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ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
ATP + L-Glu + tRNAGln
AMP + diphosphate + Glu-tRNAGln
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
ATP + L-glutamate + tRNAGln
AMP + diphosphate + Glu-tRNAGln
ATP + L-glutamate + tRNAGln
AMP + diphosphate + glutamyl-tRNAGln
-
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + Glu-tRNAGlx
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + glutamyl-tRNAGlx
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + glutaminyl-tRNAGln
-
-
-
?
additional information
?
-
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
-
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS1 charges tRNAGln(CUG)
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS2 preferetially charges tRNAGln(UUG)
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS1 charges tRNAGln(CUG)
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS2 preferetially charges tRNAGln(UUG)
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS1 charges tRNAGln(CUG)
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS2 preferetially charges tRNAGln(UUG)
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
-
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
-
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
GluRS2
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS2 is specific solely for tRNAGln
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
GluRS2
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS2 is specific solely for tRNAGln
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS2 is specific solely for tRNAGln
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
the glutamylation ability of tRNAGln by ND-GluRS is measured in the presence of the bacterial Glu-tRNAGln amidotransferase GatCAB. Glutamylation efficiency is not affected even in the presence of excess GatCAB
-
-
?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
-
GluRS1
-
-
?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
-
GluRS1
-
-
?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
-
GluRS1
-
-
?
ATP + L-Glu + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
synthesis of Glu-tRNAGln by engineered, not natural GlnRS, overview
-
-
?
ATP + L-Glu + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
-
-
-
?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
-
the L-glutamyl-queuosine tRNAAsp synthetase, Glu-Q-RS from Escherichia coli is a paralogue of the catalytic core of glutamyl-tRNA synthetase, GluRS, that catalyzes glutamylation of queuosine in the wobble position of tRNAAsp
-
-
?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
-
the L-glutamyl-queuosine tRNAAsp synthetase, Glu-Q-RS from Escherichia coli is a paralogue of the catalytic core of glutamyl-tRNA synthetase, GluRS, that catalyzes glutamylation of queuosine in the wobble position of tRNAAsp. Activation of Glu to form Glu-AMP, the intermediate of tRNA aminoacylation, in the absence of tRNA. Glu-Q-RS transfers the activated Glu to Q34 located in the anticodon loop of the noncognate tRNAAsp. A C in position 38 is crucial for glutamylation of Q34
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
the enzyme aminoacylates tRNAGLU and tRNASGln in Bacillus subtilis and efficiently misacylates Escherichia coli tRNA1Gln in vitro
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
the enzyme efficiently charges E. coli tRNAGlu and both tRNAGlu and tRNAGln from chloroplasts, no activity with the two E. coli tRNAGln species
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
the enzyme is capable of mischarging plastidal tRNAGln from barley with glutamate as well as regularly charges the plastidal tRNAGlu from Scenedesmus. The mischarged glutamyl-tRNAGln is subsequently amidated by glutamyl-tRNA amidotransferase to form the glutaminyl-tRNAGln required for plastidal protein biosynthesis
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
activity also with Gln-RS, EC 6.1.1.18, mutant C229R
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
Thermosynechococcus vestitus
-
tRNAGln is initially mischarged with glutamate by a non-discriminating glutamyl-tRNA synthetase
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
-
the enzyme aminoacylates tRNAGlu and tRNAsGln in Bacillus subtilis and efficiently misacylates Escherichia coli tRNA1Gln in vitro, not tRNA2Gln from Escherichia coli or tRNAGlu from Escherichia coli
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
-
the enzyme interacts with the G64-C50 or G64-U50 in the Tpsi stem of its tRNA substrate
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
-
major recognition element for the enzyme is U at the 34th position of both tRNA1Gln from Bacillus subtilis and tRNA1Gln from E. coli as a modified form
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
-
the enzyme efficiently charges E. coli tRNAGlu and both tRNAGlu and tRNAGln from chloroplasts, no activity with the two E. coli tRNAGln species
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
-
the enzyme is capable of mischarging plastidal tRNAGln from barley with glutamate as well as regularly charges the plastidal tRNAGlu from Scenedesmus. The mischarged glutamyl-tRNAGln is subsequently amidated by glutamyl-tRNA amidotransferase to form the glutaminyl-tRNAGln required for plastidal protein biosynthesis
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Thermosynechococcus vestitus
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Thermosynechococcus vestitus
-
preferred tRNA substrate
-
-
?
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + Glu-tRNAGlx
-
-
-
?
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + Glu-tRNAGlx
-
the enzyme is responsible for the in vivo aminoacylation of both tRNAGlu and tRNAGln in Bacillus subtilis
-
?
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + Glu-tRNAGlx
-
the enzyme aminoacylates both tRNAGlu and tRNAGln because Rhizobium meliloti contains no glutaminyl-tRNAGln ligase
-
?
