{"id":"78f9d4d1-f9fe-5fd8-ad28-f1581228cc97","stable_key":"10aa417f-4b03-599f-a453-4aa09edeb27c:alanine-agt-pmp-cycle","predicate":"retains_catalytic_intermediate","statement":"Pre-steady-state analysis of human AGXT showed that PMP remained bound during its catalytic cycle and the AGXT–PMP complex reacted efficiently with oxo-acid substrates.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"480faa7b-95cd-58fa-a864-a04fac697c23","mechanism_event_label":"The B6 cofactor changes form while helping transfer nitrogen.","subject":{"id":"e168c766-6f90-51e6-8efb-4852dd4c8220","slug":"agxt","display_name":"Human peroxisomal alanine:glyoxylate aminotransferase / AGXT","entity_type_key":"protein"},"object":{"id":"c8dec85c-c85d-5a55-ba85-ad3c1b3e332b","slug":"pyridoxamine-phosphate","display_name":"Pyridoxamine 5-prime-phosphate","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"480faa7b-95cd-58fa-a864-a04fac697c23","stable_key":"10aa417f-4b03-599f-a453-4aa09edeb27c:alanine-agt-pmp-cycle-event","event_type":"observed_relationship","label":"The B6 cofactor changes form while helping transfer nitrogen.","description":"Pre-steady-state analysis of human AGXT showed that PMP remained bound during its catalytic cycle and the AGXT–PMP complex reacted efficiently with oxo-acid substrates.","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":"c8dec85c-c85d-5a55-ba85-ad3c1b3e332b","slug":"pyridoxamine-phosphate","display_name":"Pyridoxamine 5-prime-phosphate","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":"b83bbee2-3a3b-50b9-b3b2-e3494607ecaa","slug":"glyoxylate","display_name":"Glyoxylate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":5,"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":6,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified human AGXT; PLP-form reactions with alanine/glycine and PMP-form reactions with pyruvate/glyoxylate.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Cofactor cycling is not evidence that B6 is irreversibly consumed once per reaction.","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":"The B6 cofactor changes form while helping transfer nitrogen.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17696873/ · DOI 10.1042/BJ20070637","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"801af6f7-7be9-57e4-baaa-a3fe765746c5","evidence_kind":"source_excerpt","locator":"Lines 40-46","start_line":40,"end_line":46,"excerpt":"## alanine-agt-pmp-cycle\nThe B6 cofactor changes form while helping transfer nitrogen.\nPre-steady-state analysis of human AGXT showed that PMP remained bound during its catalytic cycle and the AGXT–PMP complex reacted efficiently with oxo-acid substrates.\nModel: Purified human AGXT; PLP-form reactions with alanine/glycine and PMP-form reactions with pyruvate/glyoxylate.\nLimitations: Cofactor cycling is not evidence that B6 is irreversibly consumed once per reaction.\nEvidence access: Primary abstract\nHuman wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17696873/ · DOI 10.1042/BJ20070637","model_system":"Purified human AGXT; PLP-form reactions with alanine/glycine and PMP-form reactions with pyruvate/glyoxylate.","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; 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