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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
?
-
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
-
-
?
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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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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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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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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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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no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
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Methanococcus thermoautotrophicum
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no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
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no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
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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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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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no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
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no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
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GluRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
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GluRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
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GluRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
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GluRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
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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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D-GluRS glutamylates tRNAGlu only
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D-GluRS glutamylates tRNAGlu only
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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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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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ATP-diphosphate exchange
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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
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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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