Any feedback?
No. of entries
Information on EC 1.13.99.1 - inositol oxygenase
for references in articles please use BRENDA:EC1.13.99.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
1.13.99 Miscellaneous
1.13.99.1 inositol oxygenase
IUBMB Comments
An iron protein.
The enzyme appears in viruses and cellular organisms
- 1.13.99.1
- d-glucuronate
-
glucaric
-
diiron
-
ambience
-
mixed-valent
-
four-electron
-
glucuronate-xylulose
- medicine
- diagnostics
showSynonyms
myo-inositol oxygenase, miox4, inositol oxygenase, osmiox, rsor/miox, miox2, gsmiox1a, renal-specific oxidoreductase, miox1, miox5, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.13.1.11
-
-
formerly
-
EC 1.99.2.6
-
-
formerly
-
GsMIOX1a
Inositol oxygenase
-
-
-
-
inositol oxygenase 1
Kidney-specific protein 32
-
-
-
-
meso-Inositol oxygenase
-
-
-
-
MIOX
MIOX1
MIOX2
MIOX4
MIOX5
MOO
-
-
-
-
Myo-inositol oxygenase
Oxygenase, inositol
-
-
-
-
ppMIOX
Renal-specific oxidoreductase
-
-
-
-
MIOX
-
-
-
-
MIOX
-
Myo-inositol oxygenase
-
-
-
-
Myo-inositol oxygenase
-
-
Myo-inositol oxygenase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
myo-Inositol + O2 = D-glucuronate + H2O
the N-terminus is important, through coordination of a set of loops covering the active site, in shielding the active site during catalysis. Role of residue K127 in governing the access o the diiron cluster
-
myo-Inositol + O2 = D-glucuronate + H2O
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-H bond cleavage
redox reaction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
L-ascorbate biosynthesis VI (plants, myo-inositol pathway), UDP-alpha-D-glucuronate biosynthesis (from myo-inositol)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
myo-Inositol:oxygen oxidoreductase
An iron protein.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9029-59-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-chiro-inositol + O2
D-glucuronate
Substrates: much less active with D-chiro-inositol than with myo-inositol
Products: -
Products: -
?
myo-inositol + H2O
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
d-glucuronate
Substrates: major role in pathogenesis of diabetis
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
-
Substrates: highly specific for myo-inositol
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
-
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
-
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
-
Substrates: highly specific for myo-inositol
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
-
Substrates: highly specific for myo-inositol
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: highly specific for myo-inositol
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: conversion rate of 91.3%
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: conversion rate of 91.3%
Products: -
Products: -
?
myo-inositol + O2
D-glucuronic acid + H2O
Substrates: -
Products: -
Products: -
ir
myo-inositol + O2
D-glucuronic acid + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronic acid + H2O
Substrates: first commited step in myo-inositol catabolism
Products: -
Products: -
ir
myo-inositol + O2
D-glucuronic acid + H2O
Substrates: -
Products: -
Products: -
ir
myo-inositol + O2
D-glucuronic acid + H2O
Substrates: first commited step in myo-inositol catabolism
Products: -
Products: -
ir
myo-inositol + O2
D-glucuronic acid + H2O
Substrates: preincubation without substrate for 10 min at 30°C to acitvate the enzyme, assay at pH 8.0, 30°C
Products: -
Products: -
?
myo-inositol + O2
D-glucuronic acid + H2O
Substrates: first commited step in myo-inositol catabolism
Products: -
Products: -
ir
myo-inositol + O2
D-glucuronic acid + H2O
Substrates: -
Products: -
Products: -
ir
myo-inositol + O2
D-glucuronic acid + H2O
Substrates: -
Products: -
Products: -
ir
additional information
?
-
Substrates: interaction analysis of the enzyme amyoinositol oxygenase (OsMIOX) with PeaT1 elicitor from Alternaria tenuissima by yeast two-hybrid assay and pull-down assay, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: interaction analysis of the enzyme amyoinositol oxygenase (OsMIOX) with PeaT1 elicitor from Alternaria tenuissima by yeast two-hybrid assay and pull-down assay, overview
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
myo-inositol + O2
d-glucuronate
Substrates: major role in pathogenesis of diabetis
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
-
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: -
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: conversion rate of 91.3%
Products: -
Products: -
?
myo-inositol + O2
D-glucuronate + H2O
Substrates: conversion rate of 91.3%
Products: -
Products: -
?
myo-inositol + O2
D-glucuronic acid + H2O
Substrates: -
Products: -
Products: -
ir
myo-inositol + O2
D-glucuronic acid + H2O
Substrates: first commited step in myo-inositol catabolism
Products: -
Products: -
ir
myo-inositol + O2
D-glucuronic acid + H2O
Substrates: first commited step in myo-inositol catabolism
Products: -
Products: -
ir
myo-inositol + O2
D-glucuronic acid + H2O
Substrates: first commited step in myo-inositol catabolism
Products: -
Products: -
ir
myo-inositol + O2
D-glucuronic acid + H2O
Substrates: -
Products: -
Products: -
ir
additional information
?
-
Substrates: interaction analysis of the enzyme amyoinositol oxygenase (OsMIOX) with PeaT1 elicitor from Alternaria tenuissima by yeast two-hybrid assay and pull-down assay, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: interaction analysis of the enzyme amyoinositol oxygenase (OsMIOX) with PeaT1 elicitor from Alternaria tenuissima by yeast two-hybrid assay and pull-down assay, overview
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Fe2+
-
contains iron most probably in divalent form, enzyme consisting of 16 subunits contains 8 iron atoms per molecule
Fe2+
-
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
-
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
-
contains a non-heme dinuclear iron cluster, observations implicate the mixed-valent, diiron-(II/III) form of the enzyme as the active state
Iron
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-(4-hydroxy-3,5-dimethoxyphenyl)-4,8-dihydronaphthalene-1,3,8-triol
-
docking energy level (Kcal/mol): -6.9602
D-glucarate
a MIOX inhibitor, D-glucarate normalizes reduced autophagy and mitophagy in tubules of STZ-induced diabetic mice
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-cysteine
-
best activation system: 1 mM Fe(II) and 2 mM cysteine, L-cysteine can be replaced by D-cysteine, DL-penicillamine or gamma-L-glutamyl-L-cysteine
DL-Penicillamine
-
best activation system: 1 mM Fe(II) and 2 mM cysteine, L-cysteine can be replaced by D-cysteine, DL-penicillamine or gamma-L-glutamyl-L-cysteine
gamma-L-glutamyl-L-cysteine
-
best activation system: 1 mM Fe(II) and 2 mM cysteine, L-cysteine can be replaced by D-cysteine, DL-penicillamine or gamma-L-glutamyl-L-cysteine
palmitate
concomitant treatment with palmitate/bovine serum albumin and activators of PKA (forskolin), PDK/PI3K (insulin), and PKC (TPA) increase Miox activity. Concomitant treatment with respective inhibitors, i.e. H89 (PKA), wortmannin (PI3K), and calphostin (PKC), reduces the activity below the levels induced by palmitate/bovine serum albumin alone, confirming that fatty acid-induced activity is phosphorylation-dependent
quinolinate
-
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
-
increased secretion in a dose-dependent manner after high-glucose treatment
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acute Kidney Injury
Development of an Immunoassay for the Kidney-Specific Protein myo-Inositol Oxygenase, a Potential Biomarker of Acute Kidney Injury.
Acute Kidney Injury
Effectiveness of myo-inositol oxygenase in the early diagnosis of experimental acute kidney injury.
Acute Kidney Injury
Myo-inositol Oxygenase as a Novel Marker in the Diagnosis of Acute Kidney Injury.
Acute Kidney Injury
Myo-inositol oxygenase expression profile modulates pathogenic ferroptosis in the renal proximal tubule.
Diabetes Complications
Expression of myo-inositol oxygenase in tissues susceptible to diabetic complications.
