Information on EC 1.1.1.18 - inositol 2-dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.18
-
RECOMMENDED NAME
GeneOntology No.
inositol 2-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
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redox reaction
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-
-
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reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
myo-, chiro- and scyllo-inositol degradation
-
-
myo-inositol degradation I
-
-
myo-inositol degradation II
-
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streptomycin biosynthesis
-
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myo-inositol biosynthesis
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Streptomycin biosynthesis
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Inositol phosphate metabolism
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Metabolic pathways
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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-
SYSTEMATIC NAME
IUBMB Comments
myo-inositol:NAD+ 2-oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-25-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene iolG
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
three paralogous iol genes located in tandem within a large gene cluster, i.e. GK1897, GK1898, and GK1899
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-
Manually annotated by BRENDA team
three paralogous iol genes located in tandem within a large gene cluster, i.e. GK1897, GK1898, and GK1899
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
inducible
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-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
formerly Streptomyces glebosus
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme is related to the GFO/MocA/IDH family of dehydrogenases
metabolism
-
inositol dehydrogenase is responsible for the first step in myo-inositol degradation
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1S,2S,3R,4S,5S)-5-(allyloxy)cyclohexane-1,2,3,4-tetrol + NAD+
?
show the reaction diagram
-
-
-
-
?
(1S,2S,3R,4S,5S)-5-(benzyloxy)cyclohexane-1,2,3,4-tetrol + NAD+
?
show the reaction diagram
-
-
-
-
?
(1S,2S,3R,4S,5S)-5-methoxycyclohexane-1,2,3,4-tetrol + NAD+
?
show the reaction diagram
-
-
-
-
?
1-oxo-D-chiro-inositol + NADH + H+
D-chiro-inositol + NAD+
show the reaction diagram
4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoic acid + NAD+
?
show the reaction diagram
-
-
-
-
?
4-methylbenzenesulfonyl-myo-inositol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
4-O-((1S)-10-camphor-sulfonyl)-myo-inositol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
4-O-((4-methyloxycarbonyl)-benzyl)-myo-inositol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
4-O-(4-carboxybenzyl)-myo-inositol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
4-O-(trans-cinnamoyl)-myo-inositol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
4-O-allyl-myo-inositol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
4-O-alpha-D-glucopyranosyl-myo-inositol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
4-O-benzyl-myo-inositol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
4-O-methyl-myo-inositol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
4-O-[(2-methylphenyl)methyl]-myo-inositol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
4-O-[(3-methylphenyl)methyl]-myo-inositol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
alpha-D-glucopyranose + NAD+
D-gluconate + NADH
show the reaction diagram
-
4fold lower activity compared to myo-inositol as substrate, does not act with the beta-anomer
-
?
alpha-D-glucopyranosyl-(1,6)-myo-inositol + NAD+
?
show the reaction diagram
-
-
-
-
?
D-2,3-diketo-4-deoxy-epi-inositol + NADH
ketodeoxyinositol + NAD+
show the reaction diagram
-
-
-
?
D-chiro-inositol + NAD+
? + NADH
show the reaction diagram
-
19% of the activity with myo-inositol
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-
?
D-glucose + NAD+
D-gluconate + NADH
show the reaction diagram
D-xylose + NAD+
? + NADH
show the reaction diagram
epi-inositol + NAD+
? + NADH
show the reaction diagram
-
4% of the activity with myo-inositol
-
-
?
epi-inositol + NAD+
epi-inosose + NADH
show the reaction diagram
-
5% of the activity compared to myo-inositol as substrate, conversion of epi-inosose 5% of the activity compared to scyllo-inosose as substrate
-
r
melibiose + NAD+
?
show the reaction diagram
-
-
-
-
?
methyl 4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoate + NAD+
?
show the reaction diagram
-
-
-
-
?
myo-inositol + 2,6-dichlorophenolindophenol
2,4,6/3,5-pentahydroxycyclohexanone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
myo-inositol + NAD+
2,3,4,5,6-pentahydroxycyclohexanone + NADH
show the reaction diagram
-
-
-
-
r
myo-inositol + NAD+
2,3,4,5,6-pentahydroxycyclohexanone + NADH + H+
show the reaction diagram
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
show the reaction diagram
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
show the reaction diagram
myo-inositol + NAD+
scyllo-inosose + NADH
show the reaction diagram
myo-inositol + NAD+
scyllo-inosose + NADH + H+
show the reaction diagram
pinitol + NADH + H+
?
show the reaction diagram
scyllo-inositol + NAD+
scyllo-inosose + NADH
show the reaction diagram
-
5% of the activity compared to myo-inositol as substrate
-
?
