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Information on EC 6.1.1.17 - glutamate-tRNA ligase
for references in articles please use BRENDA:EC6.1.1.17
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EC Tree 6 Ligases
6.1 Forming carbon-oxygen bonds
6.1.1 Ligases forming aminoacyl-tRNA and related compounds
6.1.1.17 glutamate-tRNA ligase
The enzyme appears in viruses and cellular organisms
- 6.1.1.17
- synthetases
- aminoacyl-trna
- aminoacylation
- glnrs
- trnagln
- ampa
-
ionotropic
-
excitatory
-
anticodon
-
metabotropic
- kainate
- glu-trnagln
-
amidotransferase
- n-methyl-d-aspartate
-
misacylated
-
glutamatergic
-
mischarging
-
trna-dependent
-
glutaminylation
-
non-nmda
-
noncognate
-
nmdars
-
transamidation
- aspartyl-trna
- gatcab
-
aarss
- metrs
- trnatyr
-
isoacceptors
- lysyl-trna
-
non-discriminating
-
misaminoacylation
-
alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate
-
ampa-type
- glutamate-1-semialdehyde
- arginyl-trna
-
asparaginyl-trna
-
anticodon-binding
-
glur2/3
- methionyl-trna
-
trna-binding
- drug development
-
tryptophanyl-trna
showSynonyms
glurs, glutaminyl-trna synthetase, glutamyl-trna synthetase, glurs2, trna modifying enzyme, glurs1, glutamyl trna synthetase, discriminating glurs, glursat, tm1351, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bifunctional aminoacyl-tRNA synthetase
bifunctional glutamate/proline-tRNA ligase
D-GluRS
discriminating GluRS
EC 2.7.2.13
-
-
formerly, part transferred
-
EPRS
GltX
GluRS
GluRS1
Glutamate--tRNA ligase
Glutamate-tRNA synthetase
Glutamic acid translase
Glutamic acid tRNA ligase
Glutamyl tRNA synthetase
glutamyl-prolyl tRNA synthetase
Glutamyl-transfer ribonucleate synthetase
Glutamyl-transfer ribonucleic acid synthetase
Glutamyl-transfer RNA synthetase
Glutamyl-tRNA synthetase
glutamyl-tRNAsynthetase
P85
TM1351
discriminating GluRS
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
-
GltX
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
-
GluRS
-
-
-
-
GluRS
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
-
Glutamate--tRNA ligase
-
-
-
-
Glutamate-tRNA synthetase
-
-
-
-
Glutamic acid translase
-
-
-
-
Glutamic acid tRNA ligase
-
-
-
-
Glutamyl tRNA synthetase
-
-
-
-
Glutamyl-transfer ribonucleate synthetase
-
-
-
-
Glutamyl-transfer ribonucleic acid synthetase
-
-
-
-
Glutamyl-transfer RNA synthetase
-
-
-
-
Glutamyl-tRNA synthetase
-
-
-
-
Glutamyl-tRNA synthetase
-
-
Glutamyl-tRNA synthetase
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
-
P85
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
concerted mechanism
-
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
ATP and tRNAGlu bind randomly to the free enzyme, whereas glutamate binds only to the ternary enzyme-tRNAGlu-ATP complex. After interconversion of the quarternary enzyme-substrate complex the end-products dissociate in the order: diphosphate, AMP, Glu-tRNA
-
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
catalytic site structure, substrate binding and reaction mechanism
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
the major recognition element of the tRNAGlu is U at position 34
-
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
random binding of ATP and L-glutamate to the enzyme-tRNA complex
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
the transfer of amino acid to tRNA is accompanied by the protonation of AMP to H-AMP. Subsequent migration of proton to water reduces the stability of the complex and loosens the interface both in the presence and in the absence of AMP. The subsequent undocking of AMP or tRNA then proceeds along thermodynamically competitive pathways. Release of the tRNA acceptor stem is further accelerated by the deprotonation of the alpha-ammonium group on the charging amino acid. The proposed general base is Glu41
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
a two-step reaction , in the first step, the enzyme condenses the cognate amino acid and ATP, forming an aminoacyl-adenylate intermediate with a diphosphate as the leaving group. This reaction is reversible in the absence of the tRNA. In the absence of tRNAGlu, ATP binding by GluRS is nonproductive because the alpha-phosphate of ATP and the alpha-carboxyl groups of Glu are positioned too far apart for a reaction to occur. The presence of tRNAGlu causes conformational changes surrounding the ATP binding site, allowing ATP to bind in the productive state, which moves the alpha-phosphate of the ATP closer to the alpha-carboxyl groups of Glu, allowing the reaction for the formation of the glutamyl-AMP intermediate to occur
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
aminoacylation reaction via a two-step mechanism involving a very unstable aa-AMP intermediate
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
random binding of ATP and L-glutamate to the enzyme-tRNA complex
-
-
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
a two-step reaction , in the first step, the enzyme condenses the cognate amino acid and ATP, forming an aminoacyl-adenylate intermediate with a diphosphate as the leaving group. This reaction is reversible in the absence of the tRNA. In the absence of tRNAGlu, ATP binding by GluRS is nonproductive because the alpha-phosphate of ATP and the alpha-carboxyl groups of Glu are positioned too far apart for a reaction to occur. The presence of tRNAGlu causes conformational changes surrounding the ATP binding site, allowing ATP to bind in the productive state, which moves the alpha-phosphate of the ATP closer to the alpha-carboxyl groups of Glu, allowing the reaction for the formation of the glutamyl-AMP intermediate to occur
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
esterification
Aminoacylation
-
-
-
-
esterification
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
tetrapyrrole biosynthesis I (from glutamate), tRNA charging
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:tRNAGlu ligase (AMP-forming)
-
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CAS REGISTRY NUMBER
COMMENTARY
9068-76-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
Substrates: -
Products: -
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?
