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Information on EC 6.1.1.18 - glutamine-tRNA ligase and Organism(s) Escherichia coli and UniProt Accession P00962

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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
glnrs, glutaminyl trna synthetase, class i glutaminyl-trna synthetase, glutaminyl-transfer rna synthetase, cytosolic glutaminyl-trna synthetase, glutamyl/glutaminyl-trna synthetase, l-glutamine:trnagln ligase (amp-forming), more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
class I glutaminyl-tRNA synthetase
-
Glutaminyl-tRNA synthetase
-
glutaminyltRNA synthetase
-
GlnRS
Glutamine translase
-
-
-
-
Glutamine--tRNA ligase
-
-
-
-
Glutamine-tRNA synthetase
-
-
-
-
Glutaminyl-transfer ribonucleate synthetase
-
-
-
-
Glutaminyl-transfer RNA synthetase
-
-
-
-
Glutaminyl-tRNA synthetase
Synthetase, glutaminyl-transfer ribonucleate
-
-
-
-
Vegetative specific protein H4
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln
show the reaction diagram
aminoacylation reaction mechanism, substrate binding sites, Tyr211 and a water molecule are responsible for recognition of both hydrogen atoms of the nitrogen of glutamine sidechain, which is esstial for substrate recognition
ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
Aminoacylation
-
esterification
Aminoacylation
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamine:tRNAGln ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9075-59-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
show the reaction diagram
primary binding pocket structure, overview
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
show the reaction diagram
ATP + L-glutamate + tRNAGln
AMP + diphosphate + glutamyl-tRNAGln
show the reaction diagram
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
show the reaction diagram
ATP + L-glutamine + tRNAGln in unfractionated tRNA
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
show the reaction diagram
ATP + L-glutamate + tRNAGln
AMP + diphosphate + glutamyl-tRNAGln
show the reaction diagram
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
can partially replace Mg2+ in activation of ATP-diphosphate exchange
Mn2+
-
can replace Mg2+ in activation of aminoacylation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-O-[N-(L-glutaminyl)sulfamoyl] adenosine
glutaminol adenylate
-
-
glutaminol adenylate methyl phosphate ester
-
-
5'-O-[N-(L-glutaminyl)sulfamoyl] adenosine
-
i.e. QSI, competitive to glutamine
5,5'-dithiobis(2-nitrobenzoate)
-
-
Glu-AMS
-
-
glutaminol adenylate
-
competitive to glutamine
glutaminol adenylate methyl phosphate ester
-
competitive to glutamine
glutaminyl-beta-ketophosphonate-adenosine
-
i.e. Gln-KPA, selective, competitive inhibition of GlnRS, contrast, Gln-KPA inhibits GlnRS by binding competitively but weakly at two distinct sites on the enzyme, the glutamine and the AMP modules of Gln-KPA, connected by the beta-ketophosphonate linker, cannot bind GlnRS simultaneously, and that one Gln-KPA molecule binds the AMP-binding site of GlnRS through its AMP module, whereas another Gln-KPA molecule binds the glutamine-binding site through its glutamine module, mechanism, overview
glutamyl-beta-ketophosphonate-adenosine
-
i.e. Glu-KPA, competitive inhibition, non-cognate, binds weakly at one site on the monomeric enzyme
L-Glutamic acid
-
competitive inhibition of the wild-type and mutant enzymes
p-hydroxymercuribenzoate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
spermine
-
significant stimulation of ATP-diphosphate exchange and aminoacylation in presence of limited MgCl2 concentrations, cannot totally replace Mg2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26
L-glutamine
pH 7.5, 22Ā°C, wild-type enzyme
0.04 - 660
ATP
0.11 - 17.8
Gln
240
L-glutamate
mutant C229R GlnRS, with tRNAGln
0.05 - 46.3
L-glutamine
0.000019 - 0.31
tRNAGln
0.0001
tRNAGln in unfractionated tRNA
-
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.94
ATP
0.046
L-glutamate
pH 7.5, 22Ā°C, wild-type enzyme
2.94 - 6.08
L-glutamine
0.016 - 6.27
ATP
0.00041
L-glutamate
