BRENDA - Enzyme Database

ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding

Sekine, S.; Nureki, O.; Dubois, D.Y.; Bernier, S.; Chenevert, R.; Lapointe, J.; Vassylyev, D.G.; Yokoyama, S.; EMBO J. 22, 676-688 (2003)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
6.1.1.17
crystallization of the enzyme in different complexes: 1. non-productively complexed with ATP and L-glutamate, 2. with ATP, 3. with tRNAGlu and ATP, 4. with tRNAGlu and the glutamyl-AMP analogue glutamol-AMP, hanging-drop method, 0.008 ml of 5.0 mg/ml protein in 10 mM Na-MOPS, pH 6.5, 5 mM MgCl2, 2.5 mM 2-mercaptoethanol, 1% PEG 6000, 1-2 mM ATP and/or 2 mM glutamate and/or 0.5 mM glutamol-AMP, plus 1 ml reservoir solution containing 10% PEG 6000 at 4 or 20°C, 3 days or more, X-ray diffraction structure determination at 1.8 A resolution, molecular replacement, and analysis
Thermus thermophilus
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
6.1.1.17
glutamol-AMP
competitive inhibition
Thermus thermophilus
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
6.1.1.17
Mg2+
required
Thermus thermophilus
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
Thermus thermophilus
-
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Thermus thermophilus
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
6.1.1.17
Thermus thermophilus
P27000
-
-
Reaction
EC Number
Reaction
Commentary
Organism
6.1.1.17
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
catalytic site structure, substrate binding and reaction mechanism
Thermus thermophilus
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
-
651000
Thermus thermophilus
AMP + diphosphate + L-glutamyl-tRNAGlu
-
651000
Thermus thermophilus
?
6.1.1.17
ATP + L-glutamate + tRNAGlu
tRNAGlu binding causes conformational changes in the enzyme, glutamine binding mechanism, in presence or absence of tRNA
651000
Thermus thermophilus
AMP + diphosphate + L-glutamyl-tRNAGlu
-
651000
Thermus thermophilus
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
6.1.1.17
65
-
assay at
Thermus thermophilus
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.1.1.17
7.5
-
assay at
Thermus thermophilus
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
6.1.1.17
ATP
binding mechanism, in presence or absence of tRNA
Thermus thermophilus
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
6.1.1.17
0.0012
-
glutamol-AMP
pH 7.5, 65°C
Thermus thermophilus
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
6.1.1.17
ATP
binding mechanism, in presence or absence of tRNA
Thermus thermophilus
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
6.1.1.17
crystallization of the enzyme in different complexes: 1. non-productively complexed with ATP and L-glutamate, 2. with ATP, 3. with tRNAGlu and ATP, 4. with tRNAGlu and the glutamyl-AMP analogue glutamol-AMP, hanging-drop method, 0.008 ml of 5.0 mg/ml protein in 10 mM Na-MOPS, pH 6.5, 5 mM MgCl2, 2.5 mM 2-mercaptoethanol, 1% PEG 6000, 1-2 mM ATP and/or 2 mM glutamate and/or 0.5 mM glutamol-AMP, plus 1 ml reservoir solution containing 10% PEG 6000 at 4 or 20°C, 3 days or more, X-ray diffraction structure determination at 1.8 A resolution, molecular replacement, and analysis
Thermus thermophilus
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
6.1.1.17
glutamol-AMP
competitive inhibition
Thermus thermophilus
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
6.1.1.17
0.0012
-
glutamol-AMP
pH 7.5, 65°C
Thermus thermophilus
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
6.1.1.17
Mg2+
required
Thermus thermophilus
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
Thermus thermophilus
-
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Thermus thermophilus
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
-
651000
Thermus thermophilus
AMP + diphosphate + L-glutamyl-tRNAGlu
-
651000
Thermus thermophilus
?
6.1.1.17
ATP + L-glutamate + tRNAGlu
tRNAGlu binding causes conformational changes in the enzyme, glutamine binding mechanism, in presence or absence of tRNA
651000
Thermus thermophilus
AMP + diphosphate + L-glutamyl-tRNAGlu
-
651000
Thermus thermophilus
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
6.1.1.17
65
-
assay at
Thermus thermophilus
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.1.1.17
7.5
-
assay at
Thermus thermophilus