BRENDA - Enzyme Database show
show all sequences of 2.4.1.15

Enzymatic and regulatory properties of the trehalose-6-phosphate synthase from the thermoacidophilic archaeon Thermoplasma acidophilum

Gao, Y.; Jiang, Y.; Liu, Q.; Wang, R.; Liu, X.; Liu, B.; Biochimie 101, 215-220 (2014)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
chondroitin sulfate
maximal activation at 0.0005 mg; maximal stimulation at 400 ng
Thermoplasma acidophilum
heparin
0.006 mg, stimulates; heparin can stimulate the activity of the enzyme, although the activity decreases while the concentration of heparin is above 600 ng
Thermoplasma acidophilum
additional information
the enzymatic activity can be stimulated by divalent metal ions and polyanions heparin and chondroitin sulfate
Thermoplasma acidophilum
Cloned(Commentary)
Commentary
Organism
; gene TA1210, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression in Escherichia coli strains DH5alpha and BL21-CodonPlus (DE3)-RIL
Thermoplasma acidophilum
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
10% (v/v), 9% inhibition; 91% inhibition
Thermoplasma acidophilum
Ba2+
10 mM, 38% inhibition; 38% inhibition at 10 mM
Thermoplasma acidophilum
dithiothreitol
10 mM, 27% inhibition
Thermoplasma acidophilum
DTT
73% inhibition
Thermoplasma acidophilum
EDTA
10 mM, 15% inhibition; 85% inhibition
Thermoplasma acidophilum
ethanol
10% (v/v), 28% inhibition; 72% inhibition
Thermoplasma acidophilum
guanidine hydrochloride
10 mM, 63% inhibition; 37% inhibition
Thermoplasma acidophilum
Isopropanol
10% (v/v), 14% inhibition; 86% inhibition
Thermoplasma acidophilum
K+
10% inhibition at 10 mM; 10 mM, 10% inhibition
Thermoplasma acidophilum
methanol
10% (v/v), 30% inhibition; 70% inhibition
Thermoplasma acidophilum
n-butanol
10% (v/v), 48% inhibition; 52% inhibition
Thermoplasma acidophilum
Na+
10 mM, 8% inhibition; 8% inhibition at 10 mM
Thermoplasma acidophilum
Ni2+
10 mM, 21% inhibition; 21% inhibition at 10 mM
Thermoplasma acidophilum
SDS
10% (w/v), 27% inhibition; 73% inhibition
Thermoplasma acidophilum
Urea
10 mM, 15% inhibition; 85% inhibition
Thermoplasma acidophilum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.2
1
UDP-alpha-D-glucose
pH 6.0, 60°C, wild-type enzyme
Thermoplasma acidophilum
0.27
-
D-glucose 6-phosphate
pH 6.0, 60°C, wild-type enzyme
Thermoplasma acidophilum
0.34
-
D-glucose 6-phosphate
pH 6.0, 60°C, N-loop truncation mutant enzyme
Thermoplasma acidophilum
0.74
-
UDP-alpha-D-glucose
pH 6.0, 60°C, N-loop truncation mutant enzyme
Thermoplasma acidophilum
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
1.91fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 1.91fold activation by 10 mM Co2+
Thermoplasma acidophilum
Mg2+
2.33fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 2.33fold activation ba 10 mM Mg2+
Thermoplasma acidophilum
Mn2+
1.16fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 1.16fold activation by 10 mM Mn2+
Thermoplasma acidophilum
additional information
no effect by Li+ at 10 mM; the addition of monovalent metal ions Na+, K+ and Li+ has no effect on the enzyme activity
Thermoplasma acidophilum
Zn2+
2.26fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 2.26fold activation by 10 mM Zn2+
Thermoplasma acidophilum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
51400
-
2 * 51400, about, sequence calculation
Thermoplasma acidophilum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
UDP-glucose + D-glucose 6-phosphate
Thermoplasma acidophilum
-
UDP + alpha,alpha-trehalose 6-phosphate
-
-
?