mutant C229R GlnRS, with tRNAGln
0.0025 - 4.7
L-glutamine
3.3
tRNAGln
-
-
additional information
ATP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0013
5'-O-[N-(L-glutaminyl)sulfamoyl] adenosine
0.00028
glutaminol adenylate
-
versus glutamine
0.01
glutaminol adenylate methyl phosphate ester
-
versus glutamine
0.65
glutaminyl-beta-ketophosphonate-adenosine
-
pH 7.2, 37Ā°C, versus L-glutamine
2.8
glutamyl-beta-ketophosphonate-adenosine
-
pH 7.2, 37Ā°C, versus L-glutamine
17 - 96
L-Glutamic acid
additional information
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1074
-
-
additional information
-
activities of recombinant mutant enzymes
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
6.2
-
ATP-diphosphate exchange
8.5
-
aminoacylation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
22
assay at room temperature
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the class I aminoacyl-tRNA synthetase family
evolution
-
the architecture of the GlnRS RNP has differentiated over evolutionary time to maintain glutamine-binding affinity at a weak level, and provides strong evidence for long-distance communication
physiological function
-
negative allosteric coupling plays a key role in enforcing the selective RNA-amino acid pairing at the heart of the genetic code
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
-
1 * 64000
64200
-
1 * 64200, recombinant His6-tagged GlnRS, SDS-PAGE
64500
-
1 * 64500, SDS-PAGE
65400 - 71200
-
sucrose density gradient sedimentation
68500
-
electrophoresis of the native enzyme in polyacrylamide gels of various concentrations
69000
-
1 * 69000, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cocrystallization of the purified enzyme with tRNAGln and inhibitor QSI, X-ray diffraction structure determination at 2.4 A resolution and analysis
purified recombinant GlnRS C229R-tRNAGln complex, a protein solution containing 6.3mg/ml GlnRS prepared in 5 mM PIPES, pH 7.0, 5 mM 2-mercaptoethanol, is mixed with the tRNAGln solution, X-ray diffraction structure determination and analysis at 2.6 A resolution
2.5 A resolution
-
2.8 A resolution
-
analysis of the crystal structure of GlnRS-tRNAGln complex bound to the glutaminyl adenylate analogue 5'-O-[N-(L-Gln)sulfamoyl] adenosine
-
crystal structure of three misacylating mutants of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNAGln and ATP
-
crystals of the GlnRS-tRNA(2'H)Gln complex bound to the ATP analog AMPCPP and glutamine are grown by microseeding with crystals of the GlnRS-tRNAGln-ATP ternary complex. Crystals grew in 1-2 weeks by vapor diffusion over a reservoir containing 2 M ammonium sulfate, 10 mM Pipes, pH 7.5, 10 mM MgCl2 and 2 mM DTT
-
detailed structural comparison between Met-tRNA synthetase and Gln-tRNA synthetase
-
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
structure of the enzyme with its cognate glutaminyl-tRNA and ATP
-
the entire anticodon loop provides essential sites for glutaminyl tRNA synthetase discrimination among tRNA molecules
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C229R
site-directed mutagenesis, transplanting the conserved arginine residue from glutamyl-tRNA synthetase, EC 6.1.1.17, to glutaminyltRNA synthetase improves the KM of GlnRS for noncognate glutamate
C229R/Q255I
site-directed mutagenesis, comparison of mutant activity with glutamate and glutamine to charge tRNAGln to the wild-type activity, the mutant shows no activity with L-Gln, but weakly with L-Glu
C229R/Q255I/S227A/F233Y
site-directed mutagenesis, comparison of mutant activity with glutamate and glutamine to charge tRNAGln to the wild-type activity, the mutant shows no activity with L-Gln, but activity with L-Glu
D486R/L488Q
the double mutant causes a relaxed tRNA anticodon specificity
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
E222K
site-directed mutagenesis, mutational structure-function study, the residue is part of the invariant Hub, the mutation leads to mischarging and affected cognate tRNAGln recognition
F90L
