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Information on EC 6.1.1.17 - glutamate-tRNA ligase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P46655

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Saccharomyces cerevisiae
UNIPROT: P46655 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
glurs, glutaminyl-trna synthetase, glutamyl-trna synthetase, glurs2, trna modifying enzyme, glurs1, glutamyl trna synthetase, discriminating glurs, glursat, glutamate-trna synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
discriminating GluRS
-
Glutamyl-tRNA synthetase
-
glutamyl-tRNAsynthetase
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GluRS
-
-
-
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Glutamate--tRNA ligase
-
-
-
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Glutamate-tRNA synthetase
-
-
-
-
Glutamic acid translase
-
-
-
-
Glutamic acid tRNA ligase
-
-
-
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Glutamyl tRNA synthetase
-
-
-
-
Glutamyl-transfer ribonucleate synthetase
-
-
-
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Glutamyl-transfer ribonucleic acid synthetase
-
-
-
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Glutamyl-transfer RNA synthetase
-
-
-
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Glutamyl-tRNA synthetase
-
-
-
-
P85
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
-
Aminoacylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:tRNAGlu ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9068-76-2
-
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 + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
show the reaction diagram
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
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-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Arc1p
-
Arc1p-N
residues 1-122 of Arc1p, recombinantly expressed, the GluRS-N–Arc1p-N complex represents an unusual mode of interaction
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Arc1p
-
protein from Aspergillus fumigatus, Accession code Q4QTS4, mediates stimulation of tRNA glutamylation
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Cytoplasmic protein Arc1p
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forms a complex with glutamyl-tRNA synthetase, facilitates the delivery of tRNA molecules to the Arc1p-associated aminoacyl-tRNA synthetase
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
L-glutamate
pH and temperature not specified in the publication
0.0012
tRNAGlu
pH and temperature not specified in the publication
0.00045
tRNAGlu
-
in presence of the GluRS-Arc1p complex
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
L-glutamate
pH and temperature not specified in the publication
1.5
tRNAGlu
pH and temperature not specified in the publication
0.016
tRNAGlu
-
in presence of the GluRS-Arc1p complex
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.824
L-glutamate
pH and temperature not specified in the publication
1250
tRNAGlu
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme evolved by gene duplication in early eukaryotes from a nondiscriminating glutamyl-tRNAsynthetase (GluRSND, EC 6.1.1.24) that aminoacylates both tRNAGln and tRNAGlu with glutamate. This ancient GluRS also separately differentiated to exclude tRNAGln as a substrate, and the resulting discriminating GluRS and GlnRS further acquired additional protein domains assisting function in cis (the GlnRS N-terminal Yqey domain) or in trans (the Arc1p protein associating with GluRS), evolutionary modeling, detailed overview. These added domains are absent in contemporary bacterial GlnRS and GluRS. The eukaryote-specific protein domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA. Eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions and aremutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating GluRS to GlnRS. The added eukaryotic domains arose in response to distinctive selective pressures associated with the greater complexity of the eukaryotic translational apparatus. The affinity of GluRS for glutamate is significantly increased when Arc1p is not associated with the enzyme. GluRS and GlnRS are among just four aaRS families (the others are arginyl-tRNA synthetase and class I LysRS) that require the presence of tRNA for synthesis of the aminoacyl adenylate reaction intermediate. Each cytoplasmic GlxRS-tRNA pair has fully lost the ancestral nondiscriminating activity in the course of coevolution, and the more stringent specificities of Saccharomyces cerevisiae GlnRS and GluRS arise from the conserved catalytic portions of each enzyme
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant GluRS-N-Arc1p-N complex, hanging drop vapour diffusion method, 0.002 ml protein solution containing 15 mg/ml protein in 20 mM HEPES, 150 mM NaCl, 5 mM MgCl2, 1 mM DTT, pH 7.2 with NaOH, is mixed with 0.002 ml reservoir solution containing 30-35% PEG 3350, 300-500 mM NaSCN, X-ray diffraction structure determination and analysis at 2.05 A resolution
purified recombinant truncated enzyme, 0.002 ml of 20 mg/ml protein in 20 mM HEPES, 150 mM NaCl, 5 mM MgCl2, 1 mM DTT, pH 7.2 with NaOH, mixed with 0.002 ml reservoir solution at 20°C, equilibration against 0.075 ml reservoir solution, containing 1.7-1.8 M (NH4)2SO4, 200 mM KSCN for selenomethionine-substituted crystals and 1.8-1.9 M (NH4)2SO4, 200 mM NaI for native crystals, dispersion with selenomethionine, X-ray diffraction structure determination and analysis at 2.5 A resolution, modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged GluRS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant His6-tagged GluRS-N from Escherichia coli strain BL21(DE3) to homogeneity by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His6-tagged GluRS-N, comprising residues 1-197, 17-207 and 1-207, in Escherichia coli strain BL21(DE3)
expression of wild-type and mutant His-tagged GluRSs in Escherichia coli strain BL21(DE3)
gene GUS1, phylogenetic analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Simos, G.; Segref, A.; Fasiolo, F.; Hellmuth, K.; Shevchenko, A.; Mann, M.; Hurt, E.C.
The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases
EMBO J.
15
5437-5448
1996
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Graindorge, J.S.; Senger, B.; Tritch, D.; Simos, G.; Fasiolo, F.
Role of Arc1p in the modulation of yeast glutamyl-tRNA synthetase activity
Biochemistry
44
1344-1352
2005
Saccharomyces cerevisiae, Saccharomyces cerevisiae RS453
Manually annotated by BRENDA team
Simader, H.; Hothorn, M.; Suck, D.
Structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA-aminoacylation and nuclear-export cofactor Arc1p reveal a novel function for an old fold
Acta Crystallogr. Sect. D
62
1510-1519
2006
Saccharomyces cerevisiae (P46655), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Simader, H.; Hothorn, M.; Koehler, C.; Basquin, J.; Simos, G.; Suck, D.
Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes
Nucleic Acids Res.
34
3968-3979
2006
Saccharomyces cerevisiae (P46655), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Hadd, A.; Perona, J.J.
Coevolution of specificity determinants in eukaryotic glutamyl- and glutaminyl-tRNA synthetases
J. Mol. Biol.
426
3619-3633
2014
Saccharomyces cerevisiae (P46655), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 / S288c (P46655)
Manually annotated by BRENDA team