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ATP + Glu + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
-
-
-
?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
ATP + glutamate + chloroplastic tRNAGln
AMP + diphosphate + gluamyl-tRNAGln
ATP + L-glutamate + tRNA3Glu
AMP + diphosphate + L-glutamyl-tRNA3Glu
-
-
-
-
?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
-
adB gene encodes a truncated GluRS that lacks the C-terminal third of the protein and, consequently the anticodon binding domain. The YadB protein transfers Glu onto tRNAAsp. Neither tRNAGlu nor tRNAGln are substrates
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
ATP + L-glutamate + tRNAGln(CUG)
AMP + diphosphate + L-glutamyl-tRNAGln(CUG)
-
the enzyme shows a significant catalytic preference for tRNAGln(CUG) compared to the less active tRNAGln(UUG)
-
-
?
ATP + L-glutamate + tRNAGln(UUG)
AMP + diphosphate + L-glutamyl-tRNAGln(UUG)
-
the enzyme shows a significant catalytic preference for tRNAGln(CUG) compared to the less active tRNAGln(UUG)
-
-
?
ATP + L-glutamate + tRNAGlu
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
ATP + L-glutamate + tRNAGlu mutant C36G
AMP + diphosphate + L-glutamyl-tRNAGlu mutant C36G
mutant R358Q, low activity with the wild-type enzyme
-
?
ATP + L-glutamate + tRNAGlu wild-type
AMP + diphosphate + L-glutamyl-tRNAGlu wild-type
enzyme is specific for tRNAGlu
-
?
ATP + L-glutamate + wild type tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-proline + tRNAGlu
AMP + diphosphate + L-prolyl-tRNAGlu
-
enzyme has dual substrate specificity for L-glutamate and L-proline
-
?
additional information
?
-
ATP + Glu + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
-
the enzyme glutamylates the queuosine residue, a modified nucleoside at the wooble position of the tRNAASp QUC anticodon. The enzyme is not able to glutamylate tRNAAsp isolated from an Escherichia coli tRNA-guanosine transglycosylase minus strain deprived of the capacity to exchange guanosine 34 with queuosine
-
-
?
ATP + Glu + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
-
tRNAGlu is not used as substrate
-
-
?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
-
GluRS1
-
-
?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
-
GluRS1 cannot form Glu-tRNAGln
-
-
?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
-
GluRS1 cannot form Glu-tRNAGln
-
-
?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
-
GluRS1
-
-
?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
-
GluRS1
-
-
?
ATP + glutamate + chloroplastic tRNAGln
AMP + diphosphate + gluamyl-tRNAGln
-
misacylation
-
-
?
ATP + glutamate + chloroplastic tRNAGln
AMP + diphosphate + gluamyl-tRNAGln
-
misacylation
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
isozyme 2 expressed in an Escherichia coli mutant strain, tRNAGln UUG from Escherichia coli
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
enzyme is active with the tRNAGln from Bacillus subtilis and the isoacceptor tRNAGln1, but not tRNAGln2, from Escherichia coli, the major recognition element is U at position 34
-
?
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
-
enzyme expressed in an Escherichia coli mutant strain, tRNAGln UUG from Escherichia coli
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
mitochondrial glutamyl-tRNA synthetase efficiently aminoacylates both tRNAGln to form Glu-tRNAGln and tRNAGlu to form Glu-tRNAGlu
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
?
-
involved in synthesis of 5-aminolevulinate (a committed and regulated precursor in the chlorophyll biosynthetic pathway)
-
-
?
ATP + L-glutamate + tRNAGlu
?
-
involved in synthesis of 5-aminolevulinate (a committed and regulated precursor in the chlorophyll biosynthetic pathway)
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
isozyme 1 expressed in an Escherichia coli mutant strain, tRNAGlu from Escherichia coli
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
glutamyl-tRNA, formed by Glu-tRNA synthetase, is a substrate for protein biosynthesis and tetrapyrrole formation by the C5 pathway
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
wild-type tRNAGlu and tRNA AE(GU)
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
wild-type tRNAGlu and tRNA AE(GU)
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
enzyme utilizes tRNAGlu from Bacillus subtilis, not from Escherichia coli
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
recombinant mutant Q373R expressed in Escherichia coli mutant strain, tRNAGlu from Escherichia coli
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Caesalpinia bondue
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
glutamylate E. coli tRNAGluF, not cytoplasmic tRNAGlu from yeast and barley
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
r
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
r
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
existence of an enzyme-AMP-Glu intermediate in the aminoacylation reaction
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
specific modification of the 5-(methylaminomethyl)-2-thiouridine group in the anticodon of E. coli tRNAGlu by cyanogen bromide results in a 5fold decrease of the maximal rate of Glu-tRNAGlu synthesis, but unaffected rate of tRNAGlu-promoted ATP-diphosphate exchange
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
the major recognition element of the tRNAGlu is U at position 34, activity with wild-type and mutant tRNAs, overview
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
a two-step reaction
-
-
r
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
ERS recognizes the 2-thionyl group of 2-thio-5-methylaminomethyluridine in the first or wobble anticodon position of tRNAGlu, specific, though tenuous interaction, recognition determinants and mechanism, overview
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
wild-type enzyme and chimeric mutant cGluGlnRS, overview
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
analysis of domain functions in enzyme-substrate interactions, overview
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
mitochondrial glutamyl-tRNA synthetase efficiently aminoacylates both tRNAGln to form Glu-tRNAGln and tRNAGlu to form Glu-tRNAGlu
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
