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Information on EC 1.13.99.1 - inositol oxygenase and Organism(s) Rattus norvegicus and UniProt Accession Q9QXN4
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1.13.99.1 inositol oxygenaseIUBMB Comments
An iron protein.
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Word Map
- 1.13.99.1
- d-glucuronate
-
glucaric
-
diiron
-
ambience
-
mixed-valent
-
four-electron
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glucuronate-xylulose
- medicine
- diagnostics
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
myo-inositol oxygenase, miox4, inositol oxygenase, osmiox, rsor/miox, gsmiox1a, miox2, renal-specific oxidoreductase, ppmiox, mmiox, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Inositol oxygenase
-
-
-
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Kidney-specific protein 32
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-
-
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meso-Inositol oxygenase
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-
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MIOX
MOO
-
-
-
-
Myo-inositol oxygenase
Oxygenase, inositol
-
-
-
-
Renal-specific oxidoreductase
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-
-
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MIOX
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-
-
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Myo-inositol oxygenase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
-
-
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
myo-Inositol:oxygen oxidoreductase
An iron protein.
CAS REGISTRY NUMBER
COMMENTARY
9029-59-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
myo-inositol + O2
D-glucuronate + H2O
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highly specific for myo-inositol
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-
?
myo-inositol + O2
D-glucuronic acid + H2O
first commited step in myo-inositol catabolism
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-
ir
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
myo-inositol + O2
D-glucuronic acid + H2O
first commited step in myo-inositol catabolism
-
-
ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
quinolinate
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1 mM Fe(II) + 4 mM quinolinate activates 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
additional information
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increased secretion in a dose-dependent manner after high-glucose treatment
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14.6
myo-inositol
MIOX activity present in peak 2 of hydrophobic-interaction chromatography on Resource-PHE column
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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increased expression in diabetic kidneys may contribute to tubulointerstitial injury and development of diabetic nephropathy
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MIOX_RAT
285
0
33185
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16800
17000
16800
-
2 * 16800, dimer is the elementary active enzyme-building unit, oligomer (MW 270000) can be dissociated under mild conditions to monomers (MW 16800)
16800
-
x * 16800, smallest active unit is tetramer, it is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
17000
-
4 * 17000, gel filtration, smallest active unit is tetramer, which is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
17000
-
8 * 17000, smallest active unit is tetramer, it is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
17000
-
12 * 17000, smallest active unit is tetramer, it is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
17000
-
16 * 17000, smallest active unit is tetramer, it is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 16800, dimer is the elementary active enzyme-building unit, oligomer (MW 270000) can be dissociated under mild conditions to monomers (MW 16800)
dodecamer
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12 * 17000, smallest active unit is tetramer, it is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
hexadecamer
-
16 * 17000, smallest active unit is tetramer, it is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
octamer
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8 * 17000, smallest active unit is tetramer, it is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
oligomer
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x * 16800, smallest active unit is tetramer, it is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
tetramer
-
4 * 17000, gel filtration, smallest active unit is tetramer, which is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after storage at 4°C for few weeks, a specific truncation due to degradation is observed, extended storage also causes the accumulation of a small proportion of apparantly dimerized MIOX
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Highly unstable in presence of oxygen, in early stages of inactivation: reactivation by reducing agents like NaBH4
-
6870
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high-fat diet administration over a period of 6 weeks results in a marked time-dependent up-regulation of Miox
transcriptional and translational modulation of myo-inositol oxygenase (Miox) by fatty acids, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
220-227
1959
Rattus norvegicus
Koller, F.; Hoffmann-Ostenhof, O.
myo-Inositol oxygenase from rat kidneys. I: Purification by affinity chromatography; physical and catalytic properties
Hoppe-Seyler's Z. Physiol. Chem.
360
507-513
1979
Rattus norvegicus
Koller, F.; Koller, E.
Affinity chromatography of myo-inositol oxygenase from rat kidney by means of an insoluble D-galacto-hexodialdose derivative
J. Chromatogr.
283
191-197
1984
Rattus norvegicus
Koller, F.; Koller, E.
myo-inositol oxygenase from rat kidneys. Substrate-dependent oligomerization
Eur. J. Biochem.
193
421-427
1990
Rattus norvegicus
Arner, R.J.; Prabhu, K.S.; Reddy, C.C.
Molecular cloning, expression, and characterization of myo-inositol oxygenase from mouse, rat, and human kidney
Biochem. Biophys. Res. Commun.
324
1386-1392
2004
Homo sapiens (Q9UGB7), Homo sapiens, Mus musculus (Q9QXN5), Mus musculus, Rattus norvegicus (Q9QXN4)
Lu, Y.; Liu, C.; Miao, X.; Xu, K.; Wu, X.; Liu, C.
Increased expression of myo-inositol oxygenase is involved in the tubulointerstitial injury of diabetic nephropathy
Exp. Clin. Endocrinol. Diabetes
117
257-265
2009
Rattus norvegicus
Tominaga, T.; Dutta, R.K.; Joladarashi, D.; Doi, T.; Reddy, J.K.; Kanwar, Y.S.
Transcriptional and translational modulation of myo-inositol oxygenase (Miox) by fatty acids implications in renal tubular injury induced in obesity and diabetes
J. Biol. Chem.
291
1348-1367
2016
Homo sapiens (Q9UGB7), Mus musculus (Q9QXN5), Mus musculus CD1 (Q9QXN5), Rattus norvegicus (Q9QXN4), Sus scrofa (Q8WN98)
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