{"id":"1f7b9aa0-9d2e-521b-95fe-0006528fc140","stable_key":"ec174d5a-4903-5745-8646-df0e9d4265e8:folate-gcpii-arene-recognition","predicate":"recognizes","statement":"Human GCPII structures and mutagenesis identified an arene-binding site that recognizes the folate portion of polyglutamate substrates.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"ba3197b5-4231-586b-b0af-7fec11c49d0a","mechanism_event_label":"The enzyme recognizes more than the glutamate tail.","subject":{"id":"f75b6059-4033-5997-8b92-acc37f81289d","slug":"folh1","display_name":"Human glutamate carboxypeptidase II / FOLH1","entity_type_key":"protein"},"object":{"id":"81c45abb-713d-521f-9854-23288f880831","slug":"folate-polyglutamates","display_name":"Folate polyglutamates","entity_type_key":"chemical_species"},"evidence_count":1,"mechanism_event":{"id":"ba3197b5-4231-586b-b0af-7fec11c49d0a","stable_key":"ec174d5a-4903-5745-8646-df0e9d4265e8:folate-gcpii-arene-recognition-event","event_type":"biochemical_relationship","label":"The enzyme recognizes more than the glutamate tail.","description":"Human GCPII structures and mutagenesis identified an arene-binding site that recognizes the folate portion of polyglutamate substrates.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"f75b6059-4033-5997-8b92-acc37f81289d","slug":"folh1","display_name":"Human glutamate carboxypeptidase II / FOLH1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"81c45abb-713d-521f-9854-23288f880831","slug":"folate-polyglutamates","display_name":"Folate polyglutamates","entity_type_key":"chemical_species"},"role":"object","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"experimental_model","value_text":"Recombinant human GCPII structure and enzyme assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Substrate complexes and arene-site mutants","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Catalytically inactive structures require the accompanying kinetic experiments for functional interpretation.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"folate","display_name":"Folate (vitamin B9)","entity_type_key":"chemical_species"}},{"dimension":"organism","value_text":"Homo sapiens","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The enzyme recognizes more than the glutamate tail.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[navratil2014] Structural and biochemical characterization of the folyl-poly-γ-l-glutamate hydrolyzing activity of human glutamate carboxypeptidase II (2014). https://pubmed.ncbi.nlm.nih.gov/24863754/ DOI: 10.1111/febs.12857","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified recombinant protein","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"2a3c9052-d65d-5ae3-a48b-fa5b3c7f3c4f","evidence_kind":"source_excerpt","locator":"Lines 106-116","start_line":106,"end_line":116,"excerpt":"### folate-gcpii-arene-recognition\nHuman GCPII structures and mutagenesis identified an arene-binding site that recognizes the folate portion of polyglutamate substrates.\nCondition category: normal\nnutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The enzyme recognizes more than the glutamate tail.\norganism: Homo sapiens\ntissue_or_cell_type: Purified recombinant protein\nexperimental_model: Recombinant human GCPII structure and enzyme assays\nlimitations: Catalytically inactive structures require the accompanying kinetic experiments for functional interpretation.\nexposure: Substrate complexes and arene-site mutants\n[navratil2014] Structural and biochemical characterization of the folyl-poly-γ-l-glutamate hydrolyzing activity of human glutamate carboxypeptidase II (2014). https://pubmed.ncbi.nlm.nih.gov/24863754/ DOI: 10.1111/febs.12857","model_system":"Recombinant human GCPII structure and enzyme assays","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [navratil2014] Structural and biochemical characterization of the folyl-poly-γ-l-glutamate hydrolyzing activity of human glutamate carboxypeptidase II (2014). https://pubmed.ncbi.nlm.nih.gov/24863754/ DOI: 10.1111/febs.12857","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"f4ce1a62-9582-5f7a-84f5-a23d0e1bfc68","stable_key":"import-ec174d5a-4903-5745-8646-df0e9d4265e8","title":"Folate and folic acid: mechanisms, deficiency and nutrient interactions (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":"e564d43989ece1006c95cd0748e9af6fe369074599a2eebba0a99ebff864b0dd","revision_id":"76674a33-b2a1-5e41-b71b-44399038ff7c","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}