BRENDA - Enzyme Database show
show all sequences of 1.1.1.18

Probing the promiscuous active site of myo-inositol dehydrogenase using synthetic substrates, homology modeling, and active site modification

Daniellou, R.; Zheng, H.; Langill, D.M.; Sanders, D.A.; Palmer, D.R.; Biochemistry 46, 7469-7477 (2007)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
D172N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Bacillus subtilis
H176A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Bacillus subtilis
Y233F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Bacillus subtilis
Y233R
site-directed mutagenesis, inactive mutant
Bacillus subtilis
Y235F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Bacillus subtilis
Y235R
site-directed mutagenesis, inactive mutant
Bacillus subtilis
Inhibitors
Inhibitors
Commentary
Organism
Structure
diethyl dicarbonate
inactivation
Bacillus subtilis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.07
-
NAD+
pH 9.0, 25°C, recombinant mutant Y233F
Bacillus subtilis
0.08
-
NAD+
pH 9.0, 25°C, recombinant wild-type enzyme
Bacillus subtilis
0.11
-
NAD+
pH 9.0, 25°C, recombinant mutant Y235F
Bacillus subtilis
0.3
-
NAD+
pH 9.0, 25°C, recombinant mutant H176A
Bacillus subtilis
0.4
-
NAD+
pH 9.0, 25°C, recombinant mutant D179N
Bacillus subtilis
1.1
-
NAD+
pH 9.0, 25°C, recombinant mutant D172N
Bacillus subtilis
4
-
myo-inositol
pH 9.0, 25°C, recombinant mutant Y233F
Bacillus subtilis
4.4
-
myo-inositol
pH 9.0, 25°C, recombinant wild-type enzyme
Bacillus subtilis
28
-
myo-inositol
pH 9.0, 25°C, recombinant mutant D179N
Bacillus subtilis
39
-
myo-inositol
pH 9.0, 25°C, recombinant mutant Y235F
Bacillus subtilis
65
-
myo-inositol
pH 9.0, 25°C, recombinant mutant D172N
Bacillus subtilis
118
-
myo-inositol
pH 9.0, 25°C, recombinant mutant H176A
Bacillus subtilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
myo-inositol + NAD+
Bacillus subtilis
-
scyllo-inosose + NADH
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
P26935
-
-
Reaction
Reaction
Commentary
Organism
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
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4-methylbenzenesulfonyl-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-((1S)-10-camphor-sulfonyl)-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-((4-methyloxycarbonyl)-benzyl)-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-(4-carboxybenzyl)-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-(trans-cinnamoyl)-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-allyl-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-alpha-D-glucopyranosyl-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-benzyl-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-methyl-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-[(2-methylphenyl)methyl]-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-[(3-methylphenyl)methyl]-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
additional information
substrate specificity and substrate binding structure, molecular modeling, overview
685170
Bacillus subtilis
?
-
-
-
-
myo-inositol + NAD+
-
685170
Bacillus subtilis
scyllo-inosose + NADH
-
-
-
r
myo-inositol + NAD+
-
685170
Bacillus subtilis
scyllo-inosose + NADH + H+
-
-
-
?
