BRENDA - Enzyme Database
show all sequences of 5.3.1.8

Molecular characterization of a novel thermostable mannose-6-phosphate isomerase from Thermus thermophilus

Yeom, S.J.; Kim, Y.S.; Lim, Y.R.; Jeong, K.W.; Lee, J.Y.; Kim, Y.; Oh, D.K.; Biochimie 93, 1659-1667 (2011)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expressed in Escherichia coli ER2566 cells
Thermus thermophilus
Engineering
Protein Variants
Commentary
Organism
D138A
the mutant shows 59% activity compared to the wild type enzyme
Thermus thermophilus
E132A
the mutant shows 1.9% activity compared to the wild type enzyme
Thermus thermophilus
E132D
the mutant shows 0.4% activity compared to the wild type enzyme
Thermus thermophilus
E132K
inactive
Thermus thermophilus
E132Q
inactive
Thermus thermophilus
E132W
inactive
Thermus thermophilus
E67A
the mutant shows 2.5% activity compared to the wild type enzyme
Thermus thermophilus
E67D
the mutant shows 3.7% activity compared to the wild type enzyme
Thermus thermophilus
E67K
inactive
Thermus thermophilus
E67Q
the mutant shows 0.8% activity compared to the wild type enzyme
Thermus thermophilus
E67W
inactive
Thermus thermophilus
H122A
the mutant shows 2.8% activity compared to the wild type enzyme
Thermus thermophilus
H122D
inactive
Thermus thermophilus
H122K
inactive
Thermus thermophilus
H122Q
the mutant shows 2.0% activity compared to the wild type enzyme
Thermus thermophilus
H122W
inactive
Thermus thermophilus
H50A
the mutant shows 2.2% activity compared to the wild type enzyme
Thermus thermophilus
H50D
inactive
Thermus thermophilus
H50K
inactive
Thermus thermophilus
H50Q
the mutant shows 2.0% activity compared to the wild type enzyme
Thermus thermophilus
H50W
inactive
Thermus thermophilus
K37A
the mutant shows 21% activity compared to the wild type enzyme
Thermus thermophilus
K65A
the mutant shows 15% activity compared to the wild type enzyme
Thermus thermophilus
L18A
the mutant shows 78% activity compared to the wild type enzyme
Thermus thermophilus
L39A
the mutant shows 84% activity compared to the wild type enzyme
Thermus thermophilus
Q48A
the mutant shows 2.0% activity compared to the wild type enzyme
Thermus thermophilus
Q48D
inactive
Thermus thermophilus
Q48K
inactive
Thermus thermophilus
Q48N
inactive
Thermus thermophilus
Q48W
inactive
Thermus thermophilus
R11A
the mutant shows 260% activity compared to the wild type enzyme
Thermus thermophilus
R142A
the mutant shows 2.6% activity compared to the wild type enzyme
Thermus thermophilus
R142D
inactive
Thermus thermophilus
R142K
inactive
Thermus thermophilus
R142N
inactive
Thermus thermophilus
R142W
inactive
Thermus thermophilus
W13A
the mutant shows 0.4% activity compared to the wild type enzyme
Thermus thermophilus
W13D
inactive
Thermus thermophilus
W13F
the mutant shows 41% activity compared to the wild type enzyme
Thermus thermophilus
W13H
the mutant shows 52% activity compared to the wild type enzyme
Thermus thermophilus
W13K
inactive
Thermus thermophilus
W13Q
inactive
Thermus thermophilus
W13Y
the mutant shows 68% activity compared to the wild type enzyme
Thermus thermophilus
W69A
the mutant shows 50% activity compared to the wild type enzyme
Thermus thermophilus
Y124A
the mutant shows 52% activity compared to the wild type enzyme
Thermus thermophilus
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ba2+
about 30% inhibition at 0.5 mM
Thermus thermophilus
EDTA
complete inhibition at 0.5 mM
Thermus thermophilus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.18
-
D-mannose 6-phosphate
mutant enzyme E132A, pH 7.0, 80°C; mutant enzyme E67A, pH 7.0, 80°C
Thermus thermophilus
0.21
-
D-mannose 6-phosphate
wild type enzyme, pH 7.0, 80°C
Thermus thermophilus
0.22
-
D-fructose 6-phosphate
wild type enzyme, pH 7.0, 80°C
Thermus thermophilus
0.27
-
D-mannose 6-phosphate
mutant enzyme H122A, pH 7.0, 80°C
Thermus thermophilus
0.33
-
D-mannose 6-phosphate
mutant enzyme H50A, pH 7.0, 80°C
Thermus thermophilus
0.53
-
D-mannose 6-phosphate
mutant enzyme Q48A, pH 7.0, 80°C