[(4-methylphenyl)methyl]-myo-inositol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-oxo-D-chiro-inositol + NADH + H+
D-chiro-inositol + NAD+
show the reaction diagram
D-2,3-diketo-4-deoxy-epi-inositol + NADH
ketodeoxyinositol + NAD+
show the reaction diagram
-
-
-
?
myo-inositol + NAD+
2,3,4,5,6-pentahydroxycyclohexanone + NADH + H+
show the reaction diagram
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
show the reaction diagram
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
show the reaction diagram
myo-inositol + NAD+
scyllo-inosose + NADH
show the reaction diagram
myo-inositol + NAD+
scyllo-inosose + NADH + H+
show the reaction diagram
pinitol + NADH + H+
?
show the reaction diagram
additional information
?
-
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the enzyme shows a broad substrate spectrum while remaining highly stereoselective. BsIDH is able to oxidize the mono-saccharides alpha-D-glucose and alpha-D-xylose but not beta-D-glucose, D-mannose and D-galactose
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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less than 10% of the activity compared to NAD+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-keto-myo-inositol
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deoxycholate
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loss of activity within 40 h, if detergent is not removed by chromatography
diethyl dicarbonate
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inactivation
NADH
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competitive inhibition with NAD+ as variable substrate, bi-bi mechanism
scyllo-inosose
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non-competitive inhibition with myo-inositol as varied substrate, uncompetitive with NAD+ as variable substrate, bi-bi ordered mechanism
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7
(1S,2S,3R,4S,5S)-5-(allyloxy)cyclohexane-1,2,3,4-tetrol
-
25°C, pH 9.0
4
(1S,2S,3R,4S,5S)-5-(benzyloxy)cyclohexane-1,2,3,4-tetrol
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25°C, pH 9.0
8
(1S,2S,3R,4S,5S)-5-methoxycyclohexane-1,2,3,4-tetrol
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25°C, pH 9.0
44
4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoic acid
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25°C, pH 9.0
9
alpha-D-glucopyranosyl-(1,6)-myo-inositol
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-
56
alpha-D-glucose
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167
D-glucose
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190
D-xylose
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57
melibiose
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25°C, pH 9.0
3
methyl 4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoate
-
25°C, pH 9.0
4 - 430
myo-inositol
0.07 - 1.1
NAD+
1.3
scyllo-inosose
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23 - 73
myo-inositol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.07
after induction of gene expression by myo-inositol
0.241
after induction of gene expression by myo-inositol
12
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overepression in Escherichia coli
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9.5
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half-maximal activity at pH 5.5 and pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.33
E1U887;, E1U888;
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacillus subtilis (strain 168);
Q8NL86
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025);
Lactobacillus casei (strain BL23);
F9ULF9
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1);
O68965
Rhizobium meliloti (strain 1021);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
x * 30000, SDS-PAGE
34648
x * 34648, calculation from ORF of cDNA sequence
35130
x * 35130, calculation from ORF of cDNA sequence
39000
-
4 * 39000, SDS-PAGE
39170
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x * 39170, His-tagged recombiant enzyme, SDS-PAGE
42000
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4 * 42000, SDS-PAGE
160000
180000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
additional information
-
construction of an homology model of inositol dehydrogenase, to which NADH and 4-O-benzylscyllo-inosose are docked and the active site energy minimized, molecular modeling, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged native and selenomethionine-labeled enzyme, 12 mg/ml wild-type protein in 25 mM Tris, pH 8.0, and 13.8 mg/ml of selenomethionine-labeled enzyme in 20 mM Tris, pH 8.0, and 5 mM DTT, 4°C, modified microbatch method, equal volumes of protein solution and precipitant solution of 0.001 ml, the latter containing 20%w/v PEG 3350, 0.20 M potassium fluoride, pH 8.5-9.0, are mixed, overlaid with a 1:1 mixture of silicone and paraffin oils, X-ray anomalous diffraction structure determination and analysis at 1.75-2.0 A resolution, molecular replacement