chemically modified tRNAGlu modified by monobromobimane or CNBr is a poor substrate. tRNAGlu from the chloroplast of barley, Chlamydomonas reinhardtii, tobacco, cucumber, wheat, and spinach, and tRNAGlu from Synechocystis PCC6803, Escherichia coli, barley germ and bakers yeast are effective substrates, G10, A26, U35 and A37 are recognition elements of barley enzyme
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Methanobacterium thermoautotrophicus
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
wild-type tRNAGlu and tRNA AE(GU)
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Methanococcus thermoautotrophicum
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Methanococcus thermoautotrophicum
-
wild-type tRNAGlu and tRNA AE(GU)
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
wild-type tRNAGlu and tRNA AE(GU)
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
enzyme has dual substrate specificity for L-glutamate and L-proline
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
wild-type tRNAGlu and tRNA AE(GU)
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
wild-type tRNAGlu and tRNA AE(GU)
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
a two-step aminoacylation reaction
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
a two-step aminoacylation reaction
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
charges tRNAGlu from barley and from E. coli
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
in absence of tRNAGlu, GluRS binds to D-glutamate as well as L-glutamate
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
tRNAGlu binding causes conformational changes in the enzyme, glutamine binding mechanism, in presence or absence of tRNA
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
structural bases of transfer RNA-dependent L-glutamate recognition and activation by the enzyme, the glutamate-binding site is immature in the absence of tRNA, overview
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
eukaryotic-type discriminating glutamyl-tRNA synthetase, inability to utilize Escherichia coli tRNA as substrate. The enzyme is essential for growth of insect stage Trypanosoma brucei and is responsible for essentially all of the glutamyl-tRNA synthetase activity in cytosol and in mitochondria
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
eukaryotic-type discriminating glutamyl-tRNA synthetase, inability to utilize Escherichia coli tRNA as substrate
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
additional information
?
-
-
GluRS plays a major role in regulating the cellular level of heme, aminoacylation of tRNAGlu correlates with the demand of heme, a transcriptional mechanism might control the level of GluRS1 in cells grown in Fe2+, under growth conditions in which cells do not require Glu-tRNA, as precursor for heme biosynthesis, up to 85% of GluRS1 is dispensable, but no major detrimental effect in the cell growth is observed. Thus, GluRS2 and the remaining 15% of the activity of GluRS1 are sufficient to provide the Glu-tRNA substrates for protein synthesis
-
-
?
additional information
?
-
-
discriminating GluRS specifically aminoacylates tRNAGlu with glutamate. Acidithiobacillus ferrooxidans GluRS1 contains cysteines 98, 100 and 125 together with glutamate 127 clustered in the catalytic domain
-
-
?
additional information
?
-
-
no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
-
?
additional information
?
-
-
no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
-
?
additional information
?
-
-
glutamate and glutamine acceptor activity with wild-type and mutant tRNAGlns with native and recombinant enzyme, overview
-
?
additional information
?
-
-
no charging of Escherichia coli tRNAGln by enzyme mutant Q373R
-
?
additional information
?
-
-
the recombinant wild-type enzyme is toxic for Escherichia coli, probably due to its charging of both tRNAGlu and tRNAGln
-
?
additional information
?
-
Caesalpinia bondue
-
threo-4-methyl-DL-glutamic acid or threo-4-hydroxy-L-glutamic acid can promote ATP-diphosphate exchange
-
-
?
additional information
?
-
-
tRNAGlu-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
tRNAGlu-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
the identity of tRNAGlu is determined by the bases set U34,U35, C36, A37, G1.C72, U2.A71, U11.A24, U13.G22..A46, and DELTA47, if this set is transplanted to tRNAAsp in addition to C4.G69 and C12.G23..C9, the tRNAAsp is a substrate for the enzyme, while tRNAGlu modification at the bases of the determinant set results in reduced activity
-
?
additional information
?
-
-
the enzyme also catalyzes ATP-diphosphate exchange
-
-
?
additional information
?
-
-
thermal stability and structural analysis of tRNA substrates, overview
-
-
?
additional information
?
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efficient glutamylation demands optimal binding of substrates (ATP, tRNAGlu and L-glutamic acid) by GluRS. Binding of tRNAGlu induces conformational changes in GluRS that stimulates the binding of L-glutamic acid leading to the productive binding of ATP. L-glutamic acid is first activated by GluRS in presence of ATP to form the adenylate complex. This is followed by the catalytic step where the acceptor stem of tRNAGlu is glutamylated
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?
additional information
?
-
-
efficient glutamylation demands optimal binding of substrates (ATP, tRNAGlu and L-glutamic acid) by GluRS. Binding of tRNAGlu induces conformational changes in GluRS that stimulates the binding of L-glutamic acid leading to the productive binding of ATP. L-glutamic acid is first activated by GluRS in presence of ATP to form the adenylate complex. This is followed by the catalytic step where the acceptor stem of tRNAGlu is glutamylated
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?
additional information
?
-
-
isoform GluRS2 is unable to produce Glu-tRNAGlu. Within a series of tRNA chimeras containing 75% tRNAGln and 25% tRNAGlu2 character, GluRS2 recognizes major identity elements clustered in the tRNAGln acceptor stem. Mutations in the tRNA anticodon or at the discriminator base have little to no impact on enzyme specificity and activity
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-
?
additional information
?
