Information on EC 6.1.1.18 - glutamine-tRNA ligase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
6.1.1.18
-
RECOMMENDED NAME
GeneOntology No.
glutamine-tRNA ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminoacylation
esterification
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tRNA charging
-
-
Aminoacyl-tRNA biosynthesis
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamine:tRNAGln ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9075-59-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae ATCC 204508 / S288c
-
UniProt
Manually annotated by BRENDA team
Toxoplasma gondii ATCC 50611 / Me49
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
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 + glutamyl-tRNAGln
show the reaction diagram
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-glutamine + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
show the reaction diagram
-
-
-
-
?
ATP + L-glutamine + tRNAGln(CUG)
AMP + diphosphate + L-glutaminyl-tRNAGln(CUG)
show the reaction diagram
-
-
-
?
ATP + L-glutamine + tRNAGln(UUG)
AMP + diphosphate + L-glutaminyl-tRNAGln(UUG)
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + glutamyl-tRNAGln
show the reaction diagram
P00962
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
show the reaction diagram
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutamyl-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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-Methyleneglutamine
-
-
5'-O-[N-(L-glutaminyl)sulfamoyl] adenosine
5,5'-dithiobis(2-nitrobenzoate)
-
-
Br-
-
0.1 M, 50% inhibition
Cl-
-
0.2 M, 50% inhibition
Glu-AMS
-
-
Glutamic acid 4-hydroxamate
-
-
glutaminol adenylate
-
; competitive to glutamine
glutaminol adenylate methyl phosphate ester
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; competitive to glutamine
glutaminyl-beta-ketophosphonate-adenosine
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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
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i.e. Glu-KPA, competitive inhibition, non-cognate, binds weakly at one site on the monomeric enzyme
I-
-
0.06 M, 50% inhibition
L-Glutamic acid
-
competitive inhibition of the wild-type and mutant enzymes
p-hydroxymercuribenzoate
-
-
S-Carbamoylcysteine
-
-
S-Carbamoylserine
-
-
tRNA
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above 0.6 mg/ml
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
putrescine
-
can partially replace Mg2+ in activation, with 32% efficiency
spermidine
-
can partially replace Mg2+ in activation, with 12% efficiency
spermine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.038 - 660
ATP
0.028 - 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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016 - 6.27
ATP
0.00041 - 0.046
L-glutamate
0.0025 - 6.08
L-glutamine
0.002 - 3.3
tRNAGln
additional information
ATP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.824
L-glutamine
-
pH and temperature not specified in the publication
0.118 - 7368.4
tRNAGln
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
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versus glutamine
0.65
glutaminyl-beta-ketophosphonate-adenosine
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pH 7.2, 37C, versus L-glutamine
2.8
glutamyl-beta-ketophosphonate-adenosine
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pH 7.2, 37C, versus L-glutamine
17 - 96
L-Glutamic acid
additional information
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00024 - 0.00033
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recombinant mutant Y57H/R515W enzyme in crude cell extract, pH 7.5, 37C
0.00028
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recombinant mutant G45V/R403W enzyme in crude cell extract, pH 7.5, 37C
0.00041
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recombinant mutant G45V enzyme in crude cell extract, pH 7.5, 37C
0.00051
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recombinant mutant R515W enzyme in crude cell extract, pH 7.5, 37C
0.00058
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recombinant mutant Y57H enzyme in crude cell extract, pH 7.5, 37C
0.00079 - 0.00083
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recombinant wild-type enzyme in crude cell extract, pH 7.5, 37C
0.1074
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
-
ATP-diphosphate exchange
7
-
assay at
8.5
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aminoacylation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature; assay at room temperature
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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of seedlings
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
additional information
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QARS is highly expressed in the developing fetal human cerebral cortex in many cell types
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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mainly
Manually annotated by BRENDA team
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enzyme DNA sequence contains a lysine-rich nuclear targeting sequence motif
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Escherichia coli (strain B / BL21-DE3)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
-
1 * 64000
64200
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1 * 64200, recombinant His6-tagged GlnRS, SDS-PAGE
64500
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1 * 64500, SDS-PAGE
65400 - 71200
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sucrose density gradient sedimentation
68500
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electrophoresis of the native enzyme in polyacrylamide gels of various concentrations
69000
-
1 * 69000, SDS-PAGE
89100
-
x * 89100, small-angle X-ray scattering
91000
-
1 * 91000, SDS-PAGE
93100
-
x * 93100, calculated from amino acid sequence
138000
-
gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant full-length GlnRS grown in microbatch in the presence of PEG 3350, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement
vapour-diffusion method. Orthorombic crystals are obtained that belong to space group P2(1)2(1)2(1) and diffract to 2.3 A resolution
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2.5 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
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2.8 A resolution; structure of the enzyme with its cognate glutaminyl-tRNA and ATP
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analysis of the crystal structure of GlnRS-tRNAGln complex bound to the glutaminyl adenylate analogue 5'-O-[N-(L-Gln)sulfamoyl] adenosine
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cocrystallization of the purified enzyme with tRNAGln and inhibitor QSI, X-ray diffraction structure determination at 2.4 A resolution and analysis
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crystal structure of three misacylating mutants of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNAGln and ATP
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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