Diabetes Mellitus
Polymorphisms of myo-inositol oxygenase gene are associated with Type 1 diabetes mellitus.
Diabetes Mellitus, Type 1
Polymorphisms of myo-inositol oxygenase gene are associated with Type 1 diabetes mellitus.
Diabetes, Gestational
Myo-inositol oxygenese activity in second trimester of pregnancy: altered myoinositol catabolism in gestational diabetes mellitus.
Diabetic Nephropathies
CONTRIBUTION OF MYO-INOSITOL OXYGENASE IN AGE: RAGE MEDIATED RENAL TUBULO-INTERSTITIAL INJURY IN THE CONTEXT OF DIABETIC NEPHROPATHY.
Diabetic Nephropathies
Disruption of renal tubular mitochondrial quality control by Myo-inositol oxygenase in diabetic kidney disease.
Diabetic Nephropathies
Increased Expression of Myo-inositol Oxygenase is Involved in the Tubulointerstitial Injury of Diabetic Nephropathy.
Diabetic Nephropathies
myo-Inositol Oxygenase Overexpression Accentuates Generation of Reactive Oxygen Species and Exacerbates Cellular Injury following High Glucose Ambience: A NEW MECHANISM RELEVANT TO THE PATHOGENESIS OF DIABETIC NEPHROPATHY.
Diabetic Nephropathies
PATHOBIOLOGY OF RENAL SPECIFIC OXIDOREDUCTASE/MYO-INOSITOL OXYGENASE IN DIABETIC NEPHROPATHY: ITS IMPLICATIONS IN TUBULO-INTERSTITIAL FIBROSIS.
Diabetic Nephropathies
Relevance of renal-specific oxidoreductase in tubulogenesis during mammalian nephron development.
Diabetic Nephropathies
The Kidney Specific Protein myo-Inositol Oxygenase, a Potential Biomarker for Diabetic Nephropathy.
Diabetic Nephropathies
Transcriptional and Post-translational Modulation of myo-Inositol Oxygenase by High Glucose and Related Pathobiological Stresses.
Diabetic Nephropathies
Withdrawal: myo-Inositol oxygenase overexpression accentuates generation of reactive oxygen species and exacerbates cellular injury following high glucose ambience: A new mechanism relevant to the pathogenesis of diabetic nephropathy.
Obesity
Modulation of Renal Injury by Variable Expression of Myo-Inositol Oxygenase (MIOX) via Perturbation in Metabolic Sensors.
Obesity
Transcriptional and Translational Modulation of myo-Inositol Oxygenase (Miox) by Fatty Acids: IMPLICATIONS IN RENAL TUBULAR INJURY INDUCED IN OBESITY AND DIABETES.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.105
myo-inositol
mutant enzyme S173N, at 37°C, pH not specified in the publication
2.516
myo-inositol
mutant enzyme D82Y/S173N/L240M, at 37°C, pH not specified in the publication
2.905
myo-inositol
mutant enzyme Q62H, at 37°C, pH not specified in the publication
3.3
myo-inositol
MIOX activity present in peak 1 of hydrophobic-interaction chromatography on Resource-PHE column
3.5
myo-inositol
MIOX activity present in peak 3 of hydrophobic-interaction chromatography on Resource-PHE column
3.573
myo-inositol
mutant enzyme D82Y, at 37°C, pH not specified in the publication
4.55
myo-inositol
wild type enzyme, at 37°C, pH not specified in the publication
5.8
myo-inositol
MIOX activity present in peak 1 of hydrophobic-interaction chromatography on Resource-PHE column
7.629
myo-inositol
mutant enzyme L240M, at 37°C, pH not specified in the publication
8.8
myo-inositol
MIOX activity present in peak 3 of hydrophobic-interaction chromatography on Resource-PHE column
14.6
myo-inositol
MIOX activity present in peak 2 of hydrophobic-interaction chromatography on Resource-PHE column
24.7
myo-inositol
MIOX activity present in peak 2 of hydrophobic-interaction chromatography on Resource-PHE column
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
59.5
myo-inositol
mutant enzyme Q62H, at 37°C, pH not specified in the publication
76.8
myo-inositol
wild type enzyme, at 37°C, pH not specified in the publication
85.1
myo-inositol
mutant enzyme S173N, at 37°C, pH not specified in the publication
109.9
myo-inositol
mutant enzyme L240M, at 37°C, pH not specified in the publication
110.8
myo-inositol
mutant enzyme D82Y/S173N/L240M, at 37°C, pH not specified in the publication
129.4
myo-inositol
mutant enzyme D82Y, at 37°C, pH not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.042
culture condition: 12 h, supplementation with 60 mM myo-inositol, 1 mM Fe(NH4)2(SO4)2, 2 mM L-cysteine
0.18
culture condition: 6 h, supplementation with 60 mM myo-inositol, 1 mM Fe(NH4)2(SO4)2, 2 mM L-cysteine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 10
almost no activity at pH 4.5, approx. 10% of maximal ativity at pH 10.0, approx. 70% of maximal activity at pH 8.0, i.e. a second optima
7 - 8.5
7.5 - 8.5
the enzyme shows high activity (more than 70%) across the pH range from 7.5-8.5
7 - 8.5
the enzyme keeps more than 70% of the highest activity at a range from pH 7.0-8.5. When the pH is lower than 6.0, the activity decreases rapidly
7 - 8.5
the enzyme shows high activity (more than 70%) across the pH range from 7.5-8.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 60
approx. 30% of maximal activity at 0°C and 50°C, respectively
20 - 37
20 - 37
enzyme maintains approximately 75% of its highest activity at a broad range from 20°C to 37°C. The activity decreases rapidly when the temperature is higher than 50°C
20 - 37
enzyme maintains approximately 75% of its highest activity at a broad range from 20°C to 37°C. The activity decreases rapidly when the temperature is higher than 50°C
20 - 37
enzyme maintains approximately 75% of its highest activity at a broad range from 20°C to 37°C. The activity decreases rapidly when the temperature is higher than 50°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
syncytia induced by nematode Heterodera schachtii
SwissProt
brenda
syncytia induced by nematode Heterodera schachtii
UniProt
brenda
-
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
is expressed at low levels in cell types where diabetic complications occur
brenda
-
MIOX1 and MIOX2 are expressed in almost all tissues of the plant
brenda
additional information
plasma MIOX is increased in critically ill patients with acute kidney injury compared with patients without acute kidney injury and is highest in patients with oliguric acute kidney injury
brenda
from mice with acute kidney injury, MIOX expression is undetectable in healthy mice plasma
brenda
-
from mice with acute kidney injury, MIOX expression is undetectable in healthy mice plasma
-
brenda
-
MIOX4 and MIOX5 expression is largely restricted to flowers, particularly maturing pollen
brenda
MIOX expression is upregulated by hyperosmolarity, particularly by polyols like mannitol, sorbitol and xylitol
brenda
kidney-specific expression of protein myo-inositol oxygenase encoding gene miox in proximal renal tubule
brenda
kidney-specific expression of protein myo-inositol oxygenase encoding gene miox in proximal renal tubule
brenda
-
kidney-specific expression of protein myo-inositol oxygenase encoding gene miox in proximal renal tubule
-
brenda
MIOX4 is highly expressed in pollen
brenda
MIOX5 is highly expressed in pollen
brenda
MIOX1 is expressed preferentially in seedlings
brenda
MIOX2 is expressed preferentially in seedlings
brenda
high MIOX1 expression level in syncytia, induced in roots by attack through the beet cyst nematode Heterodera schachtii, metabolome analysis of syncytium, overview
brenda
high MIOX2 expression level in syncytia, induced in roots by attack through the beet cyst nematode Heterodera schachtii, metabolome analysis of syncytium, overview
brenda
high MIOX4 expression level in syncytia, induced in roots by attack through the beet cyst nematode Heterodera schachtii, metabolome analysis of syncytium, overview
brenda
high MIOX5 expression level in syncytia, induced in roots by attack through the beet cyst nematode Heterodera schachtii, metabolome analysis of syncytium, overview
brenda
-
high MIOX1 expression level in syncytia, induced in roots by attack through the beet cyst nematode Heterodera schachtii, metabolome analysis of syncytium, overview
-
brenda
-
high MIOX2 expression level in syncytia, induced in roots by attack through the beet cyst nematode Heterodera schachtii, metabolome analysis of syncytium, overview
-
brenda
-
high MIOX4 expression level in syncytia, induced in roots by attack through the beet cyst nematode Heterodera schachtii, metabolome analysis of syncytium, overview
-
brenda
-
high MIOX5 expression level in syncytia, induced in roots by attack through the beet cyst nematode Heterodera schachtii, metabolome analysis of syncytium, overview
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