-
-
erythro-4-methyl-L-glutamic acid, erythro-4-hydroxy-DL-glutamic acid, or 2(S),4(S)-4-hydroxy-4-methyl-L-glutamic acid can promote ATP-diphosphate exchange
-
-
?
additional information
?
-
-
the glutamyl-prolyl tRNA synthetase determines the specificity of the heterotetrameric GAIT complex suppressing translation of selected mRNAs in interferon-gamma-activated monocytic cells by binding to a 3' UTR element in target mRNAs, critical role of EPRS WHEP domains in targeting and regulating GAIT complex binding to RNA, mechanism, overview. The enzyme is essential in regulating inflammatory gene expression
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?
additional information
?
-
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the upstream WHEP pair of EPRS directs high-affinity binding to GAIT element-bearing mRNAs, while the overlapping, downstream pair binds NSAP1, which inhibits mRNA binding. Interaction of EPRS with ribosomal protein L13a and GAPDH induces a conformational witch that rescues mRNA binding and restores translational control, interaction analysis, overview
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-
?
additional information
?
-
-
no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
-
?
additional information
?
-
Methanococcus thermoautotrophicum
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no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
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?
additional information
?
-
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no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
-
?
additional information
?
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Pseudomonas aeruginosa GluRS is a discriminating GluRS and requires the presence of tRNAGlu to produce a glutamyl-AMP intermediate. Development of a robust aminoacylation-based scintillation proximity assay (SPA) assay. Residue Arg147 interacts with the tRNAGlu C74 phosphate, residues Asp44 and Arg47 interact with the 2'-hydroxyl group of C75, and residues Tyr187 and Thr43 interact with the adenosine base and the 5'-hydroxyl group of A76
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?
additional information
?
-
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Pseudomonas aeruginosa GluRS is a discriminating GluRS and requires the presence of tRNAGlu to produce a glutamyl-AMP intermediate. Development of a robust aminoacylation-based scintillation proximity assay (SPA) assay. Residue Arg147 interacts with the tRNAGlu C74 phosphate, residues Asp44 and Arg47 interact with the 2'-hydroxyl group of C75, and residues Tyr187 and Thr43 interact with the adenosine base and the 5'-hydroxyl group of A76
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-
?
additional information
?
-
Pseudomonas aeruginosa GluRS is a discriminating GluRS and requires the presence of tRNAGlu to produce a glutamyl-AMP intermediate. Development of a robust aminoacylation-based scintillation proximity assay (SPA) assay. Residue Arg147 interacts with the tRNAGlu C74 phosphate, residues Asp44 and Arg47 interact with the 2'-hydroxyl group of C75, and residues Tyr187 and Thr43 interact with the adenosine base and the 5'-hydroxyl group of A76
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?
additional information
?
-
-
no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
-
?
additional information
?
-
-
no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
-
?
additional information
?
-
GluRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
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?
additional information
?
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GluRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
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?
additional information
?
-
GluRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
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?
additional information
?
-
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GluRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
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?
additional information
?
-
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GtS is an age-dependent Streptococcus pneumoniae antigen and is a surface-located adhesin that is capable of inducing a partially protective immune response against Streptococcus pneumoniae in mice, overview
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?
additional information
?
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D-GluRS glutamylates tRNAGlu only
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?
additional information
?
-
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D-GluRS glutamylates tRNAGlu only
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?
additional information
?
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substrate and co-factor recognition and binding structures, GluRS and tRNAGlu collaborate to form a highly complementary L-glutamate-binding site, the collaborative site is functional, amino acid specificity is generated in the GluRS-tRNA complex, overview
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?
additional information
?
-
Tolypothrix sp.
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regulation of gltX expression, overview, the gene glxT encoding the enzyme is involved in regulation of other genes's expression, mechanisms, overview
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?
additional information
?
-
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ATP-diphosphate exchange
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?
additional information
?
-
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threo-4-methyl-DL-glutamic acid or threo-4-hydroxy-L-glutamic acid can promote ATP-diphosphate exchange
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-
?
additional information
?
-
-
erythro-4-methyl-L-glutamic acid, erythro-4-hydroxy-DL-glutamic acid, or 2(S),4(S)-4-hydroxy-4-methyl-L-glutamic acid can promote ATP-diphosphate exchange
-
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?
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ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
ATP + L-glutamate + tRNAGln(CUG)
AMP + diphosphate + L-glutamyl-tRNAGln(CUG)
-
the enzyme shows a significant catalytic preference for tRNAGln(CUG) compared to the less active tRNAGln(UUG)
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?
ATP + L-glutamate + tRNAGln(UUG)
AMP + diphosphate + L-glutamyl-tRNAGln(UUG)
-
the enzyme shows a significant catalytic preference for tRNAGln(CUG) compared to the less active tRNAGln(UUG)
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?
ATP + L-glutamate + tRNAGlu
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
additional information
?
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ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
isozyme 2 expressed in an Escherichia coli mutant strain, tRNAGln UUG from Escherichia coli
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?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
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?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
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enzyme expressed in an Escherichia coli mutant strain, tRNAGln UUG from Escherichia coli
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ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
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?
ATP + L-glutamate + tRNAGlu
?
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involved in synthesis of 5-aminolevulinate (a committed and regulated precursor in the chlorophyll biosynthetic pathway)
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?
ATP + L-glutamate + tRNAGlu
?