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detailed structural comparison between Met-tRNA synthetase and Gln-tRNA synthetase
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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; 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
purified multisynthetase complex (MSC) subcomplex comprising ArgRS, glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)/p43, X-ray diffraction structure determination and analysis
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purified recombinant His-tagged wild-type and mutant enzymes, sitting drop vapour diffusion method, apo wild-type GlnRS crystallizes from 0.1 M calcium acetate, 0.1 M Tris, pH 6.0, 12.5% w/v PEG 3350, and 60 mM Gly-Gly-Gly, the Y57H mutant crystallizes from 0.1 M ammonium acetate, 0.1 M Bis-Tris, pH 5.5, and 17% w/v PEG 10 000, and the G45V mutant crystallizes from 0.15 M ammonium acetate, 0.1 M Bis-Tris, pH 5.5, 3% w/v PEG 20 000, and 10 mM EDTA, 16C, X-ray diffraction strutcure determination and analysis at 2.4 A, 3.3 A, and 2.7 A resolution, respectively
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microbatch-under-oil method, using 50 mM NH4Br, 50 mM KC2H3O2, 100 mM HEPES (pH 7.5), and 20% (w/v) polyethylene glycol 20000
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purified recombinant His-tagged N-terminal and C-terminal domain fragments, sitting drop vapour diffusion method, mixing of 20 mg/ml protein in 25 mM Tris pH 7.5, 150 mM KCl, and 10 mM MgCl2, with 2 M ammonium sulfate, 5% isopropanol for the N-terminal fragment and 2 M ammonium sulfate for the C-terminal fragment, X-ray diffraction structure determination and analysis. No crystallization conditions can be identified for the full-length protein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
strain KL301 enzyme is stable, temperature-sensitive mutant enzyme loses about 70% of its activity
47.5
-
melting temperature of the recombinant wild-type enzyme
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 20 mM potassium phosphate, pH 7.5, 50 mM KCl, 1 mM DTT, 50% glycerol, stable for 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
IgG Sepharose column chromatography and Superdex HiLoad 16/60 gel filtration
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Ni-NTA agarose column chromatography
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recombinant His-tagged chimeric mutant enzyme from strain BL21(DE3) or the temperature sensitive strain JP1449(DE3) by nickel affinity chromatography
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recombinant His-tagged GlnRS mutants from strain BL21-DE3 by nickel affinity chromatography
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography and dialysis
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain Rosetta (DE3)pLysS by nickel affinity chromatography and gel filtration
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recombinant His6-tagged wild-type full-length enzyme and truncated mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration, optimization of purification conditions
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, enzyme contains a N-terminal lysine-rich sequence KPKKKKEK, that may function as a nuclear targetng signal as well as in regulation of gene expression, since the 8 amino acid peptide derived from the motif interacts with DNA and changes the DNA molecule form from B to Z form
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Saccharomyces cerevisiae strain BCY123
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expression of full length and C-terminal truncated GlnRS, lacking the the Yqey domain, and of the isolated Yqey protein, in Escherichia coli strain ER2566
expression of His-tagged GlnRS mutants in strain BL21-DE3
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expression of the His-tagged chimeric mutant enzyme in Escherichia coli strain BL21(DE3) or the temperature sensitive strain JP1449(DE3)
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gene GLN4, phylogenetic analysis
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gene glnS, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21
gene QARS, genotyping, recombinant expression of codon-optimized His-tagged wild-type and mutant enzymes in Escherichia coli
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gene QARS, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta (DE3)pLysS
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overexpression in Escherichia coli
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overexpression of various Myc-tagged enzyme mutants in human embryonic kidney 293 cells
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recombinant expression of His6-tagged wild-type full-length enzyme and truncated mutant enzymes in Escherichia coli strain BL21(DE3), optimization of expression conditions
recombinant expression of the enzyme in Escherichia coli
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the vector pET28a is used, Escherichia coli JP1449DE3 cells are used
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transient expression of the p.Lys496stop mutant in neuroblastoma 2A cells reveals diminished and aberrantly aggregated expression
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A29X
-
site-directed mutagenesis
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
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
D486R/L488Q
-
the double mutant causes a relaxed tRNA anticodon specificity
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
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
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
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
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
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
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
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
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
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
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
Y240G
-
site-directed mutagenesis, active site mutant, 3fold improved glutamic acid recognition in vitro, partial complementation of an enzyme-deficient strain
G45V/R403W
-
naturally occuring mutation involved in progressive microcephaly, severe seizures in infancy, atrophy of the cerebral cortex and cerebellar vermis, and mild atrophy of the cerebellar hemispheres, the mutant shows a highly reduced aminoacylation activity, heterozygous mutations
H175A
-
the mutant shows reduced activity compared to the wild-type
K496stop
-
naturally occuring mutation involved in early-onset epileptic encephalopathy (EOEE), heterozygous mutation leading to a deletion of part of the catalytic domain and the entire anticodon-binding domain, a loss-of-function mutant
Y57H/R515W
-
occuring mutation involved in progressive microcephaly, severe seizures in infancy, atrophy of the cerebral cortex and cerebellar vermis, and mild atrophy of the cerebellar hemispheres, the mutant shows a highly reduced aminoacylation activity, heterozygous mutations
additional information
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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