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glutamine-tRNA ligase activity

Known as: glutaminyl-transfer ribonucleate synthetase activity, glutamine translase activity, GlnRS 
Catalysis of the reaction: ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln). [EC:6.1.1.18]
National Institutes of Health

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Glutamine-tRNA ligase

Papers overview

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2014
2014
Atypical OmpR/PhoB subfamily response regulator GlnR of actinomycetes functions as a homodimer, stabilized by the unphosphorylated conserved Asp-focused charge interactions.
The OmpR/PhoB subfamily protein GlnR of actinomycetes is an orphan response regulator that globally coordinates the expression of… Expand
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Review
2005
Review
2005
Coevolution theory of the genetic code at age thirty.
  • J. Wong
  • BioEssays : news and reviews in molecular…
  • 2005
    • Corpus ID: 20352223
The coevolution theory of the genetic code, which postulates that prebiotic synthesis was an inadequate source of all twenty… Expand
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2005
2005
Slow solvation dynamics at the active site of an enzyme: implications for catalysis.
Solvation dynamics at the active site of an enzyme, glutaminyl-tRNA synthetase (GlnRS), was studied using a fluorescence probe… Expand
2005
2005
Genetic analysis of functional connectivity between substrate recognition domains ofEscherichia coli glutaminyl-tRNA synthetase
It has previously been shown that the single mutation E222K in glutaminyl-tRNA synthetase (GlnRS) confers a temperature-sensitive… Expand
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Review
2003
Review
2003
On the Evolution of Structure in Aminoacyl-tRNA Synthetases
SUMMARY The aminoacyl-tRNA synthetases are one of the major protein components in the translation machinery. These essential… Expand
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2000
2000
FIBRELAM GLIDER CONSTRUCTION
A new method of glider construction has been developed by Edgley Sailplanes Ltd in the UK based on Fibrelam - an epoxy glass… Expand
1998
1998
A cognate tRNA specific conformational change in glutaminyl‐tRNA synthetase and its implication for specificity
Conformational changes that occur upon substrate binding are known to play crucial roles in the recognition and specific… Expand
1996
1996
Transfer RNA‐dependent cognate amino acid recognition by an aminoacyl‐tRNA synthetase.
An investigation of the role of tRNA in the catalysis of aminoacylation of Escherichia coli glutaminyl‐tRNA synthetase (GlnRS… Expand
1994
1994
Functional communication in the recognition of tRNA by Escherichia coli glutaminyl-tRNA synthetase.
Wild-type Escherichia coli glutaminyl-tRNA synthetase (GlnRS; EC 6.1.1.18) poorly aminoacylates opal suppressors (GLN) derived… Expand
1972
1972
Further codon assignments in an extremely halophilic bacterium using a cell-free protein-synthesizing system and a ribosomal binding assay.
Further codon assignments were made in a cell-free protein-synthesizing system from Halobacterium cutirubrum by use of the random… Expand
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