Organic Solvent Stability
Organic Solvent
Commentary
Organism
Ethanol
72% inhibition
Thermoplasma acidophilum
isopropanol
86% inhibition
Thermoplasma acidophilum
Methanol
70% inhibition
Thermoplasma acidophilum
n-Butanol
52% inhibition
Thermoplasma acidophilum
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermoplasma acidophilum
Q9HIW6
; gene TA1210
-
Purification (Commentary)
Commentary
Organism
-
Thermoplasma acidophilum
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
7.33
-
purified recombinant enzyme, pH 6.0, 60°C, substrate UDP-glucose
Thermoplasma acidophilum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ADP-alpha-D-glucose + D-glucose 6-phosphate
activity with ADP-glucose is about 50% compared to the activity with UDP-glucose
727099
Thermoplasma acidophilum
ADP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
activity with GDP-glucose is about 20% compared to the activity with UDP-glucose
727099
Thermoplasma acidophilum
GDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
GDP-glucose + glucose 6-phosphate
cf. EC 2.4.1.36
727099
Thermoplasma acidophilum
GDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
additional information
the enzyme utilizes UDP-glucose, ADP-glucose (ADPG) and GDP-glucose (GDPG) as glycosyl donors and various phosphorylated monosaccharides as glycosyl acceptors. Maximal activity is found towards UDP-glucose and D-glucose 6-phosphate. The N-loop region is important for the catalytic efficiency of the enzyme, different roles of N-loop sequences in different trehalose-6-phosphate synthases
727099
Thermoplasma acidophilum
?
-
-
-
-
UDP-alpha-D-glucose + D-fructose 6-phosphate
activity with D-fructose 6-phosphate is about 10% compared to the activity with D-glucose 6-phosphate
727099
Thermoplasma acidophilum
UDP + ?
-
-
-
?
UDP-alpha-D-glucose + D-galactose 6-phosphate
activity with D-galactose 6-phosphate is about 10% compared to the activity with D-glucose 6-phosphate
727099
Thermoplasma acidophilum
UDP + ?
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
the enzyme can utilize various nucleoside diphosphate monosaccharides. Maximal activity with UDP-glucose. Various phosphorylated monosaccharides D-glucose 6-phosphate, glucosamine-6-phosphate, fructose-6-phosphate and mannose-6-phosphate can be used as catalytic acceptors, with maximal activity towards D-glucose 6-phosphate
727099
Thermoplasma acidophilum
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-alpha-D-glucose + D-mannose 6-phosphate
activity with D-mannose 6-phosphate is about 40% compared to the activity with D-glucose 6-phosphate
727099
Thermoplasma acidophilum
UDP + ?
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
-
727099
Thermoplasma acidophilum
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
; 2 * 51400, about, sequence calculation
Thermoplasma acidophilum
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
60
-
-
Thermoplasma acidophilum
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
50
80
50°C: about 50% of maximal activity, 80°C: about 75% of maximal activity
Thermoplasma acidophilum
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
60
-
half-life: 6 h
Thermoplasma acidophilum
70
-
10 h, more than 30% of the original activity remains
Thermoplasma acidophilum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Thermoplasma acidophilum
pH Range
pH Minimum
pH Maximum
Commentary
Organism
4
9
activity range, profile overview
Thermoplasma acidophilum
5
7
pH 5.0: about 50% of maximal activity, pH 7.0: about 50% of maximal activity
Thermoplasma acidophilum
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
2
-
6 h, more than half of the activity remains
Thermoplasma acidophilum
9
-
6 h, more than half of the activity remains
Thermoplasma acidophilum
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
chondroitin sulfate
maximal activation at 0.0005 mg; maximal stimulation at 400 ng
Thermoplasma acidophilum
heparin
0.006 mg, stimulates; heparin can stimulate the activity of the enzyme, although the activity decreases while the concentration of heparin is above 600 ng
Thermoplasma acidophilum
additional information
the enzymatic activity can be stimulated by divalent metal ions and polyanions heparin and chondroitin sulfate
Thermoplasma acidophilum
