afc4110d73","evidence_kind":"source_excerpt","locator":"Lines 164-170","start_line":164,"end_line":170,"excerpt":"## agmatine-sulfate-yeast-rescue\nGrowth complementation and direct enzyme catalysis answer different questions.\nHuman AGMAT expression supported growth of polyamine-biosynthesis-deficient yeast in the presence of agmatine despite absent directly measured in vitro agmatinase activity.\nModel: Saccharomyces cerevisiae TRY104Δspe1 complementation plus enzyme assays.\nLimitations: Indirect yeast rescue is retained as reported; it is not sufficient to override later direct human substrate-specificity experiments.\nEvidence access: Primary abstract\nMammalian agmatinases constitute unusual members in the family of Mn2+-dependent ureahydrolases. · 2017 · https://pubmed.ncbi.nlm.nih.gov/27846445/ · DOI 10.1016/j.jinorgbio.2016.11.015","model_system":"Saccharomyces cerevisiae TRY104Δspe1 complementation plus enzyme assays.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; evidence access and experimental limitations specified.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"e0426971-7d13-51c9-8354-6547b664f1cf","stable_key":"import-220adaab-10d8-5c4e-a3f5-a48700ea794d","title":"Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. 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