Information on EC 1.13.99.1 - inositol oxygenase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
1.13.99.1
-
RECOMMENDED NAME
GeneOntology No.
inositol oxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
myo-Inositol + O2 = D-glucuronate + H2O
show the reaction diagram
mechanism
-
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
-
myo-Inositol + O2 = D-glucuronate + H2O
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C-H bond cleavage
-
-
dehydrogenation
-
-
hydroxylation
-
-
oxidation
-
four-electron oxidation of myo-inositol to D-glucuronate
redox reaction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Ascorbate and aldarate metabolism
-
Inositol phosphate metabolism
-
UDP-alpha-D-glucuronate biosynthesis (from myo-inositol)
-
SYSTEMATIC NAME
IUBMB Comments
myo-Inositol:oxygen oxidoreductase
An iron protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
EC 1.13.1.11
-
-
formerly
-
EC 1.99.2.6
-
-
formerly
-
Inositol oxygenase
-
-
-
-
Kidney-specific protein 32
-
-
-
-
meso-Inositol oxygenase
-
-
-
-
MIOX
-
-
-
-
MIOX
O82200, Q8H1S0, Q8L799, Q9FJU4
-
MIOX
Q9UGB7
-
MIOX
-
-
MIOX
Q9QXN5
-
MIOX
Q9QXN4
-
MIOX
-
-
MOO
-
-
-
-
Myo-inositol oxygenase
-
-
-
-
Myo-inositol oxygenase
-
-
Myo-inositol oxygenase
O82200, Q8H1S0, Q8L799, Q9FJU4
-
Myo-inositol oxygenase
-
-
Myo-inositol oxygenase
-
-
Myo-inositol oxygenase
Q9QXN5
-
Myo-inositol oxygenase
-
-
Myo-inositol oxygenase
-
-
Oxygenase, inositol
-
-
-
-
Renal-specific oxidoreductase
-
-
-
-
renal-specific oxidoreductase/myo-inositol oxygenase
-
-
RSOR/MIOX
-
-
CAS REGISTRY NUMBER
COMMENTARY
9029-59-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ecotype Columbia
SwissProt
Manually annotated by BRENDA team
syncytia induced by nematode Heterodera schachtii
UniProt
Manually annotated by BRENDA team
syncytia induced by nematode Heterodera schachtii
SwissProt
Manually annotated by BRENDA team
syncytia induced by nematode Heterodera schachtii
UniProt
Manually annotated by BRENDA team
control group and diabetes group
-
-
Manually annotated by BRENDA team
SwissProt Accession Code:Q8WN98
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
increased expression in diabetic kidneys may contribute to tubulointerstitial injury and development of diabetic nephropathy
physiological function
-
biological production of glucaric acid
physiological function
-
start of catabolism of carbon skeleton of cell-signaling inositol polyphosphates and phosphoinositides
physiological function
O82200, Q8H1S0, Q8L799, Q9FJU4
control level of myoinositol, no influence on ascorbic acid; control level of myoinositol, no influence on ascorbic acid; control level of myoinositol, no influence on ascorbic acid; control level of myoinositol, no influence on ascorbic acid
metabolism
-
MIOX is the first and rate-limiting enzyme in myo-inositol metabolism pathway
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-chiro-inositol + O2
D-glucuronate
show the reaction diagram
Q8WN98, -
much less active with D-chiro-inositol than with myo-inositol
-
-
-
D-chiro-inositol + O2
?
show the reaction diagram
-
-
-
-
?
myo-inositol + H2O
D-glucuronate + H2O
show the reaction diagram
O82200, Q8H1S0, Q8L799, Q9FJU4
-
-
-
?
myo-inositol + O2
D-glucuronate + H2O
show the reaction diagram
-
-
-
-
?
myo-inositol + O2
D-glucuronate + H2O
show the reaction diagram
-
-
-
-
?
myo-inositol + O2
D-glucuronate + H2O
show the reaction diagram
-
-
-
-
ir
myo-inositol + O2
D-glucuronate + H2O
show the reaction diagram
-
-
-
-
ir
myo-inositol + O2
D-glucuronate + H2O
show the reaction diagram
O82200, Q8H1S0, Q8L799, Q9FJU4
-
-
-
?
