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Information on EC 1.1.1.18 - inositol 2-dehydrogenase
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1.1.1.18 inositol 2-dehydrogenaseSpecify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
inositol dehydrogenase, bsidh, myo-inositol 2-dehydrogenase, iolg2, inositol 2-dehydrogenase, iolg1, lcidh2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cg0204
IDH
inositol dehydrogenase
iolG
MI dehydrogenase
myo-inositol 2-dehydrogenase
myo-inositol dehydrogenase
myo-inositol:NAD2 oxidoreductase
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inositol dehydrogenase
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myo-inositol 2-dehydrogenase
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myo-inositol dehydrogenase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
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myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
His176 and Asp172 are proposed to act as the catalytic dyad, in which His176 is proposed to be the acid/base catalyst
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myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
ordered sequential Bi-Bi mechanism in the absence of products, residues Y233, Y235, H176, and D172 are important for activity
myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Lys97, Asp172, and His176 are the catalytic triad involved in the catalytic mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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-
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
myo-inositol:NAD+ 2-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
9028-25-5
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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
(1S,2S,3R,4S,5S)-5-(allyloxy)cyclohexane-1,2,3,4-tetrol + NAD+
?
-
-
-
?
(1S,2S,3R,4S,5S)-5-(benzyloxy)cyclohexane-1,2,3,4-tetrol + NAD+
?
-
-
-
?
(1S,2S,3R,4S,5S)-5-methoxycyclohexane-1,2,3,4-tetrol + NAD+
?
-
-
-
?
4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoic acid + NAD+
?
-
-
-
?
4-O-((1S)-10-camphor-sulfonyl)-myo-inositol + NAD+
? + NADH + H+
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-
-
?
4-O-((4-methyloxycarbonyl)-benzyl)-myo-inositol + NAD+
? + NADH + H+
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-
-
?
4-O-alpha-D-glucopyranosyl-myo-inositol + NAD+
? + NADH + H+
-
-
-
?
4-O-[(2-methylphenyl)methyl]-myo-inositol + NAD+
? + NADH + H+
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-
-
?
4-O-[(3-methylphenyl)methyl]-myo-inositol + NAD+
? + NADH + H+
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-
-
?
alpha-D-glucopyranose + NAD+
D-gluconate + NADH
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4fold lower activity compared to myo-inositol as substrate, does not act with the beta-anomer
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?
D-2,3-diketo-4-deoxy-epi-inositol + NADH
ketodeoxyinositol + NAD+
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-
-
?
D-chiro-inositol + NAD+
? + NADH
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19% of the activity with myo-inositol
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-
?
epi-inositol + NAD+
epi-inosose + NADH
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5% of the activity compared to myo-inositol as substrate, conversion of epi-inosose 5% of the activity compared to scyllo-inosose as substrate
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r
methyl 4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoate + NAD+
?
-
-
-
?
myo-inositol + 2,6-dichlorophenolindophenol
2,4,6/3,5-pentahydroxycyclohexanone + reduced 2,6-dichlorophenolindophenol
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-
-
?
scyllo-inositol + NAD+
scyllo-inosose + NADH
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5% of the activity compared to myo-inositol as substrate
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?
D-glucose + NAD+
D-gluconate + NADH
9% of the activity compared to myo-inositol as substrate
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?
D-xylose + NAD+
? + NADH
7% of the activity compared to myo-inositol as substrate
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?
myo-inositol + NAD+
2,3,4,5,6-pentahydroxycyclohexanone + NADH + H+
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-
-
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r
myo-inositol + NAD+
2,3,4,5,6-pentahydroxycyclohexanone + NADH + H+
-
-
-
-
r
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
-
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
-
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
-
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
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should be classified as A-type enzyme
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?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
-
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
involved in nitrogen fixation and nodulation of soybean
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?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
involved in nitrogen fixation and nodulation of soybean
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?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
involved in rhizopine utilization
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
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-
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
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i.e. scyllo-inosose
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?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
-
-
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r
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
-
-
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
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i.e. scyllo-inosose
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?