Thermus thermophilus
0.85
-
D-mannose 6-phosphate
mutant enzyme W13A, pH 7.0, 80°C
Thermus thermophilus
1.29
-
D-mannose 6-phosphate
mutant enzyme R142A, pH 7.0, 80°C
Thermus thermophilus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
the enzyme is not stimulated by Ca2+
Thermus thermophilus
Co2+
about 230% activity at 0.5 mM
Thermus thermophilus
Cu2+
about 135% activity at 0.5 mM
Thermus thermophilus
Fe2+
about 125% activity at 0.5 mM
Thermus thermophilus
Mg2+
about 175% activity at 0.5 mM
Thermus thermophilus
Mn2+
about 175% activity at 0.5 mM
Thermus thermophilus
Zn2+
Zn2+ is present at one molecule per monomer, the enzyme has about 240% activity in the presence of 0.5 mM Zn2+
Thermus thermophilus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
29000
-
1 * 29000, SDS-PAGE
Thermus thermophilus
29054
-
1 * 29054, calculated from amino acid sequence
Thermus thermophilus
29100
-
gel filtration
Thermus thermophilus
Organism
Organism
UniProt
Commentary
Textmining
Thermus thermophilus
Q5SIM4
-
-
Thermus thermophilus KCCM 40879
Q5SIM4
-
-
Purification (Commentary)
Purification (Commentary)
Organism
HisTrap HP column chromatography
Thermus thermophilus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.01
-
wild type enzyme, using ribose 5-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
0.3
-
mutant enzyme E132D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme W13A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
0.6
-
mutant enzyme E67Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
0.74
-
wild type enzyme, using ribulose 5-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
1.4
-
mutant enzyme E132A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
1.5
-
mutant enzyme H122Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme H50Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme Q48A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
1.7
-
mutant enzyme H50A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
1.9
-
mutant enzyme E67A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme R142A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
2.1
-
mutant enzyme H122A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
2.8
-
mutant enzyme E67D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
3
8
mutant enzyme W69A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
4.5
-
wild type enzyme, using D-fructose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
11
-
mutant enzyme K65A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
16
-
mutant enzyme K37A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
31
-
mutant enzyme W13F, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
39
-
mutant enzyme W13H, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme Y124A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
40
-
mutant enzyme L39A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
44
-
mutant enzyme D138A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
51
-
mutant enzyme W13Y, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
58
-
mutant enzyme L18A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
75
-
wild type enzyme, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
194
-
mutant enzyme R11A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
D-fructose 6-phosphate
-
714372
Thermus thermophilus
D-mannose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
-
714372
Thermus thermophilus KCCM 40879
D-mannose 6-phosphate
-
-
-
r
D-Mannose 6-phosphate
best substrate
714372
Thermus thermophilus
D-Fructose 6-phosphate
-
-
-
r
D-Mannose 6-phosphate
best substrate
714372
Thermus thermophilus KCCM 40879
D-Fructose 6-phosphate
-
-
-
r
D-ribose 5-phosphate
very low activity
714372
Thermus thermophilus
D-ribulose 5-phosphate
-
-
-
r
D-ribose 5-phosphate
very low activity
714372
Thermus thermophilus KCCM 40879
D-ribulose 5-phosphate
-
-
-
r
additional information
no activity with D-glucose 6-phosphate and arabinose 5-phosphate
714372
Thermus thermophilus
?
