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Information on EC 1.1.1.18 - inositol 2-dehydrogenase and Organism(s) Bacillus subtilis and UniProt Accession P26935
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1.1.1.18 inositol 2-dehydrogenaseSpecify your search results
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
inositol dehydrogenase, bsidh, myo-inositol 2-dehydrogenase, iolg2, iolg1, inositol 2-dehydrogenase, lcidh2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
inositol dehydrogenase
myo-inositol 2-dehydrogenase
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myo-inositol dehydrogenase
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myo-inositol:NAD2 oxidoreductase
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inositol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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+
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+
Lys97, Asp172, and His176 are the catalytic triad involved in the catalytic mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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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+
?
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-
-
?
(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+
?
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-
-
?
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+
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-
-
?
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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-
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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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?
methyl 4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoate + NAD+
?
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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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?
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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?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
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-
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?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
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?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
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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 + 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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?
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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?
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 + 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
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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
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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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+
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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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme is related to the GFO/MocA/IDH family of dehydrogenases
metabolism
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inositol dehydrogenase is responsible for the first step in myo-inositol degradation
physiological function
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the enzyme is involved in the myo-inositol catabolic pathway catalyzing the first step, overview
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
tetramer
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BsIDH is a tetramer, with an arrangement consisting of 2 long continuous beta-sheets, formed from all 4 monomers, in which the central 2 strands are crossed over to form the core of the tetramer. Each subunit in the tetramer consists of two domains, an N-terminal Rossmann fold domain containing the cofactor-binding site, and a C-terminal domain containing the inositol-binding site, structure-function analysis, overview
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
additional information
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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
X-ray diffraction structure determination and analysis of enzyme mutant A12K/D35S/V36R complex with NADP+
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A12K/D35S/V36R
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
Y233F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y235F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
up
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iolG expression is induced by myo-inositol, and less by scyllo-inositol
additional information
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
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged native and selenomethionine-labeled enzyme from Escherichia coli by nickel affinity chromatography to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged native and selenomethionine-labeled enzyme in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujita, Y.; Shindo, K.; Miwa, Y.; Yoshida, K.
Bacillus subtiltis inositol dehydrogenase-encoding gene (idh): sequence and expression in Escherichia coli
Gene
108
121-125
1991
Bacillus subtilis (P26935), Bacillus subtilis
Ramaley, R.; Fujita, Y.; Freese, E.
Purification and properties of Bacillus subtilis inositol dehydrogenase
J. Biol. Chem.
254
7684-7690
1979
Bacillus subtilis
Daniellou, R.; Palmer, D.R.
Appel-Lee synthesis of glycosyl inositols, substrates for inositol dehydrogenase from Bacillus subtilis
Carbohydr. Res.
341
2145-2150
2006
Bacillus subtilis
Daniellou, R.; Phenix, C.P.; Tam, P.H.; Laliberte, M.C.; Palmer, D.R.
Stereoselective oxidation of protected inositol derivatives catalyzed by inositol dehydrogenase from Bacillus subtilis
Org. Biomol. Chem.
3
401-403
2005
Bacillus subtilis (P26935), Bacillus subtilis
Van Straaten, K.E.; Hoffort, A.; Palmer, D.R.; Sanders, D.A.
Purification, crystallization and preliminary X-ray analysis of inositol dehydrogenase (IDH) from Bacillus subtilis
Acta Crystallogr. Sect. F
64
98-101
2008
Bacillus subtilis
Daniellou, R.; Zheng, H.; Langill, D.M.; Sanders, D.A.; Palmer, D.R.
Probing the promiscuous active site of myo-inositol dehydrogenase using synthetic substrates, homology modeling, and active site modification
Biochemistry
46
7469-7477
2007
Bacillus subtilis (P26935), Bacillus subtilis
van Straaten, K.E.; Zheng, H.; Palmer, D.R.; Sanders, D.A.
Structural investigation of myo-inositol dehydrogenase from Bacillus subtilis: implications for catalytic mechanism and inositol dehydrogenase subfamily classification
Biochem. J.
432
237-247
2010
Bacillus subtilis
Morinaga, T.; Ashida, H.; Yoshida, K.
Identification of two scyllo-inositol dehydrogenases in Bacillus subtilis
Microbiology
156
1538-1546
2010
Bacillus subtilis, Bacillus subtilis 168
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