{"id":"da31f43d-bce3-50d3-8638-fe1f21b77969","stable_key":"56f1d914-e7da-595a-af69-c217b2b47407:l-phenylalanine-pal-bypass","predicate":"converts_phenylalanine_to","statement":"Pegvaliase supplies a PEGylated microbial phenylalanine ammonia lyase pathway that converts phenylalanine to trans-cinnamate and ammonia rather than tyrosine.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"20f002d6-a26c-5e22-818e-d1c8dc46b92a","mechanism_event_label":"A drug can remove the accumulating substrate through a different chemical route.","subject":{"id":"9046d3cd-86ab-59b0-be95-58974ff21a51","slug":"pegvaliase","display_name":"Pegvaliase, PEGylated Anabaena variabilis phenylalanine ammonia lyase","entity_type_key":"drug"},"object":{"id":"0e11fae8-b747-569c-9712-31dcb92db7b1","slug":"trans-cinnamate","display_name":"trans-Cinnamate","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"20f002d6-a26c-5e22-818e-d1c8dc46b92a","stable_key":"56f1d914-e7da-595a-af69-c217b2b47407:l-phenylalanine-pal-bypass-event","event_type":"observed_relationship","label":"A drug can remove the accumulating substrate through a different chemical route.","description":"Pegvaliase supplies a PEGylated microbial phenylalanine ammonia lyase pathway that converts phenylalanine to trans-cinnamate and ammonia rather than tyrosine.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"9046d3cd-86ab-59b0-be95-58974ff21a51","slug":"pegvaliase","display_name":"Pegvaliase, PEGylated Anabaena variabilis phenylalanine ammonia lyase","entity_type_key":"drug"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"0e11fae8-b747-569c-9712-31dcb92db7b1","slug":"trans-cinnamate","display_name":"trans-Cinnamate","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"190407ad-0219-54b5-b05f-7c75f3895ca6","slug":"l-phenylalanine","display_name":"L-Phenylalanine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"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":3,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Enzyme mechanism described in the primary PRISM clinical report.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Lowering phenylalanine through this bypass does not restore the PAH-to-tyrosine reaction.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Phenylalanine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-phenylalanine","display_name":"L-Phenylalanine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"A drug can remove the accumulating substrate through a different chemical route.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Pegvaliase for the treatment of phenylketonuria: Results of a long-term phase 3 clinical trial program (PRISM). · 2018 · https://pubmed.ncbi.nlm.nih.gov/29653686/ · DOI 10.1016/j.ymgme.2018.03.006","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"bb3b5d9c-98cb-53d1-aec4-5b9d46a45a13","evidence_kind":"source_excerpt","locator":"Lines 238-244","start_line":238,"end_line":244,"excerpt":"## l-phenylalanine-pal-bypass\nA drug can remove the accumulating substrate through a different chemical route.\nPegvaliase supplies a PEGylated microbial phenylalanine ammonia lyase pathway that converts phenylalanine to trans-cinnamate and ammonia rather than tyrosine.\nModel: Enzyme mechanism described in the primary PRISM clinical report.\nLimitations: Lowering phenylalanine through this bypass does not restore the PAH-to-tyrosine reaction.\nEvidence access: Primary abstract\nPegvaliase for the treatment of phenylketonuria: Results of a long-term phase 3 clinical trial program (PRISM). · 2018 · https://pubmed.ncbi.nlm.nih.gov/29653686/ · DOI 10.1016/j.ymgme.2018.03.006","model_system":"Enzyme mechanism described in the primary PRISM clinical report.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; 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