-
-
-
-
additional information
no activity with D-glucose 6-phosphate and arabinose 5-phosphate
714372
Thermus thermophilus KCCM 40879
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
1 * 29000, SDS-PAGE; 1 * 29054, calculated from amino acid sequence
Thermus thermophilus
Synonyms
Synonyms
Commentary
Organism
mannose-6-phosphate isomerase
-
Thermus thermophilus
MPI
-
Thermus thermophilus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
80
-
-
Thermus thermophilus
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
70
90
-
Thermus thermophilus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
64
85
the half-lives of the enzyme at 65, 70, 75, 80, and 85°C are 13, 6.5, 3.7, 1.8, and 0.2 h, respectively
Thermus thermophilus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
11
-
D-mannose 6-phosphate
mutant enzyme W13A, pH 7.0, 80°C
Thermus thermophilus
19
-
D-mannose 6-phosphate
mutant enzyme E132A, pH 7.0, 80°C
Thermus thermophilus
31
-
D-mannose 6-phosphate
mutant enzyme E67A, pH 7.0, 80°C
Thermus thermophilus
37
-
D-mannose 6-phosphate
mutant enzyme Q48A, pH 7.0, 80°C
Thermus thermophilus
54
-
D-mannose 6-phosphate
mutant enzyme H50A, pH 7.0, 80°C
Thermus thermophilus
70
-
D-mannose 6-phosphate
mutant enzyme R142A, pH 7.0, 80°C
Thermus thermophilus
75
-
D-mannose 6-phosphate
mutant enzyme H122A, pH 7.0, 80°C
Thermus thermophilus
141
-
D-fructose 6-phosphate
wild type enzyme, pH 7.0, 80°C
Thermus thermophilus
1371
-
D-mannose 6-phosphate
wild type enzyme, pH 7.0, 80°C
Thermus thermophilus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Thermus thermophilus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6.5
8.5
-
Thermus thermophilus
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli ER2566 cells
Thermus thermophilus
Engineering (protein specific)
Protein Variants
Commentary
Organism
D138A
the mutant shows 59% activity compared to the wild type enzyme
Thermus thermophilus
E132A
the mutant shows 1.9% activity compared to the wild type enzyme
Thermus thermophilus
E132D
the mutant shows 0.4% activity compared to the wild type enzyme
Thermus thermophilus
E132K
inactive
Thermus thermophilus
E132Q
inactive
Thermus thermophilus
E132W
inactive
Thermus thermophilus
E67A
the mutant shows 2.5% activity compared to the wild type enzyme
Thermus thermophilus
E67D
the mutant shows 3.7% activity compared to the wild type enzyme
Thermus thermophilus
E67K
inactive
Thermus thermophilus
E67Q
the mutant shows 0.8% activity compared to the wild type enzyme
Thermus thermophilus
E67W
inactive
Thermus thermophilus
H122A
the mutant shows 2.8% activity compared to the wild type enzyme
Thermus thermophilus
H122D
inactive
Thermus thermophilus
H122K
inactive
Thermus thermophilus
H122Q
the mutant shows 2.0% activity compared to the wild type enzyme
Thermus thermophilus
H122W
inactive
Thermus thermophilus
H50A
the mutant shows 2.2% activity compared to the wild type enzyme
Thermus thermophilus
H50D
inactive
Thermus thermophilus
H50K
inactive
Thermus thermophilus
H50Q
the mutant shows 2.0% activity compared to the wild type enzyme
Thermus thermophilus
H50W
inactive
Thermus thermophilus
K37A
the mutant shows 21% activity compared to the wild type enzyme
Thermus thermophilus
K65A
the mutant shows 15% activity compared to the wild type enzyme
Thermus thermophilus
L18A
the mutant shows 78% activity compared to the wild type enzyme
Thermus thermophilus
L39A
the mutant shows 84% activity compared to the wild type enzyme
Thermus thermophilus
Q48A
the mutant shows 2.0% activity compared to the wild type enzyme
Thermus thermophilus
Q48D
inactive
Thermus thermophilus
Q48K
inactive
Thermus thermophilus
Q48N
inactive
Thermus thermophilus
Q48W
inactive
Thermus thermophilus
R11A
the mutant shows 260% activity compared to the wild type enzyme
Thermus thermophilus
R142A
the mutant shows 2.6% activity compared to the wild type enzyme
Thermus thermophilus
R142D
inactive
Thermus thermophilus
R142K
inactive
Thermus thermophilus
R142N
inactive
Thermus thermophilus
R142W
inactive
Thermus thermophilus
W13A
the mutant shows 0.4% activity compared to the wild type enzyme
Thermus thermophilus
W13D
inactive
Thermus thermophilus
W13F
the mutant shows 41% activity compared to the wild type enzyme
Thermus thermophilus
W13H
the mutant shows 52% activity compared to the wild type enzyme
Thermus thermophilus
W13K
inactive
Thermus thermophilus
W13Q
inactive
Thermus thermophilus
W13Y
the mutant shows 68% activity compared to the wild type enzyme
Thermus thermophilus
W69A
the mutant shows 50% activity compared to the wild type enzyme
Thermus thermophilus
Y124A
the mutant shows 52% activity compared to the wild type enzyme
