{"id":"fb3c05a2-df3b-5b37-8b71-a05833906f57","stable_key":"63ce713e-6aea-59f6-9896-ca30e010b2ce:l-tyrosine-fah-calcium","predicate":"coordinates_products_in","statement":"The mouse FAH product complex places acetoacetate at a coordinated calcium ion near a Glu-His catalytic dyad.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"b61f9bf2-26d6-5a29-aa78-19bbcd749481","mechanism_event_label":"A metal participates in the terminal cleavage chemistry.","subject":{"id":"e359bc15-e675-5d83-b0fe-1d70814e130b","slug":"calcium-ion","display_name":"Calcium ion","entity_type_key":"ion"},"object":{"id":"8d08e238-df3a-5643-ad2d-74212db9c70f","slug":"mouse-fah","display_name":"Mouse fumarylacetoacetate hydrolase / Fah","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"b61f9bf2-26d6-5a29-aa78-19bbcd749481","stable_key":"63ce713e-6aea-59f6-9896-ca30e010b2ce:l-tyrosine-fah-calcium-event","event_type":"observed_relationship","label":"A metal participates in the terminal cleavage chemistry.","description":"The mouse FAH product complex places acetoacetate at a coordinated calcium ion near a Glu-His catalytic dyad.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"e359bc15-e675-5d83-b0fe-1d70814e130b","slug":"calcium-ion","display_name":"Calcium ion","entity_type_key":"ion"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"8d08e238-df3a-5643-ad2d-74212db9c70f","slug":"mouse-fah","display_name":"Mouse fumarylacetoacetate hydrolase / Fah","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"bcfef85f-831d-5439-ba51-1aef4b090441","slug":"l-tyrosine","display_name":"L-Tyrosine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"1b77cb4a-1f79-50e2-b4f0-fd0953cb914e","slug":"acetoacetate","display_name":"Acetoacetate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Mouse FAH X-ray structure; catalytic roles proposed from structure and mutagenesis.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"This is not evidence that calcium supplementation restores FAH disease.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-tyrosine","display_name":"L-Tyrosine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"A metal participates in the terminal cleavage chemistry.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Crystal structure and mechanism of a carbon-carbon bond hydrolase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10508789/ · DOI 10.1016/s0969-2126(99)80170-1","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"5d8633d5-2eb3-5ace-baea-d0ca00391fac","evidence_kind":"source_excerpt","locator":"Lines 268-274","start_line":268,"end_line":274,"excerpt":"## l-tyrosine-fah-calcium\nA metal participates in the terminal cleavage chemistry.\nThe mouse FAH product complex places acetoacetate at a coordinated calcium ion near a Glu-His catalytic dyad.\nModel: Mouse FAH X-ray structure; catalytic roles proposed from structure and mutagenesis.\nLimitations: This is not evidence that calcium supplementation restores FAH disease.\nEvidence access: Primary abstract\nCrystal structure and mechanism of a carbon-carbon bond hydrolase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10508789/ · DOI 10.1016/s0969-2126(99)80170-1","model_system":"Mouse FAH X-ray structure; catalytic roles proposed from structure and mutagenesis.","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":"12917df2-c6e0-5b61-850f-dbff6d4b4d30","stable_key":"import-63ce713e-6aea-59f6-9896-ca30e010b2ce","title":"L-Tyrosine: catecholamines, thyroid chemistry, pigment, 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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