{"id":"b8d1fe24-82b5-5839-901c-a8c814f3fc30","stable_key":"10aa417f-4b03-599f-a453-4aa09edeb27c:alanine-agt-reaction","predicate":"transaminates","statement":"Purified untagged human AGXT catalyzed the PLP-dependent reaction alanine + glyoxylate ⇌ pyruvate + glycine; forward and reverse kinetic parameters were measured.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"9fc1e902-60c7-5b12-aa6b-3cbbcf841a73","mechanism_event_label":"Alanine supplies an amino group that turns glyoxylate into glycine.","subject":{"id":"e168c766-6f90-51e6-8efb-4852dd4c8220","slug":"agxt","display_name":"Human peroxisomal alanine:glyoxylate aminotransferase / AGXT","entity_type_key":"protein"},"object":{"id":"b83bbee2-3a3b-50b9-b3b2-e3494607ecaa","slug":"glyoxylate","display_name":"Glyoxylate","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"9fc1e902-60c7-5b12-aa6b-3cbbcf841a73","stable_key":"10aa417f-4b03-599f-a453-4aa09edeb27c:alanine-agt-reaction-event","event_type":"observed_relationship","label":"Alanine supplies an amino group that turns glyoxylate into glycine.","description":"Purified untagged human AGXT catalyzed the PLP-dependent reaction alanine + glyoxylate ⇌ pyruvate + glycine; forward and reverse kinetic parameters were measured.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"e168c766-6f90-51e6-8efb-4852dd4c8220","slug":"agxt","display_name":"Human peroxisomal alanine:glyoxylate aminotransferase / AGXT","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"b83bbee2-3a3b-50b9-b3b2-e3494607ecaa","slug":"glyoxylate","display_name":"Glyoxylate","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"ebdc4461-c059-563e-88b0-422c21fdaa25","slug":"alanine","display_name":"L-Alanine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"6b656ff5-9532-5da4-8eea-8ca163a48649","slug":"pyridoxal-phosphate","display_name":"PLP","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"91e6d4f5-fba1-542d-b68a-57cc28e1e425","slug":"pyruvate","display_name":"Pyruvate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"2b507258-430c-51fe-9fd2-e510c2c197a9","slug":"glycine","display_name":"Glycine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant human liver enzyme expressed in E. coli; kinetic and cofactor-binding assays.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Peroxisomal enzyme identity does not mean intracellular flux or supplement benefit was measured.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Alanine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"alanine","display_name":"L-Alanine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Alanine supplies an amino group that turns glyoxylate into glycine.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Construction, purification and characterization of untagged human liver alanine-glyoxylate aminotransferase expressed in Escherichia coli. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18289107/ · DOI 10.2174/092986608783489580","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"228ac2d7-f42d-5f52-9f93-ae4158a7a1d6","evidence_kind":"source_excerpt","locator":"Lines 32-38","start_line":32,"end_line":38,"excerpt":"## alanine-agt-reaction\nAlanine supplies an amino group that turns glyoxylate into glycine.\nPurified untagged human AGXT catalyzed the PLP-dependent reaction alanine + glyoxylate ⇌ pyruvate + glycine; forward and reverse kinetic parameters were measured.\nModel: Recombinant human liver enzyme expressed in E. coli; kinetic and cofactor-binding assays.\nLimitations: Peroxisomal enzyme identity does not mean intracellular flux or supplement benefit was measured.\nEvidence access: Primary abstract\nConstruction, purification and characterization of untagged human liver alanine-glyoxylate aminotransferase expressed in Escherichia coli. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18289107/ · DOI 10.2174/092986608783489580","model_system":"Recombinant human liver enzyme expressed in E. coli; kinetic and cofactor-binding assays.","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":"01c5554c-a8ba-5c86-9b01-a0fa1a886cdb","stable_key":"import-10aa417f-4b03-599f-a453-4aa09edeb27c","title":"L-Alanine: carbon, nitrogen, protein synthesis 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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