-
increase in MIOX enzyme activity is in proportion to serum glucose concentrations and may be responsible for the myo-inositol depletion found in the type I diabetes mellitus complications, detailed phenotype analysis of 130 Caucasian patients, overview
evolution
MIOX proteins are highly conserved and present in nearly all eukaryotes
evolution
Glycine soja 07256
-
MIOX proteins are highly conserved and present in nearly all eukaryotes
-
malfunction
-
increased expression in diabetic kidneys may contribute to tubulointerstitial injury and development of diabetic nephropathy
malfunction
-
loss-of-function mutants in MIOX genes contain alterations in myo-inositol levels and growth changes in the root. Miox2 mutants can be complemented with a MIOX2:green fluorescent protein fusion
malfunction
-
loss-of-function mutants in MIOX genes contain alterations in myo-inositol levels and growth changes in the root
malfunction
following increased expression of MIOX in tubular cells under high glucose ambience, there is an accentuated perturbation in cellular redox and mitochondrial homeostasis, leading to cellular apoptosis. In addition, there is an increased synthesis of extracellular matrix proteins, reflective of tubulo-interstitial injury in diabetic nephropathy
malfunction
under high-glucose ambience, MIOX overexpression accentuates redox imbalance, perturbed NAD+/NADH ratios, increased ROS generation, depleted reduced glutathione, reduced GSH/GSSG ratio, and enhanced adaptive changes in the profile of the antioxidant defense system. These changes are also accompanied by mitochondrial dysfunctions, DNA damage and induction of apoptosis, accentuated activity of profibrogenic cytokine, and expression of fibronectin, the latter two being the major hallmarks of diabetic nephropathy. These perturbations are largely blocked by various reactive oxygen species inhibitors (Mito Q, diphenyleneiodonium chloride, and N-acetylcysteine) and MIOX/NOX4 siRNA
malfunction
the quadruple myo-inositol oxygenase mutant shows a significant reduction in susceptibility to Heterodera schachtii, and syncytia have elevated myo-inositol and galactinol levels and an elevated expression level of the antimicrobial thionin gene Thi2.1. This reduction in susceptibility can also be achieved by exogenous application of galactinol to wild-type seedlings. Except for MIOX2, transcripts for the other three MIOX genes are still detected at a level of 2-14% of their abundance in the wild-type, the mutant does not show any visible phenotype and produced viable pollen, but the incorporation of myo-inositol-derived sugars into cell walls is strongly inhibited by over 90% with no change in the ultrastructure of syncytial cell walls
malfunction
the T-DNA insertion mutant atmiox1 is sensitive to alkaline stress, the phenotype can be complemented by expression of Glycine soja MIOX1 under constitutive CaMV35S promoter control
malfunction
upregulation of MIOX accompanied by mitochondrial fragmentation and depolarization, inhibition of autophagy/mitophagy, and altered expression of mitochondrial dynamic and mitophagic proteins under high-glucose ambience. Additionally, dysfunctional mitochondria accumulate in the cytoplasm. Decreasing the expression of MIOX under high-glucose ambience increases PTEN-induced putative kinase 1 expression and the dependent mitofusin-2-Parkin interaction. Overexpression of MIOX in the cells enhances the effects of high-glucose, whereas MIOX siRNA or D-glucarate, an inhibitor of MIOX, partially reverse these perturbations, D-glucarate normalizes reduced autophagy and mitophagy in tubules of STZ-induced diabetic mice
malfunction
upregulation of MIOX accompanied by mitochondrial fragmentation and depolarization, inhibition of autophagy/mitophagy, and altered expression of mitochondrial dynamic and mitophagic proteins under high-glucose ambience. Additionally, dysfunctional mitochondria accumulate in the cytoplasm. Decreasing the expression of MIOX under high-glucose ambience increases PTEN-induced putative kinase 1 expression and the dependent mitofusin-2-Parkin interaction. Overexpression of MIOX in the cells enhances the effects of high-glucose, whereas MIOX siRNA or D-glucarate, an inhibitor of MIOX, partially reverse these perturbations
malfunction
-
the quadruple myo-inositol oxygenase mutant shows a significant reduction in susceptibility to Heterodera schachtii, and syncytia have elevated myo-inositol and galactinol levels and an elevated expression level of the antimicrobial thionin gene Thi2.1. This reduction in susceptibility can also be achieved by exogenous application of galactinol to wild-type seedlings. Except for MIOX2, transcripts for the other three MIOX genes are still detected at a level of 2-14% of their abundance in the wild-type, the mutant does not show any visible phenotype and produced viable pollen, but the incorporation of myo-inositol-derived sugars into cell walls is strongly inhibited by over 90% with no change in the ultrastructure of syncytial cell walls
-
metabolism
-
MIOX is the first and rate-limiting enzyme in myo-inositol metabolism pathway
metabolism
the enzyme is important in the glucaric acid synthetic pathway
metabolism
the enzyme is important in the glucaric acid synthetic pathway
metabolism
a mechanism links MIOX to impaired mitochondrial quality control during tubular injury in the pathogenesis of diabetic kidney disease
metabolism
a mechanism links MIOX to impaired mitochondrial quality control during tubular injury in the pathogenesis of diabetic kidney disease
metabolism
-
the enzyme is important in the glucaric acid synthetic pathway
-
physiological function
control level of myoinositol, no influence on ascorbic acid
physiological function
-
start of catabolism of carbon skeleton of cell-signaling inositol polyphosphates and phosphoinositides
physiological function
-
start of catabolism of carbon skeleton of cell-signaling inositol polyphosphates and phosphoinositides
physiological function
myo-inositol oxygenase (MIOX) is a tubular enzyme that catabolizes myo-inositol to D-glucuronate via the glucuronate-xylulose pathway
physiological function
the enzyme myo-inositol oxygenase is the key enzyme of a pathway leading from myo-inositol to UDP-glucuronic acid. The primary function of myo-inositol oxygenase for syncytium development after infection with Heterodera schachtii is probably not the production of UDP-glucuronic acid as a precursor for cell wall polysaccharides, but the reduction of myo-inositol levels and thereby a reduction in the galactinol level to avoid the induction of defence-related genes
physiological function
overexpression of the PeaT1 elicitor gene from Alternaria tenuissima in Oryza sativa improves drought tolerance in rice plants via interaction with a myo-inositol oxygenase. In PeaT1-overexpressing (PeaT1OE) plants, abscisic acid and chlorophyll contents significantly increase, while the malondialdehyde (MDA) content decreases compared with the wild-type plants. Transcript levels of drought-responsive genes, including OsAM1, OsLP2, and OsDST, are prominently lower in the PeaT1OE plants. In contrast, expression levels of genes encoding positive drought stress regulators including OsSKIPa, OsCPK9, OsNAC9, OSEREBP1, and OsTPKb are upregulated in PeaT1OE plants. OsMIOX is highly expressed in PeaT1OE plants during the drought treatment
physiological function
positive function of enzyme GsMIOX1a in the alkaline response in Glycine soja plants, GsMIOX1a gene positively regulates plant tolerance to alkaline stress. Other soybean varieties, including Glycine soja 07256, Glycine soja 50109, Glycine max Suinong 28 and Glycine max Hefeng 55. Glycine max Suinong 28 and Glycine max Hefeng 55 are Chinese soybean cultivars that exhibit much lower adaptability to stress compared to Glycine soja 07256. Glycine soja 50109 is also a kind of wild soybean but is not reported to be alkaline resistant
physiological function
MIOX is a renal specific, proximal tubule protein that is increased in plasma ofanimals and critically ill patients with acute kidney injury, AKI. MIOX preceds the elevation in SCr by approximately two days in human patients
physiological function
kidney-specific expression of myo-inositol oxygenase in acute kidney injury
physiological function
