{"id":"47c0d236-a867-52fe-8888-9f9a0c663aef","stable_key":"e37461ea-ea5d-5e2c-8091-138305f6dd70:l-aspartate-succinate-atcase","predicate":"competitively_inhibits","statement":"Succinate competitively inhibited aspartate utilization by the purified human CAD ATCase domain.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"5c3a7415-5cdd-56d6-ba87-6da460b383b0","mechanism_event_label":"An accumulated carbon-cycle metabolite competes with aspartate at a nucleotide-making enzyme.","subject":{"id":"462f63ce-a2c1-5312-9c14-70b8b12e1d6e","slug":"succinate","display_name":"Succinate","entity_type_key":"small_molecule"},"object":{"id":"64cc3b93-3e99-5221-bd91-049d190e54c7","slug":"cad","display_name":"Human CAD multifunctional pyrimidine synthesis enzyme","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"5c3a7415-5cdd-56d6-ba87-6da460b383b0","stable_key":"e37461ea-ea5d-5e2c-8091-138305f6dd70:l-aspartate-succinate-atcase-event","event_type":"observed_relationship","label":"An accumulated carbon-cycle metabolite competes with aspartate at a nucleotide-making enzyme.","description":"Succinate competitively inhibited aspartate utilization by the purified human CAD ATCase domain.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"462f63ce-a2c1-5312-9c14-70b8b12e1d6e","slug":"succinate","display_name":"Succinate","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"64cc3b93-3e99-5221-bd91-049d190e54c7","slug":"cad","display_name":"Human CAD multifunctional pyrimidine synthesis enzyme","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"0a0923d3-72b7-5d6a-bf3a-5a7a3071a09b","slug":"l-aspartate","display_name":"L-Aspartate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"459b6345-058b-53d7-9c35-0b61fdf43b0b","slug":"n-carbamoyl-l-aspartate","display_name":"N-Carbamoyl-L-aspartate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary full text","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant human ATCase kinetic experiments with succinate and substrate titration.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"This is not proof that ordinary dietary succinate or aspartate concentrations cause the same inhibition in a person.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Aspartate collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-aspartate","display_name":"L-Aspartate","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"An accumulated carbon-cycle metabolite competes with aspartate at a nucleotide-making enzyme.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Succinate dehydrogenase loss suppresses pyrimidine biosynthesis via succinate-mediated inhibition of aspartate transcarbamylase. · 2026 · https://pubmed.ncbi.nlm.nih.gov/42082831/ · DOI 10.1038/s42255-026-01524-w","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"f4aaaa8c-ef6b-5b01-bd1a-82554c04e914","evidence_kind":"source_excerpt","locator":"Lines 210-216","start_line":210,"end_line":216,"excerpt":"## l-aspartate-succinate-atcase\nAn accumulated carbon-cycle metabolite competes with aspartate at a nucleotide-making enzyme.\nSuccinate competitively inhibited aspartate utilization by the purified human CAD ATCase domain.\nModel: Recombinant human ATCase kinetic experiments with succinate and substrate titration.\nLimitations: This is not proof that ordinary dietary succinate or aspartate concentrations cause the same inhibition in a person.\nEvidence access: Primary full text\nSuccinate dehydrogenase loss suppresses pyrimidine biosynthesis via succinate-mediated inhibition of aspartate transcarbamylase. · 2026 · https://pubmed.ncbi.nlm.nih.gov/42082831/ · DOI 10.1038/s42255-026-01524-w","model_system":"Recombinant human ATCase kinetic experiments with succinate and substrate titration.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; 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