site-directed mutagenesis, mutational structure-function study, the residue is part of the connection in the active site network, the mutant shows increased Glu recognition in vitro and in vivo
Q255I
site-directed mutagenesis, mutational structure-function study, the residue is part of the invariant Hub, the mutation leads to reduced specificity for cognate Gln recognition and increased Glu recognition
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
R30A
site-directed mutagenesis, comparison of mutant activity with glutamate and glutamine to charge tRNAGln to the wild-type activity, the mutant shows no activity with L-Glu
R30K
site-directed mutagenesis, comparison of mutant activity with glutamate and glutamine to charge tRNAGln to the wild-type activity, the mutant shows weak activity with L-Glu
R341A
site-directed mutagenesis, mutational structure-function study, the residue is part of the Hub common to all liganded complex, the mutation affects anticodon recognition
Y211H
site-directed mutagenesis, mutational structure-function study, the residue is part of the connection in the quaternary cognate-complex, the mutants shows slow solvation dynamics in the active site
Y240E/G
site-directed mutagenesis, mutational structure-function study, the residue is part of the Hub common to ligand-free and quaternary cognate-complex, the mutant shows increased Glu recognition in vitro and in vivo
A29X
-
site-directed mutagenesis
cGluGlnRS
-
a chimeric protein, consisting of the catalytic domain of GluRS and the anticodon-binding domain of GlnRS, is constructed
D235A
-
saturation mutagenesis, only little complementation of glnS-deficient strain
D66E
-
saturation mutagenesis, 18fold increased Km for glutamine, decreased turnover
D66F
-
saturation mutagenesis, highly increased Km for glutamine, 1200fold decrease in activity
D66G
-
saturation mutagenesis, only little complementation of glnS-deficient strain
D66H
-
saturation mutagenesis, only little complementation of glnS-deficient strain
D66R
-
saturation mutagenesis, only little complementation of glnS-deficient strain
E323A
-
site-directed mutagenesis, the mutation produces small but consistent 2 to 3fold improvements in glutamine-binding affinity compared to the wild-type enzyme
E34A
-
site-directed mutagenesis, the mutant shows highly increased Km and reduced kcat and activity compared to the wild-type enzyme
E34D
-
site-directed mutagenesis, the mutant shows highly increased Km and reduced kcat and activity compared to the wild-type enzyme
E34Q
-
site-directed mutagenesis, the mutant shows highly increased Km and reduced kcat and activity compared to the wild-type enzyme
E73A
-
site-directed mutagenesis, the mutant shows highly increased Km and reduced kcat and activity compared to the wild-type enzyme
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
F233D
-
saturation mutagenesis, highly increased Km for glutamine, 3700fold decrease in activity
F233L
-
saturation mutagenesis, 19fold increased Km for glutamine, decreased turnover
F233Y
-
saturation mutagenesis, increased Km for glutamine, increased turnover
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
K194A
-
site-directed mutagenesis, the mutation perturbs the dissociation constant in ATP binding
K401A
-
site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme
L136A
-
site-directed mutagenesis, the mutation perturbs the dissociation constant in ATP binding
N320A
-
site-directed mutagenesis, the mutation produces small but consistent 2 to 3fold improvements in glutamine-binding affinity compared to the wild-type enzyme
N336A
-
site-directed mutagenesis, the mutation removes contact with the ribose at U38, but does not significantly influence glutamine affinity
N370A
-
site-directed mutagenesis, the mutation removes contact with the base of U38, but does not significantly influence glutamine affinity
Q318A
-
site-directed mutagenesis, the mutation produces small but consistent 2 to 3fold improvements in glutamine-binding affinity compared to the wild-type enzyme
Q517A
-
site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme
R341A
R410A
-
site-directed mutagenesis, the mutation removes contact with the base of C34, but does not significantly influence glutamine affinity