ATP + L-glutamate + tRNA3Glu
AMP + diphosphate + L-glutamyl-tRNA3Glu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
-
Substrates: 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
Products: -
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?
ATP + L-glutamate + tRNAGln(CUG)
AMP + diphosphate + L-glutamyl-tRNAGln(CUG)
-
Substrates: the enzyme shows a significant catalytic preference for tRNAGln(CUG) compared to the less active tRNAGln(UUG)
Products: -
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?
ATP + L-glutamate + tRNAGln(UUG)
AMP + diphosphate + L-glutamyl-tRNAGln(UUG)
-
Substrates: the enzyme shows a significant catalytic preference for tRNAGln(CUG) compared to the less active tRNAGln(UUG)
Products: -
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?
ATP + L-glutamate + tRNAGlu mutant C36G
AMP + diphosphate + L-glutamyl-tRNAGlu mutant C36G
Substrates: mutant R358Q, low activity with the wild-type enzyme
Products: -
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?
ATP + L-glutamate + tRNAGlu wild-type
AMP + diphosphate + L-glutamyl-tRNAGlu wild-type
Substrates: enzyme is specific for tRNAGlu
Products: -
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?
ATP + L-glutamate + wild type tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
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?
ATP + L-proline + tRNAGlu
AMP + diphosphate + L-prolyl-tRNAGlu
-
Substrates: enzyme has dual substrate specificity for L-glutamate and L-proline
Products: -
Products: -
?
ATP + Glu + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
-
Substrates: 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
Products: -
Products: -
?
ATP + Glu + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
-
Substrates: tRNAGlu is not used as substrate
Products: -
Products: -
?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
-
Substrates: GluRS1
Products: -
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?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
-
Substrates: GluRS1 cannot form Glu-tRNAGln
Products: -
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?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
-
Substrates: GluRS1 cannot form Glu-tRNAGln
Products: -
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?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
-
Substrates: GluRS1
Products: -
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?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
-
Substrates: GluRS1
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?
ATP + glutamate + chloroplastic tRNAGln
AMP + diphosphate + gluamyl-tRNAGln
-
Substrates: misacylation
Products: -
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?
ATP + glutamate + chloroplastic tRNAGln
AMP + diphosphate + gluamyl-tRNAGln
-
Substrates: misacylation
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?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
Substrates: isozyme 2 expressed in an Escherichia coli mutant strain, tRNAGln UUG from Escherichia coli
Products: -
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?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
Substrates: -
Products: -
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?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
Substrates: 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
Products: -
Products: -
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
Substrates: -
Products: -
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?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
Substrates: enzyme expressed in an Escherichia coli mutant strain, tRNAGln UUG from Escherichia coli
Products: -
Products: -
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
Substrates: mitochondrial glutamyl-tRNA synthetase efficiently aminoacylates both tRNAGln to form Glu-tRNAGln and tRNAGlu to form Glu-tRNAGlu
Products: -
Products: -
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
?
-
Substrates: involved in synthesis of 5-aminolevulinate (a committed and regulated precursor in the chlorophyll biosynthetic pathway)
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
?