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involved in synthesis of 5-aminolevulinate (a committed and regulated precursor in the chlorophyll biosynthetic pathway)
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
isozyme 1 expressed in an Escherichia coli mutant strain, tRNAGlu from Escherichia coli
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
glutamyl-tRNA, formed by Glu-tRNA synthetase, is a substrate for protein biosynthesis and tetrapyrrole formation by the C5 pathway
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
recombinant mutant Q373R expressed in Escherichia coli mutant strain, tRNAGlu from Escherichia coli
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
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-
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
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-
-
r
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
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-
-
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r
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
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-
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
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-
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
wild-type enzyme and chimeric mutant cGluGlnRS, overview
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
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-
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Methanobacterium thermoautotrophicus
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
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-
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Methanococcus thermoautotrophicum
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
eukaryotic-type discriminating glutamyl-tRNA synthetase, inability to utilize Escherichia coli tRNA as substrate. The enzyme is essential for growth of insect stage Trypanosoma brucei and is responsible for essentially all of the glutamyl-tRNA synthetase activity in cytosol and in mitochondria
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?
additional information
?
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GluRS plays a major role in regulating the cellular level of heme, aminoacylation of tRNAGlu correlates with the demand of heme, a transcriptional mechanism might control the level of GluRS1 in cells grown in Fe2+, under growth conditions in which cells do not require Glu-tRNA, as precursor for heme biosynthesis, up to 85% of GluRS1 is dispensable, but no major detrimental effect in the cell growth is observed. Thus, GluRS2 and the remaining 15% of the activity of GluRS1 are sufficient to provide the Glu-tRNA substrates for protein synthesis
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?
additional information
?
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no charging of Escherichia coli tRNAGln by enzyme mutant Q373R
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?
additional information
?
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the recombinant wild-type enzyme is toxic for Escherichia coli, probably due to its charging of both tRNAGlu and tRNAGln
-
?
additional information
?
-
-
the glutamyl-prolyl tRNA synthetase determines the specificity of the heterotetrameric GAIT complex suppressing translation of selected mRNAs in interferon-gamma-activated monocytic cells by binding to a 3' UTR element in target mRNAs, critical role of EPRS WHEP domains in targeting and regulating GAIT complex binding to RNA, mechanism, overview. The enzyme is essential in regulating inflammatory gene expression
-
-
?
additional information
?
-
-
GtS is an age-dependent Streptococcus pneumoniae antigen and is a surface-located adhesin that is capable of inducing a partially protective immune response against Streptococcus pneumoniae in mice, overview
-
-
?
additional information
?
-
Tolypothrix sp.
-
regulation of gltX expression, overview, the gene glxT encoding the enzyme is involved in regulation of other genes's expression, mechanisms, overview
-
-
?
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Acidosis, Lactic
EARS2 mutations cause fatal neonatal lactic acidosis, recurrent hypoglycemia and agenesis of corpus callosum.
Amblyopia
[Effects of monocular visual deprivation on parameters of GLuRs in visual cortex in developing kittens]
Amyotrophic Lateral Sclerosis
Potential target sites in peripheral tissues for excitatory neurotransmission and excitotoxicity.
Arthritis
AMPA/kainate glutamate receptors contribute to inflammation, degeneration and pain related behaviour in inflammatory stages of arthritis.
Brain Diseases
Development of PET and SPECT probes for glutamate receptors.
Brain Diseases
Mutations in the glutaminyl-tRNA synthetase gene cause early-onset epileptic encephalopathy.
Brain Diseases
[QARS1 gene related glutaminyl-tRNA synthetase deficiency syndrome: report of three cases and a review of literature].
Carcinoma
Absence of antibodies to non-NMDA glutamate-receptor subunits in paraneoplastic cerebellar degeneration.
Cardiomyopathies
Cloning and characterization of glutamate receptors in Californian sea lions (Zalophus californianus).
Cerebral Palsy
Glutamate receptors: the cause or cure in perinatal white matter injury?
Down Syndrome
Regulation of glutamate receptor RNA editing and ADAR mRNA expression in developing human normal and Down's syndrome brains.
Drug Resistant Epilepsy
Case Report.
Epilepsy
Dual-Targeted Autoimmune Sword in Fatal Epilepsy: Patient's glutamate receptor AMPA GluR3B peptide autoimmune antibodies bind, induce Reactive Oxygen Species (ROS) in, and kill both human neural cells and T cells.
Epilepsy
Effects of Spider Venom Toxin PWTX-I (6-Hydroxytrypargine) on the Central Nervous System of Rats.
Epilepsy
Potential target sites in peripheral tissues for excitatory neurotransmission and excitotoxicity.
Epilepsy
Severe growth deficiency, microcephaly, intellectual disability, and characteristic facial features are due to a homozygous QARS mutation.
Glaucoma
Acetylcholine protection of adult pig retinal ganglion cells from glutamate-induced excitotoxicity.
Glaucoma
Factors contributing to neuronal degeneration in retinas of experimental glaucomatous rats.
glutamate-trna ligase deficiency
Case Report.
glutamate-trna ligase deficiency
Severe growth deficiency, microcephaly, intellectual disability, and characteristic facial features are due to a homozygous QARS mutation.
glutamate-trna ligase deficiency
[QARS1 gene related glutaminyl-tRNA synthetase deficiency syndrome: report of three cases and a review of literature].
Hodgkin Disease
[Antibodies to the glutamate receptor].
Hyperalgesia
Capsaicin-induced glutamate release is implicated in nociceptive processing through activation of ionotropic glutamate receptors and group I metabotropic glutamate receptor in primary afferent fibers.
Hyperalgesia
Spinal metabotropic glutamate receptor 4 is involved in neuropathic pain.