[(4-methylphenyl)methyl]-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
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
Bacillus subtilis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Bacillus subtilis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.23
-
myo-inositol
pH 9.0, 25°C, recombinant mutant H176A
Bacillus subtilis
1.9
-
myo-inositol
pH 9.0, 25°C, recombinant mutant D172N
Bacillus subtilis
34
-
myo-inositol
pH 9.0, 25°C, recombinant mutant Y235F
Bacillus subtilis
47
-
myo-inositol
pH 9.0, 25°C, recombinant mutant Y233F
Bacillus subtilis
58
-
myo-inositol
pH 9.0, 25°C, recombinant wild-type enzyme
Bacillus subtilis
73
-
myo-inositol
pH 9.0, 25°C, recombinant mutant D179N
Bacillus subtilis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
assay at
Bacillus subtilis
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Bacillus subtilis
NADH
-
Bacillus subtilis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Bacillus subtilis
NADH
-
Bacillus subtilis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D172N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Bacillus subtilis
H176A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Bacillus subtilis
Y233F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Bacillus subtilis
Y233R
site-directed mutagenesis, inactive mutant
Bacillus subtilis
Y235F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Bacillus subtilis
Y235R
site-directed mutagenesis, inactive mutant
Bacillus subtilis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
diethyl dicarbonate
inactivation
Bacillus subtilis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.07
-
NAD+
pH 9.0, 25°C, recombinant mutant Y233F
Bacillus subtilis
0.08
-
NAD+
pH 9.0, 25°C, recombinant wild-type enzyme
Bacillus subtilis
0.11
-
NAD+
pH 9.0, 25°C, recombinant mutant Y235F
Bacillus subtilis
0.3
-
NAD+
pH 9.0, 25°C, recombinant mutant H176A
Bacillus subtilis
0.4
-
NAD+
pH 9.0, 25°C, recombinant mutant D179N
Bacillus subtilis
1.1
-
NAD+
pH 9.0, 25°C, recombinant mutant D172N
Bacillus subtilis
4
-
myo-inositol
pH 9.0, 25°C, recombinant mutant Y233F
Bacillus subtilis
4.4
-
myo-inositol
pH 9.0, 25°C, recombinant wild-type enzyme
Bacillus subtilis
28
-
myo-inositol
pH 9.0, 25°C, recombinant mutant D179N
Bacillus subtilis
39
-
myo-inositol
pH 9.0, 25°C, recombinant mutant Y235F
Bacillus subtilis
65
-
myo-inositol
pH 9.0, 25°C, recombinant mutant D172N
Bacillus subtilis
118
-
myo-inositol
pH 9.0, 25°C, recombinant mutant H176A
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
myo-inositol + NAD+
Bacillus subtilis
-
scyllo-inosose + NADH
-
-
r
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4-methylbenzenesulfonyl-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-((1S)-10-camphor-sulfonyl)-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-((4-methyloxycarbonyl)-benzyl)-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-(4-carboxybenzyl)-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-(trans-cinnamoyl)-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-allyl-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-alpha-D-glucopyranosyl-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-benzyl-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-methyl-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-[(2-methylphenyl)methyl]-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
4-O-[(3-methylphenyl)methyl]-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
additional information
substrate specificity and substrate binding structure, molecular modeling, overview
685170
Bacillus subtilis
?
-
-
-
-
myo-inositol + NAD+
-
685170
Bacillus subtilis
scyllo-inosose + NADH
-
-
-
r
myo-inositol + NAD+
-
685170
Bacillus subtilis
scyllo-inosose + NADH + H+
-
-
-
?
[(4-methylphenyl)methyl]-myo-inositol + NAD+
-
685170
Bacillus subtilis
? + NADH + H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
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
Bacillus subtilis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Bacillus subtilis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.23
-
myo-inositol
pH 9.0, 25°C, recombinant mutant H176A
Bacillus subtilis
1.9
-
myo-inositol
pH 9.0, 25°C, recombinant mutant D172N
Bacillus subtilis
34
-
myo-inositol
pH 9.0, 25°C, recombinant mutant Y235F
Bacillus subtilis
47
-
myo-inositol
pH 9.0, 25°C, recombinant mutant Y233F
Bacillus subtilis
58
-
myo-inositol
pH 9.0, 25°C, recombinant wild-type enzyme
Bacillus subtilis
73
-
myo-inositol
pH 9.0, 25°C, recombinant mutant D179N
Bacillus subtilis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
assay at
Bacillus subtilis
Other publictions for EC 1.1.1.18
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
723126
Yoshida
Three inositol dehydrogenases ...
Geobacillus kaustophilus, Geobacillus kaustophilus PS8
Microbiology
158
1942-1952
2012
-
-
1
-
-
-
-
-
-
-
-
2
-
4
-
-
-
-
-
1
-
-
2
-
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
2
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
711151
van Straaten
Structural investigation of my ...
Bacillus subtilis
Biochem. J.
432
237-247
2010
-
-
1
1
1
-
-
-
-
-
-
2
-
2
-
-
-
1
-
-
-
-
4
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
712965
Morinaga
Identification of two scyllo-i ...
