{"id":"e9093a13-d12e-5ec6-82ff-e1d491da7920","stable_key":"e37461ea-ea5d-5e2c-8091-138305f6dd70:l-aspartate-cad-aspartate-reaction","predicate":"uses_aspartate_to_make","statement":"Purified human CAD aspartate-transcarbamylase domain converted carbamoyl phosphate and aspartate to carbamoyl-aspartate in an initial-rate assay.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"c647c6e7-7215-50c8-a02a-8cc41523acdd","mechanism_event_label":"Aspartate becomes part of the precursor used to build pyrimidine bases.","subject":{"id":"64cc3b93-3e99-5221-bd91-049d190e54c7","slug":"cad","display_name":"Human CAD multifunctional pyrimidine synthesis enzyme","entity_type_key":"protein"},"object":{"id":"459b6345-058b-53d7-9c35-0b61fdf43b0b","slug":"n-carbamoyl-l-aspartate","display_name":"N-Carbamoyl-L-aspartate","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"c647c6e7-7215-50c8-a02a-8cc41523acdd","stable_key":"e37461ea-ea5d-5e2c-8091-138305f6dd70:l-aspartate-cad-aspartate-reaction-event","event_type":"observed_relationship","label":"Aspartate becomes part of the precursor used to build pyrimidine bases.","description":"Purified human CAD aspartate-transcarbamylase domain converted carbamoyl phosphate and aspartate to carbamoyl-aspartate in an initial-rate assay.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"64cc3b93-3e99-5221-bd91-049d190e54c7","slug":"cad","display_name":"Human CAD multifunctional pyrimidine synthesis enzyme","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"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":"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":"b265adfe-73f7-503d-8bee-e7667a25189f","slug":"carbamoyl-phosphate","display_name":"Carbamoyl phosphate","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 CAD ATCase domain fused to MBP; biochemical assay.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Isolated-domain kinetics are not whole-cell nucleotide flux.","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":"Aspartate becomes part of the precursor used to build pyrimidine bases.","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":"43cf0e02-b32b-5503-8406-e748c801aded","evidence_kind":"source_excerpt","locator":"Lines 146-152","start_line":146,"end_line":152,"excerpt":"## l-aspartate-cad-aspartate-reaction\nAspartate becomes part of the precursor used to build pyrimidine bases.\nPurified human CAD aspartate-transcarbamylase domain converted carbamoyl phosphate and aspartate to carbamoyl-aspartate in an initial-rate assay.\nModel: Recombinant human CAD ATCase domain fused to MBP; biochemical assay.\nLimitations: Isolated-domain kinetics are not whole-cell nucleotide flux.\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 CAD ATCase domain fused to MBP; biochemical assay.","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":"67970dcb-34e0-5b0a-8c86-d8c3cc183444","stable_key":"import-e37461ea-ea5d-5e2c-8091-138305f6dd70","title":"L-Aspartate: redox transfer, nitrogen partitioning 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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