myo-inositol oxygenase (MIOX) is a tubular-specific enzyme, that modulates redox imbalance and apoptosis in tubular cells in diabetes, role of MIOX in perturbation of mitochondrial quality control, including mitochondrial dynamics and autophagy/mitophagy, under high-glucose ambience or a diabetic state, overview
physiological function
myo-inositol oxygenase (MIOX) is a tubular-specific enzyme, that modulates redox imbalance and apoptosis in tubular cells in diabetes, role of MIOX in perturbation of mitochondrial quality control, including mitochondrial dynamics and autophagy/mitophagy, under high-glucose ambience or a diabetic state, overview
physiological function
enzyme overexpression exacerbates cisplatin-induced acute kidney injury by accentuating renal tubular cell apoptosis and modulating the expression of inflammatory cytokines
physiological function
-
ferroptosis, an integral process in the pathogenesis of cisplatin-induced acute kidney injury, is modulated by the expression profile of the enzyme. Overexpression of the enzyme promotes cisplatin-induced cell death and RSL3-induced ferroptosis in HK-2 cells
physiological function
-
enzyme overexpression accentuates the cellular injury related to endoplasmic reticulum stress and accentuates tunicamycin-induced generation of reactive oxygen species
physiological function
-
enzyme overexpression accentuates the cellular injury related to endoplasmic reticulum stress and accentuates tunicamycin-induced generation of reactive oxygen species
physiological function
enzyme overexpression accentuates the cellular injury related to endoplasmic reticulum stress and accentuates tunicamycin-induced generation of reactive oxygen species
physiological function
-
the enzyme myo-inositol oxygenase is the key enzyme of a pathway leading from myo-inositol to UDP-glucuronic acid. The primary function of myo-inositol oxygenase for syncytium development after infection with Heterodera schachtii is probably not the production of UDP-glucuronic acid as a precursor for cell wall polysaccharides, but the reduction of myo-inositol levels and thereby a reduction in the galactinol level to avoid the induction of defence-related genes
-
physiological function
-
kidney-specific expression of myo-inositol oxygenase in acute kidney injury
-
physiological function
Glycine soja 07256
-
positive function of enzyme GsMIOX1a in the alkaline response in Glycine soja plants, GsMIOX1a gene positively regulates plant tolerance to alkaline stress. Other soybean varieties, including Glycine soja 07256, Glycine soja 50109, Glycine max Suinong 28 and Glycine max Hefeng 55. Glycine max Suinong 28 and Glycine max Hefeng 55 are Chinese soybean cultivars that exhibit much lower adaptability to stress compared to Glycine soja 07256. Glycine soja 50109 is also a kind of wild soybean but is not reported to be alkaline resistant
-
Show AA Sequence and Transmembrane Helices (5000 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16800
17000
32663
electrospray MS determination, gel filtration, SDS-PAGE, sedimentation equilibirum, enzyme does not undergo oligomerization in the presence of myo-inositol
33000
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
monomer
octamer
-
8 * 17000, smallest active unit is tetramer, it is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
oligomer
-
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
monomer
1 * 32663, electrospray MS determination, gel filtration, SDS-PAGE, sedimentation equilibirum, enzyme does not undergo oligomerization in the presence of myo-inositol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with myo-inosose-1 bound in a terminal mode to the enzyme's diiron cluster site. The N-terminus is important, through coordination of a set of loops covering the active site, in shielding the active site during catalysis. Role of residue K127 in governing the access o the diiron cluster
-
crystals grow from a solution containing 20 mg/ml MIOX, 20 mM myo-inositol, 50 mM Mes pH 6.0, 50 mM NaCl, 2 mM Tris(2-carboxyethyl)-phosphine hydrochloride and 4.4 M sodium formate
-
sitting drop vapour diffusion method producing crystals from unbuffered 4.4 M sodium formate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA miox 1+2
double mutant, smaller syncytia, less female nematodes per plant
delta miox 4+5
double mutant, smaller syncytia, less female nematodes per plant
DELTA miox1
single knockout mutant of one allele of MIOX
delta miox2
single knockout mutant of one allele of MIOX
delta miox5
single knockout mutant of one allele of MIOX
D82Y
the mutant displays significantly decreased Km values and better kcat value compared to the wild type enzyme
L240M
the mutant's activity shows a drastic improvement compared with the wild type enzyme
Q62H
the mutant displays significantly decreased Km values and lower kcat value compared to the wild type enzyme
Q62H/S173N/L240M
the mutant's activity shows a drastic improvement compared with the wild type enzyme
S173N
the mutant displays significantly decreased Km values and better kcat value compared to the wild type enzyme
S24A/S205A/S218A/T29A/T69A
-
mutated putative PKA phosphorylation sites: mutant is also phosphorylated but to a minor degree
S24A/S205A/S218A/T29A/T69A/S64A/T40A/T49A/T69A/T253A
-
mutated putative PKA and PKC phosphorylation sites: mutant is also phosphorylated but to a minor degree
S64A/T40A/T49A/T69A/T253A
-
mutated putative PKC phosphorylation sites: mutant is also phosphorylated but to a minor degree
additional information
additional information
construction of a quadruple (miox1/2/4/5) mutant by mutation of all four MIOX isozymes via T-DNA insertion, metabolite profiling of syncytia induced in roots of the myo-inositol oxygenase quadruple mutant, overview. The quadruple myo-inositol oxygenase mutant shows a significant reduction in susceptibility to Heterodera schachtii, and syncytia have elevated myo-inositol and galactinol levels and an elevated expression level of the antimicrobial thionin gene Thi2.1. This reduction in susceptibility can also be achieved by exogenous application of galactinol to wild-type seedlings. The miox1/2/4/5 plants show a similar reduction in the number of females to miox double mutants
additional information
construction of a quadruple (miox1/2/4/5) mutant by mutation of all four MIOX isozymes via T-DNA insertion, metabolite profiling of syncytia induced in roots of the myo-inositol oxygenase quadruple mutant, overview. The quadruple myo-inositol oxygenase mutant shows a significant reduction in susceptibility to Heterodera schachtii, and syncytia have elevated myo-inositol and galactinol levels and an elevated expression level of the antimicrobial thionin gene Thi2.1. This reduction in susceptibility can also be achieved by exogenous application of galactinol to wild-type seedlings. The miox1/2/4/5 plants show a similar reduction in the number of females to miox double mutants
additional information
construction of a quadruple (miox1/2/4/5) mutant by mutation of all four MIOX isozymes via T-DNA insertion, metabolite profiling of syncytia induced in roots of the myo-inositol oxygenase quadruple mutant, overview. The quadruple myo-inositol oxygenase mutant shows a significant reduction in susceptibility to Heterodera schachtii, and syncytia have elevated myo-inositol and galactinol levels and an elevated expression level of the antimicrobial thionin gene Thi2.1. This reduction in susceptibility can also be achieved by exogenous application of galactinol to wild-type seedlings. The miox1/2/4/5 plants show a similar reduction in the number of females to miox double mutants
additional information
construction of a quadruple (miox1/2/4/5) mutant by mutation of all four MIOX isozymes via T-DNA insertion, metabolite profiling of syncytia induced in roots of the myo-inositol oxygenase quadruple mutant, overview. The quadruple myo-inositol oxygenase mutant shows a significant reduction in susceptibility to Heterodera schachtii, and syncytia have elevated myo-inositol and galactinol levels and an elevated expression level of the antimicrobial thionin gene Thi2.1. This reduction in susceptibility can also be achieved by exogenous application of galactinol to wild-type seedlings. The miox1/2/4/5 plants show a similar reduction in the number of females to miox double mutants
additional information
