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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
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
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
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
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
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
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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
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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
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
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
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
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.
Transcriptional and Translational Modulation of myo-Inositol Oxygenase (Miox) by Fatty Acids: IMPLICATIONS IN RENAL TUBULAR INJURY INDUCED IN OBESITY AND DIABETES.
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)
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)