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Literature summary for 6.1.1.17 extracted from

  • Sekine, S.; Nureki, O.; Dubois, D.Y.; Bernier, S.; Chenevert, R.; Lapointe, J.; Vassylyev, D.G.; Yokoyama, S.
    ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding (2003), EMBO J., 22, 676-688.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Inhibitors Comment Organism Structure
glutamol-AMP competitive inhibition Thermus thermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamate + tRNAGlu Thermus thermophilus
-
AMP + diphosphate + L-glutamyl-tRNAGlu
-
?

Organism

Organism UniProt Comment Textmining
Thermus thermophilus P27000
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu catalytic site structure, substrate binding and reaction mechanism Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate + tRNAGlu
-
Thermus thermophilus AMP + diphosphate + L-glutamyl-tRNAGlu
-
?
ATP + L-glutamate + tRNAGlu tRNAGlu binding causes conformational changes in the enzyme, glutamine binding mechanism, in presence or absence of tRNA Thermus thermophilus AMP + diphosphate + L-glutamyl-tRNAGlu
-
?

Synonyms

Synonyms Comment Organism
GluRS
-
Thermus thermophilus
Glutamyl-tRNA synthetase
-
Thermus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
assay at Thermus thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Thermus thermophilus

Cofactor

Cofactor Comment Organism Structure
ATP binding mechanism, in presence or absence of tRNA Thermus thermophilus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0012
-
glutamol-AMP pH 7.5, 65°C Thermus thermophilus