generation of an AtMIOX1 gene T-DNA insertion mutant atmiox1, the AtMIOX1 gene is efficiently silenced by the T-DNA insertion in the atmiox1 mutant. Constitutive overepression of Glycine soja MIOX1 under constitutive CaMV35S promoter control can recover the phenotype leading to alkaline stress tolerance in the atmiox1 mutant plants, overview
additional information
-
construction of a quadruple (miox1/2/4/5) mutant by mutation of all four MIOX isozymes via T-DNA insertion, metabolite profiling of syncytia induced in roots of the myo-inositol oxygenase quadruple mutant, overview. The quadruple myo-inositol oxygenase mutant shows a significant reduction in susceptibility to Heterodera schachtii, and syncytia have elevated myo-inositol and galactinol levels and an elevated expression level of the antimicrobial thionin gene Thi2.1. This reduction in susceptibility can also be achieved by exogenous application of galactinol to wild-type seedlings. The miox1/2/4/5 plants show a similar reduction in the number of females to miox double mutants
-
additional information
coexpression of the Mus musculus mMIOX and the urinate dehydrogenase (Udh) from Pseudomonas putida KT2440 as fusion protein leads highly increased glutaric acid levels from myo-inositol in transfected Pichia pastoris cells. Production of glucaric acid with a fed-batch fermentation strategy, overview. Recombinant coexpression of the enzyme in Escherichia coli strains BL21(DE3) or MG1655 with myo-inositol-1-phosphate synthase from Saccharomyces cerevisiae and urinate dehydrogenase (Udh) from Pseudomonas putida KT2440 leads to highly increased glutaric acid production, especially with addition of myo-inositol instead of glucose, production parameters, overview
additional information
-
coexpression of the Mus musculus mMIOX and the urinate dehydrogenase (Udh) from Pseudomonas putida KT2440 as fusion protein leads highly increased glutaric acid levels from myo-inositol in transfected Pichia pastoris cells. Production of glucaric acid with a fed-batch fermentation strategy, overview. Recombinant coexpression of the enzyme in Escherichia coli strains BL21(DE3) or MG1655 with myo-inositol-1-phosphate synthase from Saccharomyces cerevisiae and urinate dehydrogenase (Udh) from Pseudomonas putida KT2440 leads to highly increased glutaric acid production, especially with addition of myo-inositol instead of glucose, production parameters, overview
additional information
under high-glucose ambience, MIOX overexpression accentuates redox imbalance, perturbed NAD+/NADH ratios, increased ROS generation, depleted reduced glutathione, reduced GSH/GSSG ratio, and enhanced adaptive changes in the profile of the antioxidant defense system. These changes are also accompanied by mitochondrial dysfunctions, DNA damage and induction of apoptosis, accentuated activity of profibrogenic cytokine, and expression of fibronectin, the latter two being the major hallmarks of diabetic nephropathy. These perturbations are largely blocked by various reactive oxygen species inhibitors (Mito Q, diphenyleneiodonium chloride, and N-acetylcysteine) and MIOX/NOX4 siRNA, overview. Cells under high glucose ambience or transfected with MIOX-pcDNA show increased expression of apoptogenic protein Bax. The expression is further increased following concomitant treatment with HG and MIOX transfection. Treatment with N-acetylcysteine reduces the expression of Bax
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
6 - 8
the enzyme retains more than 70% activity after 30 min at pH 6.0-8.0. After 30 min at pH 9.0, the enzyme activity drops to 50% of the original value
6 - 8
the enzyme retains more than 70% activity after 30 min at pH 6.0-8.0. After 30 min at pH 9.0, the enzyme activity drops to 50% of the original value
6 - 8
the enzyme retains more than 70% activity after 30 min at pH 6.0-8.0. After 30 min at pH 9.0, the enzyme activity drops to 50% of the original value
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
the enzyme shows less than 40% of its activity at 37 °C for 40 min
37
the enzyme exhibits approximately 70% of its activity after incubation at 37°C for 40 min and possesses 30% of its initial activity after incubation at 37°C for 1 h
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after storage at 4C 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
Completely active even in absence of Fe(II) and cysteine if it has been stored at -20°C for days to weeks at pH 6.0 with 1 mM glutathione
-
after storage at 4C 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
after storage at 4C 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
after storage at 4C 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Highly unstable in presence of oxygen, in early stages of inactivation: reactivation by reducing agents like NaBH4
-
6870
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C for weeks or months: activation -20°C, completely active even in absence of Fe(II) and cysteine for days to weeks at pH 6.0 with 1 mM glutathione
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-column, butyl-Sepharose, Superdex 75, Mono Q
Ni-NTA column chromatography
recombinant MIOX
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli in the presence of the iron chelator, 1,10-phenanthroline to create iron-free MIOX
-
expressed in Escherichia coli strain BW25113
expressed in Escherichia coli strain EA31 and Saccharomyces cerevisiae strain SG
expression in Escherichia coli
gene AtMIOX1, phylogenetic tree, semi-quantitative reverse transcriptase enzyme expression analysis
gene GsMIOX1a, genetic structure, phylogenetic tree, ectopic expression under control of the constitutive CaMV35S promoter in Arabidopsis thaliana leads to enhanced tolerance to alkaline stress, while expression of enzyme mutant atmiox1 mutant decreases alkaline stress tolerance in Arabidopsis thaliana ecotype Columbia, quantitative real-time PCR enzyme expression analysis. The expression levels of some alkaline stress-responsive and inducible marker genes, including H+-Ppase, NADP-ME, KIN1 and RD29B, are also up-regulated in GsMIOX1a overexpression lines compared with the wild-type and atmiox1 mutant expressing plants
gene MIOX, kidney-specific expression, recombinant expression of GST-tagged enzyme in HEK-293 cells, cleavage of the GST tag by thrombin
gene MIOX, quantitative enzyme expression analysis
gene MIOX, quantitative real-time PCR enzyme expression analysis
gene MIOX, quantitative real-time PCR enzyme expression analysis, overexpression of MIOX in LLC-PK1 cells boosts the generation of H2O2
gene miox, recombinant expression in Pichia pastoris, coexpression with urinate dehydrogenase (Udh) from Pseudomonas putida KT2440 as fusion protein
gene MIOX1, transient recombinant overexpression of GFP-tagged OsMIOX, co-localizing with the endoplasmic reticulum marker, in Nicotiana benthamiana protoplasts, quantitative real-Time PCR enzyme expression analysis, recombinant expression of GST-tagged OsMIOX1 with MBP-tagged PeaT1 in Saccharomyces cerevisiae in the two-hybrid-system
gene mMIOX, recombinant expression in Pichia pastoris, coexpression with urinate dehydrogenase (Udh) from Pseudomonas putida KT2440, recombinant coexpression of the enzyme in Escherichia coli with myo-inositol-1-phosphate synthase from Saccharomyces cerevisiae and urinate dehydrogenase (Udh) from Pseudomonas putida KT2440
in Arabidpsis thaliana, myo-inositol oxygenase is encoded by four genes, gene MIOX1, quantitative real-time PCR enzyme expression analysis
in Arabidpsis thaliana, myo-inositol oxygenase is encoded by four genes, gene MIOX2, quantitative real-time PCR enzyme expression analysis
in Arabidpsis thaliana, myo-inositol oxygenase is encoded by four genes, gene MIOX4, quantitative real-time PCR enzyme expression analysis
in Arabidpsis thaliana, myo-inositol oxygenase is encoded by four genes, gene MIOX5, quantitative real-time PCR enzyme expression analysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
445.7fold gene induction in syncytia induced by nematode Heterodera schachtii
7.64fold gene induction in syncytia induced by nematode Heterodera schachtii
administration of high-fat diet to CD1 mice over a period of 2-6 weeks induces a tremendous increase in the expression of Miox, exclusively confined to the tubular compartment of the kidney cortex. Besides the increased expression in superficial cortical tubules, it also extends into the deeper cortex. Upregulation of Miox is accompanied by upregulation of mSrebp1 in kidney cells. Rapamycin reverses palmitate/bovine serum albumin-induced Miox, Srebp1, and p53 expression and apoptosis in renal tubular cells