Hypoglycemia
EARS2 mutations cause fatal neonatal lactic acidosis, recurrent hypoglycemia and agenesis of corpus callosum.
Intellectual Disability
Drosophila fragile X mental retardation protein and metabotropic glutamate receptor A convergently regulate the synaptic ratio of ionotropic glutamate receptor subclasses.
Leukoencephalopathies
Expanding the Clinical and Magnetic Resonance Spectrum of Leukoencephalopathy with Thalamus and Brainstem Involvement and High Lactate (LTBL) in a Patient Harboring a Novel EARS2 Mutation.
Leukoencephalopathies
Lethal Neonatal LTBL Associated with Biallelic EARS2 Variants: Case Report and Review of the Reported Neuroradiological Features.
Leukoencephalopathies
Leukoencephalopathy with thalamus and brainstem involvement and high lactate caused by novel mutations in the EARS2 gene in two siblings.
Medulloblastoma
Expression of N-methyl-D-aspartate (NMDA) and non-NMDA glutamate receptor genes in neuroblastoma, medulloblastoma, and other cells lines.
Microcephaly
Case Report.
Microcephaly
Mutations in QARS, Encoding Glutaminyl-tRNA Synthetase, Cause Progressive Microcephaly, Cerebral-Cerebellar Atrophy, and Intractable Seizures.
Microcephaly
Progressive microcephaly is caused by compound-heterozygous mutations in QARS.
Microcephaly
Severe growth deficiency, microcephaly, intellectual disability, and characteristic facial features are due to a homozygous QARS mutation.
Microcephaly
[QARS1 gene related glutaminyl-tRNA synthetase deficiency syndrome: report of three cases and a review of literature].
Mitochondrial Diseases
Expanding the Clinical and Magnetic Resonance Spectrum of Leukoencephalopathy with Thalamus and Brainstem Involvement and High Lactate (LTBL) in a Patient Harboring a Novel EARS2 Mutation.
Mitochondrial Diseases
Lethal Neonatal LTBL Associated with Biallelic EARS2 Variants: Case Report and Review of the Reported Neuroradiological Features.
Muscle Hypotonia
[QARS1 gene related glutaminyl-tRNA synthetase deficiency syndrome: report of three cases and a review of literature].
Neoplasms
Absence of antibodies to non-NMDA glutamate-receptor subunits in paraneoplastic cerebellar degeneration.
Neoplasms
Glutamate and its receptors in cancer.
Neoplasms
Protein kinase C phosphorylates glutamyl-tRNA synthetase in rabbit reticulocytes stimulated by tumor promoting phorbol esters.
Neoplasms
The neurotransmitter glutamate and human T cells: glutamate receptors and glutamate-induced direct and potent effects on normal human T cells, cancerous human leukemia and lymphoma T cells, and autoimmune human T cells.
Nervous System Diseases
Development of PET and SPECT probes for glutamate receptors.
Neuralgia
Influence of amygdaloid glutamatergic receptors on sensory and emotional pain-related behavior in the neuropathic rat.
Neuralgia
Mammalian target of rapamycin signaling pathway is involved in synaptic plasticity of the spinal dorsal horn and neuropathic pain in rats by regulating autophagy.
Neuralgia
Spinal metabotropic glutamate receptor 4 is involved in neuropathic pain.
Neuroblastoma
Expression of N-methyl-D-aspartate (NMDA) and non-NMDA glutamate receptor genes in neuroblastoma, medulloblastoma, and other cells lines.
Neurodegenerative Diseases
Case Report.
Neurodegenerative Diseases
Potential target sites in peripheral tissues for excitatory neurotransmission and excitotoxicity.
Neurodegenerative Diseases
Structure-based functional design of chemical ligands for AMPA-subtype glutamate receptors.
Neurodegenerative Diseases
Structure-based rational design of chemical ligands for AMPA-subtype glutamate receptors.
Pneumococcal Infections
Protection against pneumococcal infection elicited by immunization with glutamyl tRNA synthetase, polyamine transport protein D and sortase A.
Seizures
Mutations in QARS, Encoding Glutaminyl-tRNA Synthetase, Cause Progressive Microcephaly, Cerebral-Cerebellar Atrophy, and Intractable Seizures.
Seizures
Progressive microcephaly is caused by compound-heterozygous mutations in QARS.
Seizures
Severe growth deficiency, microcephaly, intellectual disability, and characteristic facial features are due to a homozygous QARS mutation.
Stroke
Glutamate receptors and white matter stroke.
Stroke
Potential target sites in peripheral tissues for excitatory neurotransmission and excitotoxicity.
Teratoma
Expression of various glutamate receptors including N-methyl-D-aspartate receptor (NMDAR) in an ovarian teratoma removed from a young woman with anti-NMDAR encephalitis.
Tuberculosis
Kinetic and mechanistic characterization of Mycobacterium tuberculosis glutamyl-tRNA synthetase and determination of its oligomeric structure in solution.
