BRENDA - Enzyme Database show
show all sequences of 1.1.1.18

Identification of two scyllo-inositol dehydrogenases in Bacillus subtilis

Morinaga, T.; Ashida, H.; Yoshida, K.; Microbiology 156, 1538-1546 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene iolG, expression analysis
Bacillus subtilis
Engineering
Amino acid exchange
Commentary
Organism
up
iolG expression is induced by myo-inositol, and less by scyllo-inositol
Bacillus subtilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1-oxo-D-chiro-inositol + NADH + H+
Bacillus subtilis
-
D-chiro-inositol + NAD+
-
-
r
1-oxo-D-chiro-inositol + NADH + H+
Bacillus subtilis 168
-
D-chiro-inositol + NAD+
-
-
r
myo-inositol + NAD+
Bacillus subtilis
-
scyllo-inosose + NADH + H+
-
-
r
myo-inositol + NAD+
Bacillus subtilis 168
-
scyllo-inosose + NADH + H+
-
-
r
pinitol + NADH + H+
Bacillus subtilis
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+
Bacillus subtilis 168
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
?
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
gene iolG
-
Bacillus subtilis 168
-
gene iolG
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-oxo-D-chiro-inositol + NADH + H+
-
712965
Bacillus subtilis
D-chiro-inositol + NAD+
-
-
-
r
1-oxo-D-chiro-inositol + NADH + H+
-
712965
Bacillus subtilis 168
D-chiro-inositol + NAD+
-
-
-
r
additional information
scyllo-inositol is no substrate for the enzyme, thus IolG does not act as a scyllo-inositol dehydrogenase
712965
Bacillus subtilis
?
-
-
-
-
additional information
scyllo-inositol is no substrate for the enzyme, thus IolG does not act as a scyllo-inositol dehydrogenase
712965
Bacillus subtilis 168
?
-
-
-
-
myo-inositol + NAD+
-
712965
Bacillus subtilis
scyllo-inosose + NADH + H+
-
-
-
r
myo-inositol + NAD+
-
712965
Bacillus subtilis 168
scyllo-inosose + NADH + H+
-
-
-
r
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
712965
Bacillus subtilis
?
-
-
-
?
pinitol + NADH + H+
i.e. 3-O-methyl-D-chiro-inositol
712965
Bacillus subtilis
?
-
-
-
?
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
712965
Bacillus subtilis 168
?
-
-
-
?
pinitol + NADH + H+
i.e. 3-O-methyl-D-chiro-inositol
712965
Bacillus subtilis 168
?
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Bacillus subtilis
NADH
-
Bacillus subtilis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene iolG, expression analysis
Bacillus subtilis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Bacillus subtilis
NADH
-
Bacillus subtilis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
up
iolG expression is induced by myo-inositol, and less by scyllo-inositol
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1-oxo-D-chiro-inositol + NADH + H+
Bacillus subtilis
-
D-chiro-inositol + NAD+
-
-
r
1-oxo-D-chiro-inositol + NADH + H+
Bacillus subtilis 168
-
D-chiro-inositol + NAD+
-
-
r
myo-inositol + NAD+
Bacillus subtilis
-
scyllo-inosose + NADH + H+
-
-
r
myo-inositol + NAD+
Bacillus subtilis 168
-
scyllo-inosose + NADH + H+
-
-
r
pinitol + NADH + H+
Bacillus subtilis
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+
Bacillus subtilis 168
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
?
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-oxo-D-chiro-inositol + NADH + H+
-
712965
Bacillus subtilis
D-chiro-inositol + NAD+
-
-
-
r
1-oxo-D-chiro-inositol + NADH + H+
-
712965
Bacillus subtilis 168
D-chiro-inositol + NAD+
-
-
-
r
additional information
scyllo-inositol is no substrate for the enzyme, thus IolG does not act as a scyllo-inositol dehydrogenase
712965
Bacillus subtilis
?