myo-inositol + O2
D-glucuronate + H2O
show the reaction diagram
-
highly specific for myo-inositol
-
-
-
myo-inositol + O2
D-glucuronate + H2O
show the reaction diagram
-
highly specific for myo-inositol
-
-
-
myo-inositol + O2
D-glucuronate + H2O
show the reaction diagram
Q8WN98, -
highly specific for myo-inositol
-
-
-
myo-inositol + O2
D-glucuronate + H2O
show the reaction diagram
-
highly specific for myo-inositol
-
-
-
myo-inositol + O2
d-glucuronate
show the reaction diagram
-
-
-
-
-
myo-inositol + O2
d-glucuronate
show the reaction diagram
Q8WN98, -
major role in pathogenesis of diabetis
-
-
-
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
-
-
-
-
?
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
Q70GL3, -
-
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
-, Q9QXN5
-
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
Q9QXN4
-
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
-, Q9UGB7
-
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
-
-
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
O82200, Q8H1S0, Q8L799, Q9FJU4
-
-
-
?
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
Q8H1S0
-
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
-, Q9QXN5
first commited step in myo-inositol catabolism
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
Q9QXN4
first commited step in myo-inositol catabolism
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
-, Q9UGB7
first commited step in myo-inositol catabolism
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
-
preincubation without substrate for 10 min at 30C to acitvate the enzyme, assay at pH 8.0, 30C
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
myo-inositol + O2
d-glucuronate
show the reaction diagram
-
-
-
-
-
myo-inositol + O2
d-glucuronate
show the reaction diagram
Q8WN98, -
major role in pathogenesis of diabetis
-
-
-
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
Q70GL3, -
-
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
-
-
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
Q8H1S0
-
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
-, Q9QXN5
first commited step in myo-inositol catabolism
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
Q9QXN4
first commited step in myo-inositol catabolism
-
-
ir
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
-, Q9UGB7
first commited step in myo-inositol catabolism
-
-
ir
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
flavin
-
5. 6 mMol per mol of enzyme
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe2+
Q8WN98
1 mM Fe2+ plus 2mM cysteine required
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; 1 mM Fe(II) and 2 mM cysteine; best activation system
Fe2+
-
iron protein; less active preparations: 1.5 atoms of iron per molecule; most active preparation: 4 mol of iron per 65000 MW protein
Fe2+
-
contains iron most probably in divalent form, enzyme consisting of 16 subunits contains 8 iron atoms per molecule; iron protein
Fe2+
-
1 mM Fe(II) and 2 mM cysteine; either reagent alone gives very little activation; no other metal ion can replace Fe(II)
Fe2+
-
nonheme iron enzyme
Iron
Q8H1S0
enzyme contains non-heme iron
Iron
-
dinuclear iron cluster
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
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
-
diiron cluster
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
Q70GL3, -
-
2,4,6-Tripyridyl-(2)-1,3,5-triazine
-
-
2-Thenoyltrifluoroacetone
-
slight
3-Aminopicolinate
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
8-hydroxyquinoline
-
-
8-hydroxyquinoline
-
-
alpha,alpha'-Bipyridine
-
-
alpha-ketoglutarate
-
-
Barbital
-
-
cyanide
-
-
D-Glucodialdehyde
-
weak
diethyldithiocarbamate
-
-
Epi-Inositol
-
-
Fe3+
-
-
-
ferricyanide
-
-
ferrocyanide
-
-
Furoylthiofluoroacetone
-
slight
-
glyoxylate
-
-
hydroxylamine
-
-
iodoacetate
-
-
iodoacetate
-
-
myo-Inosose-1
-
-
N-ethylmaleimide
-
slight
o-phenanthroline
-
slight
o-phenanthroline
-
-
o-phenanthroline
-
-
oxalacetate
-
-
oxalate
-
-
p-chloromercuribenzoate
Q70GL3, -
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
Phenobarbital
-
-
Phenylmercuric nitrate
-
-
pyruvate
-
-
Quinacrine hydrochloride
-
slight
riboflavin phosphate
-
-
Sodium borohydride
-
-
tetrahydrofolic acid
