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(2004). https://pubmed.ncbi.nlm.nih.gov/15249053/ DOI: 10.1016/j.pep.2004.04.021","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified human enzyme","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"e25f395b-eeba-55be-bdf3-db975908fb21","evidence_kind":"source_excerpt","locator":"Lines 189-201","start_line":189,"end_line":201,"excerpt":"### b6-transport-pdxk-mgatp\nKinase kinetic experiments identified MgATP as the preferred phosphate-donor complex under the reported physiological assay conditions.\nCondition category: normal\nnutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Magnesium helps supply ATP to B6 activation.\norganism: Homo sapiens\ntissue_or_cell_type: Purified human enzyme\nexperimental_model: Purified recombinant human and E. coli pyridoxal kinases.\nlimitations: Metal preference depends on assay conditions and does not prove magnesium supplementation improves B6 status.\nexposure: MgATP versus ZnATP kinetic comparisons.\nevidence_location: Indexed abstract and publisher abstract; human enzyme findings only\ncross_nutrient: Magnesium-B6 activation chemistry.\n[disalvo2004] Expression, purification, and kinetic constants for human and Escherichia coli pyridoxal kinases. 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