BRENDA - Enzyme Database show
show all sequences of 1.1.1.67

Thermotoga maritima TM0298 is a highly thermostable mannitol dehydrogenase

Song, S.H.; Ahluwalia, N.; Leduc, Y.; Delbaere, L.T.; Vieille, C.; Appl. Microbiol. Biotechnol. 81, 485-495 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells; the TM0298 gene subcloned into the NdeI and XhoI sites of pET24a(+) to yield plasmid pTmMtDH, from which MtDH is expressed with a C-terminal His6-tag in Escherichia coli BL21(DE3)
Thermotoga maritima
MtDH is expressed in Escherichia coli BL21(DE3)
Lactobacillus reuteri
Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
activity of MtDH pretreated with 10 mM EDTA for 20 min at 37°C decreases 96%. Adding 20 mM ZnCl2 to the EDTA-treated enzyme restores activity up to 80% of the control (enzyme not treated with EDTA). Adding 20 mM CoCl2 and 20 mM MnCl2 to the EDTA-treated enzyme restores activity up to 132% and 94% of the control, respectively. In contrast, adding 20 mM MgCl2 or CaCl2 does not increase the activity of the EDTA-treated enzyme.; activity of MtDH pretreated with 10 mM for 20 min at 37°C decreases 96%. Adding 20 mM ZnCl2 to the EDTA-treated enzyme restores activity up to 80% of the control. Adding 20 mM CoCl2 and 20 mM MnCl2 to the EDTA-treated enzyme restores activity up to 132% and 94% of the control, respectively
Thermotoga maritima
mannitol
-
Thermotoga maritima
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.037
-
NADH
at 60°C and pH 6.1; at 60°C, pH 6.1
Thermotoga maritima
0.048
-
NADH
at 80°C and pH 6.1; at 80°C, pH 6.1
Thermotoga maritima
0.14
-
NAD+
at 80°C and pH 8.3; at 80°C, pH 8.3
Thermotoga maritima
0.17
-
NADPH
at 80°C and pH 6.1; at 80°C, pH 6.1
Thermotoga maritima
5.51
-
D-mannitol
at 80°C and pH 8.3; at 80°C, pH 8.3
Thermotoga maritima
7.5
-
NADP+
at 80°C and pH 8.3; at 80°C, pH 8.3
Thermotoga maritima
13.23
-
D-mannitol
at 60°C and pH 6.1; at 60°C, pH 6.1
Thermotoga maritima
50
-
D-fructose
at 60°C and pH 6.1; at 60°C, pH 6.1
Thermotoga maritima
50.97
-
D-fructose
at 80°C and pH 6.1; at 80°C, pH 6.1
Thermotoga maritima
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
-
Thermotoga maritima
Mn2+
-
Thermotoga maritima
additional information
20 mM MgCl2 or CaCl2 do not increase the activity of the EDTA-treated enzyme
Thermotoga maritima
Zn2+
contains 0.69 mol of Zn2+ per subunit of enzyme; MtDH contains a single catalytic zinc per subunit
Thermotoga maritima
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34000
-
4 * 34000, SDS-PAGE
Thermotoga maritima
120000
134000
gel filtration
Thermotoga maritima
120000
143000
gel filtration or analytical ultracentrifugation
Thermotoga maritima
120000
-
ultracentrifugation
Thermotoga maritima
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Lactobacillus reuteri
Q6ECH5
-
-
Thermotoga maritima
Q9WYD4
strain MSB8 (ATCC 43589)
-
Purification (Commentary)
Commentary
Organism
by heat treatment at 85°C and on Ni-NTA column; Ni-NTA agarose column chromatography
Thermotoga maritima
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
54
-
purified enzyme at 80°C with D-fructose as the substrate and NADH as the cofactor; purified enzyme, at 80°C with fructose as the substrate and NADH as the cofactor
Thermotoga maritima
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-fructose + NADPH + H+
also active on fructose with NADPH
695814
Thermotoga maritima
D-mannitol + NADP+
-
-
-
?
