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Literature summary 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)

EC Number Crystallization (Comment) 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 Comment Organism Structure
6.1.1.17 glutamol-AMP competitive inhibition Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.17 Mg2+ required Thermus thermophilus

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.17 Thermus thermophilus P27000
-
-

Reaction

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.17 ATP + L-glutamate + tRNAGlu
-
 Thermus thermophilus AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
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 Thermus thermophilus AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.17 GluRS
-
 Thermus thermophilus
6.1.1.17 Glutamyl-tRNA synthetase
-
 Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.17 65
-
 assay at Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.17 7.5
-
 assay at Thermus thermophilus

Cofactor

EC Number Cofactor Comment 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 Comment Organism Structure
6.1.1.17 0.0012
-
 glutamol-AMP pH 7.5, 65°C Thermus thermophilus