Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.13.99.1 - inositol oxygenase and Organism(s) Homo sapiens

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
IUBMB Comments
An iron protein.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
myo-inositol oxygenase, miox4, inositol oxygenase, osmiox, rsor/miox, miox2, gsmiox1a, renal-specific oxidoreductase, renal-specific oxidoreductase/myo-inositol oxygenase, miox1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Inositol oxygenase
-
-
-
-
Kidney-specific protein 32
-
-
-
-
meso-Inositol oxygenase
-
-
-
-
MOO
-
-
-
-
Myo-inositol oxygenase
Oxygenase, inositol
-
-
-
-
Renal-specific oxidoreductase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
myo-Inositol + O2 = D-glucuronate + H2O
show the reaction diagram
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
myo-Inositol:oxygen oxidoreductase
An iron protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-59-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
myo-inositol + O2
D-glucuronate + H2O
show the reaction diagram
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
myo-inositol + O2
D-glucuronate + H2O
show the reaction diagram
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
-
diiron cluster
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-(4-hydroxy-3,5-dimethoxyphenyl)-4,8-dihydronaphthalene-1,3,8-triol
-
docking energy level (Kcal/mol): -6.9602
ascochitine
-
docking energy level (Kcal/mol): -9.5382
D-glucarate
a MIOX inhibitor
heritonin
-
docking energy level (Kcal/mol): -10.4072
stigmasterol
-
docking energy level (Kcal/mol): -14.589
taraxasterol
-
docking energy level (Kcal/mol): -14.8894
tretinoin
-
docking energy level (Kcal/mol): -12.1034
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5 - 5.8
myo-inositol
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
is expressed at low levels in cell types where diabetic complications occur
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
MIOX is a tubular-specific enzyme
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MIOX_HUMAN
285
0
33010
Swiss-Prot
other Location (Reliability: 2)
A6PVH2_HUMAN
270
0
30698
TrEMBL
other Location (Reliability: 2)
A6PVH4_HUMAN
265
0
30837
TrEMBL
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 33000, deduced from nucleotide sequence, SDS-PAGE
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
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant MIOX
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in epithelial cell line LLC-PK1
expression in Escherichia coli
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
genotyping of MIOX in Caucasian type I diabetes mellitus patients, overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression increases in HK-2 cells after 4 h of cisplatin treatment
-
the concentration of the enzyme in serum is higher in the acute kidney injury group compared to the healthy control group
-
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
the kidney-specific protein myo-inositol oxygenase is a potential biomarker of acute kidney injury, AKI
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Homo sapiens, Mus musculus (Q9QXN5), Sus scrofa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team