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + Glu-tRNAGlx
-
the enzyme is capable of mischarging plastidal tRNAGln from barley with glutamate as well as regularly charges the plastidal tRNAGlu from Scenedesmus. The mischarged glutamyl-tRNAGln is subsequently amidated by glutamyl-tRNA amidotransferase to form the glutaminyl-tRNAGln required for plastidal protein biosynthesis
-
?
additional information
?
-
-
Glu-Q-RS binds the noncognate amino acids L-Gln and D-Glu fourfold and sixfold, respectively, weaker than L-Glu. Despite important structural similarities, Glu-Q-RS and GluRS diverge strongly by their functional properties, selection of the cognate amino acid and by the mechanism of its activation, overview. Structural basis of the reaction mechanism, overview
-
-
?
additional information
?
-
-
ND-GluRS recognizes both tRNAGlu and tRNAGln without significantly discriminating between them, tRNA discrimination module, overview. The first point of significant distinction between the GlnRS and ND-GluRS tRNA recognition involves residues contacting the G36 nucleobase. A second distiction involves a beta-hairpin module in the CP domain
-
-
?
additional information
?
-
the glutamyl residue of Glu-tRNAGln is then transamidated by a glutamyl-tRNAGln amidotransferase (Glu-AdT) in the presence of ATP using Gln as an amide donor, producing GlntRNAGln, coupled reaction assay
-
-
?
additional information
?
-
-
the glutamyl residue of Glu-tRNAGln is then transamidated by a glutamyl-tRNAGln amidotransferase (Glu-AdT) in the presence of ATP using Gln as an amide donor, producing GlntRNAGln, coupled reaction assay
-
-
?
additional information
?
-
the non-discriminating GluRS (ND-GluRS) can glutamylate both tRNAGlu and tRNAGln
-
-
?
additional information
?
-
-
the non-discriminating GluRS (ND-GluRS) can glutamylate both tRNAGlu and tRNAGln
-
-
?
additional information
?
-
Thermosynechococcus vestitus
-
the non-discriminating enzyme charges both tRNAGlu and tRNAGln with glutamate, anticodons of tRNAGlu, 34C/UUC36, and tRNAGln, 34C/UUG36, differ only in base 36, residue Gly366 is responsible for allowing both cytosine and the bulkier purine base G36 of tRNAGln to be tolerated, glutamate recognition structure, overview
-
-
?
additional information
?
-
ND-GluRS TM1875 glutamylates both tRNAGlu and tRNAGln
-
-
?
additional information
?
-
-
ND-GluRS TM1875 glutamylates both tRNAGlu and tRNAGln
-
-
?
additional information
?
-
TM1875 glutamylates both the tRNAGlu and tRNAGln transcripts
-
-
?
additional information
?
-
-
TM1875 glutamylates both the tRNAGlu and tRNAGln transcripts
-
-
?
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ATP + L-Glu + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
-
-
-
?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
-
the L-glutamyl-queuosine tRNAAsp synthetase, Glu-Q-RS from Escherichia coli is a paralogue of the catalytic core of glutamyl-tRNA synthetase, GluRS, that catalyzes glutamylation of queuosine in the wobble position of tRNAAsp
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + glutamyl-tRNAGln
-
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + Glu-tRNAGlx
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + glutamyl-tRNAGlx
-
-
-
-
?
additional information
?
-
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
Thermosynechococcus vestitus
-
tRNAGln is initially mischarged with glutamate by a non-discriminating glutamyl-tRNA synthetase
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Thermosynechococcus vestitus
-
-
-
-
?
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + Glu-tRNAGlx
-
-
-
?
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + Glu-tRNAGlx
-
the enzyme is responsible for the in vivo aminoacylation of both tRNAGlu and tRNAGln in Bacillus subtilis
-
?
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + Glu-tRNAGlx
-
the enzyme aminoacylates both tRNAGlu and tRNAGln because Rhizobium meliloti contains no glutaminyl-tRNAGln ligase
-
?
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + Glu-tRNAGlx
-
the enzyme is capable of mischarging plastidal tRNAGln from barley with glutamate as well as regularly charges the plastidal tRNAGlu from Scenedesmus. The mischarged glutamyl-tRNAGln is subsequently amidated by glutamyl-tRNA amidotransferase to form the glutaminyl-tRNAGln required for plastidal protein biosynthesis
-
?
additional information
?
-
-
ND-GluRS recognizes both tRNAGlu and tRNAGln without significantly discriminating between them, tRNA discrimination module, overview. The first point of significant distinction between the GlnRS and ND-GluRS tRNA recognition involves residues contacting the G36 nucleobase. A second distiction involves a beta-hairpin module in the CP domain
-
-
?
additional information
?