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Q373R
-
substrate specificity restricted to tRNAGlu compared to the wild-type which also accepts tRNAGln
H129Q
-
mutants encoding GluRS variants altered in the 98C-138C segment. Thermosensitive mutants H129Q, H131Q, H132Q and C138S. Mutants without glutamyl-tRNA synthetase activity: C100S, C125S. In the mutants C98S and H127Q the activity is 10fold lower than in cells overproducing the wild-type enzyme or the variants H129Q, H131Q, H132Q, and C138S
K236E/E328A
-
by mapping crystal contacts of the homologous GluRS from Bacillus thailandensis, PDB ID 4g6z, onto the Escherichia coli GluRS sequence, two surface residues are identified that might be hindering crystallization attempts. Accordingly, these two residues are mutated and crystallization of the double mutant is attempted
S990A
site-directed mutagenesis, the mutant is unable to rescue virus-infected cells
S990D
site-directed mutagenesis, the mutation markedly inhibits viral replication in cells
S990A
site-directed mutagenesis, the mutant is unable to rescue virus-infected cells
S990D
site-directed mutagenesis, the mutation markedly inhibits viral replication in cells
R358Q
site-directed mutagenesis, exchange of the Arg residue results in a mutant that no longer discriminates between tRNAGlu and tRNAGln anticodons YUC and YUG, respectively
additional information
-
design of orthogonal tRNAs with sequences derived from archaeal tRNAs, 3 forms: 1. AQ(GU), i.e. archaeal glutaminyl with GU base pair at position 10-26, 2. AE(GU), i.e. archaeal glutamyl with GU base pair at position 10-28, 3. AE(GC), i.e. archaeal glutamyl with GC base pair at position 10-28
additional information
-
design of orthogonal tRNAs with sequences derived from archaeal tRNAs, 3 forms: 1. AQ(GU), i.e. archaeal glutaminyl with GU base pair at position 10-26, 2. AE(GU), i.e. archaeal glutamyl with GU base pair at position 10-28, 3. AE(GC), i.e. archaeal glutamyl with GC base pair at position 10-28
additional information
-
construction and expression in Escherichia coli of mutant forms of Escherichia coli tRNAGln2 and tRNAGln1 and of Bacillus subtilis tRNAGln
additional information
-
construction and overexpression of tRNAGlu variants, the enzyme shows altered activity with the tRNA mutants, structural characterization
additional information
-
construction of a chimeric glutamyl:glutaminyl-tRNA synthetase, cGluGlnRS, consisting of the catalytic domain of the GluRS and the anti-codon binding domain of the GlnRS. In contrast to the isolated GluRS catalytic domain, the chimeric mutant shows detectable glutamylation activity with Escherichia coli tRNAGlu and is capable of complementing a ts-GluRS strain at non-permissive temperatures. The GlnRS anticodon-binding domain in cGluGlnRS enhances kcat for glutamylation, interaction analysis, overview
additional information
construction of constructed a chimaeric protein, cGluGlnRS, consisting of the catalytic domain, GluRS, and the anticodon binding domain of Escherichia coli GlnRS. cGluGlnRS shows detectable activity of glutamylation of Escherichia coli tRNAGlu and is capable of complementing an Escherichia coli temperature-sensitive GluRS strain at non-permissive temperatures. Both cGluGlnRS and N-terminal residues 1-314 of GluRS bind Escherichia coli tRNAglu with native GluRS-like affinity, suggesting that the anticodon-binding domain in cGluGlnRS enhances kcat for glutamylation. The kcat value of cGluGlnRS is approx. 500fold lower than that of GluRS, whereas the Km value is only moderately higher at the same solution conditions
additional information
-
construction of constructed a chimaeric protein, cGluGlnRS, consisting of the catalytic domain, GluRS, and the anticodon binding domain of Escherichia coli GlnRS. cGluGlnRS shows detectable activity of glutamylation of Escherichia coli tRNAGlu and is capable of complementing an Escherichia coli temperature-sensitive GluRS strain at non-permissive temperatures. Both cGluGlnRS and N-terminal residues 1-314 of GluRS bind Escherichia coli tRNAglu with native GluRS-like affinity, suggesting that the anticodon-binding domain in cGluGlnRS enhances kcat for glutamylation. The kcat value of cGluGlnRS is approx. 500fold lower than that of GluRS, whereas the Km value is only moderately higher at the same solution conditions
additional information
generation of pZBD-chimeras of Ec-GluRS, four chimeric versions with partly replaced zinc-binding motif, pZBD. In the first chimera [Ec(Te)-GluRS], the pZBD of Ec-GluRS is replaced by the corresponding pZBD from Thermosynechococcus elongatus GluRS (Te-GluRS) whose structure is devoid of a bound Zn2+ despite containing the modified ZB-motif CxCxnYx3H. In the second chimera [Ec(EQRS)-GluRS] the pZBD of Ec-GluRS is replaced by the corresponding pZBD from Escherichia coli Glu-QRS (Ec-EQRS) whose zinc-bound structure contains the ZB-motif CxCxnYx3C. In the third chimera [Ec(Bt)-GluRS], the pZBD of Ec-GluRS is replaced by a 19-residue stretch from the pZBD of Bt-GluRS which contains a disrupted zinc binding motif CxMx20Yx3W and whose structure is devoid of a bound Zn2+ ion. The 19-residue stretch starts from the residue preceding the fourth zinc-co-ordinating cysteine residue in Ec-GluRS and continues until the last beta-strand of the pZBD fold. The overall secondary structure and compactness of wild-type Ec-GluRS remains unaltered in the chimeric constructs. The association of GluRS with tRNAGlu but not with ATP is sensitive to pZBD perturbations. Except for Ec(Bt)-GluRS, all pZBD-chimeras show 100fold or more reduced catalytic efficiency and contain zinc. Natively zinc-bound Ec-GluRS does not require zinc to be active
