EC |
1.13.99.1 |
Accepted name: |
inositol oxygenase |
Reaction: |
myo-inositol + O2 = D-glucuronate + H2O |
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For diagram of mammalian ascorbic-acid biosynthesis, click here |
Other name(s): |
meso-inositol oxygenase; myo-inositol oxygenase; MOO |
Systematic name: |
myo-inositol:oxygen oxidoreductase |
Comments: |
An iron protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-59-8 |
References: |
1. |
Charalampous, F.C. Biochemical studies on inositol. V. Purification and properties of the enzyme that cleaves inositol to D-glucuronic acid. J. Biol. Chem. 234 (1959) 220–227. [PMID: 13630882] |
2. |
Reddy, C.C., Swan, J.S. and Hamilton, G.A. 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 (1981) 8510–8518. [PMID: 7263666] |
3. |
Arner, R.J., Prabhu, K.S., Thompson, J.T., Hildenbrandt, G.R., Liken, A.D. and Reddy, C.C. myo-Inositol oxygenase: molecular cloning and expression of a unique enzyme that oxidizes myo-inositol and D-chiro-inositol. Biochem. J. 360 (2001) 313–320. [PMID: 11716759] |
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[EC 1.13.99.1 created 1961 as EC 1.99.2.6, transferred 1965 to EC 1.13.1.11, transferred 1972 to EC 1.13.99.1, modified 2002] |
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