-
the glutamyl residue of Glu-tRNAGln is then transamidated by a glutamyl-tRNAGln amidotransferase (Glu-AdT) in the presence of ATP using Gln as an amide donor, producing GlntRNAGln, coupled reaction assay
-
-
?
additional information
?
-
-
the glutamyl residue of Glu-tRNAGln is then transamidated by a glutamyl-tRNAGln amidotransferase (Glu-AdT) in the presence of ATP using Gln as an amide donor, producing GlntRNAGln, coupled reaction assay
-
-
?
additional information
?
-
ND-GluRS TM1875 glutamylates both tRNAGlu and tRNAGln
-
-
?
additional information
?
-
-
ND-GluRS TM1875 glutamylates both tRNAGlu and tRNAGln
-
-
?
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240
L-glutamate
mutant C229R GlnRS, with tRNAGln
0.21
L-glutamine
mutant C229R GlnRS, with tRNAGln
0.000038 - 0.0076
tRNAGln
additional information
additional information
-
0.62
ATP
-
recombinant hybrid GlnRS S1/L1/L2, pH not specified in the publication, temperature not specified in the publication
3.1
ATP
-
recombinant hybrid GlnRS S1/L1/L2, pH not specified in the publication, temperature not specified in the publication
5.8
L-Glu
-
recombinant hybrid GlnRS S1/L1/L2, pH not specified in the publication, temperature not specified in the publication
6.2
L-Glu
-
recombinant hybrid GlnRS S1/L1/L2, pH not specified in the publication, temperature not specified in the publication
0.000038
tRNAGln
-
recombinant hybrid GlnRS S1/L1/L2, pH not specified in the publication, temperature not specified in the publication
0.00045
tRNAGln
-
homologous tRNAGln, in absence of regulatory factor beta
0.00065
tRNAGln
-
homologous tRNAGln, in presence of regulatory factor beta
0.0037
tRNAGln
Thermosynechococcus vestitus
-
-
0.0076
tRNAGln
-
recombinant hybrid GlnRS S1/L1/L2, pH not specified in the publication, temperature not specified in the publication
0.00079
tRNAGlu
Thermosynechococcus vestitus
-
-
0.00083
tRNAGlu
-
homologous tRNAGlu, in absence of regulatory factor beta
0.0014
tRNAGlu
-
homologous tRNAGlu, in presence of regulatory factor beta
additional information
additional information
Thermosynechococcus vestitus
-
kinetics
-
additional information
additional information
-
kinetics and binding constants
-
additional information
additional information
kinetics of the mutant enzyme compared to wild-type GlnRS, EC 6.1.1.18, overview
-
additional information
additional information
-
detailed comparison of kinetic parameters between Methanothermobacter thermautotrophicus GluRSND and Escherichia coli recombinant hybrid GlnRS mutants, which are also capable of Glu-tRNAGln synthesis, overview
-
additional information
additional information
-
detailed comparison of kinetic parameters between recombinant hybrid GlnRS S1/L1/L2 and other recombinant hybrid mutant enzymes, with the naturally occurring Methanothermobacter thermautotrophicus GluRSND, which is also capable of Glu-tRNAGln synthesis, overview. Both kcat and Km for glutamate are recapitulated in the engineered enzyme, but Km for tRNA is 200fold higher
-
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GlnRS-tRNAGln complex, 6.6 mg/ml protein in 10 mM PIPES, pH 7.5, 10 mM MgCl2, and 1.8-5.4 mM tRNA. The tRNA/analog solution is then mixed with equal volumes of a 6.3 mg/ml solution of GlnRS, containing 5mM PIPES, pH 7.0, and 5 mM 2-mercaptoethanol, X-ray diffraction structure determination and analysis at 2.6 A resolution
Glu-QRS complexed to Glu, sitting drop vapour diffusion method, mixing of 0.002 ml of protein solution, containing 9.7 mg/ml protein in 20 mM Na-HEPES buffer, pH 7.2, and 50 mM NaCl, with 0.002 ml of reservoir solution containing 0.1 M Mg-acetate and Na-cacodylate buffer, pH 5.5, 0.2 M KCl, 10% polyethylene glycol 8000, and 2 mM L-Glu, a few days, X-ray diffraction structure determination and analysis at 1.5 A resolution
-
full-length ND-GluRS encompassing residues 1-552, including four cysteines and 18 methionine residues, hanging-drop method by mixing 0.001 ml of reservoir buffer containing 50 mM sodium cacodylate, pH 7.0, 50 mM calcium chloride and 8% PEG 6000, with 0.001 ml of protein solution at 20 mg/ml, 20°C, 5 days, X-ray diffraction structure determination and analysis, single-wavelength anomalous dispersion method, using sulfur anomalous dispersion, modelling
