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Literature summary extracted from

  • Hong, K.W.; Ibba, M.; Soll, D.
    Retracing the evolution of amino acid specificity in glutaminyl-tRNA synthetase (1998), FEBS Lett., 434, 149-154.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.18 F90L site-directed mutagenesis, active site mutant, 5fold improved glutamic acid recognition in vitro, in vivo the mutant shows a 40% reduced growth rate, partial complementation of an enzyme-deficient strain Escherichia coli
6.1.1.18 additional information construction of a truncated enzyme form, partial complementation of an enzyme-deficient strain, reduced growth rate in vivo Escherichia coli
6.1.1.18 Y240E site-directed mutagenesis, active site mutant, 5fold improved glutamic acid recognition in vitro, partial complementation of an enzyme-deficient strain Escherichia coli
6.1.1.18 Y240G site-directed mutagenesis, active site mutant, 3fold improved glutamic acid recognition in vitro, partial complementation of an enzyme-deficient strain Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.1.1.18 L-Glutamic acid competitive inhibition of the wild-type and mutant enzymes Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.18 0.05
-
 L-glutamine mutant F90L, pH 7.2, 37°C Escherichia coli
6.1.1.18 0.06
-
 L-glutamine truncated mutant, pH 7.2, 37°C Escherichia coli
6.1.1.18 0.07
-
 L-glutamine mutant Y240E, pH 7.2, 37°C Escherichia coli
6.1.1.18 0.12
-
 L-glutamine mutant Y240G, pH 7.2, 37°C Escherichia coli
6.1.1.18 0.19
-
 L-glutamine wild-type enzyme, pH 7.2, 37°C Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.18 ATP + L-glutamine + tRNAGln Escherichia coli
-
 AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?
6.1.1.18 additional information Escherichia coli phylogenetic analysis ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.18 Escherichia coli
-
 purified recombinant wild-type and mutant enzymes
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.18 ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln active site residues are Tyr240 and Phe90 Escherichia coli
a

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
-
 ?
6.1.1.18 additional information phylogenetic analysis Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.18 GlnRS
-
 Escherichia coli
6.1.1.18 Glutaminyl-tRNA synthetase
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.18 37
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.18 1.4
-
 L-glutamine mutant Y240E, pH 7.2, 37°C Escherichia coli
6.1.1.18 2
-
 L-glutamine mutant F90L, pH 7.2, 37°C Escherichia coli
6.1.1.18 3.4
-
 L-glutamine mutant Y240G, pH 7.2, 37°C Escherichia coli
6.1.1.18 4.7
-
 L-glutamine wild-type enzyme and truncated mutant, pH 7.2, 37°C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.18 7.2
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.18 ATP
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.1.1.18 17
-
 L-Glutamic acid truncated mutant, pH 7.2, 37°C Escherichia coli
6.1.1.18 21
-
 L-Glutamic acid mutant Y240E, pH 7.2, 37°C Escherichia coli
6.1.1.18 29
-
 L-Glutamic acid mutant F90L, pH 7.2, 37°C Escherichia coli
6.1.1.18 47
-
 L-Glutamic acid mutant Y240G, pH 7.2, 37°C Escherichia coli
6.1.1.18 96
-
 L-Glutamic acid wild-type enzyme, pH 7.2, 37°C Escherichia coli