myo-inositol + NAD+
scyllo-inosose + NADH
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first enzyme in the catabolic pathway of myo-inositol
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r
myo-inositol + NAD+
scyllo-inosose + NADH
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oxidation of the axial hydroxyl group of myo-inositol
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r
myo-inositol + NAD+
scyllo-inosose + NADH
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75 times lower activity compared to the reverse reaction
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r
myo-inositol + NAD+
scyllo-inosose + NADH + H+
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the NAD+-dependent enzyme catalyses the oxidation of the axial hydroxyl group of myo-inositol to form scyllo-inosose
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?
pinitol + NADH + H+
?
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i.e. 3-O-methyl-D-chiro-inositol. Bacillus subtilis can utilize pinitol as the sole carbon source via the same myo-inositol catabolic pathway
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?
pinitol + NADH + H+
?
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i.e. 3-O-methyl-D-chiro-inositol. Bacillus subtilis can utilize pinitol as the sole carbon source via the same myo-inositol catabolic pathway
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?
additional information
?
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a nonpolar cavity adjacent to the active site, allows racemic protected inositol derivatives such as 4-O-benzyl-myo-inositol to be recognized with very high stereoselectivity. Trace activity with (1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl dihydrogen phosphate
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?
additional information
?
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a nonpolar cavity adjacent to the active site, allows racemic protected inositol derivatives such as 4-O-benzyl-myo-inositol to be recognized with very high stereoselectivity. Trace activity with (1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl dihydrogen phosphate
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?
additional information
?
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substrate specificity and substrate binding structure, molecular modeling, overview
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?
additional information
?
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substrate specificity and substrate binding structure, molecular modeling, overview
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-
?
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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?
additional information
?
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scyllo-inositol is no substrate for the enzyme, thus IolG does not act as a scyllo-inositol dehydrogenase
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?
additional information
?
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scyllo-inositol is no substrate for the enzyme, thus IolG does not act as a scyllo-inositol dehydrogenase
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?
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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
D-2,3-diketo-4-deoxy-epi-inositol + NADH
ketodeoxyinositol + NAD+
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-
-
?
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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?
myo-inositol + NAD+
2,3,4,5,6-pentahydroxycyclohexanone + NADH + H+
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r
myo-inositol + NAD+
2,3,4,5,6-pentahydroxycyclohexanone + NADH + H+
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-
-
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r
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
-
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
-
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
should be classified as A-type enzyme
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
-
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
involved in nitrogen fixation and nodulation of soybean
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
involved in nitrogen fixation and nodulation of soybean
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
involved in rhizopine utilization
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
-
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
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i.e. scyllo-inosose
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?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
-
-
-
r
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
-
-
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
-
i.e. scyllo-inosose
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?
myo-inositol + NAD+
scyllo-inosose + NADH
-
first enzyme in the catabolic pathway of myo-inositol
-
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r
myo-inositol + NAD+
scyllo-inosose + NADH
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75 times lower activity compared to the reverse reaction
-
r
myo-inositol + NAD+
scyllo-inosose + NADH + H+
-
the NAD+-dependent enzyme catalyses the oxidation of the axial hydroxyl group of myo-inositol to form scyllo-inosose
-
-
?
pinitol + NADH + H+
?
-
i.e. 3-O-methyl-D-chiro-inositol. Bacillus subtilis can utilize pinitol as the sole carbon source via the same myo-inositol catabolic pathway
-
-
?
pinitol + NADH + H+
?
-
i.e. 3-O-methyl-D-chiro-inositol. Bacillus subtilis can utilize pinitol as the sole carbon source via the same myo-inositol catabolic pathway
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
deoxycholate
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loss of activity within 40 h, if detergent is not removed by chromatography
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
25°C, pH 9.0
44
4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoic acid
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