-
GluRS in complex with glutamate, hanging drop vapor diffusion at 20°C, 0.003 ml protein solution containing 3 mg/ml protein in 20 mM HEPES, pH 7.9, 20 mM NaCl, 10 mM DTT, 0.25 mM zinc acetate and 0.25 mM MgCl2, is mixed with 0.003 ml reservoir solution containing 740 mM sodium citrate, 140 mM citric acid, pH 5.8, and 10 mM DTT, 1-2 weeks, cryoprotection using 25% v/v of a 50% w/v trehalose solution, X-ray diffraction structure determination and analysis at 2.45 A resolution
Thermosynechococcus vestitus
-
the crystal structure of the Thermotoga maritima ND-GluRS, TM1875, is determined in complex with a Glu-AMP analogue at 2.0 A resolution. ND-GluRS contains a characteristic structure in the connective-peptide domain, which is inserted into the catalytic Rossmann-fold domain
TM1875 in complex with a Glu-AMP analogue, mixing of 0.0018 ml of 15 mg/ml protein in 20 mM Tris-HCl, pH 7.0, containing 5 mM MgCl2, 10 mM 2-mercaptoethanol, 50 mM NaCl, and 1 mM L-glutamylsulfamoyl adenosine, with 0.0018 ml reservoir solution containing 100 mM HEPES-NaOH, pH 7.5, 8% ethylene glycol and 15% PEG 8000, and 0.0004 ml of 30% D-sorbitol, equilibration against 0.5 ml reservoir solution, 20°C, 1 week, X-ray diffraction structure determination and analysis at 2.0 A resolution
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Schn, A.; Sll, D.
tRNA specificity of a mischarging aminoacyl-tRNA synthetase: glutamyl-tRNA synthetase from barley chloroplasts
FEBS Lett.
228
241-244
1988
Hordeum vulgare
-
brenda
Kim, S.I.; Soll, D.
Major identity element of glutamine tRNAs from Bacillus subtilis and Escherichia coli in the reaction with B. subtilis glutamyl-tRNA synthetase
Mol. Cells
8
459-465
1998
Bacillus subtilis
brenda
Vothknecht, U.C.; Doernemann, D.
Charging of both, plastidial tRNAgln and tRNAglu with glutamate and subsequent amidation of the misacylated tRNAgln by a glutamyl-tRNA amidotransferase in the unicellular green alga Scenedesmus obliquus, mutant C-2A'
Z. Naturforsch. C
50
789-795
1995
Tetradesmus obliquus
-
brenda
Freist, W.; Gauss, D.H.; Soell, D.; Lapointe, J.
Glutamyl-tRNA synthetase
Biol. Chem.
378
1313-1329
1997
Geobacillus stearothermophilus, Bacillus subtilis, Sinorhizobium meliloti
brenda
Lapointe, J.; Duplain, L.; Proulx, M.
A single glutamyl-tRNA synthetase aminoacylates tRNAGlu and tRNAGln in Bacillus subtilis and efficiently misacylates Escherichia coli tRNA1Gln in vitro
J. Bacteriol.
165
88-93
1986
Bacillus subtilis
brenda
Pelchat, M.; Lacoste, L.; Yang, F.; Lapointe, J.
Overproduction of the Bacillus subtilis glutamyl-tRNA synthetase in its host and its toxicity to Escherichia coli
Can. J. Microbiol.
44
378-381
1998
Bacillus subtilis
brenda
Nunez, H.; Lefimil, C.; Min, B.; Soll, D.; Orellana, O.
In vivo formation of glutamyl-tRNA(Gln) in Escherichia coli by heterologous glutamyl-tRNA synthetases
FEBS Lett.
557
133-135
2004
Acidithiobacillus ferrooxidans, Helicobacter pylori
brenda
Baick, J.W.; Yoon, J.H.; Namgoong, S.; Soll, D.; Kim, S.I.; Eom, S.H.; Hong, K.W.
Growth inhibition of Escherichia coli during heterologous expression of Bacillus subtilis glutamyl-tRNA synthetase that catalyzes the formation of mischarged glutamyl-tRNA1 Gln
J. Microbiol.
42
111-116
2004
Bacillus subtilis
brenda
Lee, J.; Hendrickson, T.L.
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Ito, T.; Kiyasu, N.; Matsunaga, R.; Takahashi, S.; Yokoyama, S.
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Rodriguez-Hernandez, A.; Bhaskaran, H.; Hadd, A.; Perona, J.J.
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Rampias, T.; Sheppard, K.; Soell, D.
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Methanothermobacter thermautotrophicus
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Liao, C.C.; Lin, C.H.; Chen, S.J.; Wang, C.C.
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Plasmodium falciparum (Q8IDD3), Plasmodium falciparum
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