additional information
-
generation of pZBD-chimeras of Ec-GluRS, four chimeric versions with partly replaced zinc-binding motif, pZBD. In the first chimera [Ec(Te)-GluRS], the pZBD of Ec-GluRS is replaced by the corresponding pZBD from Thermosynechococcus elongatus GluRS (Te-GluRS) whose structure is devoid of a bound Zn2+ despite containing the modified ZB-motif CxCxnYx3H. In the second chimera [Ec(EQRS)-GluRS] the pZBD of Ec-GluRS is replaced by the corresponding pZBD from Escherichia coli Glu-QRS (Ec-EQRS) whose zinc-bound structure contains the ZB-motif CxCxnYx3C. In the third chimera [Ec(Bt)-GluRS], the pZBD of Ec-GluRS is replaced by a 19-residue stretch from the pZBD of Bt-GluRS which contains a disrupted zinc binding motif CxMx20Yx3W and whose structure is devoid of a bound Zn2+ ion. The 19-residue stretch starts from the residue preceding the fourth zinc-co-ordinating cysteine residue in Ec-GluRS and continues until the last beta-strand of the pZBD fold. The overall secondary structure and compactness of wild-type Ec-GluRS remains unaltered in the chimeric constructs. The association of GluRS with tRNAGlu but not with ATP is sensitive to pZBD perturbations. Except for Ec(Bt)-GluRS, all pZBD-chimeras show 100fold or more reduced catalytic efficiency and contain zinc. Natively zinc-bound Ec-GluRS does not require zinc to be active
additional information
siRNA-mediated enzyme knockout in HEK-293T cells. Cells in which EPRS is knocked down show considerable attenuation of the production of antiviral cytokines (IFN-beta and interleukin-6) following viral infection or treatment with the synthetic double-stranded RNA poly(I:C). Activation of the interferon-related signaling molecules IRF3 and STAT1 is significantly lower in cells in which EPRS is knocked down than in their EPRS-sufficient counterparts
additional information
-
design of orthogonal tRNAs with sequences derived from archaeal tRNAs, 3 forms: 1. AQ(GU), i.e. archaeal glutaminyl with GU base pair at position 10-26, 2. AE(GU), i.e. archaeal glutamyl with GU base pair at position 10-28, 3. AE(GC), i.e. archaeal glutamyl with GC base pair at position 10-28
additional information
Methanococcus thermoautotrophicum
-
design of orthogonal tRNAs with sequences derived from archaeal tRNAs, 3 forms: 1. AQ(GU), i.e. archaeal glutaminyl with GU base pair at position 10-26, 2. AE(GU), i.e. archaeal glutamyl with GU base pair at position 10-28, 3. AE(GC), i.e. archaeal glutamyl with GC base pair at position 10-28
additional information
-
design of orthogonal tRNAs with sequences derived from archaeal tRNAs, 3 forms: 1. AQ(GU), i.e. archaeal glutaminyl with GU base pair at position 10-26, 2. AE(GU), i.e. archaeal glutamyl with GU base pair at position 10-28, 3. AE(GC), i.e. archaeal glutamyl with GC base pair at position 10-28
additional information
siRNA-mediated enzyme knockout in RAW-264.7 cells. Activation of the interferon-related signaling molecules IRF3 and STAT1 is significantly lower in cells in which EPRS is knocked down than in their EPRS-sufficient counterparts . RAW-264.7 cells stably overexpressing EPRS show significantly less viral replication and more production of IFN-beta and interleukin-6 following infection with PR8 or VSV than those of their counterparts with basal expression of EPRS
additional information
-
transfection of MEF cells with the PTK-EPRS-Luc reporter followed by either halofuginone treatment or no treatment
additional information
protein is not toxic when overproduced in Escherichia coli cells indicating that it does not catalyze the mischarging of Escherichia coli tRNAGln with l-Glu and that GluRS /tRNAGln recognition is species specific
additional information
-
protein is not toxic when overproduced in Escherichia coli cells indicating that it does not catalyze the mischarging of Escherichia coli tRNAGln with l-Glu and that GluRS /tRNAGln recognition is species specific
additional information
-
protein is not toxic when overproduced in Escherichia coli cells indicating that it does not catalyze the mischarging of Escherichia coli tRNAGln with l-Glu and that GluRS /tRNAGln recognition is species specific
-
additional information
-
design of orthogonal tRNAs with sequences derived from archaeal tRNAs, 3 forms: 1. AQ(GU), i.e. archaeal glutaminyl with GU base pair at position 10-26, 2. AE(GU), i.e. archaeal glutamyl with GU base pair at position 10-28, 3. AE(GC), i.e. archaeal glutamyl with GC base pair at position 10-28
additional information
-
design of orthogonal tRNAs with sequences derived from archaeal tRNAs, 3 forms: 1. AQ(GU), i.e. archaeal glutaminyl with GU base pair at position 10-26, 2. AE(GU), i.e. archaeal glutamyl with GU base pair at position 10-28, 3. AE(GC), i.e. archaeal glutamyl with GC base pair at position 10-28
additional information
construction of truncated enzyme GluRS-N, comprising residues 1-197, 17-207 and 1-207
additional information
-
construction of truncated enzyme GluRS-N, comprising residues 1-197, 17-207 and 1-207
additional information
-
mutant enzymes with higher Km and lower turnover numbers
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Escherichia coli
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Sekine, S.; Shichiri, M.; Bernier, S.; Chenevert, R.; Lapointe, J.; Yokoyama, S.
