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Literature summary for 6.1.1.18 extracted from

  • Druart, K.; Guennec, M.L.; Palmai, Z.; Simonson, T.
    Probing the stereospecificity of tyrosyl- and glutaminyl-tRNA synthetase with molecular dynamics (2017), J. Mol. Graph. Model., 71, 192-199 .
    View publication on PubMed
Search for more literature for 6.1.1.18

Protein Variants

Protein Variants Comment Organism
D81Q site-diretced mutagenesis, the mutant has and increased, inverted stereospecificity. D81Q is predicted to lead to a rotated ligand backbone and an increased, not a decreased L-Tyr preference Escherichia coli
R260Q site-diretced mutagenesis, mutating Arg260 to the homologous but neutral Gln does not reduce the L-GlnAMP preference, instead, the mutation produces a change in the DELTADELTAG value that is much smaller than the wild-type free energy component Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamine + tRNAGln Escherichia coli
-
 AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P00962
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamine + tRNAGln
-
 Escherichia coli AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?
additional information GlnRS has adetectable tRNA-acylation activity for its D-amino acid substrate Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
class I glutaminyl-tRNA synthetase
-
 Escherichia coli
GlnRS
-
 Escherichia coli
Glutaminyl-tRNA synthetase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

General Information

General Information Comment Organism
evolution the enzyme belongs to the class I aminoacyl-tRNA synthetase family Escherichia coli
additional information molecular dynamics modeling of L-GlnAMP using the PDB ID 1QTQ X-ray structure, superimposed based on their protein/tRNA environment, enzyme molecular dynamics simulation amd modeling, structure-function analysis, detailed overview Escherichia coli