Inositol oxygenase is a non-hemedi-ironenzyme which oxidizes myo-inositol to glucuronic acid.  It will also oxidize the less abundant chiroisomer of inositol.  This enzyme is part of the only known pathway for the catabolism of inositol in humans. It is expressed mostly in the kidneys. Depletion of Inositol Oxygenase and accumulation of polyols, such as inositol and xylitol, have been cited as contributing factors in complications associated with diabetes.
^Bollinger JM, Jr; Diao, Y; Matthews, ML; Xing, G; Krebs, C (2009 Feb 14). "myo-Inositol oxygenase: a radical new pathway for O(2) and C-H activation at a nonheme diiron cluster.". Dalton transactions (Cambridge, England : 2003) (6): 905–14. doi:10.1039/b811885j. PMID19173070.Check date values in: |date= (help)
^Arner, R.J., Prabhu, K.S., Thompson, J.T., Hildenbrandt, G.R., Liken, A.D. and Reddy, C.C. (2001). "myo-Inositol oxygenase: molecular cloning and expression of a unique enzyme that oxidizes myo-inositol and D-chiro-inositol". Biochem. J.360 (Pt 2): 313–320. PMC1222231. PMID11716759.
^Hankes, LV; Politzer, WM; Touster, O; Anderson, L (17 Oct 1969). "Myo-inositol catabolism in human pentosurics: the predominant role of the glucuronate-xylulose-pentose phosphate pathway.". Annals of the New York Academy of Sciences165 (2): 564–76. PMID5259614.
^Reddy, C.C., Swan, J.S. and Hamilton, G.A. (1981). "myo-Inositol oxygenase from hog kidney. I. Purification and characterization of the oxygenase and of an enzyme complex containing the oxygenase and D-glucuronate reductase". J. Biol. Chem.256 (16): 8510–8518. PMID7263666.
^Charalampous, F.C. (1959). "Biochemical studies on inositol. V. Purification and properties of the enzyme that cleaves inositol to D-glucuronic acid". J. Biol. Chem.234 (2): 220–227. PMID13630882.
^Cohen, RA; MacGregor, LC; Spokes, KC; Silva, P; Epstein, FH (1990 Oct). "Effect of myo-inositol on renal Na-K-ATPase in experimental diabetes.". Metabolism: clinical and experimental39 (10): 1026–32. PMID2170818.Check date values in: |date= (help)