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Information on EC 1.13.99.1 - inositol oxygenase and Organism(s) Mus musculus and UniProt Accession Q9QXN5
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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
-
glucuronate-xylulose
- medicine
- diagnostics
The taxonomic range for the selected organisms is: Mus musculus
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, miox2, gsmiox1a, renal-specific oxidoreductase, renal-specific oxidoreductase/myo-inositol oxygenase, miox1, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MIOX
-
Myo-inositol oxygenase
-
Inositol oxygenase
-
-
-
-
Kidney-specific protein 32
-
-
-
-
meso-Inositol oxygenase
-
-
-
-
MIOX
MOO
-
-
-
-
Myo-inositol oxygenase
Oxygenase, inositol
-
-
-
-
Renal-specific oxidoreductase
-
-
-
-
MIOX
-
-
-
-
Myo-inositol oxygenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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-glucuronic acid + H2O
first commited step in myo-inositol catabolism
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
preincubation without substrate for 10 min at 30°C to acitvate the enzyme, assay at pH 8.0, 30°C
-
-
?
myo-inositol + O2
D-glucuronate + H2O
-
-
-
-
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
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
-
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
-
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glucarate
a MIOX inhibitor, D-glucarate normalizes reduced autophagy and mitophagy in tubules of STZ-induced diabetic mice
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
3.573
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
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
24.7
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
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.5
the enzyme shows high activity (more than 70%) across the pH range from 7.5-8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
from mice with acute kidney injury, MIOX expression is undetectable in healthy mice plasma
additional information
kidney-specific expression of protein myo-inositol oxygenase encoding gene miox in proximal renal tubule
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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, D-glucarate normalizes reduced autophagy and mitophagy in tubules of STZ-induced diabetic mice
metabolism
physiological function
physiological function
-
start of catabolism of carbon skeleton of cell-signaling inositol polyphosphates and phosphoinositides
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
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
enzyme overexpression accentuates the cellular injury related to endoplasmic reticulum stress and accentuates tunicamycin-induced generation of reactive oxygen species
physiological function
enzyme overexpression exacerbates cisplatin-induced acute kidney injury by accentuating renal tubular cell apoptosis and modulating the expression of inflammatory cytokines
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_MOUSE
285
0
33164
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
764595
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain EA31 and Saccharomyces cerevisiae strain SG
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
expressed in Escherichia coli in the presence of the iron chelator, 1,10-phenanthroline to create iron-free MIOX
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
cisplatin increases the enzyme expression via demethylation of its promoter
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
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
antioxidants N-acetylcysteine, beta-naphthoflavone, and tertiary butyl hydroquinone reduces MIOX expression
-
high glucose levels, exposure of cells to oxidants H2O2 and methylglyoxal up-regulates MIOX expression
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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)
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
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
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
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
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
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
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
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
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)
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
Mammalia, Mus musculus
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
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)
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
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)
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)
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
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
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)
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)
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)
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