{"id":"cd9fe5cf-0454-54b8-a5bf-973bad4d39c3","stable_key":"1310afbd-6010-586e-805d-551d846da421:b6-transport-pdxp-plp","predicate":"dephosphorylates","statement":"Catalytically active recombinant human pyridoxal phosphatase hydrolyzed pyridoxal-phosphate.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"43e42410-7dd3-58b7-b001-562361d3ff95","mechanism_event_label":"PDXP removes phosphate from a B6 vitamer.","subject":{"id":"a0d74853-72b7-546d-a7c7-d37602ba990a","slug":"pdxp","display_name":"Human pyridoxal phosphatase / PDXP","entity_type_key":"protein"},"object":{"id":"6b656ff5-9532-5da4-8eea-8ca163a48649","slug":"pyridoxal-phosphate","display_name":"PLP","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"43e42410-7dd3-58b7-b001-562361d3ff95","stable_key":"1310afbd-6010-586e-805d-551d846da421:b6-transport-pdxp-plp-event","event_type":"biochemical_relationship","label":"PDXP removes phosphate from a B6 vitamer.","description":"Catalytically active recombinant human pyridoxal phosphatase hydrolyzed pyridoxal-phosphate.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"6b656ff5-9532-5da4-8eea-8ca163a48649","slug":"pyridoxal-phosphate","display_name":"PLP","entity_type_key":"small_molecule"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"9bf6269d-9e01-553d-bd8b-11a0d613bfca","slug":"pyridoxal","display_name":"Pyridoxal","entity_type_key":"small_molecule"},"role":"dephosphorylated product","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"b28dfc54-a5ef-5f9e-ac1f-890b68e58dc3","slug":"inorganic-phosphate","display_name":"Inorganic phosphate","entity_type_key":"chemical_species"},"role":"released phosphate","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"a0d74853-72b7-546d-a7c7-d37602ba990a","slug":"pdxp","display_name":"Human pyridoxal phosphatase / PDXP","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_location","value_text":"Indexed abstract: cloning and substrate hydrolysis","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant human pyridoxal phosphatase expressed in E. coli.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Recombinant-enzyme characterization.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Model-specific evidence; no dietary threshold or treatment benefit established.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"vitamin-b6","display_name":"Vitamin B6","entity_type_key":"chemical_species"}},{"dimension":"organism","value_text":"Homo sapiens","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"PDXP removes phosphate from a B6 vitamer.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[jang2003] Human pyridoxal phosphatase. 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(2003). https://pubmed.ncbi.nlm.nih.gov/14522954/ DOI: 10.1074/jbc.m309619200","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified recombinant human enzyme","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"d65ae46c-64b0-569c-8b6a-d93861df9d86","evidence_kind":"source_excerpt","locator":"Lines 256-267","start_line":256,"end_line":267,"excerpt":"### b6-transport-pdxp-plp\nCatalytically active recombinant human pyridoxal phosphatase hydrolyzed pyridoxal-phosphate.\nCondition category: normal\nnutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: PDXP removes phosphate from a B6 vitamer.\norganism: Homo sapiens\ntissue_or_cell_type: Purified recombinant human enzyme\nexperimental_model: Recombinant human pyridoxal phosphatase expressed in E. coli.\nlimitations: Model-specific evidence; no dietary threshold or treatment benefit established.\nexposure: Recombinant-enzyme characterization.\nevidence_location: Indexed abstract: cloning and substrate hydrolysis\n[jang2003] Human pyridoxal phosphatase. 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