all MIOX genes are strongly expressed in syncytia induced by the beet cyst nematode Heterodera schachtii in Arabidopsis thaliana roots
antioxidants N-acetylcysteine, beta-naphthoflavone, and tertiary butyl hydroquinone reduces MIOX expression
-
cisplatin increases the enzyme expression via demethylation of its promoter
coexpression of the Pichia pastoris ppMIOX and the urinate dehydrogenase (Udh) from Pseudomonas putida KT2440 does not lead to accumulation of glucaric acid from myo-inositol or increased enzyme activity of neither MIOX nor Udh
enzyme expression is significantly up-regulated by heat (5fold), cold (7fold), and drought (5fold) stresses as compared to transgenic plants grown without stress-induced conditions
-
gene induction in syncytia induced by nematode Heterodera schachtii
GsMIOX1a is rapidly induced by alkaline stress. Under alkaline stress, GsMIOX1a expression levels increase and reach a maximum level at 6 h that is approximately 42fold higher than that at 0 h
high glucose levels, exposure of cells to oxidants H2O2 and methylglyoxal up-regulates MIOX expression
-
high-fat diet administration over a period of 6 weeks results in a marked time-dependent up-regulation of Miox
MIOX2 expression is suppressed by exogenous glucose addition in the shoot, but not in the root
-
MIOX4 expression is suppressed by exogenous glucose addition in the shoot,but not in the root
-
OsMIOX enzyme expression is highly enhanced in rice plants overexpressing the Alternaria tenuissima PeaT1 gene during drought stress, the plants show enhanced drought stress tolerance and increased the survival rate following a drought treatment
palmitate-conjugated bovine serum albumin causes a dose-dependent increase in Miox expression and activity in LLCPK-1 cells. Concomitant with Miox upregulation, a dose-dependent increased Bax protein expression is observed following palmitate/BSA treatment of LLCPK-1 cells. Concomitant treatment with palmitate/bovine serum albumin and activators of PKA (forskolin), PDK/PI3K (insulin), and PKC (TPA) further increase Miox activity
the concentration of the enzyme in serum is higher in the acute kidney injury group compared to the healthy control group
-
the enzyme expression is upregulated under high glucose treatment in LLC-PK1 cells, a tubular cell line. Under high-glucose ambience, MIOX overexpression accentuates redox imbalance, perturbed NAD+/NADH ratios, increased ROS generation, depleted reduced glutathione, reduced GSH/GSSG ratio, and enhanced adaptive changes in the profile of the antioxidant defense system. These changes are also accompanied by mitochondrial dysfunctions, DNA damage and induction of apoptosis, accentuated activity of profibrogenic cytokine, and expression of fibronectin, the latter two being the major hallmarks of diabetic nephropathy. These perturbations are largely blocked by various reactive oxygen species inhibitors (Mito Q, diphenyleneiodonium chloride, and N-acetylcysteine) and MIOX/NOX4 siRNA, overview
transcriptional and translational modulation of myo-inositol oxygenase (Miox) by fatty acids, overview
treatment of HK-2 cells with palmitate/bovine serum albumin for 24 h induces an increased Miox expression with a concomitant decrease in the membrane-bound precursor form of pre-Srebp1 in the cytoplasmic fraction. No change in the expression of beta-actin or laminB1 is observed. Miox is transcriptionally upregulated by high glucose ambience. A dose-dependent increase in the expression of Miox is observed following insulin treatment. At the same time, a dose-dependent increase in the mSrebp1 is observed. Rapamycin reverses palmitate/bovine serum albumin-induced Miox, Srebp1, and p53 expression and apoptosis in renal tubular cells
under high-glucose (30 mM) ambience, the enzyme expression increases compared with the control low-glucose (5 mM) ambience
upregulation of MIOX accompanied by mitochondrial fragmentation and depolarization, inhibition of autophagy/mitophagy, and altered expression of mitochondrial dynamic and mitophagic proteins under high-glucose ambience
administration of high-fat diet to CD1 mice over a period of 2-6 weeks induces a tremendous increase in the expression of Miox, exclusively confined to the tubular compartment of the kidney cortex. Besides the increased expression in superficial cortical tubules, it also extends into the deeper cortex. Upregulation of Miox is accompanied by upregulation of mSrebp1 in kidney cells. Rapamycin reverses palmitate/bovine serum albumin-induced Miox, Srebp1, and p53 expression and apoptosis in renal tubular cells
administration of high-fat diet to CD1 mice over a period of 2-6 weeks induces a tremendous increase in the expression of Miox, exclusively confined to the tubular compartment of the kidney cortex. Besides the increased expression in superficial cortical tubules, it also extends into the deeper cortex. Upregulation of Miox is accompanied by upregulation of mSrebp1 in kidney cells. Rapamycin reverses palmitate/bovine serum albumin-induced Miox, Srebp1, and p53 expression and apoptosis in renal tubular cells
-
-
all MIOX genes are strongly expressed in syncytia induced by the beet cyst nematode Heterodera schachtii in Arabidopsis thaliana roots
all MIOX genes are strongly expressed in syncytia induced by the beet cyst nematode Heterodera schachtii in Arabidopsis thaliana roots
-
-
coexpression of the Pichia pastoris ppMIOX and the urinate dehydrogenase (Udh) from Pseudomonas putida KT2440 does not lead to accumulation of glucaric acid from myo-inositol or increased enzyme activity of neither MIOX nor Udh
coexpression of the Pichia pastoris ppMIOX and the urinate dehydrogenase (Udh) from Pseudomonas putida KT2440 does not lead to accumulation of glucaric acid from myo-inositol or increased enzyme activity of neither MIOX nor Udh
-
-
GsMIOX1a is rapidly induced by alkaline stress. Under alkaline stress, GsMIOX1a expression levels increase and reach a maximum level at 6 h that is approximately 42fold higher than that at 0 h
GsMIOX1a is rapidly induced by alkaline stress. Under alkaline stress, GsMIOX1a expression levels increase and reach a maximum level at 6 h that is approximately 42fold higher than that at 0 h
Glycine soja 07256
-
-
transcriptional and translational modulation of myo-inositol oxygenase (Miox) by fatty acids, overview
transcriptional and translational modulation of myo-inositol oxygenase (Miox) by fatty acids, overview
transcriptional and translational modulation of myo-inositol oxygenase (Miox) by fatty acids, overview
transcriptional and translational modulation of myo-inositol oxygenase (Miox) by fatty acids, overview
transcriptional and translational modulation of myo-inositol oxygenase (Miox) by fatty acids, overview
-
-
under high-glucose (30 mM) ambience, the enzyme expression increases compared with the control low-glucose (5 mM) ambience
under high-glucose (30 mM) ambience, the enzyme expression increases compared with the control low-glucose (5 mM) ambience
-
upregulation of MIOX accompanied by mitochondrial fragmentation and depolarization, inhibition of autophagy/mitophagy, and altered expression of mitochondrial dynamic and mitophagic proteins under high-glucose ambience
upregulation of MIOX accompanied by mitochondrial fragmentation and depolarization, inhibition of autophagy/mitophagy, and altered expression of mitochondrial dynamic and mitophagic proteins under high-glucose ambience
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
the kidney-specific protein myo-inositol oxygenase is a potential biomarker of acute kidney injury, AKI
medicine
medicine
the enzyme is a possible target for treatment of diabetic kidney disease. MIOX enzyme inhibitor D-glucarate might be a potential therapeutic agent for the amelioration of diabetic kidney disease
medicine
the enzyme is a possible target for treatment of diabetic kidney disease. MIOX enzyme inhibitor D-glucarate might be a potential therapeutic agent for the amelioration of diabetic kidney disease
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
Moskala, R.; Reddy, C.C.; Minard, R.D.; Hamilton, G.A.