D-mannitol + NAD(P)+
-
695814
Thermotoga maritima
D-fructose + NAD(P)H + H+
-
-
-
r
D-mannitol + NAD+
100% activity
695814
Thermotoga maritima
D-fructose + NADH + H+
-
-
-
r
D-tagatose + NAD(P)+
29% relative activity compared to D-fructose
695814
Thermotoga maritima
? + NAD(P)H
-
-
-
?
D-tagatose + NAD+
29% relative activity on D-tagatose compared to 100% activity on D-fructose
695814
Thermotoga maritima
?
-
-
-
?
D-xylulose + NAD(P)+
18% relative activity compared to D-fructose
695814
Thermotoga maritima
? + NAD(P)H
-
-
-
?
D-xylulose + NAD+
18% relative activity on D-xylulose compared to 100% activity on D-fructose
695814
Thermotoga maritima
?
-
-
-
?
L-sorbose + NAD(P)+
5% relative activity compared to D-fructose
695814
Thermotoga maritima
? + NAD(P)H
-
-
-
?
L-sorbose + NADH + H+
5% relative activity on L-sorbose compared to 100% activity on D-fructose
695814
Thermotoga maritima
L-sorbitol + NAD+
-
-
-
?
additional information
mannitol can be produced directly from glucose in a two-step enzymatic process, using a Thermotoga neapolitana xylose isomerase mutant and TmMtDH at 60°C. No activity with glucose, xylose, threonine, arabinose, acetaldehyde, 2-butanone, sorbitol, xylitol, ethanol, or 2-butanol
695814
Thermotoga maritima
?
-
-
-
-
additional information
TM0298 shows no detectable activity on glucose, xylose, threonine, arabinose, acetaldehyde, 2-butanone, sorbitol, xylitol, ethanol, or 2-butanol
695814
Thermotoga maritima
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
gel filtration at room temperature, MtDH in solution
Lactobacillus reuteri
octamer
gel filtration at room temperature, MtDH in solution
Lactobacillus reuteri
tetramer
gel filtration at room temperature, MtDH in solution
Lactobacillus reuteri
tetramer
4 * 34000, SDS-PAGE; gel filtration or analytical ultracentrifugation, MtDH in solution
Thermotoga maritima
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
90
100
most active around 95°C
Thermotoga maritima
95
-
-
Thermotoga maritima
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
90
120
MtDH retains 63% of its activity at 120°C but shows no detectable activity at 25°C
Thermotoga maritima
95
120
retains 63% of its activity at 120°C but shows no detectable activity at room temperature
Thermotoga maritima
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
80
-
half-life: 57 min; half-lives of 57 min
Thermotoga maritima
95
-
half-life: 6 min; half-lives of 6 min
Thermotoga maritima
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
pH 5.5-6 is the optimum for D-fructose reduction and pH 8.3-8.6 is the optimum for mannitol reduction
Thermotoga maritima
5.5
6
optimally reduces L-fructose at pH values between pH 5.5 and 6.0
Thermotoga maritima
8.3
8.6
optimally oxidizes L-mannitol between pH 8.3 and 8.6
Thermotoga maritima
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
8.5
-
TM0298 is sensitive to proteolytic degradation in purification protocols at pH 8.5
Thermotoga maritima
Cofactor
Cofactor
Commentary
Organism
Structure
NAD(P)+
its catalytic efficiency is 33times higher with NAD+ than with NADP+
Thermotoga maritima
NAD(P)H
MtDH has a higher Vmax with NADPH than with NADH, whereas its catalytic efficiency is 2.2times higher with NADH than with NADPH. Cofactor specificity is due to the high density of negatively charged residues (Glu193, Asp195, and Glu196) downstream of the NAD(P) interaction site, the glycine motif
Thermotoga maritima
NAD+
although MtDH has a higher Vmax with NADPH than with NADH, its catalytic efficiency is 33 times higher with NAD+ than with NADP+
Thermotoga maritima
NADH
although MtDH has a higher Vmax with NADPH than with NADH, its catalytic efficiency is 2.2times higher with NADH than with NADPH
Thermotoga maritima
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
99
-
mannitol
-
Thermotoga maritima
