{"id":"679381b0-eb27-5984-b9d0-6adb6636dcc3","stable_key":"41a89233-da9a-5b7b-9c18-e19bbadcfe2d:methionine-mta-prmt5","predicate":"inhibits","statement":"Biochemical methyltransferase profiling identified MTA as a potent selective PRMT5 inhibitor; MTAP-deleted cells had reduced PRMT5 methylation activity.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"45ec7766-7ef6-5eb4-9f16-536c23b27b8c","mechanism_event_label":"A recycling product can inhibit another methylation enzyme.","subject":{"id":"525860da-a986-5d19-97f0-a257a454b649","slug":"5-methylthioadenosine","display_name":"5′-Methylthioadenosine","entity_type_key":"small_molecule"},"object":{"id":"4f3fefcc-85f6-5420-9931-195aa5022834","slug":"prmt5","display_name":"Human protein arginine methyltransferase 5 / PRMT5","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"45ec7766-7ef6-5eb4-9f16-536c23b27b8c","stable_key":"41a89233-da9a-5b7b-9c18-e19bbadcfe2d:methionine-mta-prmt5-event","event_type":"observed_relationship","label":"A recycling product can inhibit another methylation enzyme.","description":"Biochemical methyltransferase profiling identified MTA as a potent selective PRMT5 inhibitor; MTAP-deleted cells had reduced PRMT5 methylation activity.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"525860da-a986-5d19-97f0-a257a454b649","slug":"5-methylthioadenosine","display_name":"5′-Methylthioadenosine","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"4f3fefcc-85f6-5420-9931-195aa5022834","slug":"prmt5","display_name":"Human protein arginine methyltransferase 5 / PRMT5","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"9d39f561-740b-5f67-bba7-8a72ef612a99","slug":"methionine","display_name":"L-Methionine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"825f2da2-01bc-5874-a3c6-64f5ac867db5","slug":"s-adenosylmethionine","display_name":"S-Adenosyl-L-methionine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"fcd3b947-abdf-5e52-904f-a24f475e446c","slug":"mtap","display_name":"Human methylthioadenosine phosphorylase / MTAP","entity_type_key":"protein"},"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":"Human cancer-cell and purified-enzyme study.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Selectivity applies to the tested panel and conditions; not all methyltransferases.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"methionine","display_name":"L-Methionine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"A recycling product can inhibit another methylation enzyme.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"MTAP Deletions in Cancer Create Vulnerability to Targeting of the MAT2A/PRMT5/RIOK1 Axis. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27068473/ · DOI 10.1016/j.celrep.2016.03.043","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"62d196dd-ebaa-5085-b188-d775f3d74f0e","evidence_kind":"source_excerpt","locator":"Lines 292-298","start_line":292,"end_line":298,"excerpt":"## methionine-mta-prmt5\nA recycling product can inhibit another methylation enzyme.\nBiochemical methyltransferase profiling identified MTA as a potent selective PRMT5 inhibitor; MTAP-deleted cells had reduced PRMT5 methylation activity.\nModel: Human cancer-cell and purified-enzyme study.\nLimitations: Selectivity applies to the tested panel and conditions; not all methyltransferases.\nEvidence access: Primary abstract\nMTAP Deletions in Cancer Create Vulnerability to Targeting of the MAT2A/PRMT5/RIOK1 Axis. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27068473/ · DOI 10.1016/j.celrep.2016.03.043","model_system":"Human cancer-cell and purified-enzyme study.","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":"d969b004-ccc2-5bb4-9109-8ac649137ad1","stable_key":"import-41a89233-da9a-5b7b-9c18-e19bbadcfe2d","title":"L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. 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