{"id":"c475d3b7-fa76-59bc-a06f-c804ca1325c9","stable_key":"584c58f5-ab9f-53f3-97a9-55783db943b0:tryptophan-acmsd-diversion","predicate":"decarboxylates_to","statement":"Human ACMSD decarboxylates unstable ACMS, competing with its spontaneous conversion toward quinolinate in the NAD synthesis pathway.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"4be32d71-a259-54eb-ac1d-99053618ba29","mechanism_event_label":"A branch enzyme diverts material away from the quinolinate-to-NAD route.","subject":{"id":"ee9dbaa7-c987-5a0c-bea1-45a0c926187c","slug":"acmsd","display_name":"Human ACMS decarboxylase / ACMSD","entity_type_key":"protein"},"object":{"id":"f83b255b-f512-5b92-94e0-261533f2b79e","slug":"ams","display_name":"2-Aminomuconate-6-semialdehyde / AMS","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"4be32d71-a259-54eb-ac1d-99053618ba29","stable_key":"584c58f5-ab9f-53f3-97a9-55783db943b0:tryptophan-acmsd-diversion-event","event_type":"observed_relationship","label":"A branch enzyme diverts material away from the quinolinate-to-NAD route.","description":"Human ACMSD decarboxylates unstable ACMS, competing with its spontaneous conversion toward quinolinate in the NAD synthesis pathway.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"ee9dbaa7-c987-5a0c-bea1-45a0c926187c","slug":"acmsd","display_name":"Human ACMS decarboxylase / ACMSD","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"f83b255b-f512-5b92-94e0-261533f2b79e","slug":"ams","display_name":"2-Aminomuconate-6-semialdehyde / AMS","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"769339cb-213b-559e-acc0-07ed00368b94","slug":"l-tryptophan","display_name":"L-Tryptophan","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"f15dac08-9a7c-5aee-9208-ef2a09f02ff6","slug":"acms","display_name":"2-Amino-3-carboxymuconate-6-semialdehyde / ACMS","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"ab444b3c-c8ec-5ada-8450-36ac9934d6b6","slug":"quinolinic-acid","display_name":"Quinolinic acid","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"49c806c2-7041-5020-8b3b-fa04ffa122ac","slug":"zinc-ion","display_name":"Zinc(II) ion","entity_type_key":"ion"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary full text, pathway and enzyme results","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human recombinant enzyme biochemistry.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Not evidence that zinc intake universally lowers NAD or that inhibiting this branch is always desirable.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-tryptophan","display_name":"L-Tryptophan","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"A branch enzyme diverts material away from the quinolinate-to-NAD route.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Human α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD): a structural and mechanistic unveiling. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25392945/ · DOI 10.1002/prot.24722","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"a22f51aa-f5ce-595a-8451-eff98f976e23","evidence_kind":"source_excerpt","locator":"Lines 226-232","start_line":226,"end_line":232,"excerpt":"## tryptophan-acmsd-diversion\nA branch enzyme diverts material away from the quinolinate-to-NAD route.\nHuman ACMSD decarboxylates unstable ACMS, competing with its spontaneous conversion toward quinolinate in the NAD synthesis pathway.\nModel: Human recombinant enzyme biochemistry.\nLimitations: Not evidence that zinc intake universally lowers NAD or that inhibiting this branch is always desirable.\nEvidence access: Primary full text, pathway and enzyme results\nHuman α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD): a structural and mechanistic unveiling. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25392945/ · DOI 10.1002/prot.24722","model_system":"Human recombinant enzyme biochemistry.","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":"73f9d3e7-fdc9-5418-8f3c-f4ef145f6efa","stable_key":"import-584c58f5-ab9f-53f3-97a9-55783db943b0","title":"Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary-abstract references and experimental limitations individually identified. 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