{"id":"1d73aeaa-bc42-56e7-9d8a-e7b7cf862dd4","stable_key":"ec174d5a-4903-5745-8646-df0e9d4265e8:rat-ftcd-cyclodeamination","predicate":"cyclodeaminates","statement":"Rat FTCD cyclodeaminase converts 5-formimino-THF to 5,10-methenyl-THF with ammonia release.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"4f4f4e3d-7924-54a9-8e5d-d07bbd277368","mechanism_event_label":"A second enzyme domain converts the transferred group into methenyl-folate.","subject":{"id":"061381b6-694e-5039-a62a-3f1b8cfc9381","slug":"rat-ftcd","display_name":"Rat formiminotransferase cyclodeaminase / FTCD","entity_type_key":"protein"},"object":{"id":"0770ecec-23d8-5681-8c71-c7899075d20e","slug":"5-formiminotetrahydrofolate","display_name":"5-Formiminotetrahydrofolate","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"4f4f4e3d-7924-54a9-8e5d-d07bbd277368","stable_key":"ec174d5a-4903-5745-8646-df0e9d4265e8:rat-ftcd-cyclodeamination-event","event_type":"biochemical_relationship","label":"A second enzyme domain converts the transferred group into methenyl-folate.","description":"Rat FTCD cyclodeaminase converts 5-formimino-THF to 5,10-methenyl-THF with ammonia release.","status":"provisional","compartment":{"slug":"cytosol","display_name":"Cytosol"},"participants":[{"entity":{"id":"7978c99f-fb17-5d91-a9e4-178558bfa69f","slug":"5-10-methenyltetrahydrofolate","display_name":"5,10-Methenyltetrahydrofolate","entity_type_key":"small_molecule"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"1374ec24-1a5b-552b-982f-51f9082f4187","slug":"ammonia","display_name":"Ammonia","entity_type_key":"small_molecule"},"role":"coproduct","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"061381b6-694e-5039-a62a-3f1b8cfc9381","slug":"rat-ftcd","display_name":"Rat formiminotransferase cyclodeaminase / FTCD","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"0770ecec-23d8-5681-8c71-c7899075d20e","slug":"5-formiminotetrahydrofolate","display_name":"5-Formiminotetrahydrofolate","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_location","value_text":"Cyclodeaminase active-site results and enzyme assay methods.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant protein catalytic assay and mutagenesis","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Recombinant rat FTCD and CD-site mutants.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Rat enzyme; human catalytic rates are not measured.","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":"Rattus norvegicus","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"A second enzyme domain converts the transferred group into methenyl-folate.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mao-2004] Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer (2004). https://pubmed.ncbi.nlm.nih.gov/15272307/ DOI: 10.1038/sj.emboj.7600327","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Cell-free","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"ce8d1c1e-a4db-5e81-9bd4-3d668664b3aa","evidence_kind":"source_excerpt","locator":"Lines 1308-1319","start_line":1308,"end_line":1319,"excerpt":"### rat-ftcd-cyclodeamination\nRat FTCD cyclodeaminase converts 5-formimino-THF to 5,10-methenyl-THF with ammonia release.\nCondition category: normal\nnutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: A second enzyme domain converts the transferred group into methenyl-folate.\norganism: Rattus norvegicus\ntissue_or_cell_type: Cell-free\nexperimental_model: Recombinant protein catalytic assay and mutagenesis\nlimitations: Rat enzyme; human catalytic rates are not measured.\nexposure: Recombinant rat FTCD and CD-site mutants.\nevidence_location: Cyclodeaminase active-site results and enzyme assay methods.\n[mao-2004] Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer (2004). https://pubmed.ncbi.nlm.nih.gov/15272307/ DOI: 10.1038/sj.emboj.7600327","model_system":"Recombinant protein catalytic assay and mutagenesis","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [mao-2004] Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer (2004). https://pubmed.ncbi.nlm.nih.gov/15272307/ DOI: 10.1038/sj.emboj.7600327","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}