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Literature summary for 6.1.1.18 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
Search for more literature for 6.1.1.18

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Organism

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

Reaction

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

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 phylogenetic analysis Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
GlnRS
-
 Escherichia coli
Glutaminyl-tRNA synthetase
-
 Escherichia coli

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

Ki Value [mM]

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