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Literature summary extracted from

  • Xing, G.; Diao, Y.; Hoffart, L.M.; Barr, E.W.; Prabhu, K.S.; Arner, R.J.; Reddy, C.C.; Krebs, C.; Bollinger, J.M.
    Evidence for C-H cleavage by an iron-superoxide complex in the glycol cleavage reaction catalyzed by myo-inositol oxygenase (2006), Proc. Natl. Acad. Sci. USA, 103, 6130-6135.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.99.1 expressed in Escherichia coli Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.99.1 Iron the mixed-valent, II/III state of iron, rather than the conventional II/II state, activates O2 for D-glucuronate production in the MIOX reaction Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
1.13.99.1 Mus musculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.99.1
-
 Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.13.99.1 kidney
-
 Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.99.1 myo-inositol + O2
-
 Mus musculus D-glucuronate + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.99.1 MIOX
-
 Mus musculus
1.13.99.1 Myo-inositol oxygenase
-
 Mus musculus