Bacillus subtilis 168, Bacillus subtilis
Microbiology
156
1538-1546
2010
-
-
1
-
1
-
-
-
-
-
-
6
-
72
-
-
-
-
-
-
-
-
10
-
-
-
-
-
-
-
-
2
-
-
-
-
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1
2
-
1
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
10
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
684205
Van Straaten
Purification, crystallization ...
Bacillus subtilis
Acta Crystallogr. Sect. F
64
98-101
2008
-
-
1
1
-
-
-
-
-
-
1
1
-
2
-
-
1
1
-
-
-
-
2
1
-
-
-
-
-
-
-
2
-
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-
-
-
1
2
1
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684557
Yebra
Identification of a gene clust ...
Lactobacillus casei
Appl. Environ. Microbiol.
73
3850-3858
2007
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
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-
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-
-
-
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685170
Daniellou
Probing the promiscuous active ...
Bacillus subtilis
Biochemistry
46
7469-7477
2007
-
-
-
-
6
-
1
12
-
-
-
1
-
2
-
-
-
1
-
-
-
-
15
1
1
-
-
6
1
-
-
2
-
-
-
-
-
-
2
-
6
-
-
1
-
12
-
-
-
1
-
-
-
-
-
-
-
-
15
1
1
-
-
6
1
-
-
-
-
-
-
-
-
-
668169
Daniellou
Appel-Lee synthesis of glycosy ...
Bacillus subtilis
Carbohydr. Res.
341
2145-2150
2006
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
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-
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-
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-
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-
-
-
-
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1
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-
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-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670456
Daniellou
Stereoselective oxidation of p ...
Bacillus subtilis
Org. Biomol. Chem.
3
401-403
2005
-
-
-
-
-
-
-
7
-
-
-
-
-
2
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
655247
Yamakoshi
Determination of urinary myo-i ...
Flavobacterium sp.
Clin. Chim. Acta
328
163-171
2003
-
1
-
-
-
-
-
-
-
-
-
-
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1
-
-
-
-
-
-
-
-
3
-
1
-
1
-
1
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
1
-
1
-
1
-
1
-
-
-
-
-
-
-
656606
Ono
Specific determination of myo- ...
Enterobacter aerogenes
J. Pharm. Biomed. Anal.
33
1175-1180
2003
-
-
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-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
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1
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-
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-
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-
-
-
-
-
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389427
Jiang
A functional myo-inositol dehy ...
Sinorhizobium fredii, Sinorhizobium fredii USDA191
J. Bacteriol.
183
2595-2604
2001
-
-
-
-
-
-
-
-
-
-
1
2
-
2
-
-
-
-
-
1
1
-
2
1
-
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-
-
-
-
-
1
-
-
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-
-
1
-
-
-
-
-
-
-
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389428
Galbraith
A functional myo-inositol cata ...
Sinorhizobium meliloti
Microbiology
144
2915-2924
1998
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1
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389429
Stein
myo-Inositol dehydrogenase fro ...
Galdieria sulphuraria
Phytochemistry
46
17-20
1997
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2
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1
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3
1
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1
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389430
Fujita
Bacillus subtiltis inositol de ...
Bacillus subtilis
Gene
108
121-125
1991
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1
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1
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389431
Ramaley
Purification and properties of ...
Bacillus subtilis
J. Biol. Chem.
254
7684-7690
1979
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5
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4
1
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5
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1
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4
1
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1
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389432
Fawole
Inositol dehydrogenase from Se ...
Serratia marcescens
Z. Allg. Mikrobiol.
16
327-328
1976
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389435
Alizade
Chirality of the hydrogen tran ...
Klebsiella pneumoniae
Z. Naturforsch. C
31
624-625
1976
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389433
Walker
myo-Inositol:NAD+ 2-oxidoreduc ...
Streptomyces hygroscopicus
Methods Enzymol.
43
433-439
1975
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389434
Criddle
myo-Inositol dehydrogenase(s) ...
Gluconobacter oxydans
Biochem. J.
137
449-452
1974
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1
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1
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389436
Vidal-Leiria
Inositol dehydrogenase from th ...
Myxozyma melibiosi
Biochim. Biophys. Acta
293
295-303
1973
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2
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1
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5706
Berman
The pathway of myo-inositol de ...
Enterobacter aerogenes
J. Biol. Chem.
241
800-806
1966
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