Thermus thermophilus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ba2+
about 30% inhibition at 0.5 mM
Thermus thermophilus
EDTA
complete inhibition at 0.5 mM
Thermus thermophilus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.18
-
D-mannose 6-phosphate
mutant enzyme E132A, pH 7.0, 80°C; mutant enzyme E67A, pH 7.0, 80°C
Thermus thermophilus
0.21
-
D-mannose 6-phosphate
wild type enzyme, pH 7.0, 80°C
Thermus thermophilus
0.22
-
D-fructose 6-phosphate
wild type enzyme, pH 7.0, 80°C
Thermus thermophilus
0.27
-
D-mannose 6-phosphate
mutant enzyme H122A, pH 7.0, 80°C
Thermus thermophilus
0.33
-
D-mannose 6-phosphate
mutant enzyme H50A, pH 7.0, 80°C
Thermus thermophilus
0.53
-
D-mannose 6-phosphate
mutant enzyme Q48A, pH 7.0, 80°C
Thermus thermophilus
0.85
-
D-mannose 6-phosphate
mutant enzyme W13A, pH 7.0, 80°C
Thermus thermophilus
1.29
-
D-mannose 6-phosphate
mutant enzyme R142A, pH 7.0, 80°C
Thermus thermophilus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
the enzyme is not stimulated by Ca2+
Thermus thermophilus
Co2+
about 230% activity at 0.5 mM
Thermus thermophilus
Cu2+
about 135% activity at 0.5 mM
Thermus thermophilus
Fe2+
about 125% activity at 0.5 mM
Thermus thermophilus
Mg2+
about 175% activity at 0.5 mM
Thermus thermophilus
Mn2+
about 175% activity at 0.5 mM
Thermus thermophilus
Zn2+
Zn2+ is present at one molecule per monomer, the enzyme has about 240% activity in the presence of 0.5 mM Zn2+
Thermus thermophilus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
29000
-
1 * 29000, SDS-PAGE
Thermus thermophilus
29054
-
1 * 29054, calculated from amino acid sequence
Thermus thermophilus
29100
-
gel filtration
Thermus thermophilus
Purification (Commentary) (protein specific)
Commentary
Organism
HisTrap HP column chromatography
Thermus thermophilus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.01
-
wild type enzyme, using ribose 5-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
0.3
-
mutant enzyme E132D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme W13A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
0.6
-
mutant enzyme E67Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
0.74
-
wild type enzyme, using ribulose 5-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
1.4
-
mutant enzyme E132A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
1.5
-
mutant enzyme H122Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme H50Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme Q48A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
1.7
-
mutant enzyme H50A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
1.9
-
mutant enzyme E67A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme R142A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
2.1
-
mutant enzyme H122A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
2.8
-
mutant enzyme E67D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
3
8
mutant enzyme W69A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
4.5
-
wild type enzyme, using D-fructose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
11
-
mutant enzyme K65A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
16
-
mutant enzyme K37A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
31
-
mutant enzyme W13F, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
39
-
mutant enzyme W13H, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme Y124A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
40
-
mutant enzyme L39A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
44
-
mutant enzyme D138A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
51
-
mutant enzyme W13Y, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
58
-
mutant enzyme L18A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
75
-
wild type enzyme, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
194
-
mutant enzyme R11A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
Thermus thermophilus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
D-fructose 6-phosphate
-
714372
Thermus thermophilus
D-mannose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
-
714372
Thermus thermophilus KCCM 40879
D-mannose 6-phosphate
-
-
-
r
D-Mannose 6-phosphate
best substrate
714372
Thermus thermophilus
D-Fructose 6-phosphate
-
-
-
r
D-Mannose 6-phosphate
best substrate
714372
Thermus thermophilus KCCM 40879
D-Fructose 6-phosphate
-
-
-
r
D-ribose 5-phosphate
very low activity
714372
Thermus thermophilus
D-ribulose 5-phosphate
-
-
-
r
D-ribose 5-phosphate
very low activity
714372
Thermus thermophilus KCCM 40879
D-ribulose 5-phosphate
-
-
-
r
additional information
no activity with D-glucose 6-phosphate and arabinose 5-phosphate
714372
Thermus thermophilus
?