An oxygen-18 tracer investigation of the mechanism of myo-inositol oxygenase
Biochem. Biophys. Res. Commun.
99
107-113
1981
Sus scrofa
brenda
Reddy, C.C.; Hamilton, G.A.
Activation of homogeneous preparations of hog kidney myo-inositol oxygenase by quinolinic acid and ferrous ions
Biochem. Biophys. Res. Commun.
100
1389-1395
1981
Sus scrofa
brenda
Reddy, C.C.; Swan, J.S.; 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.
156
8510-8518
1981
Sus scrofa
brenda
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
brenda
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
brenda
Graham, M.N.; Mantle, T.J.
Partial purification of myo-inositol oxygenase from ox kidney by using phenyl-Sepharose
Biochem. Soc. Trans.
13
481
1985
Bos taurus
-
brenda
Koller, F.; Koller, E.
myo-inositol oxygenase from rat kidneys. Substrate-dependent oligomerization
Eur. J. Biochem.
193
421-427
1990
Rattus norvegicus
brenda
Reddy, C.C.; Pierzchala, P.A.; Hamilton, G.A.
myo-Inositol oxygenase from hog kidney. II. Catalytic properties of the homogeneous enzyme
J. Biol. Chem.
256
8519-8524
1981
Sus scrofa
brenda
Naber, N.I.; Swan, J.S.; Hamilton, G.A.
L-myo-Inosose-1 as a probable intermediate in the reaction catalyzed by myo-inositol oxygenase
Biochemistry
25
7201-7207
1986
Sus scrofa
brenda
Arner, R.J.; Prabhu, K.S.; Thompson, J.T.; Hildenbrandt, G.R.; Liken, A.D.; 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
313-320
2001
Sus scrofa (Q8WN98), Sus scrofa
brenda
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)
brenda
Prabhu, K.S.; Arner, R.J.; Vunta, H.; Reddy, C.C.
Up-regulation of human myo-inositol oxygenase by hyperosmotic stress in renal proximal tubular epithelial cells
J. Biol. Chem.
280
19895-19901
2005
Homo sapiens (Q9UGB7), Homo sapiens
brenda
Lorence, A.; Chevone, B.I.; Mendes, P.; Nessler, C.L.
myo-Inositol oxygenase offers a possible entry point into plant ascorbate biosynthesis
Plant Physiol.
134
1200-1205
2004
Arabidopsis thaliana (Q8H1S0)
brenda
Kanter, U.; Becker, M.; Friauf, E.; Tenhaken, R.
Purification, characterization and functional cloning of inositol oxygenase from Cryptococcus
Yeast
20
1317-1329
2003
Sporopachydermia lactativora (Q70GL3), Sporopachydermia lactativora
brenda
Brown, P.M.; Caradoc-Davies, T.T.; Dickson, J.M.; Cooper, G.J.; Loomes, K.M.; Baker, E.N.
Purification, crystallization and preliminary crystallographic analysis of mouse myo-inositol oxygenase
Acta Crystallogr. Sect. F
F62
811-813
2006
Mus musculus
brenda
Arner, R.J.; Prabhu, K.S.; Krishnan, V.; Johnson, M.C.; Reddy, C.C.
Expression of myo-inositol oxygenase in tissues susceptible to diabetic complications
Biochem. Biophys. Res. Commun.
339
816-820
2006
Homo sapiens, Mus musculus, Sus scrofa
brenda
Xing, G.; Hoffart, L.M.; Diao, Y.; Prabhu, K.S.; Arner, R.J.; Reddy, C.C.; Krebs, C.; Bollinger, J.M.
A coupled dinuclear iron cluster that is perturbed by substrate binding in myo-inositol oxygenase
Biochemistry
45
5393-5401
2006
Mus musculus
brenda
Xing, G.; Barr, E.W.; Diao, Y.; Hoffart, L.M.; Prabhu, K.S.; Arner, R.J.; Reddy, C.C.; Krebs, C.; Bollinger, J.M.
Oxygen activation by a mixed-valent, diiron(II/III) cluster in the glycol cleavage reaction catalyzed by myo-inositol oxygenase
Biochemistry
45
5402-5412
2006
Mus musculus
brenda
Kim, S.H.; Xing, G.; Bollinger, J.M.; Krebs, C.; Hoffman, B.M.
Demonstration by 2H ENDOR spectroscopy that myo-inositol binds via an alkoxide bridge to the mixed-valent diiron center of myo-inositol oxygenase
J. Am. Chem. Soc.
128
10374-10375
2006
Mus musculus
brenda
Kanter, U.; Usadel, B.; Guerineau, F.; Li, Y.; Pauly, M.; Tenhaken, R.
The inositol oxygenase gene family of Arabidopsis is involved in the biosynthesis of nucleotide sugar precursors for cell-wall matrix polysaccharides
Planta
221
243-254
2005
Arabidopsis thaliana
brenda
Nayak, B.; Xie, P.; Akagi, S.; Yang, Q.; Sun, L.; Wada, J.; Thakur, A.; Danesh, F.R.; Chugh, S.S.; Kanwar, Y.S.
Modulation of renal-specific oxidoreductase/myo-inositol oxygenase by high-glucose ambience
Proc. Natl. Acad. Sci. USA
102
17952-17957
2005
Mus musculus
brenda
Brown, P.M.; Caradoc-Davies, T.T.; Dickson, J.M.; Cooper, G.J.; Loomes, K.M.; Baker, E.N.
Crystal structure of a substrate complex of myo-inositol oxygenase, a di-iron oxygenase with a key role in inositol metabolism
Proc. Natl. Acad. Sci. USA
103
15032-15037
2006
Mus musculus
brenda
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
Proc. Natl. Acad. Sci. USA
103
6130-6135
2006
Mus musculus
brenda
Thorsell, A.G.; Persson, C.; Voevodskaya, N.; Busam, R.D.; Hammarstroem, M.; Graeslund, S.; Graeslund, A.; Hallberg, B.M.
Structural and biophysical characterization of human myo-inositol oxygenase
J. Biol. Chem.
283
15209-15216
2008
Homo sapiens
brenda
Moon, T.S.; Yoon, S.H.; Lanza, A.M.; Roy-Mayhew, J.D.; Prather, K.L.
Production of glucaric acid from a synthetic pathway in recombinant Escherichia coli
Appl. Environ. Microbiol.
75
589-595
2009
Mus musculus (Q9QXN5)
brenda
Bollinger, J.M.; Diao, Y.; Matthews, M.L.; Xing, G.; Krebs, C.
myo-Inositol oxygenase: a radical new pathway for O(2) and C-H activation at a nonheme diiron cluster
Dalton Trans.
2009
905-914
2009
Mus musculus, Mammalia
brenda
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
brenda
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
184
457-472
2009
Arabidopsis thaliana (Q8H1S0), Arabidopsis thaliana (O82200), Arabidopsis thaliana (Q9FJU4), Arabidopsis thaliana (Q8L799)
brenda
Endres, S.; Tenhaken, R.
Myoinositol oxygenase controls the level of myoinositol in Arabidopsis, but does not increase ascorbic acid
Plant Physiol.