-
Substrates: involved in synthesis of 5-aminolevulinate (a committed and regulated precursor in the chlorophyll biosynthetic pathway)
Products: -
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: isozyme 1 expressed in an Escherichia coli mutant strain, tRNAGlu from Escherichia coli
Products: -
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: glutamyl-tRNA, formed by Glu-tRNA synthetase, is a substrate for protein biosynthesis and tetrapyrrole formation by the C5 pathway
Products: -
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: wild-type tRNAGlu and tRNA AE(GU)
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: wild-type tRNAGlu and tRNA AE(GU)
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: enzyme utilizes tRNAGlu from Bacillus subtilis, not from Escherichia coli
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: recombinant mutant Q373R expressed in Escherichia coli mutant strain, tRNAGlu from Escherichia coli
Products: -
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Caesalpinia bondue
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: glutamylate E. coli tRNAGluF, not cytoplasmic tRNAGlu from yeast and barley
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
201, 202, 206, 210, 211, 212, 213, 215, 216, 217, 220, 227, 232, 651050, 651055, 659591, 677107, 743955
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
r
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: existence of an enzyme-AMP-Glu intermediate in the aminoacylation reaction
Products: -
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: 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
Products: -
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ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: the major recognition element of the tRNAGlu is U at position 34, activity with wild-type and mutant tRNAs, overview
Products: -
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ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: a two-step reaction
Products: -
Products: -
r
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: 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
Products: -
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ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: wild-type enzyme and chimeric mutant cGluGlnRS, overview
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: analysis of domain functions in enzyme-substrate interactions, overview
Products: -
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: mitochondrial glutamyl-tRNA synthetase efficiently aminoacylates both tRNAGln to form Glu-tRNAGln and tRNAGlu to form Glu-tRNAGlu
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: 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
Products: -
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ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Methanobacterium thermoautotrophicus
Substrates: -
Products: -
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ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
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?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: wild-type tRNAGlu and tRNA AE(GU)
Products: -
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ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Methanococcus thermoautotrophicum
-
Substrates: -
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ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Methanococcus thermoautotrophicum
-
Substrates: wild-type tRNAGlu and tRNA AE(GU)
Products: -
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ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: wild-type tRNAGlu and tRNA AE(GU)
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
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ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
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ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
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ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: enzyme has dual substrate specificity for L-glutamate and L-proline
Products: -
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ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
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ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: wild-type tRNAGlu and tRNA AE(GU)
Products: -
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ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: wild-type tRNAGlu and tRNA AE(GU)
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: a two-step aminoacylation reaction
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Saccharomyces cerevisiae ATCC 204508 / S288c
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Saccharomyces cerevisiae ATCC 204508 / S288c
Substrates: a two-step aminoacylation reaction
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: charges tRNAGlu from barley and from E. coli
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: in absence of tRNAGlu, GluRS binds to D-glutamate as well as L-glutamate
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: tRNAGlu binding causes conformational changes in the enzyme, glutamine binding mechanism, in presence or absence of tRNA
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: 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
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: 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
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: eukaryotic-type discriminating glutamyl-tRNA synthetase, inability to utilize Escherichia coli tRNA as substrate
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
Products: -
Products: -
?
additional information
?
-
-
Substrates: no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
Products: -
Products: -
?
additional information
?
-
-
Substrates: glutamate and glutamine acceptor activity with wild-type and mutant tRNAGlns with native and recombinant enzyme, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: no charging of Escherichia coli tRNAGln by enzyme mutant Q373R
Products: -
Products: -
?
additional information
?
-
-
Substrates: the recombinant wild-type enzyme is toxic for Escherichia coli, probably due to its charging of both tRNAGlu and tRNAGln
Products: -
Products: -
?
additional information
?
-
Caesalpinia bondue
-
Substrates: threo-4-methyl-DL-glutamic acid or threo-4-hydroxy-L-glutamic acid can promote ATP-diphosphate exchange
Products: -
Products: -
?
additional information
?
-
-
Substrates: tRNAGlu-dependent ATP-diphosphate exchange
Products: -
Products: -
?
additional information
?
-
-
Substrates: tRNAGlu-dependent ATP-diphosphate exchange
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also catalyzes ATP-diphosphate exchange
Products: -
Products: -
?
additional information
?
-
-
Substrates: thermal stability and structural analysis of tRNA substrates, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
Products: -
Products: -
?
additional information
?
-
Methanococcus thermoautotrophicum
-
Substrates: no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
Products: -
Products: -
?
additional information
?
-
-
Substrates: no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
Products: -
Products: -
?
additional information
?
-
-
Substrates: no recognition of recombinant tRNA mutants AQ(GU) and AQ(GC)
Products: -
Products: -
?
additional information
?
-
Substrates: GluRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: GluRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
Products: -
Products: -
?
additional information
?
-
Substrates: GluRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: GluRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: D-GluRS glutamylates tRNAGlu only
Products: -
Products: -
?
additional information
?
-
-
Substrates: D-GluRS glutamylates tRNAGlu only
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Tolypothrix sp.
-
Substrates: regulation of gltX expression, overview, the gene glxT encoding the enzyme is involved in regulation of other genes's expression, mechanisms, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: ATP-diphosphate exchange
Products: -
Products: -
?
additional information
?
-
-
Substrates: threo-4-methyl-DL-glutamic acid or threo-4-hydroxy-L-glutamic acid can promote ATP-diphosphate exchange
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate + tRNAGln(CUG)
AMP + diphosphate + L-glutamyl-tRNAGln(CUG)
-
Substrates: the enzyme shows a significant catalytic preference for tRNAGln(CUG) compared to the less active tRNAGln(UUG)
Products: -
Products: -
?
