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show all sequences of 1.1.1.17

Molecular and biochemical characterization of mannitol-1-phosphate dehydrogenase from the model brown alga Ectocarpus sp.

Bonin, P.; Groisillier, A.; Raimbault, A.; Guibert, A.; Boyen, C.; Tonon, T.; Phytochemistry 117, 509-520 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene MPDH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis; gene MPDH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis, recombinant expression of His-tagged EsM1PDH1 in Escherichia coli; gene MPDH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis, recombinant expression of His-tagged EsM1PDH1 in Escherichia coli; gene MPDH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis, recombinant expression of His-tagged EsM1PDH1 in Escherichia coli; gene MPDH2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis
Ectocarpus siliculosus
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
no inhibition by EDTA; no inhibition by EDTA; no inhibition by EDTA
Ectocarpus siliculosus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics; Michaelis-Menten kinetics; Michaelis-Menten kinetics
Ectocarpus siliculosus
0.02
-
NAD+
recombinant enzyme, pH 9.0, 30°C; recombinant enzyme, pH 9.0, 30°C; recombinant enzyme, pH 9.0, 30°C
Ectocarpus siliculosus
0.19
-
D-fructose 6-phosphate
recombinant enzyme, pH 7.0, 30°C; recombinant enzyme, pH 7.0, 30°C; recombinant enzyme, pH 7.0, 30°C
Ectocarpus siliculosus
0.38
-
D-mannitol 1-phosphate
recombinant enzyme, pH 9.0, 30°C; recombinant enzyme, pH 9.0, 30°C; recombinant enzyme, pH 9.0, 30°C
Ectocarpus siliculosus
16
-
NADH
recombinant enzyme, pH 7.0, 30°C; recombinant enzyme, pH 7.0, 30°C; recombinant enzyme, pH 7.0, 30°C
Ectocarpus siliculosus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
NaCl
activates; activates; activates
Ectocarpus siliculosus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42000
-
-
Ectocarpus siliculosus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-mannitol 1-phosphate + NAD+
Ectocarpus siliculosus
-
D-fructose 6-phosphate + NADH + H+
-
-
r
additional information
Ectocarpus siliculosus
mannitol is present in large amounts in brown algae, where its synthesis involved two steps: a mannitol-1-phosphate dehydrogenase (M1PDH) catalyzes a reversible reaction between fructose-6-phosphate (F6P) and mannitol-1-phosphate (M1P) (EC 1.1.1.17), and a mannitol-1-phosphatase hydrolyzes M1P to mannitol (EC 3.1.3.22)
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Ectocarpus siliculosus
D7FMJ8
MPDH1
-
Ectocarpus siliculosus
D7G793
MPDH3
-
Ectocarpus siliculosus
D8LI09
MPDH2
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged EsM1PDH1 from Escherichia coli by nickel affinity chromatography and gel filtration; recombinant His-tagged EsM1PDH1 from Escherichia coli by nickel affinity chromatography and gel filtration; recombinant His-tagged EsM1PDH1 from Escherichia coli by nickel affinity chromatography and gel filtration
Ectocarpus siliculosus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.014
-
recombinant enzyme, D-mannitol 1-phosphate oxidation, pH 9.0, 30°C; recombinant enzyme, D-mannitol 1-phosphate oxidation, pH 9.0, 30°C; recombinant enzyme, D-mannitol 1-phosphate oxidation, pH 9.0, 30°C
Ectocarpus siliculosus
0.016
-
purified recombinant enzyme, D-mannitol 1-phosphate oxidation, pH 9.0, 30°C; purified recombinant enzyme, D-mannitol 1-phosphate oxidation, pH 9.0, 30°C; purified recombinant enzyme, D-mannitol 1-phosphate oxidation, pH 9.0, 30°C
Ectocarpus siliculosus
0.026
-
recombinant enzyme, D-fructose 6-phosphate reduction, pH 7.0, 30°C; recombinant enzyme, D-fructose 6-phosphate reduction, pH 7.0, 30°C; recombinant enzyme, D-fructose 6-phosphate reduction, pH 7.0, 30°C
Ectocarpus siliculosus
0.046
-
purified recombinant enzyme, D-fructose 6-phosphate reduction, pH 7.0, 30°C; purified recombinant enzyme, D-fructose 6-phosphate reduction, pH 7.0, 30°C; purified recombinant enzyme, D-fructose 6-phosphate reduction, pH 7.0, 30°C
Ectocarpus siliculosus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-mannitol 1-phosphate + NAD+
-
741122
Ectocarpus siliculosus
D-fructose 6-phosphate + NADH + H+
-
-
-
r
additional information
mannitol is present in large amounts in brown algae, where its synthesis involved two steps: a mannitol-1-phosphate dehydrogenase (M1PDH) catalyzes a reversible reaction between fructose-6-phosphate (F6P) and mannitol-1-phosphate (M1P) (EC 1.1.1.17), and a mannitol-1-phosphatase hydrolyzes M1P to mannitol (EC 3.1.3.22)
741122
Ectocarpus siliculosus
?