-
-
-
-
additional information
no activity with D-glucose 6-phosphate and arabinose 5-phosphate
714372
Thermus thermophilus KCCM 40879
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 29000, SDS-PAGE; 1 * 29054, calculated from amino acid sequence
Thermus thermophilus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
80
-
-
Thermus thermophilus
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
70
90
-
Thermus thermophilus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
64
85
the half-lives of the enzyme at 65, 70, 75, 80, and 85°C are 13, 6.5, 3.7, 1.8, and 0.2 h, respectively
Thermus thermophilus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
11
-
D-mannose 6-phosphate
mutant enzyme W13A, pH 7.0, 80°C
Thermus thermophilus
19
-
D-mannose 6-phosphate
mutant enzyme E132A, pH 7.0, 80°C
Thermus thermophilus
31
-
D-mannose 6-phosphate
mutant enzyme E67A, pH 7.0, 80°C
Thermus thermophilus
37
-
D-mannose 6-phosphate
mutant enzyme Q48A, pH 7.0, 80°C
Thermus thermophilus
54
-
D-mannose 6-phosphate
mutant enzyme H50A, pH 7.0, 80°C
Thermus thermophilus
70
-
D-mannose 6-phosphate
mutant enzyme R142A, pH 7.0, 80°C
Thermus thermophilus
75
-
D-mannose 6-phosphate
mutant enzyme H122A, pH 7.0, 80°C
Thermus thermophilus
141
-
D-fructose 6-phosphate
wild type enzyme, pH 7.0, 80°C
Thermus thermophilus
1371
-
D-mannose 6-phosphate
wild type enzyme, pH 7.0, 80°C
Thermus thermophilus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Thermus thermophilus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6.5
8.5
-
Thermus thermophilus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
13
-
D-mannose 6-phosphate
mutant enzyme W13A, pH 7.0, 80°C
Thermus thermophilus
54
-
D-mannose 6-phosphate
mutant enzyme R142A, pH 7.0, 80°C
Thermus thermophilus
69
-
D-mannose 6-phosphate
mutant enzyme Q48A, pH 7.0, 80°C
Thermus thermophilus
109
-
D-mannose 6-phosphate
mutant enzyme E132A, pH 7.0, 80°C
Thermus thermophilus
166
-
D-mannose 6-phosphate
mutant enzyme H50A, pH 7.0, 80°C
Thermus thermophilus
174
-
D-mannose 6-phosphate
mutant enzyme E67A, pH 7.0, 80°C
Thermus thermophilus
278
-
D-mannose 6-phosphate
mutant enzyme H122A, pH 7.0, 80°C
Thermus thermophilus
641
-
D-fructose 6-phosphate
wild type enzyme, pH 7.0, 80°C
Thermus thermophilus
6685
-
D-mannose 6-phosphate
wild type enzyme, pH 7.0, 80°C
Thermus thermophilus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
13
-
D-mannose 6-phosphate
mutant enzyme W13A, pH 7.0, 80°C
Thermus thermophilus
54
-
D-mannose 6-phosphate
mutant enzyme R142A, pH 7.0, 80°C
Thermus thermophilus
69
-
D-mannose 6-phosphate
mutant enzyme Q48A, pH 7.0, 80°C
Thermus thermophilus
109
-
D-mannose 6-phosphate
mutant enzyme E132A, pH 7.0, 80°C
Thermus thermophilus
166
-
D-mannose 6-phosphate
mutant enzyme H50A, pH 7.0, 80°C
Thermus thermophilus
174
-
D-mannose 6-phosphate
mutant enzyme E67A, pH 7.0, 80°C
Thermus thermophilus
278
-
D-mannose 6-phosphate
mutant enzyme H122A, pH 7.0, 80°C
Thermus thermophilus
641
-
D-fructose 6-phosphate
wild type enzyme, pH 7.0, 80°C
Thermus thermophilus
6685
-
D-mannose 6-phosphate
wild type enzyme, pH 7.0, 80°C
Thermus thermophilus
Other publictions for EC 5.3.1.8
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
Synonyms
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)
747781
Ahmad
Crystal structure of phosphom ...
Candida albicans, Candida albicans ATCC MYA-2876
FEBS Lett.
592
1667-1680
2018
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1
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748577
Islam
Experimental validation of in ...
Dehalococcoides mccartyi
Microb. Biotechnol.
9
47-60
2016
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1
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1
1
749318
Hu
Plant phosphomannose isomeras ...
Chlorella variabilis, Oryza sativa Japonica Group
Sci. Rep.
6
25921
2016
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2
2
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3
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10
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733811
Akutsu
Identification and characteriz ...
Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428
Extremophiles
19
1077-1085
2015
-
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1
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1
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4
1
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5
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2
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2
1
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748119
Chen
-
Improved genetic transformati ...
Jatropha curcas
J. Biobased Mat. Bioenergy
9
9-15
2015
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1
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748644
Zhang
Phosphomannose isomerase affe ...
Escherichia coli
Mol. Breed.
35
100
2015
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1
1
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748963
Qiu
-
A novel plant code optimizati ...
Escherichia coli
Plant OMICS
8
30-36
2015
-
1
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1
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-
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-
-
-
-
749059
Sigdel
Characterization of a mannose ...
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens DSM 7
PLoS ONE
10
e0131585
2015
-
-
1
-
-
-
1
1
-
1
1
-
-
6
-
-
-
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-
1
-
8
1
1
1
-
3
1
1
2
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1
-
-
-
-
-
1
-
1
-
1
1
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1
-
8
1
1
-
3
1
1
2
-
-
-
-
-
-
1
1
728283
Wang
BcPMI2, isolated from non-head ...
