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Literature summary extracted from

  • Kern, D.; Lapointe, J.
    The glutamyl-tRNA synthetase of Escherichia coli: substrate-induced protection against its thermal inactivation (1979), Nucleic Acids Res., 7, 501-515.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.17 Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.17 47
-
aminoacylation Escherichia coli

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
6.1.1.17 35 55 35°C: about 70% of maximal activity, 55°C: about 60% of maximal activity Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
6.1.1.17 additional information
-
tRNAGlu and ATP protect efficiently against thermal inactivation, glutamate does not. Weak synergism between ATP and tRNAGlu, no synergism between ATP and glutamate. Highest stabilization with ATP, glutamate and tRNAGlu Escherichia coli
6.1.1.17 42
-
stable up to, without addition of substrate Escherichia coli
6.1.1.17 50
-
50% loss of activity, when temperature is increased gradually at the rate of 1 C per min, without addition of substrate Escherichia coli
6.1.1.17 60
-
complete loss of activity, when temperature is increased gradually at the rate of 1°C per min, without addition of substrate Escherichia coli