-
-
-
-
additional information
scyllo-inositol is no substrate for the enzyme, thus IolG does not act as a scyllo-inositol dehydrogenase
712965
Bacillus subtilis 168
?
-
-
-
-
myo-inositol + NAD+
-
712965
Bacillus subtilis
scyllo-inosose + NADH + H+
-
-
-
r
myo-inositol + NAD+
-
712965
Bacillus subtilis 168
scyllo-inosose + NADH + H+
-
-
-
r
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
712965
Bacillus subtilis
?
-
-
-
?
pinitol + NADH + H+
i.e. 3-O-methyl-D-chiro-inositol
712965
Bacillus subtilis
?
-
-
-
?
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
712965
Bacillus subtilis 168
?
-
-
-
?
pinitol + NADH + H+
i.e. 3-O-methyl-D-chiro-inositol
712965
Bacillus subtilis 168
?
-
-
-
?
General Information
General Information
Commentary
Organism
physiological function
the enzyme is involved in the myo-inositol catabolic pathway catalyzing the first step, overview
Bacillus subtilis
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme is involved in the myo-inositol catabolic pathway catalyzing the first step, overview
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
-
-
-
-
-
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
-
-
-
-
-
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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1
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-
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-
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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
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
-
-
-
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
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
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-
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-
-
1
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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
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
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-
1
2
-
-
-
-
-
1
1
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389428
Galbraith
A functional myo-inositol cata ...
Sinorhizobium meliloti
Microbiology
144
2915-2924
1998
-
-
-
-
-
-
-
-
-
-
1
1
-
1
-
-
-
-
-
1
1
-
1
1
-
-
-
-
-
-
-
1
-
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-
-
-
1
-
-
-
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-
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1
1
-
-
-
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-
1
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389429
Stein
myo-Inositol dehydrogenase fro ...
Galdieria sulphuraria
Phytochemistry
46
17-20
1997
-
-
-
-
-
-
-
2
-
-
3
1
-
1
-
-
1
-
-
1
1
-
3
1
-
-
1
-
1
1
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
3
1
-
-
-
1
-
1
1
-
3
1
-
-
1
-
1
1
-
-
-
-
-
-
-
-
389430
Fujita
Bacillus subtiltis inositol de ...
Bacillus subtilis
Gene
108
121-125
1991
-
-
1
-
-
-
-
-
-
-
2
1
-
3
-
-
1
-
-
1
1
-
3
1
-
-
-
-
-
-
-
1
-
-
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-
-
1
1
-
-
-
-
-
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-
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2
1
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1
-
1
1
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389431
Ramaley
Purification and properties of ...
Bacillus subtilis
J. Biol. Chem.
254
7684-7690
1979
-
-
-
-
-
-
-
5
-
-
2
1
-
2
-
-
1
-
-
1
1
-
4
1
-
-
-
-
1
-
1
1
-
-
-
-
-
-
1
-
-
-
-
-
-
5
-
-
2
1
-
-
-
1
-
1
1
-
4
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
389432
Fawole
Inositol dehydrogenase from Se ...
Serratia marcescens
Z. Allg. Mikrobiol.
16
327-328
1976
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
1
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
389435
Alizade
Chirality of the hydrogen tran ...
Klebsiella pneumoniae
Z. Naturforsch. C
31
624-625
1976
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
1
-
-
1
-
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-
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1
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1
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-
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-
1
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-
1
-
-
1
-
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-
-
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-
-
-
-
-
-
-
-
389433
Walker
myo-Inositol:NAD+ 2-oxidoreduc ...
Streptomyces hygroscopicus
Methods Enzymol.
43
433-439
1975
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
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389434
Criddle
myo-Inositol dehydrogenase(s) ...
Gluconobacter oxydans
Biochem. J.
137
449-452
1974
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389436
Vidal-Leiria
Inositol dehydrogenase from th ...
Myxozyma melibiosi
Biochim. Biophys. Acta
293
295-303
1973
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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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