149
1042-1049
2009
Arabidopsis thaliana (Q8H1S0), Arabidopsis thaliana (O82200), Arabidopsis thaliana (Q9FJU4), Arabidopsis thaliana (Q8L799)
brenda
Yang, B.; Hodgkinson, A.; Millward, B.; Demaine, A.
Polymorphisms of myo-inositol oxygenase gene are associated with type 1 diabetes mellitus
J. Diabetes Complicat.
24
404-408
2010
Homo sapiens
brenda
Alford, S.R.; Rangarajan, P.; Williams, P.; Gillaspy, G.E.
myo-Inositol oxygenase is required for responses to low energy conditions in Arabidopsis thaliana
Front. Plant Sci.
3
69
2012
Arabidopsis thaliana
brenda
Senthilraja, P.; Paul Aime, N.; Manikandaprabhu, S.; Prakash, M.
Computational screening and docking analysis of natural compounds derived from mangrove plant against type-2 diabetes, myo-inositol oxygenase enzyme (MIOX)
Int. J. Pharm. Sci. Rev. Res.
20
158-161
2013
Homo sapiens
-
brenda
Nayak, B.; Kondeti, V.K.; Xie, P.; Lin, S.; Viswakarma, N.; Raparia, K.; Kanwar, Y.S.
Transcriptional and post-translational modulation of myo-inositol oxygenase by high glucose and related pathobiological stresses
J. Biol. Chem.
286
27594-27611
2011
Mus musculus
brenda
Gaut, J.P.; Crimmins, D.L.; Ohlendorf, M.F.; Lockwood, C.M.; Griest, T.A.; Brada, N.A.; Hoshi, M.; Sato, B.; Hotchkiss, R.S.; Jain, S.; Ladenson, J.H.
Development of an immunoassay for the kidney-specific protein myo-inositol oxygenase, a potential biomarker of acute kidney injury
Clin. Chem.
60
747-757
2014
Homo sapiens (Q9UGB7), Homo sapiens, Mus musculus (Q9QXN5), Mus musculus, Mus musculus C57BL/6 (Q9QXN5)
brenda
Liu, Y.; Gong, X.; Wang, C.; Du, G.; Chen, J.; Kang, Z.
Production of glucaric acid from myo-inositol in engineered Pichia pastoris
Enzyme Microb. Technol.
91
8-16
2016
Komagataella phaffii (C4QZH8), Komagataella phaffii GS115 (C4QZH8), Mus musculus (Q9QXN5), Mus musculus
brenda
Shi, F.; Dong, Y.; Zhang, Y.; Yang, X.; Qiu, D.
Overexpression of the PeaT1 elicitor gene from Alternaria tenuissima improves drought tolerance in rice plants via interaction with a myo-inositol oxygenase
Front. Plant Sci.
8
970
2017
Oryza sativa (Q5Z8T3), Oryza sativa
brenda
Zhan, M.; Usman, I.M.; Sun, L.; Kanwar, Y.S.
Disruption of renal tubular mitochondrial quality control by myo-inositol oxygenase in diabetic kidney disease
J. Am. Soc. Nephrol.
26
1304-1321
2015
Mus musculus (Q9QXN5), Homo sapiens (Q9UGB7)
brenda
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)
brenda
Sun, L.; Dutta, R.K.; Xie, P.; Kanwar, Y.S.
myo-Inositol oxygenase overexpression accentuates generation of reactive oxygen species and exacerbates cellular injury following high glucose ambience a new mechanism relevant to the pathogenesis of diabetic nephropathy
J. Biol. Chem.
291
5688-5707
2016
Sus scrofa (Q8WN98)
brenda
Siddique, S.; Endres, S.; Sobczak, M.; Radakovic, Z.; Fragner, L.; Grundler, F.; Weckwerth, W.; Tenhaken, R.; Bohlmann, H.
Myo-inositol oxygenase is important for the removal of excess myo-inositol from syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
201
476-485
2014
Arabidopsis thaliana (Q8H1S0), Arabidopsis thaliana (O82200), Arabidopsis thaliana (Q9FJU4), Arabidopsis thaliana (Q8L799), Arabidopsis thaliana Col-0 (Q8L799), Arabidopsis thaliana Col-0 (O82200), Arabidopsis thaliana Col-0 (Q8H1S0), Arabidopsis thaliana Col-0 (Q9FJU4)
brenda
Chen, C.; Sun, X.; Duanmu, H.; Yu, Y.; Liu, A.; Xiao, J.; Zhu, Y.
Ectopic expression of a Glycine soja myo-inositol oxygenase gene (GsMIOX1a) in Arabidopsis enhances tolerance to alkaline stress
PLoS ONE
10
e0129998
2015
Arabidopsis thaliana (Q8L799), Glycine soja (A0A0B2PCG9), Glycine soja, Glycine soja 07256 (A0A0B2PCG9)
brenda
Sharma, I.; Dutta, R.K.; Singh, N.K.; Kanwar, Y.S.
High glucose-induced hypomethylation promotes binding of Sp-1 to myo-inositol oxygenase implication in the pathobiology of diabetic tubulopathy
Am. J. Pathol.
187
724-739
2017
Homo sapiens, Mus musculus (Q9QXN5), Mus musculus
brenda
Tominaga, T.; Sharma, I.; Fujita, Y.; Doi, T.; Wallner, A.K.; Kanwar, Y.S.
Myo-inositol oxygenase accentuates renal tubular injury initiated by endoplasmic reticulum stress
Am. J. Physiol. Renal Physiol.
316
F301-F315
2019
Mus musculus (Q9QXN5), Homo sapiens, Sus scrofa
brenda
Alok, A.; Kaur, J.; Tiwari, S.
Functional characterization of wheat myo-inositol oxygenase promoter under different abiotic stress conditions in Arabidopsis thaliana
Biotechnol. Lett.
42
2035-2047
2020
Triticum aestivum
brenda
Teng, F.; You, R.; Hu, M.; Liu, W.; Wang, L.; Tao, Y.
Production of D-glucuronic acid from myo-inositol using Escherichia coli whole-cell biocatalyst overexpressing a novel myo-inositol oxygenase from Thermothelomyces thermophile
Enzyme Microb. Technol.
127
70-74
2019
Arabidopsis thaliana (A0A178V136), Arabidopsis thaliana, Mus musculus (Q9QXN5), Mus musculus, Thermothelomyces thermophilus (G2QA66), Thermothelomyces thermophilus, Thermothelomyces thermophilus ATCC 42464 (G2QA66)
brenda
Dutta, R.K.; Kondeti, V.K.; Sharma, I.; Chandel, N.S.; Quaggin, S.E.; Kanwar, Y.S.
Beneficial effects of myo-inositol oxygenase deficiency in cisplatin-induced AKI
J. Am. Soc. Nephrol.
28
1421-1436
2017
Mus musculus (Q9QXN5)
brenda
Deng, F.; Sharma, I.; Dai, Y.; Yang, M.; Kanwar, Y.S.
Myo-inositol oxygenase expression profile modulates pathogenic ferroptosis in the renal proximal tubule
J. Clin. Invest.
129
5033-5049
2019
Homo sapiens
brenda
Mertoglu, C.; Gunay, M.; Gurel, A.; Gungor, M.
Myo-inositol oxygenase as a novel marker in the diagnosis of acute kidney injury
J. Med. Biochem.
37
1-6.
2018
Homo sapiens
brenda
Zheng, S.; Hou, J.; Zhou, Y.; Fang, H.; Wang, T.T.; Liu, F.; Wang, F.S.; Sheng, J.Z.
One-pot two-strain system based on glucaric acid biosensor for rapid screening of myo-inositol oxygenase mutations and glucaric acid production in recombinant cells
Metab. Eng.
49
212-219
2018
Mus musculus (Q9QXN5)
brenda
EXTERNAL LINKS (specific for EC-Number 1.13.99.1)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