R520A
-
site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme
R545A
-
site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme
T316A
-
site-directed mutagenesis, the mutation produces small but consistent 2 to 3fold improvements in glutamine-binding affinity compared to the wild-type enzyme
T547A
-
site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme
Y211F
-
saturation mutagenesis, 60fold increased Km for glutamine, decreased turnover
Y211F/F233Y
-
saturation mutagenesis, increased Km for glutamine, about 6fold decreased activity
Y211G
-
saturation mutagenesis, only little complementation of glnS-deficient strain
Y211L
-
saturation mutagenesis, unaffected Km for glutamine, decreased turnover
Y211S
-
saturation mutagenesis, 1700fold decrease in activity
Y240E
-
site-directed mutagenesis, active site mutant, 5fold improved glutamic acid recognition in vitro, partial complementation of an enzyme-deficient strain
Y240G
-
site-directed mutagenesis, active site mutant, 3fold improved glutamic acid recognition in vitro, partial complementation of an enzyme-deficient strain
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
strain KL301 enzyme is stable, temperature-sensitive mutant enzyme loses about 70% of its activity
additional information
-
several noncognate tRNAs protect the enzyme against thermal inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20Ā°C, 20 mM potassium phosphate, pH 7.5, 50 mM KCl, 1 mM DTT, 50% glycerol, stable for 6 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21
recombinant His-tagged chimeric mutant enzyme from strain BL21(DE3) or the temperature sensitive strain JP1449(DE3) by nickel affinity chromatography
-
recombinant His-tagged GlnRS mutants from strain BL21-DE3 by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
gene glnS, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21
expression of His-tagged GlnRS mutants in strain BL21-DE3
-
expression of the His-tagged chimeric mutant enzyme in Escherichia coli strain BL21(DE3) or the temperature sensitive strain JP1449(DE3)
-
the vector pET28a is used, Escherichia coli JP1449DE3 cells are used
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
urea induces equilibrium denaturation of glutaminyl-tRNA synthetase, existence of a stable intermediate state at around 2 M urea, existence of an induced molten globule state in a large multidomain protein which is separated from the native and the denatured protein by high activation energy barriers
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rould, M.A.; Perona, J.J.; Söll, D.; Steitz, T.A.
Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNAGln and ATP at 2.8 A resolution
Science
246
1135-1142
1989
Escherichia coli
Manually annotated by BRENDA team
Conley, J.; Sherman, J.; Thomann, H.U.; Söll, D.
Domains of E. coli glutaminyl-tRNA synthetase disordered in the crystal structure are essential for function or stability
Nucleosides Nucleotides
13
1581-1595
1994
Escherichia coli
-
Manually annotated by BRENDA team
Thomann, H.U.; Ibba, M.; Hong, K.W.; Söll, D.
Homologous expression and purification of mutants of an essential protein by reverse epitope-tagging
Bio/Technology
14
50-55
1996
Escherichia coli
Manually annotated by BRENDA team
Rogers, M.J.; Weygand-Durasevic, I.; Schwob, E.; Sherman, J.M.; Rogers, K.C.; Adachi, T.; Inokuchi, H.; Söll, D.
Selectivity and specificity in the recognition of tRNA by E. coli glutaminyl-tRNA synthetase
Biochimie
75
1083-1090
1993
Escherichia coli
Manually annotated by BRENDA team
Perona, J.J.; Rould, M.A.; Steitz, T.A.; Risler, J.L.; Zelwer, C.; Brunie, S.
Structural similarities in glutaminyl- and methionyl-tRNA synthetases suggest a common overall orientation of tRNA binding
Proc. Natl. Acad. Sci. USA
88
2903-2907
1991
Escherichia coli
Manually annotated by BRENDA team
Rould, M.A.; Perona, J.J.; Steitz, T.A.
Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase
Nature
352
213-218
1991
Escherichia coli
Manually annotated by BRENDA team
Bhattacharyya, T.; Bhattacharyya, A.; Roy, S.
