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Literature summary for 6.1.1.17 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

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

Metals/Ions

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

Organism

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

Substrates and Products (Substrate)

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