Brassica rapa subsp. chinensis
Mol. Biol. Rep.
41
2207-2216
2014
-
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1
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-
-
-
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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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1
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1
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1
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-
1
1
-
-
-
746775
Kim
L-ribose production from L-ar ...
Geobacillus thermodenitrificans
Appl. Biochem. Biotechnol.
172
275-288
2014
-
1
1
-
1
-
-
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-
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3
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1
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1
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726723
Lim
Production of L-ribose from L- ...
Geobacillus thermodenitrificans
Appl. Environ. Microbiol.
78
3880-3884
2012
-
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1
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5
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1
4
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3
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1
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3
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1
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4
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1
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5
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1
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1
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1
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4
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4
4
727158
Desvergnes
Synthesis and evaluation of ma ...
Escherichia coli
Bioorg. Med. Chem.
20
1511-1520
2012
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3
1
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1
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4
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1
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2
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3
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3
3
1
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1
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1
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728469
Duan
An efficient and high-throughp ...
Escherichia coli
Plant Cell Rep.
31
1611-1624
2012
-
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1
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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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1
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1
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-
713854
Yeom
Characterization of a mannose- ...
Thermus thermophilus, Thermus thermophilus KCCM 40879
Appl. Environ. Microbiol.
77
762-767
2011
-
-
1
-
20
-
2
7
-
5
2
-
-
5
-
-
-
-
-
-
36
-
16
1
1
1
-
1
7
1
-
-
-
-
-
-
-
-
1
-
-
20
-
-
2
-
7
-
5
2
-
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-
-
-
-
-
36
-
16
1
1
-
1
7
1
-
-
-
-
-
-
-
7
7
713855
Amos
Influence of the Photorhabdus ...
Photorhabdus luminescens, Photorhabdus luminescens TT01
Appl. Environ. Microbiol.
77
776-785
2011
-
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4
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2
2
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714372
Yeom
Molecular characterization of ...
Thermus thermophilus, Thermus thermophilus KCCM 40879
Biochimie
93
1659-1667
2011
-
-
1
-
45
-
2
8
-
7
3
-
-
4
-
-
1
-
-
-
22
-
8
1
2
1
1
1
9
1
1
-
-
-
-
-
-
-
1
-
-
45
-
-
2
-
8
-
7
3
-
-
-
-
1
-
-
22
-
8
1
1
1
1
9
1
1
-
-
-
-
-
-
9
9
716507
Thiruvengadam
-
Phosphomannose-isomerase as a ...
Onchidium sp., Oncidium hybrid cultivar
Plant Cell Tissue Organ Cult.
104
239-246
2011
-
2
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4
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716883
Roux
The reaction mechanism of type ...
Escherichia coli, Homo sapiens
Proteins
79
203-220
2011
-
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1
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-
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4
2
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2
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7
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1
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2
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4
-
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2
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4
-
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1
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4
4
2
-
2
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1
-
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-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
2
2
701879
Li
Biosynthetic pathway of sugar ...
Alcaligenes sp., Alcaligenes sp. CGMCC2428
Appl. Microbiol. Biotechnol.
86
295-303
2010
-
-
-
-
-
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2
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3
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3
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2
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2
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3
-
2
-
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-
-
-
-
-
-
-
-
1
1
-
-
-
693999
Nic Lochlainn
Phosphomannose isomerase and p ...
Streptomyces nodosus
Metab. Eng.
11
40-47
2009
-
1
1
-
1
-
-
-
-
-
-
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3
-
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1
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-
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-
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-
-
-
-
694521
Mizanur
Phosphomannose isomerase/GDP-m ...
Pyrococcus furiosus
Org. Biomol. Chem.
7
2135-2139
2009
-
-
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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1
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1
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1
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700488
Siddique
Myo-inositol oxygenase genes a ...
Arabidopsis thaliana
New Phytol.
184
457-472
2009
-
-
1
-
-
-
-
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-
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1
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2
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701472
Sagurthi
Structures of mannose-6-phosph ...
Salmonella enterica subsp. enterica serovar Typhimurium
Acta Crystallogr. Sect. D
65
724-732
2009
-
-
1
1
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2
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7
-
1
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2
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1
1
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1
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1
1
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1
1
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1
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1
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2
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7
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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
1
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-
-
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701797
Yeom
Substrate specificity of a man ...
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1
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1
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6
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13
1
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1
1
7
6
1
1
-
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-
-
-
-
1
1
-
-
-
-
-
1
-
6
-
9
3
1
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-
-
1
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-
6
-
13
1
1
1
7
6
1
1
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701812
Yeom
L-ribose production from L-ara ...