ATP + L-glutamate + tRNAGln(UUG)
AMP + diphosphate + L-glutamyl-tRNAGln(UUG)
-
Substrates: the enzyme shows a significant catalytic preference for tRNAGln(CUG) compared to the less active tRNAGln(UUG)
Products: -
Products: -
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
Substrates: isozyme 2 expressed in an Escherichia coli mutant strain, tRNAGln UUG from Escherichia coli
Products: -
Products: -
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
Substrates: enzyme expressed in an Escherichia coli mutant strain, tRNAGln UUG from Escherichia coli
Products: -
Products: -
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
?
-
Substrates: involved in synthesis of 5-aminolevulinate (a committed and regulated precursor in the chlorophyll biosynthetic pathway)
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
?
-
Substrates: involved in synthesis of 5-aminolevulinate (a committed and regulated precursor in the chlorophyll biosynthetic pathway)
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: isozyme 1 expressed in an Escherichia coli mutant strain, tRNAGlu from Escherichia coli
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: glutamyl-tRNA, formed by Glu-tRNA synthetase, is a substrate for protein biosynthesis and tetrapyrrole formation by the C5 pathway
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: recombinant mutant Q373R expressed in Escherichia coli mutant strain, tRNAGlu from Escherichia coli
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
r
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: wild-type enzyme and chimeric mutant cGluGlnRS, overview
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Methanobacterium thermoautotrophicus
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Methanococcus thermoautotrophicum
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Saccharomyces cerevisiae ATCC 204508 / S288c
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Substrates: -
Products: -
Products: -
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no charging of Escherichia coli tRNAGln by enzyme mutant Q373R
Products: -
Products: -
?
additional information
?
-
-
Substrates: the recombinant wild-type enzyme is toxic for Escherichia coli, probably due to its charging of both tRNAGlu and tRNAGln
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Tolypothrix sp.
-
Substrates: regulation of gltX expression, overview, the gene glxT encoding the enzyme is involved in regulation of other genes's expression, mechanisms, overview
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
ATP binds to the 'productive' subsite, due to the tRNA-induced rearrangement of the binding site, which is, at least partially, the structural basis of the tRNA-dependent enzyme activation for amino acid activation
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
-
can partially replace Mg2+ in activation, maximal efficiency at 5 mM is 71% of Mg2+-activation
Zinc
Zn2+
Mg2+
Caesalpinia bondue
-
Km: 2.2 mM, ATP-diphosphate exchange, 6.3 mM, glutamate-tRNA formation
Mg2+
-
Km: 0.46 mM, enzyme form GluRSC, aminoacylation, Km: 0.38 mM, enzyme form GluRSP, aminoacylation
Mg2+
-
Km: 1.8 mM, ATP-diphosphate exchange, 4.8 mM, glutamate-tRNA formation
Zinc
-
no direct interaction of the zinc atom with tRNA. It may stabilize a region of polypeptide chain which is involved in acceptor stem binding
Zinc
-
enzyme contains one zinc atom strongly bound, which is essential for its native conformation and its catalytic acitivity
Zn2+
-
bound at the active site, Zn2+ is essential for the proper binding of glutamate to GluRS. GluRS1 contains one Zn2+ ion per enzyme molecule, determination of the Zn2+ content of GluRS1 by mass spectrometry, overview. A relatively canonical SWIM motif, C-X-C-X24-C-X-E, forms a Zn2+-binding site
Zn2+
dispensability of zinc and the putative zinc-binding domain in bacterial glutamyl-tRNA synthetase, overview. The association of enzyme GluRS with tRNAGlu but not with ATP is sensitive to perturbations of the zinc binding domain. Natively zinc-bound Ec-GluRS does not require zinc to be active
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2R)-1-(4-methylsulfonylphenyl)-2-(L-methionylsulfone-amido)-1,3-propanediol
-
-
(1R,2R)-1-(4-nitrophenyl)-2-(L-ethionyl-sulfoneamido)-1,3-propanediol
-
competitive inhibition with respect to Asp-tRNAAsn
(1R,2S)-1-(4-nitrophenyl)-2-(L-methionyl-sulfoneamido)-1,3-propanediol
-
-
(1S,2R)-1-(4-nitrophenyl)-2-(L-methionyl-sulfoneamido)-1,3-propanediol
-
-
(1S,2S)-1-(4-nitrophenyl)-2-(L-methionyl-sulfone-amido)-1,3-propanediol
-
-
5'-O-[N-(L-glutamyl)sulfamoyl]adenosine
i.e. glutamyl-sulfamoyl-adenosine or Glu-AMS, tRNAGlu increases the affinity of glutamyl-tRNA synthetase for its inhibitor glutamyl-sulfamoyl-adenosine, an analogue of the aminoacylation reaction intermediate glutamyl-AMP, thermodynamics of the enzyme-inhibitor interactions, overview. A significant entropic contribution for the interactions between Glu-AMS and GluRS in the absence of tRNA or in the presence of the cognate tRNAGlu or of the non-cognate tRNAPhe is indicated. The large negative enthalpy is the dominant contribution to DELTAGb in the absence of tRNA. The affinity of GluRS for Glu-AMS is not altered in the presence of the non-cognate tRNAPhe, but the dissociation constant Kd is decreased 50fold in the presence of tRNAGlu. Presence of an H-bond between Glu-AMS and the 3'-OH oxygen of the 3'-terminal ribose of tRNAGlu in the Glu-AMS/GluRS/tRNAGlu complex, molecular dynamics study
