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Literature summary extracted from

  • Kohda, D.; Hara, M.; Yokoyama, S.; Miyazawa, T.
    Aminoacyl-tRNA synthetases from an extreme thermophile, Thermus thermophilus HB8 (1983), Nucleic Acids Symp. Ser., 12, 153-154.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.1.1.17 KCl aminoacylation Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.17 Zinc enzyme does not contain zinc Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.17 Thermus thermophilus
-
-
-
6.1.1.17 Thermus thermophilus
-
wild-type and mutant enzymes
-
6.1.1.17 Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-

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
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 AMP + diphosphate + L-glutamyl-tRNAGlu
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
6.1.1.17 65
-
8 h, no loss of activity, in absence of substrate Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.17 8 8.5 aminoacylation Thermus thermophilus