-
-
Uridine diphosphoglucose
-
-
xanthurenic acid
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-Mercaptopicolinate
-
activation
cysteine
Q8WN98
1 mM Fe2+ plus 2 mM cysteine required
cysteine
-
best activation system: 1 mM Fe(II) and 2 mM cysteine
cysteine
-
activation
cysteine
-
best activation system: 1 mM Fe(II) and 2 mM cysteine; DL-penicillamine; either reagent alone gives very little activation; L-cysteine can be replaced by D-cysteine; or gamma-L-glutamyl-L-cysteine
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
L-cysteine
-
-
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
Quinolinate
-
activation
L-cysteine
-
2 mM
additional information
-
activation during storage at -20C for weeks or months
-
additional information
-
increased secretion in a dose-dependent manner after high-glucose treatment
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.2
-
Inositol
-
with Fe(II) and quinolinic acid as activators
5
-
Inositol
-
with Fe(II) and L-cysteine as activators
5
-
Inositol
-
-
22.1
-
Inositol
-
-
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
5
-
myo-Inositol
Q70GL3, -
30C, pH 6.5
5.8
-
myo-Inositol
-
MIOX activity present in peak 1 of hydrophobic-interaction chromatography on Resource-PHE column
5.9
-
myo-Inositol
Q8WN98
with Fe(2+) and L-cysteine as activators
8.8
-
myo-Inositol
-
MIOX activity present in peak 3 of hydrophobic-interaction chromatography on Resource-PHE column
14.6
-
myo-Inositol
Q9QXN4
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
45
-
myo-Inositol
-
-
0.0095
-
O2
-
-
0.06
-
O2
Q70GL3, -
30C, pH 6.5
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7.22
-
Inositol
-
-
0.183
-
myo-Inositol
Q8WN98
with Fe(2+) and L-cysteine as activators
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.02
-
1,10-phenanthroline
Q70GL3, -
-
0.01
-
p-chloromercuribenzoate
Q70GL3, -
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.005
-
-
culture condition: 1 day, 30C
0.008
-
-
culture condition: 2 day, 30C
0.01
-
-
culture condition: 3 day, 30C
0.015
-
-
culture condition: 12 h, without supplementation of myo-inositol
0.028
-
-
culture condition: without supplementation of myo-inositol
0.042
-
-
culture condition: 12 h, supplementation with 60 mM myo-inositol, 1 mM Fe(NH4)2(SO4)2, 2 mM L-cysteine
0.076
-
-
culture condition: 12 h, supplementation with 60 mM myo-inositol
0.18
-
-
culture condition: 6 h, supplementation with 60 mM myo-inositol, 1 mM Fe(NH4)2(SO4)2, 2 mM L-cysteine
0.43
-
-
culture condition: 6 h, supplementation with 60 mM myo-inositol
2.17
-
Q8H1S0
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
-
6
-
-
-
6
-
-
-
6.8
7.2
-
-
8
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
10
Q70GL3, -
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
6.5
7.4
-
sharp decrease of activity below pH 6.5 and above pH 7.4
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
35
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
60
Q70GL3, -
approx. 30% of maximal activity at 0C and 50C, respectively
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
is expressed at low levels in cell types where diabetic complications occur
Manually annotated by BRENDA team
-
MIOX4 and MIOX5 expression is largely restricted to flowers, particularly maturing pollen
Manually annotated by BRENDA team
-
MIOX expression is upregulated by hyperosmolarity, particularly by polyols like mannitol, sorbitol and xylitol
Manually annotated by BRENDA team
-
only in proximal tubular epithelial cells
Manually annotated by BRENDA team
-
MIOX1 and MIOX2 are expressed in almost all tissues of the plant
Manually annotated by BRENDA team
Q8H1S0
low expression
Manually annotated by BRENDA team
O82200, Q8H1S0, Q8L799, Q9FJU4
-
Manually annotated by BRENDA team
O82200, Q8H1S0, Q8L799, Q9FJU4
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
32000
-
-
SDS-PAGE
32663
-
Q8WN98
electrospray MS determination, gel filtration, SDS-PAGE, sedimentation equilibirum, enzyme does not undergo oligomerization in the presence of myo-inositol
33000
-
-
dynamic light-scattering
33000
-
-
SDS-PAGE
36000
-
Q70GL3, -
gel filtration
65000
-
-
pig, gel filtration, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 16800, rat, dimer is the elementary active enzyme-building unit, oligomer (MW 270000) can be dissociated under mild conditions to monomers (MW 16800)