5'-O-[N-(Lglutamyl)sulfamoyl]adenosine
-
competitive inhibitor with respect to L-glutamate
amino levulinic acid
-
indirect inhibition, growth of Acidithiobacillus ferrooxidans in aminolevulic acid inhibits the activity of GluRS1, the reduced activity of GluRS1 is the result of an interaction of the enzyme with heme or any other intermediate tetrrapyrrole, amino levulic acid added to the reaction mixture has no effect in the activity of GluRSs
glutaminyl-beta-ketophosphonate-adenosine
-
i.e. Gln-KPA, competitive inhibition, non-cognate, binds at one site on the monomeric enzyme
glutamyl-beta-ketophosphonate-adenosine
-
i.e. Glu-KPA, selective, competitive inhibition of GluRS, binds at one site on the monomeric enzyme
H2O2
-
GluRS1 activity is reversibly inactivated upon oxidation by hydrogen peroxide, the enzyme loses 90% activity after 10 min at 0.3 mM H2O2. tRNAGlu is able to protect GluRS1 against oxidative inactivation by hemin plus hydrogen peroxide. GluRS1 is the main enzyme responsible for supplying Glu-tRNAGlu for heme biosynthesis. Partial recovery of the enzymatic activity by treatment with DTT or 2-mercaptoethanol
LiCl
-
100 mM, 22% inhibition of ATP-diphosphate exchange, 500 mM, 73% inhibition
N'-(3-chlorophenyl)-N-(5,5-dimethyl-3-[(E)-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]amino]-2-sulfanylidene-1,3-thiazolidin-4-yl)-N-hydroxyurea
competitive with glutamic acid but noncompetitive with ATP
N-(2,4-difluorophenyl)-N'-[4-[1-phenyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]phenyl]urea
noncompetitive with both ATP and glutamic acid
N6-Benzoyl-L-glutamyl AMP
-
specific for glutamyl-tRNA synthetase, does not inhibit glutaminyl-tRNA synthetase
NaCl
-
100 mM, 40% inhibition of ATP-diphosphate exchange, 500 mM, 91% inhibition
NH4Cl
-
100 mM, 31% inhibition of ATP-diphosphate exchange, 500 mM, 82% inhibition of ATP-diphosphate exchange
5'-O-(N-(L-glutamyl)-sulfamoyl)adenosine
-
potent competitive with respect to glutamic acid
5'-O-(N-(L-glutamyl)-sulfamoyl)adenosine
-
potent competitive with respect to glutamic acid
diphosphate
competitive to ATP and L-glutamate, uncompetitive to tRNAGlu
heme
-
indirect mechanism, when intracellular heme is in excess, the cells respond by a dramatic decrease of GluRS activity, heme or any other precursor tetrapyrrole is the intracellular effector that triggers this regulatory mechanism
hemin
-
recombinant GluRS1 enzyme is inhibited in vitro by hemin, but NADPH restores its activity, GluRS2 is also inhibited by hemin to a similar extent as GluRS1
hemin
-
GluRS1 activity is reversibly inactivated upon oxidation by hemin. tRNAGlu is able to protect GluRS1 against oxidative inactivation by hemin plus hydrogen peroxide
KCl
-
100 mM, 15% inhibition of ATP-diphosphate exchange, 500 mM, 62% inhibition
additional information
-
ERS aminoacylation of tRNAGlu is inhibited by the tRNA fragments, RNA-protein interactions, ERS binding of minihelixGlu and fragments ASLGlu and ASLGlu-s2U34, overview
-
additional information
screening of 890 synthetic compounds for inhibitory activity against enzyme GluRS, fourteen compounds with inhibitory activity are identified, overview. Minimum inhibitory concentrations (MICs) are determined for each of the compounds against a panel of pathogenic bacteria
-
additional information
-
screening of 890 synthetic compounds for inhibitory activity against enzyme GluRS, fourteen compounds with inhibitory activity are identified, overview. Minimum inhibitory concentrations (MICs) are determined for each of the compounds against a panel of pathogenic bacteria
-
additional information
-
rGtS and anti-rGtS antiserum significantly inhibits the adhesion of 3 pairs of encapsulated and unencapsulated strains of Streptococcus pneumoniae to human epithelial A549 cells
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Arc1p-N
residues 1-122 of Arc1p, recombinantly expressed, the GluRS-NArc1p-N complex represents an unusual mode of interaction
-
Cytoplasmic protein Arc1p
-
forms a complex with glutamyl-tRNA synthetase, facilitates the delivery of tRNA molecules to the Arc1p-associated aminoacyl-tRNA synthetase
-
Diphosphatase
-
the addition of diphosphatase dramatically stimulates the reaction rate
-
tRNA
GluRS is one of the aminoacyl-tRNA synthetases that require the cognate tRNA for specific amino acid recognition and activation, tRNA serves as the enzyme activator in the first step, and as the substrate in the second step of aminoacylation, overview, On the other hand, the main chain of the glutamate is immature glutamate-binding site in the absence of tRNA
additional information
-
under high heme requirement for respiration increased levels of GluRS occur
-
Arc1p
-
protein from Aspergillus fumigatus, Accession code Q4QTS4, mediates stimulation of tRNA glutamylation
-
Arc1p
accessory protein Arc1p, structure of the interacting domains, crystals structure determination and analysis at 1.9 A resolution, phasing, model building, and refinement of Arc1p, unusual noncrystallographic symmetry in the structure of Arc1p, overview
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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
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).
