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Literature summary for 6.1.1.18 extracted from

  • Uter, N.T.; Perona, J.J.
    Active-site assembly in glutaminyl-tRNA synthetase by tRNA-mediated induced fit (2006), Biochemistry, 45, 6858-6865.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.18

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged GlnRS mutants in strain BL21-DE3 Escherichia coli

Protein Variants

Protein Variants Comment Organism
E34A site-directed mutagenesis, the mutant shows highly increased Km and reduced kcat and activity compared to the wild-type enzyme Escherichia coli
E34D site-directed mutagenesis, the mutant shows highly increased Km and reduced kcat and activity compared to the wild-type enzyme Escherichia coli
E34Q site-directed mutagenesis, the mutant shows highly increased Km and reduced kcat and activity compared to the wild-type enzyme Escherichia coli
E73A site-directed mutagenesis, the mutant shows highly increased Km and reduced kcat and activity compared to the wild-type enzyme Escherichia coli
E73Q site-directed mutagenesis, the mutant shows highly increased Km and reduced kcat and activity compared to the wild-type enzyme, product release remains the rate-limiting step in E73Q Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information single turnover kinetics, and steady-state kinetics of recombinant mutant enzymes, overview Escherichia coli
22.3
-
 L-glutamine pH 7.2, 37°C, recombinant mutant E73Q Escherichia coli
34.9
-
 L-glutamine pH 7.2, 37°C, recombinant mutant E34Q Escherichia coli
45
-
 L-glutamine pH 7.2, 37°C, recombinant mutant E34D Escherichia coli
46.3
-
 L-glutamine pH 7.2, 37°C, recombinant mutant E34A Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 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
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged GlnRS mutants from strain BL21-DE3 by nickel affinity chromatography Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 activities of recombinant mutant enzymes Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamine + tRNAGln
-
 Escherichia coli AMP + diphosphate + L-glutaminyl-tRNAGln
-
 r
ATP + L-glutamine + tRNAGln a two-step reaction, with a distinct role in induced-fit for Glu73 Escherichia coli AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?
additional information structure function analysis, overview Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More structure function analysis, overview 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
0.004
-
 L-glutamine pH 7.2, 37°C, recombinant mutant E73Q Escherichia coli
0.034
-
 L-glutamine pH 7.2, 37°C, recombinant mutant E34D Escherichia coli
0.065
-
 L-glutamine pH 7.2, 37°C, recombinant mutant E34Q Escherichia coli
0.14
-
 L-glutamine pH 7.2, 37°C, recombinant mutant E34A 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