dodecamer
-
12 * 17000, rat, smallest active unit is tetramer, it is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
hexadecamer
-
16 * 17000, rat, smallest active unit is tetramer, it is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
monomer
Q8WN98
1 * 32663, electrospray MS determination, gel filtration, SDS-PAGE, sedimentation equilibirum, enzyme does not undergo oligomerization in the presence of myo-inositol
monomer
-
1 * 33000, deduced from nucleotide sequence, SDS-PAGE
monomer
Q9QXN4
1 * 33000, deduced from nucleotide sequence, SDS-PAGE
monomer
Q70GL3, -
1 * 37000, SDS-PAGE
monomer
-
1 * 33000, X-ray crystallography
monomer
-
x-ray crystallography
octamer
-
8 * 17000, rat, smallest active unit is tetramer, it is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
oligomer
-
x * 16800, rat, smallest active unit is tetramer, it is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
tetramer
-
4 * 17000, rat, gel filtration, smallest active unit is tetramer, which is in a pH-dependent equilibrium with species consisting of 8, 12 and 16 subunits
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
34
-
-
inactivation during 15 min assay
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
Q9QXN4
Catalase protects from H2O2 inactivation
-
Completely active even in absence of Fe(II) and cysteine if it has been stored at -20C for days to weeks at pH 6.0 with 1 mM glutathione
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Highly unstable in presence of oxygen, in early stages of inactivation: reactivation by reducing agents like NaBH4
-
6870
Sensitive to oxidants: H2O2, ferricyanide, FeCl3, CuSO4, HgCl2
-
6875
Sensitive to reductants, e.g. ferrocyanide
-
6875
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, extensive loss of activity after 1 or 2 days
-
0C, 12 h, extensive loss of activity
-
-20C for weeks or months: activation -20C, completely active even in absence of Fe(II) and cysteine for days to weeks at pH 6.0 with 1 mM glutathione
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant MIOX4
Q8H1S0
recombinant MIOX
-
AG1-X8 resin column chromatography
-
DEAESepharose FF column chromatography and Sephacryl S-200 HR chromatography
-
Ni2+-affinity chromatography
-
Ni2+-affinity chromatography and S200 HR10/30 column chromatography
-
recombinant MIOX
-
affinity chromatography
-
recombinant MIOX
Q9QXN4
ammonium sulfate, DEAE-column, butyl-Sepharose, Superdex 75, Mono Q
Q70GL3, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
O82200, Q8H1S0, Q8L799, Q9FJU4
expression in Escherichia coli
Q8H1S0
expression in epithelial cell line LLC-PK1
-
expression in Escherichia coli
-
genotyping of MIOX in Caucasian type I diabetes mellitus patients, overview
-
expression in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli in the presence of the iron chelator, 1,10-phenanthroline to create iron-free MIOX
-
expression in Escherichia coli
-
expression in Escherichia coli
Q9QXN4
transfection into NRK-52E cells
-
open reading frame of 849 base pairs
Q8WN98
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
445.7fold gene induction in syncytia induced by nematode Heterodera schachtii; 445.7fold gene induction in syncytia induced by nematode Heterodera schachtii; 7.64fold gene induction in syncytia induced by nematode Heterodera schachtii; gene induction in syncytia induced by nematode Heterodera schachtii
O82200, Q8H1S0, Q8L799, Q9FJU4
diabetic, nephropathy
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
DELTA miox 1+2
O82200, Q8H1S0, Q8L799, Q9FJU4
double mutant, smaller syncytia, less female nematodes per plant; double mutant, smaller syncytia, less female nematodes per plant
delta miox 4+5
O82200, Q8H1S0, Q8L799, Q9FJU4
double mutant, smaller syncytia, less female nematodes per plant; double mutant, smaller syncytia, less female nematodes per plant
DELTA miox1
O82200, Q8H1S0, Q8L799, Q9FJU4
single knockout mutant of one allele of MIOX
delta miox2
O82200, Q8H1S0, Q8L799, Q9FJU4
single knockout mutant of one allele of MIOX
delta miox5
O82200, Q8H1S0, Q8L799, Q9FJU4
single knockout mutant of one allele of MIOX; single knockout mutant of one allele of MIOX