Cloned(Commentary) (protein specific)
Commentary
Organism
; gene TA1210, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression in Escherichia coli strains DH5alpha and BL21-CodonPlus (DE3)-RIL
Thermoplasma acidophilum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
10% (v/v), 9% inhibition; 91% inhibition
Thermoplasma acidophilum
Ba2+
10 mM, 38% inhibition; 38% inhibition at 10 mM
Thermoplasma acidophilum
dithiothreitol
10 mM, 27% inhibition
Thermoplasma acidophilum
DTT
73% inhibition
Thermoplasma acidophilum
EDTA
10 mM, 15% inhibition; 85% inhibition
Thermoplasma acidophilum
ethanol
10% (v/v), 28% inhibition; 72% inhibition
Thermoplasma acidophilum
guanidine hydrochloride
10 mM, 63% inhibition; 37% inhibition
Thermoplasma acidophilum
Isopropanol
10% (v/v), 14% inhibition; 86% inhibition
Thermoplasma acidophilum
K+
10% inhibition at 10 mM; 10 mM, 10% inhibition
Thermoplasma acidophilum
methanol
10% (v/v), 30% inhibition; 70% inhibition
Thermoplasma acidophilum
n-butanol
10% (v/v), 48% inhibition; 52% inhibition
Thermoplasma acidophilum
Na+
10 mM, 8% inhibition; 8% inhibition at 10 mM
Thermoplasma acidophilum
Ni2+
10 mM, 21% inhibition; 21% inhibition at 10 mM
Thermoplasma acidophilum
SDS
10% (w/v), 27% inhibition; 73% inhibition
Thermoplasma acidophilum
Urea
10 mM, 15% inhibition; 85% inhibition
Thermoplasma acidophilum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.2
1
UDP-alpha-D-glucose
pH 6.0, 60°C, wild-type enzyme
Thermoplasma acidophilum
0.27
-
D-glucose 6-phosphate
pH 6.0, 60°C, wild-type enzyme
Thermoplasma acidophilum
0.34
-
D-glucose 6-phosphate
pH 6.0, 60°C, N-loop truncation mutant enzyme
Thermoplasma acidophilum
0.74
-
UDP-alpha-D-glucose
pH 6.0, 60°C, N-loop truncation mutant enzyme
Thermoplasma acidophilum
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
1.91fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 1.91fold activation by 10 mM Co2+
Thermoplasma acidophilum
Mg2+
2.33fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 2.33fold activation ba 10 mM Mg2+
Thermoplasma acidophilum
Mn2+
1.16fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 1.16fold activation by 10 mM Mn2+
Thermoplasma acidophilum
additional information
no effect by Li+ at 10 mM; the addition of monovalent metal ions Na+, K+ and Li+ has no effect on the enzyme activity
Thermoplasma acidophilum
Zn2+
2.26fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 2.26fold activation by 10 mM Zn2+
Thermoplasma acidophilum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
51400
-
2 * 51400, about, sequence calculation
Thermoplasma acidophilum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
UDP-glucose + D-glucose 6-phosphate
Thermoplasma acidophilum
-
UDP + alpha,alpha-trehalose 6-phosphate
-
-
?
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
Ethanol
72% inhibition
Thermoplasma acidophilum
isopropanol
86% inhibition
Thermoplasma acidophilum
Methanol
70% inhibition
Thermoplasma acidophilum
n-Butanol
52% inhibition
Thermoplasma acidophilum
Purification (Commentary) (protein specific)
Commentary
Organism
-
Thermoplasma acidophilum
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
7.33
-
purified recombinant enzyme, pH 6.0, 60°C, substrate UDP-glucose
Thermoplasma acidophilum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ADP-alpha-D-glucose + D-glucose 6-phosphate
activity with ADP-glucose is about 50% compared to the activity with UDP-glucose
727099
Thermoplasma acidophilum
ADP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
activity with GDP-glucose is about 20% compared to the activity with UDP-glucose
727099
Thermoplasma acidophilum
GDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
GDP-glucose + glucose 6-phosphate
cf. EC 2.4.1.36
727099
Thermoplasma acidophilum
GDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
additional information
the enzyme utilizes UDP-glucose, ADP-glucose (ADPG) and GDP-glucose (GDPG) as glycosyl donors and various phosphorylated monosaccharides as glycosyl acceptors. Maximal activity is found towards UDP-glucose and D-glucose 6-phosphate. The N-loop region is important for the catalytic efficiency of the enzyme, different roles of N-loop sequences in different trehalose-6-phosphate synthases
727099
Thermoplasma acidophilum
?