-
-
-
-
additional information
EsM1PDH1cat isozyme is specific for D-fructose 6-phosphate and D-mannitol 1-phosphate
741122
Ectocarpus siliculosus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 42000, recombinant His-tagged EsM1PDH1 isozyme, SDS-PAGE; x * 42000, recombinant His-tagged EsM1PDH1 isozyme, SDS-PAGE; x * 42000, recombinant His-tagged EsM1PDH1 isozyme, SDS-PAGE
Ectocarpus siliculosus
More
structure-based sequence comparisons, overview; structure-based sequence comparisons, overview; structure-based sequence comparisons, overview
Ectocarpus siliculosus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Ectocarpus siliculosus
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
5
50
35% of maximum activity at 5-10°C, less than 5% at 50°C; 35% of maximum activity at 5-10°C, less than 5% at 50°C; 35% of maximum activity at 5-10°C, less than 5% at 50°C
Ectocarpus siliculosus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
D-fructose 6-phosphate reduction; D-fructose 6-phosphate reduction; D-fructose 6-phosphate reduction
Ectocarpus siliculosus
9
-
D-mannitol 1-phosphate oxidation; D-mannitol 1-phosphate oxidation; D-mannitol 1-phosphate oxidation
Ectocarpus siliculosus
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH; isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH; isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH
Ectocarpus siliculosus
NAD+
-
Ectocarpus siliculosus
NADH
-
Ectocarpus siliculosus
Cloned(Commentary) (protein specific)
Commentary
Organism
gene MPDH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis, recombinant expression of His-tagged EsM1PDH1 in Escherichia coli
Ectocarpus siliculosus
gene MPDH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis, recombinant expression of His-tagged EsM1PDH1 in Escherichia coli; gene MPDH2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis
Ectocarpus siliculosus
gene MPDH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis; gene MPDH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis, recombinant expression of His-tagged EsM1PDH1 in Escherichia coli
Ectocarpus siliculosus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
isozyme EsM1PDH1 highly prefers NADH/NAD+ to NADP+/NADPH
Ectocarpus siliculosus
NAD+
-
Ectocarpus siliculosus
NADH
-
Ectocarpus siliculosus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
no inhibition by EDTA
Ectocarpus siliculosus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Ectocarpus siliculosus
0.02
-
NAD+
recombinant enzyme, pH 9.0, 30°C
Ectocarpus siliculosus
0.19
-
D-fructose 6-phosphate
recombinant enzyme, pH 7.0, 30°C
Ectocarpus siliculosus
0.38
-
D-mannitol 1-phosphate
recombinant enzyme, pH 9.0, 30°C
Ectocarpus siliculosus
16
-
NADH
recombinant enzyme, pH 7.0, 30°C
Ectocarpus siliculosus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
NaCl
activates
Ectocarpus siliculosus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42000
-
-
Ectocarpus siliculosus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-mannitol 1-phosphate + NAD+
Ectocarpus siliculosus
-
D-fructose 6-phosphate + NADH + H+
-
-
r
additional information
Ectocarpus siliculosus
mannitol is present in large amounts in brown algae, where its synthesis involved two steps: a mannitol-1-phosphate dehydrogenase (M1PDH) catalyzes a reversible reaction between fructose-6-phosphate (F6P) and mannitol-1-phosphate (M1P) (EC 1.1.1.17), and a mannitol-1-phosphatase hydrolyzes M1P to mannitol (EC 3.1.3.22)
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged EsM1PDH1 from Escherichia coli by nickel affinity chromatography and gel filtration
