{"id":"a0cdadf4-fae2-57df-8a56-e9fabed77031","stable_key":"63ce713e-6aea-59f6-9896-ca30e010b2ce:l-tyrosine-fah-products","predicate":"hydrolyzes","statement":"Mouse FAH structural and biochemical studies support cleavage of fumarylacetoacetate into fumarate and acetoacetate.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"ab4a5033-6c0f-58b5-b8ab-9aede51cede7","mechanism_event_label":"The pathway connects the amino-acid carbon skeleton to central metabolism.","subject":{"id":"8d08e238-df3a-5643-ad2d-74212db9c70f","slug":"mouse-fah","display_name":"Mouse fumarylacetoacetate hydrolase / Fah","entity_type_key":"protein"},"object":{"id":"ef632139-c932-5dab-ae28-4bffb9f50bd6","slug":"fumarylacetoacetate","display_name":"Fumarylacetoacetate","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"ab4a5033-6c0f-58b5-b8ab-9aede51cede7","stable_key":"63ce713e-6aea-59f6-9896-ca30e010b2ce:l-tyrosine-fah-products-event","event_type":"observed_relationship","label":"The pathway connects the amino-acid carbon skeleton to central metabolism.","description":"Mouse FAH structural and biochemical studies support cleavage of fumarylacetoacetate into fumarate and acetoacetate.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"8d08e238-df3a-5643-ad2d-74212db9c70f","slug":"mouse-fah","display_name":"Mouse fumarylacetoacetate hydrolase / Fah","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"ef632139-c932-5dab-ae28-4bffb9f50bd6","slug":"fumarylacetoacetate","display_name":"Fumarylacetoacetate","entity_type_key":"small_molecule"},"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":"0d6dab6c-2d8c-5b60-a115-63f238631e1d","slug":"fumarate","display_name":"Fumarate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"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":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Mouse enzyme structure and physiological-product complexes.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"The product-bound structure is mouse evidence; the separate human FAH gene/disease record is retained.","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":"The pathway connects the amino-acid carbon skeleton to central metabolism.","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":"e9164504-ca68-546d-9001-74335fcefad5","evidence_kind":"source_excerpt","locator":"Lines 260-266","start_line":260,"end_line":266,"excerpt":"## l-tyrosine-fah-products\nThe pathway connects the amino-acid carbon skeleton to central metabolism.\nMouse FAH structural and biochemical studies support cleavage of fumarylacetoacetate into fumarate and acetoacetate.\nModel: Mouse enzyme structure and physiological-product complexes.\nLimitations: The product-bound structure is mouse evidence; the separate human FAH gene/disease record is retained.\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 enzyme structure and physiological-product complexes.","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. Not publisher full text.","file_path":"","sha256":"7777f4440a8bfb14a04ff73e73392ccc45d8ee89f7853ecbcc0027d6f563b8a0","revision_id":"e1206111-3a75-5809-b8e9-231ff809ff1e","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}