{"id":"5c96fa52-2c16-5937-9226-fb9e6884a4d3","stable_key":"1310afbd-6010-586e-805d-551d846da421:b6-met-cth-t67i-activity","predicate":"reduces-function-of","statement":"Expressed human CTH Thr67Ile had 13% of wild-type catalytic activity in the 2009 study.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"negative","is_public":true,"mechanism_event_id":"f264b72f-0582-50a6-95f0-e5f882b6b480","mechanism_event_label":"This inherited enzyme change reduces catalytic capacity.","subject":{"id":"89035279-3693-59aa-9866-1c6f5baaf92e","slug":"cth-t67i","display_name":"Human CTH Thr67Ile variant","entity_type_key":"protein_state"},"object":{"id":"4014ee3a-0e44-5379-b541-174aa75bcf90","slug":"cth","display_name":"Human cystathionine gamma-lyase / CTH","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"f264b72f-0582-50a6-95f0-e5f882b6b480","stable_key":"1310afbd-6010-586e-805d-551d846da421:b6-met-cth-t67i-activity-event","event_type":"biochemical_relationship","label":"This inherited enzyme change reduces catalytic capacity.","description":"Expressed human CTH Thr67Ile had 13% of wild-type catalytic activity in the 2009 study.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"89035279-3693-59aa-9866-1c6f5baaf92e","slug":"cth-t67i","display_name":"Human CTH Thr67Ile variant","entity_type_key":"protein_state"},"role":"variant enzyme","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"4014ee3a-0e44-5379-b541-174aa75bcf90","slug":"cth","display_name":"Human cystathionine gamma-lyase / CTH","entity_type_key":"protein"},"role":"wild-type comparator","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"6b656ff5-9532-5da4-8eea-8ca163a48649","slug":"pyridoxal-phosphate","display_name":"PLP","entity_type_key":"small_molecule"},"role":"cofactor","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"availability_state","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null},{"dimension":"experimental_model","value_text":"Human families; expressed human CTH variants","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Recombinant assay result; not proof of a universal clinical syndrome.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"vitamin-b6","display_name":"Vitamin B6","entity_type_key":"chemical_species"}},{"dimension":"organism","value_text":"Homo sapiens","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"This inherited enzyme change reduces catalytic capacity.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[b6-cth-2009] Cystathionine gamma-lyase: Clinical, metabolic, genetic, and structural studies. (2009). https://pmc.ncbi.nlm.nih.gov/articles/PMC2752209/ DOI: 10.1016/j.ymgme.2009.04.001","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified recombinant protein; no intact tissue","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"trigger_kind","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null}],"evidence":[{"id":"4f2b3020-978f-5239-824a-21fd66f39c7d","evidence_kind":"source_excerpt","locator":"Lines 566-575","start_line":566,"end_line":575,"excerpt":"### b6-met-cth-t67i-activity\nExpressed human CTH Thr67Ile had 13% of wild-type catalytic activity in the 2009 study.\nCondition category: machinery_impairment\nnutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: This inherited enzyme change reduces catalytic capacity.\norganism: Homo sapiens\ntissue_or_cell_type: Purified recombinant protein; no intact tissue\nexperimental_model: Human families; expressed human CTH variants\nlimitations: Recombinant assay result; not proof of a universal clinical syndrome.\n[b6-cth-2009] Cystathionine gamma-lyase: Clinical, metabolic, genetic, and structural studies. (2009). https://pmc.ncbi.nlm.nih.gov/articles/PMC2752209/ DOI: 10.1016/j.ymgme.2009.04.001","model_system":"Human families; expressed human CTH variants","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [b6-cth-2009] Cystathionine gamma-lyase: Clinical, metabolic, genetic, and structural studies. (2009). https://pmc.ncbi.nlm.nih.gov/articles/PMC2752209/ DOI: 10.1016/j.ymgme.2009.04.001","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"251773bb-16f5-5903-b135-db4a61d9dec4","stable_key":"import-1310afbd-6010-586e-805d-551d846da421","title":"Vitamin B6: 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":"ef0019b344b2219220f801a84d0d138ff6880c1be1a59540d9034bfa4334f61e","revision_id":"cac3555f-48af-5c52-a84e-add4482c87fb","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}