Ectocarpus siliculosus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.014
-
recombinant enzyme, D-mannitol 1-phosphate oxidation, pH 9.0, 30°C
Ectocarpus siliculosus
0.016
-
purified recombinant enzyme, D-mannitol 1-phosphate oxidation, pH 9.0, 30°C
Ectocarpus siliculosus
0.026
-
recombinant enzyme, D-fructose 6-phosphate reduction, pH 7.0, 30°C
Ectocarpus siliculosus
0.046
-
purified recombinant enzyme, D-fructose 6-phosphate reduction, pH 7.0, 30°C
Ectocarpus siliculosus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-mannitol 1-phosphate + NAD+
-
741122
Ectocarpus siliculosus
D-fructose 6-phosphate + NADH + H+
-
-
-
r
additional information
mannitol is present in large amounts in brown algae, where its synthesis involved two steps: a mannitol-1-phosphate dehydrogenase (M1PDH) catalyzes a reversible reaction between fructose-6-phosphate (F6P) and mannitol-1-phosphate (M1P) (EC 1.1.1.17), and a mannitol-1-phosphatase hydrolyzes M1P to mannitol (EC 3.1.3.22)
741122
Ectocarpus siliculosus
?
-
-
-
-
additional information
EsM1PDH1cat isozyme is specific for D-fructose 6-phosphate and D-mannitol 1-phosphate
741122
Ectocarpus siliculosus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 42000, recombinant His-tagged EsM1PDH1 isozyme, SDS-PAGE
Ectocarpus siliculosus
More
structure-based sequence comparisons, overview
Ectocarpus siliculosus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Ectocarpus siliculosus
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
5
50
35% of maximum activity at 5-10°C, less than 5% at 50°C
Ectocarpus siliculosus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
D-fructose 6-phosphate reduction
Ectocarpus siliculosus
9
-
D-mannitol 1-phosphate oxidation
Ectocarpus siliculosus
General Information
General Information
Commentary
Organism
evolution
sequence analysis suggests that algal and apicomplexa M1PDHs represent a distinct type of mannitol-1-phosphate dehydrogenase in the PSLDR family; sequence analysis suggests that algal and apicomplexa M1PDHs represent a distinct type of mannitol-1-phosphate dehydrogenase in the PSLDR family; sequence analysis suggests that algal and apicomplexa M1PDHs represent a distinct type of mannitol-1-phosphate dehydrogenase in the PSLDR family
Ectocarpus siliculosus
General Information (protein specific)
General Information
Commentary
Organism
evolution
sequence analysis suggests that algal and apicomplexa M1PDHs represent a distinct type of mannitol-1-phosphate dehydrogenase in the PSLDR family
Ectocarpus siliculosus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
29
-
D-mannitol 1-phosphate
recombinant enzyme, pH 9.0, 30°C; recombinant enzyme, pH 9.0, 30°C; recombinant enzyme, pH 9.0, 30°C
Ectocarpus siliculosus
170
-
D-fructose 6-phosphate
recombinant enzyme, pH 7.0, 30°C; recombinant enzyme, pH 7.0, 30°C; recombinant enzyme, pH 7.0, 30°C
Ectocarpus siliculosus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
29
-
D-mannitol 1-phosphate
recombinant enzyme, pH 9.0, 30°C
Ectocarpus siliculosus
170
-
D-fructose 6-phosphate
recombinant enzyme, pH 7.0, 30°C
Ectocarpus siliculosus
Other publictions for EC 1.1.1.17
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)
741451
Goudarzi
-
Transgenic sugar beet expressi ...
Escherichia coli
Sugar Tech.
18
192-203
2016
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
729646
Sand
Mannitol-1-phosphate dehydroge ...
Acinetobacter baylyi, Acinetobacter baylyi ATCC 33305
Environ. Microbiol.
17
711-719
2015
-
-
1
-
-
-
-
-
-
-
-
4
-
3
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
741122
Bonin
Molecular and biochemical char ...
