1.13.99.1: inositol oxygenase
This is an abbreviated version!
For detailed information about inositol oxygenase, go to the full flat file.
Word Map on EC 1.13.99.1
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1.13.99.1
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d-glucuronate
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glucaric
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diiron
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ambience
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mixed-valent
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four-electron
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glucuronate-xylulose
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medicine
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diagnostics
- 1.13.99.1
- d-glucuronate
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glucaric
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diiron
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ambience
-
mixed-valent
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four-electron
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glucuronate-xylulose
- medicine
- diagnostics
Reaction
Synonyms
amyoinositol oxygenase, AtMIOX, EC 1.13.1.11, EC 1.99.2.6, GsMIOX1a, Inositol oxygenase, inositol oxygenase 1, InOx, Kidney-specific protein 32, meso-Inositol oxygenase, MIOX, MIOX1, MIOX2, MIOX4, MIOX5, mMIOX, MOO, Myo-inositol oxygenase, OsMIOX, Oxygenase, inositol, ppMIOX, Renal-specific oxidoreductase, renal-specific oxidoreductase/myo-inositol oxygenase, RSOR/MIOX
ECTree
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Metals Ions
Metals Ions on EC 1.13.99.1 - inositol oxygenase
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Fe2+
Iron
Fe2+
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contains iron most probably in divalent form, enzyme consisting of 16 subunits contains 8 iron atoms per molecule
Fe2+
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1 mM Fe(II) + 4 mM quinolinate activate to 70% of the Fe(II)/cysteine system, Fe(II) alone causes very little activation, quinolinate gives considerable activation in absence of Fe(II), activation by Fe(II) and quinolinate is very temperature dependent
Iron
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contains a non-heme dinuclear iron cluster, observations implicate the mixed-valent, diiron-(II/III) form of the enzyme as the active state
Iron
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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
Iron
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uses its dinuclear iron cluster to activate O2 for cleavage of myo-inositol that binds to the mixed-valence diiron center via a bridging alkoxide