BRENDA - Enzyme Database

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
EC Number
Activating Compound
Commentary
Organism
Structure
2.4.1.15
chondroitin sulfate
maximal activation at 0.0005 mg; maximal stimulation at 400 ng
Thermoplasma acidophilum
2.4.1.15
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
2.4.1.15
additional information
the enzymatic activity can be stimulated by divalent metal ions and polyanions heparin and chondroitin sulfate
Thermoplasma acidophilum
Cloned(Commentary)
EC Number
Commentary
Organism
2.4.1.15
; 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
EC Number
Inhibitors
Commentary
Organism
Structure
2.4.1.15
2-mercaptoethanol
10% (v/v), 9% inhibition; 91% inhibition
Thermoplasma acidophilum
2.4.1.15
Ba2+
10 mM, 38% inhibition; 38% inhibition at 10 mM
Thermoplasma acidophilum
2.4.1.15
dithiothreitol
10 mM, 27% inhibition
Thermoplasma acidophilum
2.4.1.15
DTT
73% inhibition
Thermoplasma acidophilum
2.4.1.15
EDTA
10 mM, 15% inhibition; 85% inhibition
Thermoplasma acidophilum
2.4.1.15
ethanol
10% (v/v), 28% inhibition; 72% inhibition
Thermoplasma acidophilum
2.4.1.15
guanidine hydrochloride
10 mM, 63% inhibition; 37% inhibition
Thermoplasma acidophilum
2.4.1.15
Isopropanol
10% (v/v), 14% inhibition; 86% inhibition
Thermoplasma acidophilum
2.4.1.15
K+
10% inhibition at 10 mM; 10 mM, 10% inhibition
Thermoplasma acidophilum
2.4.1.15
methanol
10% (v/v), 30% inhibition; 70% inhibition
Thermoplasma acidophilum
2.4.1.15
n-butanol
10% (v/v), 48% inhibition; 52% inhibition
Thermoplasma acidophilum
2.4.1.15
Na+
10 mM, 8% inhibition; 8% inhibition at 10 mM
Thermoplasma acidophilum
2.4.1.15
Ni2+
10 mM, 21% inhibition; 21% inhibition at 10 mM
Thermoplasma acidophilum
2.4.1.15
SDS
10% (w/v), 27% inhibition; 73% inhibition
Thermoplasma acidophilum
2.4.1.15
Urea
10 mM, 15% inhibition; 85% inhibition
Thermoplasma acidophilum
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.4.1.15
0.2
1
UDP-alpha-D-glucose
pH 6.0, 60°C, wild-type enzyme
Thermoplasma acidophilum
2.4.1.15
0.27
-
D-glucose 6-phosphate
pH 6.0, 60°C, wild-type enzyme
Thermoplasma acidophilum
2.4.1.15
0.34
-
D-glucose 6-phosphate
pH 6.0, 60°C, N-loop truncation mutant enzyme
Thermoplasma acidophilum
2.4.1.15
0.74
-
UDP-alpha-D-glucose
pH 6.0, 60°C, N-loop truncation mutant enzyme
Thermoplasma acidophilum
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
2.4.1.15
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
2.4.1.15
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
2.4.1.15
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
2.4.1.15
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
2.4.1.15
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]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
2.4.1.15
51400
-
2 * 51400, about, sequence calculation
Thermoplasma acidophilum
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.4.1.15
UDP-glucose + D-glucose 6-phosphate
Thermoplasma acidophilum
-
UDP + alpha,alpha-trehalose 6-phosphate
-
-
?
Organic Solvent Stability
EC Number
Organic Solvent
Commentary
Organism
2.4.1.15
Ethanol
72% inhibition
Thermoplasma acidophilum
2.4.1.15
isopropanol
86% inhibition
Thermoplasma acidophilum
2.4.1.15
Methanol
70% inhibition
Thermoplasma acidophilum
2.4.1.15
n-Butanol
52% inhibition
Thermoplasma acidophilum
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.4.1.15
Thermoplasma acidophilum
Q9HIW6
; gene TA1210
-
Purification (Commentary)
EC Number
Commentary
Organism
2.4.1.15
-
Thermoplasma acidophilum
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.4.1.15
7.33
-
purified recombinant enzyme, pH 6.0, 60°C, substrate UDP-glucose
Thermoplasma acidophilum
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.1.15
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
-
-
-
?