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells; the TM0298 gene subcloned into the NdeI and XhoI sites of pET24a(+) to yield plasmid pTmMtDH, from which MtDH is expressed with a C-terminal His6-tag in Escherichia coli BL21(DE3)
Thermotoga maritima
MtDH is expressed in Escherichia coli BL21(DE3)
Lactobacillus reuteri
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD(P)+
its catalytic efficiency is 33times higher with NAD+ than with NADP+
Thermotoga maritima
NAD(P)H
MtDH has a higher Vmax with NADPH than with NADH, whereas its catalytic efficiency is 2.2times higher with NADH than with NADPH. Cofactor specificity is due to the high density of negatively charged residues (Glu193, Asp195, and Glu196) downstream of the NAD(P) interaction site, the glycine motif
Thermotoga maritima
NAD+
although MtDH has a higher Vmax with NADPH than with NADH, its catalytic efficiency is 33 times higher with NAD+ than with NADP+
Thermotoga maritima
NADH
although MtDH has a higher Vmax with NADPH than with NADH, its catalytic efficiency is 2.2times higher with NADH than with NADPH
Thermotoga maritima
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
activity of MtDH pretreated with 10 mM EDTA for 20 min at 37°C decreases 96%. Adding 20 mM ZnCl2 to the EDTA-treated enzyme restores activity up to 80% of the control (enzyme not treated with EDTA). Adding 20 mM CoCl2 and 20 mM MnCl2 to the EDTA-treated enzyme restores activity up to 132% and 94% of the control, respectively. In contrast, adding 20 mM MgCl2 or CaCl2 does not increase the activity of the EDTA-treated enzyme.; activity of MtDH pretreated with 10 mM for 20 min at 37°C decreases 96%. Adding 20 mM ZnCl2 to the EDTA-treated enzyme restores activity up to 80% of the control. Adding 20 mM CoCl2 and 20 mM MnCl2 to the EDTA-treated enzyme restores activity up to 132% and 94% of the control, respectively
Thermotoga maritima
mannitol
-
Thermotoga maritima
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
99
-
mannitol
-
Thermotoga maritima
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.037
-
NADH
at 60°C and pH 6.1; at 60°C, pH 6.1
Thermotoga maritima
0.048
-
NADH
at 80°C and pH 6.1; at 80°C, pH 6.1
Thermotoga maritima
0.14
-
NAD+
at 80°C and pH 8.3; at 80°C, pH 8.3
Thermotoga maritima
0.17
-
NADPH
at 80°C and pH 6.1; at 80°C, pH 6.1
Thermotoga maritima
5.51
-
D-mannitol
at 80°C and pH 8.3; at 80°C, pH 8.3
Thermotoga maritima
7.5
-
NADP+
at 80°C and pH 8.3; at 80°C, pH 8.3
Thermotoga maritima
13.23
-
D-mannitol
at 60°C and pH 6.1; at 60°C, pH 6.1
Thermotoga maritima
50
-
D-fructose
at 60°C and pH 6.1; at 60°C, pH 6.1
Thermotoga maritima
50.97
-
D-fructose
at 80°C and pH 6.1; at 80°C, pH 6.1
Thermotoga maritima
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
-
Thermotoga maritima
Mn2+
-
Thermotoga maritima
additional information
20 mM MgCl2 or CaCl2 do not increase the activity of the EDTA-treated enzyme
Thermotoga maritima
Zn2+
contains 0.69 mol of Zn2+ per subunit of enzyme; MtDH contains a single catalytic zinc per subunit
Thermotoga maritima
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34000
-
4 * 34000, SDS-PAGE
Thermotoga maritima
120000
134000
gel filtration
Thermotoga maritima
120000
143000
gel filtration or analytical ultracentrifugation
Thermotoga maritima
120000
-
ultracentrifugation
Thermotoga maritima
Purification (Commentary) (protein specific)
Commentary
Organism
by heat treatment at 85°C and on Ni-NTA column; Ni-NTA agarose column chromatography
Thermotoga maritima
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
54
-
purified enzyme at 80°C with D-fructose as the substrate and NADH as the cofactor; purified enzyme, at 80°C with fructose as the substrate and NADH as the cofactor
Thermotoga maritima
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-fructose + NADPH + H+
also active on fructose with NADPH
695814
Thermotoga maritima
D-mannitol + NADP+
-
-
-
?
