{"id":"4448e146-527b-53c1-a182-d128aec6474e","stable_key":"220adaab-10d8-5c4e-a3f5-a48700ea794d:agmatine-sulfate-agmat-manganese","predicate":"supports","statement":"Expressing human AGMAT R105 in medium supplemented with 0.5 mM manganese increased its subsequent taurocyamine-hydrolysis activity approximately fourfold.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"a677a651-deba-5580-88d7-c725ca34010e","mechanism_event_label":"Metal handling during enzyme production affects measured activity.","subject":{"id":"a8082b11-c484-5792-bb81-48e8e699cbe4","slug":"manganese-ion","display_name":"Mn2+","entity_type_key":"ion"},"object":{"id":"bba88813-506c-5bbf-b85e-fc33beefc748","slug":"agmat","display_name":"Human AGMAT, guanidino acid hydrolase candidate / historically annotated agmatinase","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"a677a651-deba-5580-88d7-c725ca34010e","stable_key":"220adaab-10d8-5c4e-a3f5-a48700ea794d:agmatine-sulfate-agmat-manganese-event","event_type":"observed_relationship","label":"Metal handling during enzyme production affects measured activity.","description":"Expressing human AGMAT R105 in medium supplemented with 0.5 mM manganese increased its subsequent taurocyamine-hydrolysis activity approximately fourfold.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"a8082b11-c484-5792-bb81-48e8e699cbe4","slug":"manganese-ion","display_name":"Mn2+","entity_type_key":"ion"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"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":"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":"8a2c2166-001d-5945-ac81-a303d5795133","slug":"taurocyamine","display_name":"Taurocyamine / guanidinotaurine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary full text; Figure 3B","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant human enzyme produced in bacterial expression culture.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"This is not evidence that manganese supplements activate human agmatine breakdown; agmatine was not an accepted substrate.","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":"Metal handling during enzyme production affects measured activity.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"9b8019c1-db6c-5ce4-9382-e9eea9519baa","evidence_kind":"source_excerpt","locator":"Lines 140-146","start_line":140,"end_line":146,"excerpt":"## agmatine-sulfate-agmat-manganese\nMetal handling during enzyme production affects measured activity.\nExpressing human AGMAT R105 in medium supplemented with 0.5 mM manganese increased its subsequent taurocyamine-hydrolysis activity approximately fourfold.\nModel: Recombinant human enzyme produced in bacterial expression culture.\nLimitations: This is not evidence that manganese supplements activate human agmatine breakdown; agmatine was not an accepted substrate.\nEvidence access: Primary full text; Figure 3B\nGuanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4","model_system":"Recombinant human enzyme produced in bacterial expression culture.","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. Not publisher full text.","file_path":"","sha256":"b55d70e22d07b80964f825770d92fdd1745221420ed8af8d94ca5182b9994509","revision_id":"fc7be029-20e0-5943-b74e-3b06ba694571","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}