Down Syndrome
Regulation of glutamate receptor RNA editing and ADAR mRNA expression in developing human normal and Down's syndrome brains.
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
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].
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.
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
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
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.
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.
Neuroblastoma
Expression of N-methyl-D-aspartate (NMDA) and non-NMDA glutamate receptor genes in neuroblastoma, medulloblastoma, and other cells lines.
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
Severe growth deficiency, microcephaly, intellectual disability, and characteristic facial features are due to a homozygous QARS mutation.
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00133
tRNAGln(CUG)
-
wild type enzyme, pH and temperature not specified in the publication
0.00539
tRNAGln(UUG)
-
wild type enzyme, pH and temperature not specified in the publication
0.00235
ATP
-
in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
0.001401
L-glutamate
-
in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
20
L-glutamate
pH and temperature not specified in the publication
0.0000767
tRNAGln
-
in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
0.0000911
tRNAGln
-
in the presence of diphosphatase, in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
0.0000032
tRNAGlu
-
in the presence of diphosphatase, in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
0.0000497
tRNAGlu
-
in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
0.0012
tRNAGlu
pH and temperature not specified in the publication
0.00361
tRNAGlu
-
wild type enzyme, pH and temperature not specified in the publication
additional information
additional information
-
as the KCl concentration is raised from 0 to 100 mM, the Km value for L-glutamate in the reaction with E. coli tRNAGlu is remarkably increased wheras the Km value for glutamate with Thermus thermophilus tRNAGlu is slightly increased
-
additional information
additional information
-
Km-values of mutant enzymes
-
additional information
additional information
-
kinetics, diverse tRNAGlu mutants
-
additional information
additional information
-
Km for diverse modified forms of tRNAAsp and tRNAGlu
-
additional information
additional information
-
steady-state kinetics of isozymes GluRS1 and GluRS2
-
additional information
additional information
Michaelis-Menten steady-state kinetic model
-
additional information
additional information
-
Michaelis-Menten steady-state kinetic model
-
additional information
additional information
steady-state and transient kinetic analysis
-
additional information
additional information
-
steady-state and transient kinetic analysis
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.041
tRNAGln(CUG)
-
wild type enzyme, pH and temperature not specified in the publication
0.006
tRNAGln(UUG)
-
wild type enzyme, pH and temperature not specified in the publication
1.18
ATP
-
in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
1.39
L-glutamate
-
in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
1.5
L-glutamate
pH and temperature not specified in the publication
0.42
tRNAGln
-
in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
2.11
tRNAGln
-
in the presence of diphosphatase, in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
0.04
tRNAGlu
-
wild type enzyme, pH and temperature not specified in the publication
0.43
tRNAGlu
-
in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
1.5
tRNAGlu
pH and temperature not specified in the publication
3.61
tRNAGlu
-
in the presence of diphosphatase, in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
additional information
additional information
-
turnover numbers of wild-type and mutant enzymes
-
additional information
additional information
-
activity with diverse modified forms of tRNAAsp and tRNAGlu
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
704
ATP
-
in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
310
tRNAGln(CUG)
-
wild type enzyme, pH and temperature not specified in the publication
1
tRNAGln(UUG)
-
wild type enzyme, pH and temperature not specified in the publication
0.824
L-glutamate
pH and temperature not specified in the publication
990
L-glutamate
-
in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
5430
tRNAGln
-
in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
23170
tRNAGln
-
in the presence of diphosphatase, in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
10
tRNAGlu
-
wild type enzyme, pH and temperature not specified in the publication
1250
tRNAGlu
pH and temperature not specified in the publication
8650
tRNAGlu
-
in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
112700
tRNAGlu
-
in the presence of diphosphatase, in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.12
(1R,2R)-1-(4-methylsulfonylphenyl)-2-(L-methionylsulfone-amido)-1,3-propanediol
-