-
-
-
-
UDP-alpha-D-glucose + D-fructose 6-phosphate
activity with D-fructose 6-phosphate is about 10% compared to the activity with D-glucose 6-phosphate
727099
Thermoplasma acidophilum
UDP + ?
-
-
-
?
UDP-alpha-D-glucose + D-galactose 6-phosphate
activity with D-galactose 6-phosphate is about 10% compared to the activity with D-glucose 6-phosphate
727099
Thermoplasma acidophilum
UDP + ?
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
the enzyme can utilize various nucleoside diphosphate monosaccharides. Maximal activity with UDP-glucose. Various phosphorylated monosaccharides D-glucose 6-phosphate, glucosamine-6-phosphate, fructose-6-phosphate and mannose-6-phosphate can be used as catalytic acceptors, with maximal activity towards D-glucose 6-phosphate
727099
Thermoplasma acidophilum
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-alpha-D-glucose + D-mannose 6-phosphate
activity with D-mannose 6-phosphate is about 40% compared to the activity with D-glucose 6-phosphate
727099
Thermoplasma acidophilum
UDP + ?
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
-
727099
Thermoplasma acidophilum
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
; 2 * 51400, about, sequence calculation
Thermoplasma acidophilum
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
60
-
-
Thermoplasma acidophilum
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
50
80
50°C: about 50% of maximal activity, 80°C: about 75% of maximal activity
Thermoplasma acidophilum
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
60
-
half-life: 6 h
Thermoplasma acidophilum
70
-
10 h, more than 30% of the original activity remains
Thermoplasma acidophilum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Thermoplasma acidophilum
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
4
9
activity range, profile overview
Thermoplasma acidophilum
5
7
pH 5.0: about 50% of maximal activity, pH 7.0: about 50% of maximal activity
Thermoplasma acidophilum
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
2
-
6 h, more than half of the activity remains
Thermoplasma acidophilum
9
-
6 h, more than half of the activity remains
Thermoplasma acidophilum
General Information
General Information
Commentary
Organism
additional information
the conserved residues Arg9, Trp45, Tyr81, Trp90, Asp135 and Arg284 are involved in glycosyl acceptor binding, and residues Gly29, His159, Arg246, Lys251, Asp345 and Glu353 are involved in glycosyl donor binding. Homology modeling of the enzyme using the enzyme structure from Escherichia coli, OtsA, PDB ID 1GZ5, chain A, as the template
Thermoplasma acidophilum
General Information (protein specific)
General Information
Commentary
Organism
additional information
the conserved residues Arg9, Trp45, Tyr81, Trp90, Asp135 and Arg284 are involved in glycosyl acceptor binding, and residues Gly29, His159, Arg246, Lys251, Asp345 and Glu353 are involved in glycosyl donor binding. Homology modeling of the enzyme using the enzyme structure from Escherichia coli, OtsA, PDB ID 1GZ5, chain A, as the template
Thermoplasma acidophilum
Other publictions for EC 2.4.1.15
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)
743566
Chen
A trehalose biosynthetic enzy ...
Arthrobacter alpinus
PLoS Genet.
13
e1007062
2017
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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
2
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736372
Ozer Uyar
Cloning and expression of treh ...
Rhizopus oryzae
J. Basic Microbiol.
56
459-468
2016
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-
1
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-
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-
-
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1
1
-
4
-
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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
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1
1
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-
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1
1
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735637
Delorge
Trehalose-6-phosphate synthase ...