A fluorescence spectroscopic study of glutaminyl-tRNA synthetase from Escherichia coli and its implications for the enzyme mechanism
Eur. J. Biochem.
200
739-745
1991
Escherichia coli
Manually annotated by BRENDA team
Das, B.K.; Bhattacharyya, T.; Roy, S.
Characterization of a urea induced molten globule intermediate state of glutaminyl-tRNA synthetase from Escherichia coli
Biochemistry
34
5242-5247
1995
Escherichia coli
Manually annotated by BRENDA team
Arnez, J.G.; Steitz, T.A.
Crystal structures of three misacylating mutants of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNAGln and ATP
Biochemistry
35
14725-14733
1996
Escherichia coli
Manually annotated by BRENDA team
Körner, A.; Magee, B.B.; Liska, B.; Low, K.B.; Adelberg, E.A.; Söll, D.
Isolation and partial characterization of a temperature-sensitive Escherichia coli mutant with altered glutaminyl-transfer ribonucleic acid synthetase
J. Bacteriol.
120
154-158
1974
Escherichia coli
Manually annotated by BRENDA team
Seno, T.; Nakamura, A.; Fukuhara, S.; Iwata, K.
Interaction of Escherichia coli glutaminyl-tRNA synthetase with noncognate tRNA's
Nucleic Acids Res.
5
1561-1570
1978
Escherichia coli
Manually annotated by BRENDA team
Kern, D.; Potier, S.; Lapointe, J.; Boulanger, Y.
The glutaminyl-transfer RNA synthetase of Escherichia coli. Purification, structure and function relationship
Biochim. Biophys. Acta
607
65-80
1980
Escherichia coli
Manually annotated by BRENDA team
Yamao, F.; Inokuchi, H.; Cheung, A.; Ozeki, H.; Söll, D.
Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene
J. Biol. Chem.
257
11639-11643
1982
Escherichia coli
Manually annotated by BRENDA team
Hoben, P.; Royal, N.; Cheung, A.; Yamao, F.; Biemann, K.; Söll, D.
Escherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product
J. Biol. Chem.
257
11644-11650
1982
Escherichia coli
Manually annotated by BRENDA team
Hoben, P.; Söll, D.
Glutaminyl-tRNA synthetase of Escherichia coli
Methods Enzymol.
113
55-59
1985
Escherichia coli
Manually annotated by BRENDA team
Liu, J.; Ibba, M.; Hong, K.W.; Soll, D.
The terminal adenosine of tRNA(Gln) mediates tRNA-dependent amino acid recognition by glutaminyl-tRNA synthetase
Biochemistry
37
9836-9842
1998
Escherichia coli
Manually annotated by BRENDA team
Bernier, S.; Dubois, D.Y.; Therrien, M.; Lapointe, J.; Chenevert, R.
Synthesis of glutaminyl adenylate analogues that are inhibitors of glutaminyl-tRNA synthetase
Bioorg. Med. Chem. Lett.
10
2441-2444
2000
Escherichia coli
Manually annotated by BRENDA team
Hong, K.W.; Ibba, M.; Soll, D.
Retracing the evolution of amino acid specificity in glutaminyl-tRNA synthetase
FEBS Lett.
434
149-154
1998
Escherichia coli
Manually annotated by BRENDA team
Mandal, A.K.; Bhattacharyya, A.; Bhattacharyya, S.; Bhattacharyya, T.; Roy, S.
A cognate tRNA specific conformational change in glutaminyl-tRNA synthetase and its implication for specificity
Protein Sci.
7
1046-1051
1998
Escherichia coli
Manually annotated by BRENDA team
Rath, V.L.; Silvian, L.F.; Beijer, B.; Sproat, B.S.; Steitz, T.A.
