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Literature summary extracted from

  • Perona, J.J.; Rould, M.A.; Steitz, T.A.; Risler, J.L.; Zelwer, C.; Brunie, S.
    Structural similarities in glutaminyl- and methionyl-tRNA synthetases suggest a common overall orientation of tRNA binding (1991), Proc. Natl. Acad. Sci. USA, 88, 2903-2907.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.18 detailed structural comparison between Met-tRNA synthetase and Gln-tRNA synthetase Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.1.1.18 additional information
-
 structural similarities in glutaminyl-tRNA synthetase and methionyl-tRNA synthetase outside the respective dinucleotide-fold domains Escherichia coli

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.18 ATP + L-glutamine + tRNAGln
-
 Escherichia coli AMP + diphosphate + L-glutaminyl-tRNAGln
-
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