pH 7.0, temperature not specified in the publication
0.027
(1R,2R)-1-(4-nitrophenyl)-2-(L-ethionyl-sulfoneamido)-1,3-propanediol
-
pH 7.0, temperature not specified in the publication
0.4
(1R,2R)-1-phenyl-2-(L-methionyl-sulfone-amido)-1,3-propanediol
-
pH 7.0, temperature not specified in the publication
0.37
(1R,2S)-1-(4-nitrophenyl)-2-(L-methionyl-sulfoneamido)-1,3-propanediol
-
pH 7.0, temperature not specified in the publication
2.8
(1S,2R)-1-(4-nitrophenyl)-2-(L-methionyl-sulfoneamido)-1,3-propanediol
-
pH 7.0, temperature not specified in the publication
0.16
(1S,2S)-1-(4-nitrophenyl)-2-(L-methionyl-sulfone-amido)-1,3-propanediol
-
pH 7.0, temperature not specified in the publication
0.0000028
5'-O-[N-(L-glutamyl)sulfamoyl]adenosine
pH and temperature not specified in the publication
0.0007
5'-O-[N-(Lglutamyl)sulfamoyl]adenosine
-
in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C
1.85
chloramphenicol
-
pH 7.0, temperature not specified in the publication
2.9
glutaminyl-beta-ketophosphonate-adenosine
-
pH 7.2, 37°C, versus L-glutamate
0.018
glutamyl-beta-ketophosphonate-adenosine
-
pH 7.2, 37°C, versus L-glutamate
additional information
additional information
-
kinetics of inhibitory tRNA fragments, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0249
N'-(3-chlorophenyl)-N-(5,5-dimethyl-3-[(E)-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]amino]-2-sulfanylidene-1,3-thiazolidin-4-yl)-N-hydroxyurea
Pseudomonas aeruginosa
pH 7.5, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
glutamate and glutamine acceptor activity with wild-type and mutant tRNAGlns with native and recombinant enzyme, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
65
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 55
-
35°C: about 70% of maximal activity, 55°C: about 60% of maximal activity
additional information
additional information
microcalorimetry analysis at 20°C, 30°C and 37°C, thermodynamics in presence and absence of tRNAGlu and inhibitor Glu-AMS and non-cognate aa-AMP
additional information
-
microcalorimetry analysis at 20°C, 30°C and 37°C, thermodynamics in presence and absence of tRNAGlu and inhibitor Glu-AMS and non-cognate aa-AMP
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme has dual substrate specificity for L-glutamate and L-proline, enzyme is part of a large aminoacyl-tRNA synthetases complex
-
-
brenda
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
UniProt
brenda
strain ATCC 23270, isoform 1 and 2, genes gltX1 and gltX2
-
-
brenda
-
201, 210, 211, 212, 213, 215, 216, 217, 218, 219, 220, 232, 651050, 659591, 660375, 672564, 677107, 690792
-
-
brenda
the YadB protein displays 34% identity with the catalytic core of glutamy-tRNA synthetase but lacks the anticodon-binding domain
-
-
brenda
yadB gene encodes a truncated GluRS that lacks the C-terminal third of the protein and, consequently the anticodon binding domain
-
-
brenda
no glutaminyl-tRNA synthetase activity found in crude extract, but a specific aminotransferase activity that changes Glu-tRNAGln to Gln-tRNAGln
-
-
brenda
discriminating enzyme form, purified recombinant enzyme from overexpressing Escherichia coli strain JM109(DE3)
Uniprot
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
EPRS-haploid (Eprs+/-) mice show enhanced viremia and inflammation and delayed viral clearance
metabolism
physiological function
additional information
evolution
-
many bacterial GluRS are capable of recognizing two tRNA substrates: tRNAGlu and tRNAGln, e.g. GluRS from such as Bacillus subtilis, Thermosynechococcus elongatus, and Mycobacterium tuberculosis. In bacteria such as Escherichia coli and Thermus thermophilus that possess glutaminyl-tRNA synthetase (GlnRS), the cognate aminoacylating enzyme for tRNAGln, GluRS exclusively glutamylates tRNAGlu. tRNA-GluRS interaction in bacteria is also associated with phylum-specific idiosyncrasies, structure-function analysis, overview
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
evolution
the structures of the active sites of bacterial and mammalian GluRSs differ significantly
evolution
the tRNA binding site is less conserved than either the Glu or the ATP binding site. Certain amino acids, including Arg147, which interacts with the tRNAGlu C74 phosphate, and Asp44 and Arg47, which interact with the 2'-hydroxyl group of C75, as well as Tyr187 and Thr43, which interact with the adenosine base and the 5'-hydroxyl group of A76, are strictly conserved
evolution
Saccharomyces cerevisiae ATCC 204508 / S288c
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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
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evolution
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
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the tRNA binding site is less conserved than either the Glu or the ATP binding site. Certain amino acids, including Arg147, which interacts with the tRNAGlu C74 phosphate, and Asp44 and Arg47, which interact with the 2'-hydroxyl group of C75, as well as Tyr187 and Thr43, which interact with the adenosine base and the 5'-hydroxyl group of A76, are strictly conserved