How glutaminyl-tRNA synthetase selects glutamine
Structure
6
439-449
1998
Escherichia coli (P00962)
Manually annotated by BRENDA team
Gruic-Sovulj, I.; Uter, N.; Bullock, T.; Perona, J.J.
tRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting class I aminoacyl-tRNA synthetase
J. Biol. Chem.
280
23978-23986
2005
Escherichia coli
Manually annotated by BRENDA team
Green, D.F.; Tidor, B.
Escherichia coli glutaminyl-tRNA synthetase is electrostatically optimized for binding of its cognate substrates
J. Mol. Biol.
342
435-452
2004
Escherichia coli
Manually annotated by BRENDA team
Uter, N.T.; Perona, J.J.
Long-range intramolecular signaling in a tRNA synthetase complex revealed by pre-steady-state kinetics
Proc. Natl. Acad. Sci. USA
101
14396-14401
2004
Escherichia coli
Manually annotated by BRENDA team
Uter, N.T.; Perona, J.J.
Active-site assembly in glutaminyl-tRNA synthetase by tRNA-mediated induced fit
Biochemistry
45
6858-6865
2006
Escherichia coli
Manually annotated by BRENDA team
Balg, C.; Blais, S.P.; Bernier, S.; Huot, J.L.; Couture, M.; Lapointe, J.; Chenevert, R.
Synthesis of beta-ketophosphonate analogs of glutamyl and glutaminyl adenylate, and selective inhibition of the corresponding bacterial aminoacyl-tRNA synthetases
Bioorg. Med. Chem.
15
295-304
2007
Escherichia coli
Manually annotated by BRENDA team
Yamasaki, S.; Nakamura, S.; Terada, T.; Shimizu, K.
Mechanism of the difference in the binding affinity of E. coli tRNAGln to glutaminyl-tRNA synthetase caused by noninterface nucleotides in variable loop
Biophys. J.
92
192-200
2007
Escherichia coli (P00962)
Manually annotated by BRENDA team
Sathyapriya, R.; Vishveshwara, S.
Structure networks of E. coli glutaminyl-tRNA synthetase: effects of ligand binding
Proteins
68
541-550
2007
Escherichia coli (P00962), Escherichia coli
Manually annotated by BRENDA team
Saha, R.; Dasgupta, S.; Basu, G.; Roy, S.
A chimeric glutamyl: glutaminyl-tRNA synthetase: implications for evolution
Biochem. J.
15
449-455
2008
Escherichia coli
Manually annotated by BRENDA team
Bullock, T.L.; Rodriguez-Hernandez, A.; Corigliano, E.M.; Perona, J.J.
A rationally engineered misacylating aminoacyl-tRNA synthetase
Proc. Natl. Acad. Sci. USA
105
7428-7433
2008
Escherichia coli, Escherichia coli (P00962)
Manually annotated by BRENDA team
Dasgupta, S.; Saha, R.; Dey, C.; Banerjee, R.; Roy, S.; Basu, G.
The role of the catalytic domain of E. coli GluRS in tRNAGln discrimination
FEBS Lett.
583
2114-2120
2009
Escherichia coli
Manually annotated by BRENDA team
Rodriguez-Hernandez, A.; Perona, J.J.
Heat maps for intramolecular communication in an RNP enzyme encoding glutamine
Structure
19
386-396
2011
Escherichia coli
Manually annotated by BRENDA team
Saha, R.; Dasgupta, S.; Banerjee, R.; Mitra-Bhattacharyya, A.; Soell, D.; Basu, G.; Roy, S.
A functional loop spanning distant domains of glutaminyl-tRNA synthetase also stabilizes a molten globule state
Biochemistry
51
4429-4437
2012
Escherichia coli (P00962)
Manually annotated by BRENDA team
Druart, K.; Guennec, M.L.; Palmai, Z.; Simonson, T.
Probing the stereospecificity of tyrosyl- and glutaminyl-tRNA synthetase with molecular dynamics
J. Mol. Graph. Model.
71
192-199
2017
Escherichia coli (P00962), Escherichia coli
Manually annotated by BRENDA team