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Structure
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Thermus thermophilus (P27000)
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A chimeric glutamyl: glutaminyl-tRNA synthetase: implications for evolution
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Escherichia coli
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Jia, J.; Arif, A.; Ray, P.S.; Fox, P.L.
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Mol. Cell
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Homo sapiens
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A chimaeric glutamyl:glutaminyl-tRNA synthetase: Implications for evolution
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Escherichia coli (P04805), Escherichia coli
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Paul, S.K.; Goldar, M.M.; Yakura, M.; Oowatari, Y.; Kawamukai, M.
Glutamyl tRNA synthetases and glutamic acid induce sexual differentiation of Schizosaccharomyces pombe
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Schizosaccharomyces pombe
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Paravisi, S.; Fumagalli, G.; Riva, M.; Morandi, P.; Morosi, R.; Konarev, P.V.; Petoukhov, M.V.; Bernier, S.; Chenevert, R.; Svergun, D.I.; Curti, B.; Vanoni, M.A.
Kinetic and mechanistic characterization of Mycobacterium tuberculosis glutamyl-tRNA synthetase and determination of its oligomeric structure in solution
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Mycobacterium tuberculosis (P9WFV9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WFV9)
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Escherichia coli
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Thermus thermophilus (P27000), Thermus thermophilus
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Recognition of tRNAGln by Helicobacter pylori GluRS2 - a tRNAGln-specific glutamyl-tRNA synthetase
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Nagao, A.; Suzuki, T.; Katoh, T.; Sakaguchi, Y.; Suzuki, T.
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Homo sapiens
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Ito, T.; Kiyasu, N.; Matsunaga, R.; Takahashi, S.; Yokoyama, S.
Structure of nondiscriminating glutamyl-tRNA synthetase from Thermotoga maritima
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Thermotoga maritima, Thermotoga maritima TM1351
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Katz, A.; Banerjee, R.; de Armas, M.; Ibba, M.; Orellana, O.
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Acidithiobacillus ferrooxidans
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Balg, C.; De Mieri, M.; Huot, J.L.; Blais, S.P.; Lapointe, J.; Chenevert, R.
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Helicobacter pylori
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Pedroni, M.J.; Luu, T.N.; Lau, A.O.
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Mailu, B.M.; Ramasamay, G.; Mudeppa, D.G.; Li, L.; Lindner, S.E.; Peterson, M.J.; DeRocher, A.E.; Kappe, S.H.; Rathod, P.K.; Gardner, M.J.
A nondiscriminating glutamyl-tRNA synthetase in the Plasmodium apicoplast: the first enzyme in an indirect aminoacylation pathway
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Plasmodium falciparum
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Grant, T.D.; Luft, J.R.; Wolfley, J.R.; Snell, M.E.; Tsuruta, H.; Corretore, S.; Quartley, E.; Phizicky, E.M.; Grayhack, E.J.; Snell, E.H.
The structure of yeast glutaminyl-tRNA synthetase and modeling of its interaction with tRNA
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Methanobacterium thermoautotrophicus (O26157)
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O'Donoghue, P.; Sheppard, K.; Nureki, O.; Soell, D.
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Methanothermobacter thermautotrophicus
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Chongdar, N.; Dasgupta, S.; Datta, A.B.; Basu, G.
Preliminary X-ray crystallographic analysis of an engineered glutamyl-tRNA synthetase from Escherichia coli
Acta Crystallogr. Sect. F
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Escherichia coli
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Chongdar, N.; Dasgupta, S.; Datta, A.B.; Basu, G.
Dispensability of zinc and the putative zinc-binding domain in bacterial glutamyl-tRNA synthetase
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Escherichia coli (P04805), Escherichia coli
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Young, S.K.; Baird, T.D.; Wek, R.C.
Translation regulation of the glutamyl-prolyl-tRNA synthetase gene EPRS through bypass of upstream open reading frames with noncanonical initiation codons
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Mus musculus
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Hu, Y.; Guerrero, E.; Keniry, M.; Manrrique, J.; Bullard, J.M.
Identification of chemical compounds that inhibit the function of glutamyl-tRNA synthetase from Pseudomonas aeruginosa
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Pseudomonas aeruginosa (Q9XCL6), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 (Q9XCL6)
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Hadd, A.; Perona, J.J.
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Saccharomyces cerevisiae (P46655), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 / S288c (P46655)
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Lee, E.Y.; Lee, H.C.; Kim, H.K.; Jang, S.Y.; Park, S.J.; Kim, Y.H.; Kim, J.H.; Hwang, J.; Kim, J.H.; Kim, T.H.; Arif, A.; Kim, S.Y.; Choi, Y.K.; Lee, C.; Lee, C.H.; Jung, J.U.; Fox, P.L.; Kim, S.; Lee, J.S.; Kim, M.H.
Infection-specific phosphorylation of glutamyl-prolyl tRNA synthetase induces antiviral immunity
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Homo sapiens (P07814), Mus musculus (Q8CGC7), Mus musculus C57BL/6 (Q8CGC7)
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Blais, S.P.; Kornblatt, J.A.; Barbeau, X.; Bonnaure, G.; Laguee, P.; Chenevert, R.; Lapointe, J.
tRNAGlu increases the affinity of glutamyl-tRNA synthetase for its inhibitor glutamyl-sulfamoyl-adenosine, an analogue of the aminoacylation reaction intermediate glutamyl-AMP mechanistic and evolutionary implications
PLoS ONE
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2015
Escherichia coli (P04805), Escherichia coli
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