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(2004). https://pubmed.ncbi.nlm.nih.gov/15024000/ DOI: 10.1074/jbc.m312078200","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified enzyme; yeast cultures","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"62ac5737-7f30-527e-a2af-68aa86a41e44","evidence_kind":"source_excerpt","locator":"Lines 171-182","start_line":171,"end_line":182,"excerpt":"### ino-isyna-synthesis\nRecombinant human ISYNA1 converted D-glucose 6-phosphate to 1D-myo-inositol 3-phosphate, an entry step in de novo inositol synthesis.\nCondition category: normal\nnutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Cells have a route to build the inositol ring from a glucose-derived molecule.\norganism: Human protein expressed in bacteria and yeast\ntissue_or_cell_type: Purified enzyme; yeast cultures\nexperimental_model: Recombinant human enzyme and complementation of yeast ino1 deletion\nlimitations: Purified-enzyme and yeast results do not establish supplement effects or a human dietary deficiency threshold.\nexposure: Substrate, NAD+, cation and valproate experiments\nevidence_span: {\"source_cache\": \"artifacts/inositol-research/15024000.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"5ab3a8eda77989c3e4a681b4a971fb7e969c285d3e5c8e41bc31713a7f88c9ac\", \"start_char\": 0, \"end_char\": 1427, \"text_sha256\": \"5ab3a8eda77989c3e4a681b4a971fb7e969c285d3e5c8e41bc31713a7f88c9ac\"}\n[ino-p15024000] Human 1-D-myo-inositol-3-phosphate synthase is functional in yeast. 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