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purified wild-type BsIDH and K97V mutant in apo-, holo- and ternary complexes with inositol and inosose, mixing of 0.002 ml of protein solution containing 10mg/ml protein in 25 mM Tris pH 8.0, with 0.002 ml reservoir solution containing 0.1-0.2 M tri-sodium citrate, pH 5.4, and 1.6-2.9 M ammonium sulfate, for the holo-enzyme complexes with 0.1 M tri-sodium citrate pH 5.4, 2.6 M ammonium sulfate and either inositol or inosose at 4 mg/0.1 ml mother liquid, cryoprotection with 25% ethylene glycol, X-ray diffraction structure determination and analysis at 2.3 A resolution
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X-ray diffraction structure determination and analysis of enzyme mutant A12K/D35S/V36R complex with NADP+
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purified recombinant His-tagged enzyme, microbatch crystallization, mixing of 0.001 ml of 10 mg/ml protein in 25 mM Tris-HCl, pH 8.0, with 0.001 ml of crystallization solution containing 2.8 M ammonium sulfate, 0.18 M citric acid, pH 5.0, room temperature, X-ray diffraction structure determination and analysis at 1.6 A resolution, molecular replacement and model building, the room-temperature radiation tolerance of a protein crystal and its pseudo-translation symmetry, overview
E1U887;, E1U888;
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
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-
655247
6.5
-
optimal pH-value for stability
389431
6.8
-
most stable at
389434
8
-
sharp decrease of activity below or above
389432
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
30 min, 85% residual activity
50
-
stable for 2 h
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
90% homogeneity, recombinant enzyme
-
partial
recombinant His-tagged native and selenomethionine-labeled enzyme from Escherichia coli by nickel affinity chromatography to homogeneity
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain XL1-Blue by ammonium sulfate fractionation, nickel affinity chromatography and dialysis
E1U887;, E1U888;
to homogeneity, chromatography steps
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression of His-tagged native and selenomethionine-labeled enzyme in Escherichia coli
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gene iolG, encoded and transcribed in the iolTABCDG1G2EJK operon, DNA and amino acid sequence determination and analysis, genetic organization, genes encoded in the iolTABCDG1G2EJK operon transcribe a complete MI catabolic pathway, transcriptional regulation pattern, phalogenetic analysis, overview
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gene iolG, expression analysis
-
gene iolG2, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain XL1-Blue
E1U887;, E1U888;
organization of iol genes, three paralogous iol genes GK1897, GK1898, and GK1899 located in tandem within a large gene cluster, determination of the transcription start site, individual expression as His6-tagged proteins in Escherichia coli strain BL21(DE3)
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A12K/D35S/V36R
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site-directed mutagenesis, the triple mutant has a value of 570000 M/s in reaction with NADP+, higher than that of the wild-type IDH with NAD+. The binding of the coenzyme in the mutant is altered such that although the nicotinamide ring maintains the required position for catalysis, the coenzyme has twisted by nearly 90°, so the adenine moiety no longer binds to a hydrophobic cleft in the Rossmann fold as in the wild-type enzyme
D172N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D35S/V36R
-
site-directed mutagenesis, the double mutant prefers NADP+ to NAD+ by a factor of 5. The mutant is an excellent catalyst with a second-order rate constant with respect to NADP of 370000 M/s
H176A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K97V
-
site-directed mutagenesis, inactive mutant
up
-
iolG expression is induced by myo-inositol, and less by scyllo-inositol
Y233F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y233R
-
site-directed mutagenesis, inactive mutant
Y235F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y235R
-
site-directed mutagenesis, inactive mutant
up
-
iolG expression is induced by myo-inositol, and less by scyllo-inositol
-
analysis
-
specific determination of myo-inositol using a fluorophotometer to measure the fluorescence of NADH released by enzyme immobilized on porous glass
additional information
-
convertion of NAD+-specific inositol dehydrogenase to an efficient NADP+-selective catalyst to enhance understanding of coenzyme selectivity and to create an enzyme capable of recycling NADP+ in biocatalytic processes
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
determination of urinary myo-inositol by an improved enzymatic cycling method
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