D-mannitol + NAD(P)+
-
695814
Thermotoga maritima
D-fructose + NAD(P)H + H+
-
-
-
r
D-mannitol + NAD+
100% activity
695814
Thermotoga maritima
D-fructose + NADH + H+
-
-
-
r
D-tagatose + NAD(P)+
29% relative activity compared to D-fructose
695814
Thermotoga maritima
? + NAD(P)H
-
-
-
?
D-tagatose + NAD+
29% relative activity on D-tagatose compared to 100% activity on D-fructose
695814
Thermotoga maritima
?
-
-
-
?
D-xylulose + NAD(P)+
18% relative activity compared to D-fructose
695814
Thermotoga maritima
? + NAD(P)H
-
-
-
?
D-xylulose + NAD+
18% relative activity on D-xylulose compared to 100% activity on D-fructose
695814
Thermotoga maritima
?
-
-
-
?
L-sorbose + NAD(P)+
5% relative activity compared to D-fructose
695814
Thermotoga maritima
? + NAD(P)H
-
-
-
?
L-sorbose + NADH + H+
5% relative activity on L-sorbose compared to 100% activity on D-fructose
695814
Thermotoga maritima
L-sorbitol + NAD+
-
-
-
?
additional information
mannitol can be produced directly from glucose in a two-step enzymatic process, using a Thermotoga neapolitana xylose isomerase mutant and TmMtDH at 60°C. No activity with glucose, xylose, threonine, arabinose, acetaldehyde, 2-butanone, sorbitol, xylitol, ethanol, or 2-butanol
695814
Thermotoga maritima
?
-
-
-
-
additional information
TM0298 shows no detectable activity on glucose, xylose, threonine, arabinose, acetaldehyde, 2-butanone, sorbitol, xylitol, ethanol, or 2-butanol
695814
Thermotoga maritima
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
gel filtration at room temperature, MtDH in solution
Lactobacillus reuteri
octamer
gel filtration at room temperature, MtDH in solution
Lactobacillus reuteri
tetramer
gel filtration at room temperature, MtDH in solution
Lactobacillus reuteri
tetramer
4 * 34000, SDS-PAGE; gel filtration or analytical ultracentrifugation, MtDH in solution
Thermotoga maritima
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
90
100
most active around 95°C
Thermotoga maritima
95
-
-
Thermotoga maritima
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
90
120
MtDH retains 63% of its activity at 120°C but shows no detectable activity at 25°C
Thermotoga maritima
95
120
retains 63% of its activity at 120°C but shows no detectable activity at room temperature
Thermotoga maritima
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
80
-
half-life: 57 min; half-lives of 57 min
Thermotoga maritima
95
-
half-life: 6 min; half-lives of 6 min
Thermotoga maritima
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
pH 5.5-6 is the optimum for D-fructose reduction and pH 8.3-8.6 is the optimum for mannitol reduction
Thermotoga maritima
5.5
6
optimally reduces L-fructose at pH values between pH 5.5 and 6.0
Thermotoga maritima
8.3
8.6
optimally oxidizes L-mannitol between pH 8.3 and 8.6
Thermotoga maritima
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
8.5
-
TM0298 is sensitive to proteolytic degradation in purification protocols at pH 8.5
Thermotoga maritima
Other publictions for EC 1.1.1.67
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)
737257
Jordan
Hxt13, Hxt15, Hxt16 and Hxt17 ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae EBY.VW4000
Sci. Rep.
