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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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This record set is specific for:
Bacillus subtilis
UNIPROT: P26935 not found.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The taxonomic range for the selected organisms is: Bacillus subtilis
Synonyms
BsIDH, IDH, inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase, inositol dehydrogenase, iolG, iolG1, iolG2, LcIDH1, LcIDH2, MI dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
inositol dehydrogenase
iolG
150
gene name
MI dehydrogenase
150
-
myo-inositol 2-dehydrogenase
-
-
-
-
myo-inositol dehydrogenase
myo-inositol:NAD2 oxidoreductase
-
-
-
-
additional information
150
IDH is a member of the GFOR/IDH/MocA family
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
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
myo-inositol:NAD+ 2-oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-25-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glucose + NAD+
D-gluconate + NADH
show the reaction diagram
9% of the activity compared to myo-inositol as substrate
-
?
D-xylose + NAD+
? + NADH
show the reaction diagram
7% of the activity compared to myo-inositol as substrate
-
?
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
-
-
i.e. scyllo-inosose
-
?
(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
-
-
-
-
r
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-glucose + NAD+
D-gluconate + NADH
show the reaction diagram
-
-
-
?
D-xylose + NAD+
? + NADH
show the reaction diagram
-
very low activity
-
?
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 + 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
[(4-methylphenyl)methyl]-myo-inositol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
show the reaction diagram
P26935
-
-
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
show the reaction diagram
-
-
i.e. scyllo-inosose
-
?
1-oxo-D-chiro-inositol + NADH + H+
D-chiro-inositol + NAD+
show the reaction diagram
-
-
-
-
r
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
-
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
-
-
?
additional information
?
-
-
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diethyl dicarbonate
-
inactivation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7
(1S,2S,3R,4S,5S)-5-(allyloxy)cyclohexane-1,2,3,4-tetrol
-
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
-
25C, pH 9.0
9
alpha-D-glucopyranosyl-(1,6)-myo-inositol
-
-
56
alpha-D-glucose
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-
167
D-glucose
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-
190
D-xylose
-
-
57
melibiose
-
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 - 118
myo-inositol
0.07 - 1.1
NAD+
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
12
-
overepression in Escherichia coli
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
-
the enzyme is involved in the myo-inositol catabolic pathway catalyzing the first step, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
-
-
-
-
-
-
-
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
x * 30000, SDS-PAGE
160000
-
gel filtration
39000
-
4 * 39000, SDS-PAGE
39170
-
x * 39170, His-tagged recombiant enzyme, SDS-PAGE
160000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 30000, SDS-PAGE
?
-
x * 39170, His-tagged recombiant enzyme, SDS-PAGE
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
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, 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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
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
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 hide
LITERATURE
6.5
-
optimal pH-value for stability
389431
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
90% homogeneity, recombinant enzyme
-
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
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gene iolG, expression analysis
-
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, Bacillus subtilis (P26935)
Manually annotated by BRENDA team
Ramaley, R.; Fujita, Y.; Freese, E.
Purification and properties of Bacillus subtilis inositol dehydrogenase
J. Biol. Chem.
254
7684-7690
1979
Bacillus subtilis
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Bacillus subtilis (P26935)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Bacillus subtilis (P26935)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Morinaga, T.; Ashida, H.; Yoshida, K.
Identification of two scyllo-inositol dehydrogenases in Bacillus subtilis
Microbiology
156
1538-1546
2010
Bacillus subtilis 168, Bacillus subtilis
Manually annotated by BRENDA team
Zheng, H.; Bertwistle, D.; Sanders, D.A.; Palmer, D.R.
Converting NAD-specific inositol dehydrogenase to an efficient NADP-selective catalyst, with a surprising twist
Biochemistry
52
5876-5883
2013
Bacillus subtilis, Bacillus subtilis (P26935)
Manually annotated by BRENDA team
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