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(2008). https://pubmed.ncbi.nlm.nih.gov/18364358/ DOI: 10.1074/jbc.m800348200","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified MIOX","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"ee3003bd-30ea-51bc-85d1-26007c8f8843","evidence_kind":"source_excerpt","locator":"Lines 457-468","start_line":457,"end_line":468,"excerpt":"### ino-miox-cleavage\nHuman MIOX catalyzes oxidative cleavage of myo-inositol to D-glucuronate.\nCondition category: normal\nnutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: MIOX opens the inositol ring, providing a route for its breakdown.\norganism: Homo sapiens\ntissue_or_cell_type: Purified MIOX\nexperimental_model: Human enzyme crystallography and catalytic analysis\nlimitations: Catabolism of inositol is not evidence that humans synthesize vitamin C from it; the crystal ligand was an inhibitor.\nexposure: Diiron center and inhibitor-bound structure\nevidence_span: {\"source_cache\": \"artifacts/inositol-research/18364358.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"9992644d489f26782d7ef0a70dc13ec5ca48e2b660a011173fba8e0d4e43ae19\", \"start_char\": 0, \"end_char\": 1004, \"text_sha256\": \"9992644d489f26782d7ef0a70dc13ec5ca48e2b660a011173fba8e0d4e43ae19\"}\n[ino-p18364358] Structural and biophysical characterization of human myo-inositol oxygenase. 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