6
0000
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2
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16
-
12
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-
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19
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-
-
-
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-
-
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-
-
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2
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16
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19
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-
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-
725508
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Dynamic mechanism of proton tr ...
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J. Biol. Chem.
287
6655-6667
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-
-
-
1
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-
-
-
-
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-
3
-
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2
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1
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2
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-
722234
Krahulec
Enzymes of mannitol metabolism ...
Aspergillus fumigatus
FEBS J.
278
1264-1276
2011
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-
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-
2
7
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-
2
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2
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-
1
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-
7
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-
2
5
-
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-
3
4
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3
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2
4
7
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2
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7
-
-
-
2
5
-
-
-
-
-
-
-
-
6
6
711136
Klimacek
The oxyanion hole of Pseudomon ...
Pseudomonas fluorescens
Biochem. J.
425
455-463
2010
-
-
-
-
3
-
-
16
-
-
-
-
-
2
-
-
-
1
-
-
-
-
2
-
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-
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8
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3
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16
-
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2
-
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8
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-
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16
16
712470
Klimacek
From alcohol dehydrogenase to ...
Pseudomonas fluorescens
J. Biol. Chem.
285
30644-30653
2010
-
-
1
-
3
-
2
22
-
-
1
-
-
2
-
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-
-
-
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2
1
-
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-
11
-
-
-
2
6
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-
1
2
-
3
-
-
2
6
22
-
-
1
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-
-
-
-
-
-
-
-
2
1
-
-
-
11
-
-
-
-
-
-
-
-
21
21
697276
Krahulec
Polyol-specific long-chain deh ...
Aspergillus fumigatus
Chem. Biol. Interact.
178
274-282
2009
-
-
1
-
-
-
-
4
-
1
1
-
-
5
-
-
1
-
-
-
2
-
2
1
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-
-
-
-
1
-
2
-
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-
-
-
1
2
-
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Structure-guided engineering o ...
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Thermotoga maritima TM0298 is ...
Lactobacillus reuteri, Thermotoga maritima
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700553
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Isomalt production by cloning, ...
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11
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2008
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Puttick
Crystallization, preliminary X ...
Thermotoga maritima
Acta Crystallogr. Sect. F
63
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2007
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685726
Baeumchen
D-mannitol production by resti ...
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2007
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Watanabe
-
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Saccharomyces cerevisiae
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2006
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667238
Liu
Cloning, expression, purificat ...
Lactobacillus brevis
Appl. Biochem. Biotechnol.
121-124
391-401
2005
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667367
Parmentier
-
Enzymatic production of D-mann ...
Leuconostoc pseudomesenteroides
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2005
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668058
Parmentier
Gluconobacter oxydans NAD-depe ...
Gluconobacter oxydans, Gluconobacter oxydans LMG 1489
Biotechnol. Lett.
27
305-311
2005
2
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654309
Kaup
Metabolic engineering of Esche ...
Leuconostoc pseudomesenteroides
Appl. Microbiol. Biotechnol.
64
333-339
2004
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654390
Hahn
A zinc-containing mannitol-2-d ...
Leuconostoc pseudomesenteroides
Arch. Microbiol.
179
101-107
2003
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654531
Klimacek
On the role of Bronsted cataly ...
Pseudomonas fluorescens
Biochem. J.
375
141-149
2003
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655223
Kavanagh
Crystal structure of Pseudomon ...
Pseudomonas fluorescens
Chem. Biol. Interact.
143-144
551-558
2003
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655244
Graefe
Sensitive and specific photome ...
Leuconostoc mesenteroides
Clin. Chem. Lab. Med.
41
1049-1055
2003
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Korakli
Purification and characterisat ...
Lactobacillus sanfranciscensis
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220
281-286
2003
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654295
Aarnikunnas
The mannitol dehydrogenase gen ...
Leuconostoc mesenteroides, Leuconostoc mesenteroides ATCC-9135
Appl. Microbiol. Biotechnol.
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665-671
2002
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654504
Klimacek
A catalytic consensus motif fo ...
