1.13.99.1: inositol oxygenase

This is an abbreviated version!
For detailed information about inositol oxygenase, go to the full flat file.

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

     1 Oxidoreductases

         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

             1.13.99 Miscellaneous

                1.13.99.1 inositol oxygenase

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Results	in table
20	Activating Compound
3894	AA Sequence
4	Application
1	CAS Registry Number
42	Cloned(Commentary)
1	Cofactor
3	Crystallization (Commentary)
45	Disease/ Diagnostics
35	Expression
41	General Information
5	General Stability
76	Inhibitors
2	Ki Value [mM]
21	KM Value [mM]
11	Localization
24	Metals/Ions
19	Molecular Weight [Da]
43	Natural Substrates/ Products (Substrates)
86	Organism
3	Oxidation Stability
5	Pathway
4	PDB ID
18	pH Optimum
5	pH Range
3	pH Stability
1	pI Value
1	Posttranslational Modification
18	Protein Variants
19	Purification (Commentary)
3	Reaction
6	Reaction Type
74	Reference
116	Source Tissue
14	Specific Activity [micromol/min/mg]
4	Storage Stability
69	Substrates and Products (Substrate)
23	Subunits
180	Synonyms
1	Systematic Name
14	Temperature Optimum [°C]
4	Temperature Range [°C]
4	Temperature Stability [°C]
8	Turnover Number [1/s]

Posttranslational Modification

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Posttranslational Modification on EC 1.13.99.1 - inositol oxygenase

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

phosphoprotein

Mus musculus

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mutants with substituted phosphorylation sites have a minimal increase in activity. Treatment of cells with PKC, PKA, and PDK1 kinase activators increased activity, whereas inhibitors reduced it. Protein kinases A, C, and PDK1 are capable of phosphorylating mouse in both prokaryotic and eukaryotic systems. Using deletion constructs it is shown that the N-terminus contains the critical phosphorylation sites that are highly relevant to the functionality of the protein

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