Arabidopsis thaliana
Biochem. J.
466
283-290
2015
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1
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4
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1
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3
3
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736474
Petitjean
Yeast tolerance to various str ...
Saccharomyces cerevisiae
J. Biol. Chem.
290
16177-16190
2015
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-
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4
-
-
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1
-
4
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1
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4
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1
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1
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3
3
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737083
Hespeels
Against all odds: trehalose-6- ...
Adineta vaga
PLoS ONE
10
e0131313
2015
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1
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6
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1
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1
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1
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2
2
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-
727099
Gao
Enzymatic and regulatory prope ...
Thermoplasma acidophilum
Biochimie
101
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4
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15
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9
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2
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1
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2
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729302
Sengupta
Purification, characterization ...
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Biochim. Biophys. Acta
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736176
Shi
Trehalose metabolism in the bl ...
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4
4
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736565
Yadav
The sucrose-trehalose 6-phosph ...
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J. Exp. Bot.
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Properties of trehalose-6-phos ...
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Zaparty
The first prokaryotic trehalos ...
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Trehalose phosphate synthases ...
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Trehalose-6-phosphate synthase ...
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A trehalose-6-phosphate syntha ...
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1
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1
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718977
Sengupta
Arginine mediated purification ...
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1
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1
1
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8
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4
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1
2
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1
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3
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10
1
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1
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719153
An
Enhanced thermotolerance for e ...
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1
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Regulation of expression of tr ...
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2
1
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Fernandez
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The sugar sensor, trehalose-6- ...
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2011
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1
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1
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Avonce
The Cytophaga hutchinsonii ChT ...
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2010
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1
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1
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Jiang
The catalytic efficiency of tr ...
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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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2
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1
1
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1
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1
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Gomez
AtTPS1-mediated trehalose 6-ph ...
Arabidopsis thaliana
Plant J.
64
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2010
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1
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2
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1
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2
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1
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Martinez-Esparza
Role of trehalose-6P phosphata ...
Candida albicans
Int. J. Med. Microbiol.
299
453-464
2009
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702423
Chaudhuri
Studies on substrate specifici ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1790
368-374
2009
6
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1
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703894
Xu
Identification of a novel gene ...
Helicoverpa armigera
Glycobiology
19
250-257
2009
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1
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1
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1
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1
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704031
Cui
-
Isolation and characterization ...
Locusta migratoria manilensis
Insect Sci.
16
287-295
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1
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1
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1
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4
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1
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-
-
-
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1
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Cai
Trehalose-6-phosphate synthase ...
Metarhizium anisopliae
J. Biosci. Bioeng.
107
499-505
2009
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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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2
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1
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-
-
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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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682433
Chary
Trehalose-6-phosphate synthase ...
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Plant Physiol.
146
97-107
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1
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1
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1
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-
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1
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1
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5
-
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1
-
-
-
-
-
-
-
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-
-
-
-
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Lee
Three trehalose synthetic path ...
Actinoplanes sp., Actinoplanes sp. SN223/29
Appl. Microbiol. Biotechnol.
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2008
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1
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2
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1
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4
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-
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8
1
1
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1
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-
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1
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-
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1
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2
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2
1
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8
1
1
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1
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691066
Chaudhuri
Aggregation dependent enhancem ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1780
289-297
2008
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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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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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694275
Suarez
Improvement of drought toleran ...
Rhizobium etli
Mol. Plant Microbe Interact.
21
958-966
2008
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1
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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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1
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694773
Stiller
Effects of drought on water co ...
Saccharomyces cerevisiae
Planta
227
299-308
2008
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1
1
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-
-
-
-
-
-
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1
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3
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-
-
-
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1
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1
1
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-
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1
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-
-
-
-
-
1
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-
-
-
-
-
-
-
-
-
-
-
-
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695123
Chung
A trehalose 6-phosphate syntha ...
Callinectes sapidus
Saline Syst.