2.4.1.15
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
-
-
-
?
2.4.1.15
GDP-glucose + glucose 6-phosphate
cf. EC 2.4.1.36
727099
Thermoplasma acidophilum
GDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
2.4.1.15
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
?
-
-
-
-
2.4.1.15
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 + ?
-
-
-
?
2.4.1.15
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 + ?
-
-
-
?
2.4.1.15
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
-
-
-
?
2.4.1.15
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 + ?
-
-
-
?
2.4.1.15
UDP-glucose + D-glucose 6-phosphate
-
727099
Thermoplasma acidophilum
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
2.4.1.15
dimer
; 2 * 51400, about, sequence calculation
Thermoplasma acidophilum
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
2.4.1.15
60
-
-
Thermoplasma acidophilum
Temperature Range [°C]
EC Number
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
2.4.1.15
50
80
50°C: about 50% of maximal activity, 80°C: about 75% of maximal activity
Thermoplasma acidophilum
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
2.4.1.15
60
-
half-life: 6 h
Thermoplasma acidophilum
2.4.1.15
70
-
10 h, more than 30% of the original activity remains
Thermoplasma acidophilum
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.4.1.15
6
-
-
Thermoplasma acidophilum
pH Range
EC Number
pH Minimum
pH Maximum
Commentary
Organism
2.4.1.15
4
9
activity range, profile overview
Thermoplasma acidophilum
2.4.1.15
5
7
pH 5.0: about 50% of maximal activity, pH 7.0: about 50% of maximal activity
Thermoplasma acidophilum
pH Stability
EC Number
pH Stability
pH Stability Maximum
Commentary
Organism
2.4.1.15
2
-
6 h, more than half of the activity remains
Thermoplasma acidophilum
2.4.1.15
9
-
6 h, more than half of the activity remains
Thermoplasma acidophilum
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
2.4.1.15
chondroitin sulfate
maximal activation at 0.0005 mg; maximal stimulation at 400 ng
Thermoplasma acidophilum
2.4.1.15
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
2.4.1.15
additional information
the enzymatic activity can be stimulated by divalent metal ions and polyanions heparin and chondroitin sulfate
Thermoplasma acidophilum
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
2.4.1.15
; 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)
EC Number
Inhibitors
Commentary
Organism
Structure
2.4.1.15
2-mercaptoethanol
10% (v/v), 9% inhibition; 91% inhibition
Thermoplasma acidophilum
2.4.1.15
Ba2+
10 mM, 38% inhibition; 38% inhibition at 10 mM
Thermoplasma acidophilum
2.4.1.15
dithiothreitol
10 mM, 27% inhibition
Thermoplasma acidophilum
2.4.1.15
DTT
73% inhibition
Thermoplasma acidophilum
2.4.1.15
EDTA
10 mM, 15% inhibition; 85% inhibition
Thermoplasma acidophilum
2.4.1.15
ethanol
10% (v/v), 28% inhibition; 72% inhibition
Thermoplasma acidophilum
2.4.1.15
guanidine hydrochloride
10 mM, 63% inhibition; 37% inhibition
Thermoplasma acidophilum
2.4.1.15
Isopropanol
10% (v/v), 14% inhibition; 86% inhibition
Thermoplasma acidophilum
2.4.1.15
K+
10% inhibition at 10 mM; 10 mM, 10% inhibition
Thermoplasma acidophilum
2.4.1.15
methanol
10% (v/v), 30% inhibition; 70% inhibition
Thermoplasma acidophilum
2.4.1.15
n-butanol
10% (v/v), 48% inhibition; 52% inhibition
Thermoplasma acidophilum
2.4.1.15
Na+
10 mM, 8% inhibition; 8% inhibition at 10 mM
Thermoplasma acidophilum
2.4.1.15
Ni2+
10 mM, 21% inhibition; 21% inhibition at 10 mM
Thermoplasma acidophilum
2.4.1.15
SDS
10% (w/v), 27% inhibition; 73% inhibition
Thermoplasma acidophilum
2.4.1.15
Urea
10 mM, 15% inhibition; 85% inhibition
Thermoplasma acidophilum
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.4.1.15
0.2
1
UDP-alpha-D-glucose
pH 6.0, 60°C, wild-type enzyme
Thermoplasma acidophilum
2.4.1.15
0.27