Pseudomonas fluorescens
Biochem. J.
367
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2002
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Kavanagh
Crystal structure of Pseudomon ...
Pseudomonas fluorescens
J. Biol. Chem.
277
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2002
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667571
Klimacek
Examining the relative timing ...
Pseudomonas fluorescens
Biochemistry
41
10158-10165
2002
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287261
Slatner
Kinetic study of the catalytic ...
Pseudomonas fluorescens
Biochemistry
38
10489-10498
1999
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2
2
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287260
Slatner
Enzymic synthesis of mannitol: ...
Pseudomonas fluorescens
Ann. N. Y. Acad. Sci.
864
450-453
1998
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1
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287259
Schafer
Mannitol dehydrogenase from Rh ...
Rhodobacter sphaeroides
Appl. Microbiol. Biotechnol.
48
47-52
1997
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287262
Brunker
Cloning, nucleotide sequence a ...
Pseudomonas fluorescens
Biochim. Biophys. Acta
1351
157-167
1997
-
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1
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94720
Schmatz D.M.; Baginsky W.F.; Turner
Evidence for and characterizat ...
Eimeria tenella
Mol. Biochem. Parasitol.
32
263-270
1989
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2
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1
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3
-
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1
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1
1
-
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287237
Schneider
Purification and properties of ...
Rhodobacter sphaeroides
Eur. J. Biochem.
184
15-19
1989
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6
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2
1
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1
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1
5
1
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1
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2
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287238
Quain
Growth and metabolism of manni ...
Saccharomyces cerevisiae
J. Gen. Microbiol.
133
1675-1684
1987
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287239
Richter
D-Mannitol dehydrogenase and D ...
Tetraselmis subcordiformis
Planta
170
528-534
1987
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2
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2
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2
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287240
Mori
Pyruvate formation and sugar m ...
Brevibacterium flavum, Brevibacterium flavum 2247
Agric. Biol. Chem.
51
129-138
1987
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4
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4
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287241
Kulbe
-
Anwendung von Membranverfahren ...
Saccharomyces cerevisiae
GBF Monogr.
9
189-200
1986
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1
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5
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4
5
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5
1
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1
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287242
Mathis
Characterization of a mannitol ...
Bradyrhizobium japonicum
Appl. Environ. Microbiol.
52
81-85
1986
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2
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1
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2
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287243
Davis
Maintenance of different manni ...
Pseudomonas sp.
Appl. Environ. Microbiol.
50
743-748
1985
-
-
-
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1
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1
-
1
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2
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1
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1
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2
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287244
Allenza
Enzymes related to fructose ut ...
Burkholderia cepacia
J. Bacteriol.
150
1348-1356
1982
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-
-
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1
1
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1
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2
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2
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2
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1
1
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2
-
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-
-
94717
Hult
The distribution of the NADPH ...
Fomes pinicola
Arch. Microbiol.
128
253-255
1980
-
-
-
-
-
-
-
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1
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1
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2
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2
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2
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1
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2
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-
287246
Mulongoy
-
Some effects of mannitol on th ...
Bradyrhizobium japonicum
Curr. Microbiol.
1
335-340
1978
-
-
-
-
-
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-
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1
-
1
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3
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2
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2
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1
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3
-
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-
287247
Yamanaka
-
Physicochemical properties of ...
Leuconostoc mesenteroides
Agric. Biol. Chem.
41
1695-1699
1977
-
-
-
1
-
-
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2
1
-
1
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2
1
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2
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2
1
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2
1
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2
1
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287248
Mehta
Mannitol oxidation in two Micr ...
Actinoplanes missouriensis, Gluconobacter oxydans, Lactobacillus brevis, Mycobacterium smegmatis, Nocardia erythropolis, Sinorhizobium meliloti, Streptomyces lavendulae
Appl. Environ. Microbiol.
