{"id":"0bc301db-3529-5545-8d15-ed613baa95ca","stable_key":"e37461ea-ea5d-5e2c-8091-138305f6dd70:l-aspartate-asns-reaction","predicate":"converts_aspartate_to","statement":"Human ASNS catalyzes ATP-dependent conversion of aspartate and glutamine to asparagine and glutamate through coupled glutaminase and synthetase chemistry.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"0879db53-f665-5ff9-a0be-d3f0277db4c4","mechanism_event_label":"Making asparagine needs both aspartate and a nitrogen donor, plus energy.","subject":{"id":"d963b556-e89d-551f-960b-24d695590bda","slug":"asns","display_name":"Human asparagine synthetase / ASNS","entity_type_key":"protein"},"object":{"id":"22df3254-9178-50c5-899c-d004c1316ab0","slug":"l-asparagine","display_name":"L-Asparagine","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"0879db53-f665-5ff9-a0be-d3f0277db4c4","stable_key":"e37461ea-ea5d-5e2c-8091-138305f6dd70:l-aspartate-asns-reaction-event","event_type":"observed_relationship","label":"Making asparagine needs both aspartate and a nitrogen donor, plus energy.","description":"Human ASNS catalyzes ATP-dependent conversion of aspartate and glutamine to asparagine and glutamate through coupled glutaminase and synthetase chemistry.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"d963b556-e89d-551f-960b-24d695590bda","slug":"asns","display_name":"Human asparagine synthetase / ASNS","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"22df3254-9178-50c5-899c-d004c1316ab0","slug":"l-asparagine","display_name":"L-Asparagine","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":"8637bb39-2c30-5168-baaf-3e613d831db0","slug":"glutamine","display_name":"L-Glutamine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"7da684a4-2641-5bc6-93ae-8c6aa384e487","slug":"glutamate","display_name":"L-Glutamate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"58b974f1-d389-5bf6-81cd-889c44442c42","slug":"atp","display_name":"ATP","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""},{"entity":{"id":"d47321ac-44bb-5a88-afdb-6435b57a91b9","slug":"amp","display_name":"AMP","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":6,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary full text","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human recombinant ASNS structural and biochemical study; reaction characterized in the study framework.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"A functioning reaction does not guarantee that adding substrate raises the product in every tissue. Correction record: The 2019 author correction added omitted author affiliations and funding acknowledgements; no mechanism or data change was stated. PMID 31799439; DOI 10.1038/s42003-019-0690-1. https://www.nature.com/articles/s42003-019-0690-1","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":"Making asparagine needs both aspartate and a nitrogen donor, plus energy.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"High-resolution crystal structure of human asparagine synthetase enables analysis of inhibitor binding and selectivity. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31552298/ · DOI 10.1038/s42003-019-0587-z","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"b0676663-c479-5ebd-9221-af5b49a7add7","evidence_kind":"source_excerpt","locator":"Lines 186-192","start_line":186,"end_line":192,"excerpt":"## l-aspartate-asns-reaction\nMaking asparagine needs both aspartate and a nitrogen donor, plus energy.\nHuman ASNS catalyzes ATP-dependent conversion of aspartate and glutamine to asparagine and glutamate through coupled glutaminase and synthetase chemistry.\nModel: Human recombinant ASNS structural and biochemical study; reaction characterized in the study framework.\nLimitations: A functioning reaction does not guarantee that adding substrate raises the product in every tissue. Correction record: The 2019 author correction added omitted author affiliations and funding acknowledgements; no mechanism or data change was stated. PMID 31799439; DOI 10.1038/s42003-019-0690-1. https://www.nature.com/articles/s42003-019-0690-1\nEvidence access: Primary full text\nHigh-resolution crystal structure of human asparagine synthetase enables analysis of inhibitor binding and selectivity. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31552298/ · DOI 10.1038/s42003-019-0587-z","model_system":"Human recombinant ASNS structural and biochemical study; reaction characterized in the study framework.","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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