Inositol oxygenase is a non-heme di-iron enzyme which oxidizes myo-inositol to glucuronic acid.  It will also oxidize the less abundant chiro isomer 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. PMID 19173070.
- ^ 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: 313–320. PMID 11716759.
- ^ 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 Sciences 165 (2): 564–76. PMID 5259614.
- ^ 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: 8510–8518. PMID 7263666.
- ^ 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: 220–227. PMID 13630882.
- ^ 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 experimental 39 (10): 1026–32. PMID 2170818.
See also 
External links