4
18
2008
-
-
-
-
-
-
-
-
-
-
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-
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2
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3
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3
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1
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1
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702847
Tao
-
Transformation of maize with t ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae AS.1416
Biotechnology
7
258-265
2008
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1
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1
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2
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-
675853
Cardoso
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The natural osmolyte trehalose ...
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Almeida
Immunogold localization of tre ...
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682472
Miranda
A bifunctional TPS-TPP enzyme ...
Saccharomyces cerevisiae
Planta
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Trehalose-6-P synthase AtTPS1 ...
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Petzold
Characterization and regulatio ...
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Molecular cloning, characteriz ...
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674967
Leyman
Trehalose-6-phosphate synthase ...
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676512
Gomez
Delayed embryo development in ...
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657904
Gomez
The role of trehalose-6-phosph ...
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Biochem. Soc. Trans.
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658670
Silva
Trehalose biosynthesis in Ther ...
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Extremophiles
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Kolbe
Trehalose 6-phosphate regulate ...
Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
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657760
Valenzuela-Soto
Trehalose 6-phosphate synthase ...
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Gibson
The donor subsite of trehalose ...
Escherichia coli
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Role of trehalose phosphate sy ...
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Avonce
The Arabidopsis trehalose-6-P ...
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Jang
Expression of a bifunctional f ...
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488611
Eastmond
Trehalose-6-phosphate synthase ...
Arabidopsis thaliana
Plant J.
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225-235
2002
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488618
Pan
Trehalose-phosphate synthase o ...
Mycobacterium tuberculosis
Eur. J. Biochem.
269
6091-6100
2002
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488619
Gibson
Characterization of Escherichi ...
Escherichia coli
Acta Crystallogr. Sect. D
58
349-351
2002
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742254
Gibson
Insights into trehalose synth ...
Escherichia coli
Chem. Biol.
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1337-1346
2002
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488610
De Silva-Udawatta
Roles of trehalose phosphate s ...
Saccharomyces cerevisiae
Mol. Microbiol.
40
1345-1356
2001
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1
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1
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488613
Noubhani
Reconstitution of ethanolic fe ...
Saccharomyces cerevisiae
Eur. J. Biochem.
267
4566-4576
2000
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488614
Seo
Characterization of a bifuncti ...
Escherichia coli
Appl. Environ. Microbiol.
66
2484-2490
2000
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1
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5
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-
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488615
De Smet
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Three pathways for trehalose b ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis variant bovis, Mycolicibacterium smegmatis
Microbiology
146
199-208
2000
-
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3
-
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488612
Blazquez
Isolation and molecular charac ...
Arabidopsis thaliana
Plant J.
13
685-689
1998
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1
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488608
Arisan-Atac
Trehalose-6-phosphate synthase ...
Aspergillus niger
FEMS Microbiol. Lett.
140
77-83
1996
-
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1
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488609
Pan
Inhibition of the trehalose-P ...
Mycolicibacterium smegmatis
Arch. Biochem. Biophys.
335
258-266
1996
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488616
Noventa-Jordao
Effects of temperature shifts ...
Neurospora crassa
FEBS Lett.
378
32-36
1996
-
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1
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488617
Blazquez
Trehalose-6-P synthase is disp ...
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176
3895-3902
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742610
Kaasen
Analysis of the otsBA operon ...
Escherichia coli
Gene
145
9-15
1994
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1
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488594
Lippert
Biosynthesis and function of t ...
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1993
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Bell
Characterization of the 56-kDa ...
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134590
Londesborough
Trehalose-6-phosphate synthase ...
Saccharomyces cerevisiae
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488605
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Characterization of trehalose- ...
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488597
Killick
Trehalose 6-phosphate synthase ...
Dictyostelium discoideum
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Pan
Studies on the trehalose-phosp ...
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Elbein
Effects of polyanions and poly ...
Mycolicibacterium smegmatis
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Murphy
The enzymes of glycogen and tr ...
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Purification and properties of ...
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Candy
The biosynthesis of trehalose ...
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Cabib
The biosynthesis of trehalose ...
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