33
1013-1015
1977
-
-
-
-
-
-
-
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7
-
7
-
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-
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-
-
14
-
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-
-
-
-
14
-
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-
14
-
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7
-
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-
-
-
14
-
-
-
-
-
-
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-
-
-
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-
-
-
-
287249
Kuykendall
Some features of mannitol meta ...
Bradyrhizobium japonicum
J. Gen. Microbiol.
98
291-295
1977
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-
-
-
-
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-
3
-
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1
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1
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5
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2
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2
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3
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1
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5
-
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-
287250
Ueng
D-Mannitol dehydrogenase from ...
Absidia glauca
Biochemistry
16
107-111
1977
-
-
-
-
-
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1
4
-
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1
-
1
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2
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1
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2
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2
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1
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4
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1
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2
-
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-
1
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-
287251
Ueng
D-Mannitol dehydrogenase from ...
Absidia glauca
Biochemistry
15
1743-1749
1976
-
-
-
-
-
-
2
-
-
-
2
1
-
2
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1
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1
1
3
1
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-
1
-
2
1
-
2
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2
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2
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2
1
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1
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1
1
3
1
-
-
1
-
2
1
-
-
-
-
-
-
-
-
287252
Yamanaka
D-Mannitol dehydrogenase from ...
Lactobacillus brevis, Lactobacillus gayonii, Lactobacillus pentoaceticus, Leuconostoc mesenteroides
Methods Enzymol.
41B
138-142
1975
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-
-
1
-
-
-
9
-
-
1
4
-
4
-
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1
-
-
1
1
-
8
-
-
-
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-
4
-
2
8
-
-
-
-
-
-
8
1
-
-
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-
-
9
-
-
1
4
-
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-
1
-
1
1
-
8
-
-
-
-
-
4
-
2
-
-
-
-
-
-
-
285866
Sasajima
-
Polyol dehydrogenases in the s ...
Gluconobacter oxydans
Agric. Biol. Chem.
32
161-169
1968
-
-
-
-
-
-
3
-
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-
1
-
1
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1
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-
1
1
2
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1
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2
2
-
2
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2
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3
-
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1
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1
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1
1
2
-
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-
1
-
2
2
-
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-
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-
-
287253
Yamanaka
Production of polyol dehydroge ...
Lactobacillus brevis, Lactobacillus gayonii, Lactobacillus pentoaceticus, Leuconostoc mesenteroides, Pseudomonas aeruginosa, Pseudomonas coronafaciens, Pseudomonas fluorescens, Sarcina aurantiaca, Sarcina marginata
Can. J. Microbiol.
14
391-396
1968
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9
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9
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18
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18
-
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18
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9
-
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-
18
-
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-
-
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-
-
-
-
287255
Sakai
-
Crystalline D-mannitol:NAD oxi ...
Leuconostoc mesenteroides, no activity in Lactobacillus plantarum
Agric. Biol. Chem.
32
894-899
1968
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1
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1
4
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1
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2
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3
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2
2
2
2
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2
1
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1
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4
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1
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3
-
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2
2
2
-
-
-
-
-
-
-
287256
Sakai
Crystalline D-mannitol:NAD+ ox ...
Leuconostoc mesenteroides
Biochim. Biophys. Acta
151
684-686
1968
-
-
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1
-
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1
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1
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1
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1
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2
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2
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2
1
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1
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1
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1
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2
-
-
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-
-
-
-
-
-
-
-
-
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-
-
287257
Horecker
-
Mannitol dehydrogenase (crysta ...
Lactobacillus brevis
Methods Enzymol.
9
143-146
1966
-
-
-
1
-
-
-
-
-
-
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1
-
1
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1
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1
2
2
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2
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1
2
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2
1
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1
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1
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1
2
2
-
-
-
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-
2
-
1
-
-
-
-
-
-
-
287258
Martinez
-
A specific mannitol dehydrogen ...
Lactobacillus brevis
J. Biol. Chem.
238
1598-1603
1963
-
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1
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4
-
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1
-
1
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1
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2
2
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2
2
1
2
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2
1
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4
-
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1
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1
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2
2
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2
2
1
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-