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
-
-
-
-
redox reaction
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-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
myo-, chiro- and scillo-inositol degradation
-
-
myo-inositol degradation I
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-
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
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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
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-
Manually annotated by BRENDA team
strain BL23, no activity in strain ATCC 334, gene iolG
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
inducible
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-
Manually annotated by BRENDA team
strain USDA191
SwissProt
Manually annotated by BRENDA team
strain USDA191
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
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
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-
-
-
?
methyl 4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoate + NAD+
?
show the reaction diagram
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-
-
-
?
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+
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+
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
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25C, pH 9.0
4
(1S,2S,3R,4S,5S)-5-(benzyloxy)cyclohexane-1,2,3,4-tetrol
-
25C, pH 9.0
8
(1S,2S,3R,4S,5S)-5-methoxycyclohexane-1,2,3,4-tetrol
-
25C, pH 9.0
44
4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoic acid
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25C, 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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25C, pH 9.0
3
methyl 4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoate
-
25C, 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
-
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Lactobacillus casei (strain BL23)
Lactobacillus casei (strain BL23)
Lactobacillus casei (strain BL23)
Lactobacillus casei (strain BL23)
Lactobacillus casei (strain BL23)
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Rhizobium meliloti (strain 1021)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
180000
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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, 4C, 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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
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655247
6.5
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optimal pH-value for stability
389431
6.8
-
most stable at
389434
8
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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
-10C, 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
-
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
-
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
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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
D172N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
determination of urinary myo-inositol by an improved enzymatic cycling method
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