-
D-glucose 6-phosphate
pH 6.0, 60°C, wild-type enzyme
Thermoplasma acidophilum
2.4.1.15
0.34
-
D-glucose 6-phosphate
pH 6.0, 60°C, N-loop truncation mutant enzyme
Thermoplasma acidophilum
2.4.1.15
0.74
-
UDP-alpha-D-glucose
pH 6.0, 60°C, N-loop truncation mutant enzyme
Thermoplasma acidophilum
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
2.4.1.15
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
2.4.1.15
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
2.4.1.15
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
2.4.1.15
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
2.4.1.15
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)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
2.4.1.15
51400
-
2 * 51400, about, sequence calculation
Thermoplasma acidophilum
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.4.1.15
UDP-glucose + D-glucose 6-phosphate
Thermoplasma acidophilum
-
UDP + alpha,alpha-trehalose 6-phosphate
-
-
?
Organic Solvent Stability (protein specific)
EC Number
Organic Solvent
Commentary
Organism
2.4.1.15
Ethanol
72% inhibition
Thermoplasma acidophilum
2.4.1.15
isopropanol
86% inhibition
Thermoplasma acidophilum
2.4.1.15
Methanol
70% inhibition
Thermoplasma acidophilum
2.4.1.15
n-Butanol
52% inhibition
Thermoplasma acidophilum
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
2.4.1.15
-
Thermoplasma acidophilum
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.4.1.15
7.33
-
purified recombinant enzyme, pH 6.0, 60°C, substrate UDP-glucose
Thermoplasma acidophilum
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.1.15
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
-
-
-
?
2.4.1.15
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
-
-
-
?
2.4.1.15
GDP-glucose + glucose 6-phosphate
cf. EC 2.4.1.36
727099
Thermoplasma acidophilum
GDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
2.4.1.15
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
?
-
-
-
-
2.4.1.15
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 + ?
-
-
-
?
2.4.1.15
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 + ?
-
-
-
?
2.4.1.15
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
-
-
-
?
2.4.1.15
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 + ?
-
-
-
?
2.4.1.15
UDP-glucose + D-glucose 6-phosphate
-
727099
Thermoplasma acidophilum
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
2.4.1.15
dimer
; 2 * 51400, about, sequence calculation
Thermoplasma acidophilum
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
2.4.1.15
60
-
-
Thermoplasma acidophilum
Temperature Range [°C] (protein specific)
EC Number
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
2.4.1.15
50
80
50°C: about 50% of maximal activity, 80°C: about 75% of maximal activity
Thermoplasma acidophilum
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
2.4.1.15
60
-
half-life: 6 h
Thermoplasma acidophilum
2.4.1.15
70
-
10 h, more than 30% of the original activity remains
Thermoplasma acidophilum
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.4.1.15
6
-
-
Thermoplasma acidophilum
pH Range (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
Organism
2.4.1.15
4
9
activity range, profile overview
Thermoplasma acidophilum
2.4.1.15
5
7
pH 5.0: about 50% of maximal activity, pH 7.0: about 50% of maximal activity
Thermoplasma acidophilum
pH Stability (protein specific)
EC Number
pH Stability
pH Stability Maximum
Commentary
Organism
2.4.1.15
2
-
6 h, more than half of the activity remains
Thermoplasma acidophilum
2.4.1.15
9
-
6 h, more than half of the activity remains
Thermoplasma acidophilum
General Information
EC Number
General Information
Commentary
Organism
2.4.1.15
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)
EC Number
General Information
Commentary
Organism
2.4.1.15
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