Ectocarpus siliculosus
Phytochemistry
117
509-520
2015
-
-
1
-
-
-
1
5
-
1
1
4
-
8
-
-
1
-
-
-
4
-
7
2
1
1
-
-
2
-
-
3
-
-
-
-
-
3
9
-
-
-
-
3
-
15
-
3
3
4
-
-
-
3
-
-
12
-
7
6
3
3
-
-
6
-
-
-
-
1
3
-
2
6
741439
Bhauso
Overexpression of bacterial mt ...
Escherichia coli
ScientificWorldJournal
2014
125967
2014
-
-
1
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
722126
Sand
Mannitol, a compatible solute ...
Acinetobacter baylyi
Environ. Microbiol.
15
2187-2197
2013
-
-
1
-
-
-
-
1
-
1
1
2
-
2
-
-
1
-
-
-
1
-
2
1
1
1
-
-
1
1
-
4
-
-
-
-
-
1
4
-
-
-
-
-
-
1
-
1
1
2
-
-
-
1
-
-
1
-
2
1
1
1
-
-
1
1
-
-
1
2
2
1
-
-
722234
Krahulec
Enzymes of mannitol metabolism ...
Aspergillus fumigatus
FEBS J.
278
1264-1276
2011
-
1
1
-
-
-
2
5
-
-
-
1
-
2
-
-
-
1
-
-
-
-
2
-
1
-
1
2
2
-
-
3
1
-
-
-
1
1
3
-
-
-
-
2
1
5
-
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
1
2
2
-
-
-
1
2
2
1
2
2
722935
Rambhatla
Molecular cloning and characte ...
Vibrio cholerae, Vibrio cholerae O395
J. Microbiol. Biotechnol.
21
914-920
2011
-
-
1
-
-
-
-
-
-
1
-
2
-
5
-
-
1
-
-
1
1
-
2
-
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
1
-
2
-
-
-
1
-
1
1
-
2
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
723496
Rousvoal
Mannitol-1-phosphate dehydroge ...
Ectocarpus siliculosus, Ectocarpus siliculosus Ec32 / CCAP 1310/4
Planta
233
261-273
2011
-
-
1
-
-
-
1
-
-
1
3
6
-
10
-
-
-
-
-
-
1
-
12
1
1
-
-
-
2
-
-
2
-
3
-
-
-
3
6
-
-
-
-
3
-
-
-
3
3
6
-
-
-
-
-
-
3
-
12
3
3
-
-
-
6
-
-
3
-
1
3
-
-
-
711681
Wang
Gene cloning and catalysis fea ...
Beauveria bassiana
Carbohydr. Res.
345
50-54
2010
-
-
1
-
-
-
9
-
-
-
-
1
-
3
-
-
1
-
-
-
1
1
1
-
1
1
-
-
1
1
-
2
-
-
-
-
-
1
2
-
-
-
-
9
-
-
-
-
-
1
-
-
-
1
-
-
1
1
1
-
1
1
-
-
1
1
-
-
1
1
1
1
1
1
711878
Aguilar-Osorio
Spatial and developmental diff ...
Aspergillus niger
Eukaryot. Cell
9
1398-1402
2010
-
-
1
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
2
4
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
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Mannitol 1-phosphate metabolis ...
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Enhanced tolerance to salt str ...
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The mtl genes and the mannitol ...
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Cloning, expression, and isola ...
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Isolation and characterization ...
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389416
Honeyman
Isolation, characterization, a ...
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Fischer
Mannitol-specific phosphoenolp ...
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94720
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389418
Chase
Mannitol-1-phosphate dehydroge ...
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Foreman
Zn2+-induced cooperativity of ...
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Purification and kinetic chara ...
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287248
Mehta
Mannitol oxidation in two Micr ...
Amycolatopsis lactamdurans, Micromonospora sp., no activity in Actinoplanes missouriensis, no activity in Mycobacterium smegmatis, no activity in Nocardia erythropolis
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389423
Brown
Polyol metabolism by a caries- ...
Streptococcus mutans
Infect. Immun.
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1977
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389424
Hankinson
Regulation of mannitol-1-phosp ...
Aspergillus nidulans
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21
99-101
1975
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Liss
D-Mannitol 1-phosphate dehydro ...
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389426
Wolff
-
D-Mannitol-1-phosphate dehydro ...
Escherichia coli
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1955
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