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Literature summary extracted from

  • Liu, J.; Lin, S.X.; Blochet, J.E.; Pezolet, M.; Lapointe, J.
    The glutamyl-tRNA synthetase of Escherichia coli contains one atom of zinc essential for its native conformation and its catalytic activity (1993), Biochemistry, 32, 11390-11396.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.1.1.17 1,10-phenanthroline ATP protects the enzyme against zinc removal Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.17 Zinc zinc metalloenzyme Bacillus subtilis
6.1.1.17 Zinc zinc metalloenzyme Escherichia coli
6.1.1.17 Zinc enzyme contains one zinc atom strongly bound, which is essential for its native conformation and its catalytic acitivity Escherichia coli
6.1.1.17 Zinc enzyme does not contain zinc Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.17 Bacillus subtilis
-
-
-
6.1.1.17 Escherichia coli
-
-
-
6.1.1.17 Thermus thermophilus
-
 wild-type and mutant enzymes
-

Substrates and Products (Substrate)

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