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1
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1
1
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1
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1
1
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1
-
1
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1
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1
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1
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702663
Foret
Synthesis and evaluation of no ...
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4
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2
2
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2
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2
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10
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10
24
2
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-
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2
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-
-
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4
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2
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2
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702817
Yeom
Characterization of a mannose- ...
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1
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4
1
1
1
1
4
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1
1
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-
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-
-
1
-
-
-
-
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1
-
1
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9
2
1
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1
-
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1
-
4
1
1
1
4
-
1
1
-
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702869
Tran
Cloning and characterization o ...
Sphingobium chungbukense, Sphingobium chungbukense DJ77
BMB Rep.
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2009
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1
2
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2
3
1
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1
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1
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-
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2
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6
1
2
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1
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-
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4
2
1
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1
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1
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705394
Pichaud
-
Metabolic capacities and immun ...
Placopecten magellanicus
J. Shellfish Res.
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865-876
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1
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1
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4
1
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1
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705568
Fang
Characterization of the Asperg ...
Aspergillus fumigatus, Aspergillus fumigatus YJ-407
Microbiology
155
3281-3293
2009
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1
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8
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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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2
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1
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1
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2
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706204
Wallbraun
-
Phosphomannose-isomerase (pmi) ...
Brassica napus
Plant Cell Tissue Organ Cult.
99
345-351
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1
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1
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690273
Gowda
Cloning, expression, purificat ...
Salmonella enterica subsp. enterica serovar Typhimurium
Acta Crystallogr. Sect. F
64
81-84
2008
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1
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6
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690577
Sousa
Functional analysis of the Bur ...
Burkholderia cenocepacia
Appl. Microbiol. Biotechnol.
80
1015-1022
2008
5
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1
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1
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1
1
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692361
Lee
Identification of amino acid r ...
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3479-3483
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1
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8
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1
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1
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8
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1
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9
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8
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1
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Maruta
Arabidopsis phosphomannose iso ...
Arabidopsis thaliana
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283
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1
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2
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1
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693863
Kato
Mannose accommodation of Vigna ...
Vigna angularis
J. Plant Res.
121
339-349
2008
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Sousa
The Burkholderia cepacia bceA ...
Burkholderia cepacia
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353
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2
1
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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1
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3
2
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2
1
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1
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1
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682359
Min
Successful genetic transformat ...
Escherichia coli
Plant Cell Rep.
26
337-344
2007
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1
1
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3
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-
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1
1
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-
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682360
Lamblin
The use of the phosphomannose ...
Escherichia coli
Plant Cell Rep.
26
765-772
2007
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1
1
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-
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-
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6
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-
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1
1
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-
-
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-
-
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746961
Sousa
The Burkholderia cepacia bceA ...
Burkholderia cepacia
Biochem. Biophys. Res. Commun.
353
200-206
2007
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1
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1
1
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2
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5
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1
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-
-
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1
-
3
-
-
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1
1
-
-
-
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1
-
-
-
1
-
-
-
-
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1
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1
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5
2
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-
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1
-
-
-
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1
-
-
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1
1
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1
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2
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Derossi
Ablation of mouse phosphomanno ...
Mus musculus
J. Biol. Chem.
281
5916-5927
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1
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1
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1
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681498
Xiao
Computational study of human p ...
Homo sapiens
J. Mol. Graph. Model.
25
289-295
2006
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1
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-
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1
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-
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681607
Ku
-
A non-antibiotic selection sys ...
Escherichia coli
J. Plant Biol.
49
115-122
2006
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1
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1
1
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682353
Degenhardt
The use of the phosphomannose- ...
Escherichia coli
Plant Cell Rep.
25
1149-1156
2006
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1
1
-
-
-
-
-
-
-
-
-
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5
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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682354
Aswath
-
Agrobacterium and biolistic tr ...
Escherichia coli
Plant Cell Rep.
25
747
2006
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1
1
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-
-
-
-
-
-
-
-
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1
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
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660706
Gao
Mechanism and kinetics of meta ...
Escherichia coli
Anal. Chem.
77
5596-5603
2005
-
-
-
-
-
-
2
-
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1
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-
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1
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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661902
Gao
-
Kinetic measurements of phosph ...
Escherichia coli
Int. J. Mass Spectrom.
240
291-299
2005
-
-
-
-
-
-
-
2
-
-
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-
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1
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
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663078
Zhu
Effective selection of transge ...
Escherichia coli
Plant Cell Rep.
24
426-432
2005
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
663079
Aswath
Agrobacterium and biolistic tr ...
Escherichia coli
Plant Cell Rep.
25
92-99
2005
-
1
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
660585
Swan
Crystallization and preliminar ...
Pyrobaculum aerophilum
Acta Crystallogr. Sect. D
60
1481-1483
2004
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
661100
Swan
Structural basis for phosphoma ...
Pyrobaculum aerophilum
Biochemistry
43
14088-14095
2004
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
661119
Roux
Inhibition of type I and type ...
Pseudomonas aeruginosa, Saccharomyces cerevisiae
Biochemistry
43
2926-2934
2004
-
-
-
-
-
-
4
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
4
2
2
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
661679
Hansen
Bifunctional phosphoglucose/ph ...
Pyrobaculum aerophilum
Extremophiles
8
507-512
2004
-
-
1
-
-
-
2
3
-
-
3
-
-
1
-
-
-
-
-
-
-
-
2
1
-
1
-
1
-
1
1
-
-
2
-
-
-
-
1
-
-
-
-
-
2
2
3
-
-
3
-
-
-
-
-
-
-
-
-
2
1
1
-
1
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A novel phosphoglucose isomera ...
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The role of phosphomannose iso ...
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Phosphomannose isomerase of Xa ...
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Inhibition of phosphomannose i ...
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The X-ray crystal structure of ...
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Wells
Mechanism of irreversible inac ...
Candida albicans, Escherichia coli
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Selenomethionine labelling pho ...
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Wells
Inhibition of phosphomannose i ...
Candida albicans, Homo sapiens, Saccharomyces cerevisiae, Sus scrofa
Biochemistry
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1994
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2820
Tolley
Crystallization and preliminar ...
Candida albicans
J. Mol. Biol.
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1994
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2
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2823
May
Identification of amino acid r ...
Pseudomonas aeruginosa
J. Biol. Chem.
269
4872-4877
1994
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1
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2826
Proudfoot
Purification, cDNA cloning and ...
Homo sapiens
Eur. J. Biochem.
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1994
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2828
Proudfoot
Purification and characterizat ...
Candida albicans, Homo sapiens, Saccharomyces cerevisiae, Sus scrofa
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2816
Wells
Phosphomannose isomerase from ...
Saccharomyces cerevisiae
Biochemistry
32
1294-1301
1993
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2819
Payton
A novel Saccharomyces cerevisi ...
Saccharomyces cerevisiae
J. Bacteriol.
173
2006-2010
1991
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2824
Shinabarger
Purification and characterizat ...
Pseudomonas aeruginosa
J. Biol. Chem.
266
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1991
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2829
Froman
Isolation and characterization ...
Escherichia coli
Mol. Gen. Genet.
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1989
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3354
Sa-Correia
Alginate biosynthetic enzymes ...
Escherichia coli, Pseudomonas aeruginosa
J. Bacteriol.
169
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1987
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2
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3
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2814
Gill
Overproduction and assay of Ps ...
Pseudomonas aeruginosa
J. Bacteriol.
167
611-615
1986
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1
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1
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1
1
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-
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-
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2813
Lee
-
Phosphomannoisomerase and phos ...
Cassia coluteoides, Cyamopsis tetragonoloba, Glycine max, Trigonella foenum-graecum
Phytochemistry
23
983-987
1984
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5
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5
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2
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6
1
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5
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5
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1
1
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2812
Anjaneyulu
The stimulus-secretion couplin ...
Rattus norvegicus
Arch. Biochem. Biophys.
212
54-62
1981
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2811
Schray
Phosphomannose isomerase. Isom ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
189
106-108
1978
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2809
Murata
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Studies on the phosphomannose ...
Amorphophallus konjac
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963-970
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2810
Murata
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Studies on the phosphomannose ...
Amorphophallus konjac
Plant Cell Physiol.
16
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1
1
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2807
Rose
Mannose 6-phosphate: anomeric ...
Saccharomyces cerevisiae
J. Biol. Chem.
248
2232-2234
1973
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2624
Noltmann
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Aldose-ketose isomerases ...
Apis mellifera, Ascaris suum, Bos taurus, Cavia porcellus, Homo sapiens, Klebsiella aerogenes, Mammalia, Microorganisms, Nakazawaea holstii, Oryctolagus cuniculus, Ovis aries, Pseudomonas aeruginosa, Rattus norvegicus, Saccharomyces cerevisiae, Sus scrofa
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1972
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12
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21
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1
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12
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1
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6
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12
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21
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1
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2806
Gracy
Studies on phosphomannose isom ...
Saccharomyces cerevisiae
J. Biol. Chem.
243
4109-4116
1968
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6
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4
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1
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1
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6
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4
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1
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