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metabolism
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the sensitivity to oxidation of GluRS1 might provide a means to regulate tetrapyrrole and protein biosynthesis in response to extreme changes in both the redox and heme status of the cell via a single enzyme. The glutamate moiety of Glu-tRNAGlu is transformed to glutamate semialdehyde by the glutamyl-tRNA reductase and is subsequently transformed to 4-aminolevulinic acid, the universal precursor of tetrapyrroles, by the glutamate semialdehyde amidotransferase
metabolism
under conditions of stress, several MSC components, including EPRS, methionyl-tRNA synthetase (MRS), lysyl-tRNA synthetase (KRS), AIMP1 and AIMP2, are released from the complex through post-translational modifications to exert activities during non-translational events such as inflammation, cell metabolism, angiogenesis, and tumorigenesis. Phosphorylation is the critical regulatory mechanism that determines the non-translational function of ARSs in cells, overview
metabolism
under conditions of stress, several MSC components, including EPRS, methionyl-tRNA synthetase (MRS), lysyl-tRNA synthetase (KRS), AIMP1 and AIMP2, are released from the complex through post-translational modifications to exert activities during non-translational events such as inflammation, cell metabolism, angiogenesis, and tumorigenesis. Phosphorylation is the critical regulatory mechanism that determines the non-translational function of ARSs in cells, overview
physiological function
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cytoplasmic glutamyl tRNA synthetase gene ers1 is an Moc3 interacting element. Cell growth is moderately affected by cGluRS over-expression under de-repressed conditions. Over-expression of ers1 stimulates sexual differentiation
physiological function
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mitochondrial glutamyl tRNA synthetase gene ers2 is an Moc3 interacting element. Cell growth is severely affected by ers2 over-expression under de-repressed conditions. Under repressed conditions, the cells multiply quickly. In addition, cells over-expressing ers2 show higher mating efficiency than control
physiological function
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in cells containing glutaminyl-tRNA synthetase, GlnRS, discriminating GluRS specifically aminoacylates tRNAGlu with glutamate. One of two GluRSs from the extremophile Acidithiobacillus ferrooxidans, is inactivated when intracellular heme is elevated suggesting a specific role for GluRS1 in the regulation of tetrapyrrole biosynthesis
physiological function
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mechanism of translation control of enzyme EPRS involving increased translation initiation stringency during stress-induced eIF2alpha-P, facilitated ribosome bypass of upstream ORFs, allowing for increased translation of the EPRS coding region. The 5'-leader of the EPRS mRNA directs preferential translation. Although a portion of the ribosomes that translate uORF2 can reinitiate downstream, scanning ribosomes also bypass uORF2 because of its noncanonical UUG1 initiation codon and initiate translation at the downstream coding sequence. UUG1 and CUG2 are overall repressing elements in EPRS translation control. Model for EPRS translation control, overview
physiological function
the multi-tRNA synthetase complex (MSC) component glutamyl-prolyl-tRNA synthetase (EPRS) switched its function following viral infection and exhibited potent antiviral activity. Infection-specific phosphorylation of EPRS at a Ser induces its dissociation from the MSC, after which it is guided to the antiviral signaling pathway, where it interacts with PCBP2, a negative regulator of mitochondrial antiviral signaling protein (MAVS) that is critical for antiviral immunity. EPRS protects MAVS from PCBP2-mediated ubiquitination. The stimulus-inducible activation of MAVS by enzyme EPRS suggests an unexpected role for the MSC as a regulator of immune responses to viral infection. Phosphorylation of EPRS at a Ser is the driving force that leads to the antiviral roles of EPRS in regulating MAVS
physiological function
the multi-tRNA synthetase complex (MSC) component glutamyl-prolyl-tRNA synthetase (EPRS) switched its function following viral infection and exhibited potent antiviral activity. Infection-specific phosphorylation of EPRS at Ser990 induces its dissociation from the MSC, after which it is guided to the antiviral signaling pathway, where it interacts with PCBP2, a negative regulator of mitochondrial antiviral signaling protein (MAVS) that is critical for antiviral immunity. EPRS protects MAVS from PCBP2-mediated ubiquitination. The stimulus-inducible activation of MAVS by enzyme EPRS suggests an unexpected role for the MSC as a regulator of immune responses to viral infection. Phosphorylation of EPRS at Ser990 is the driving force that leads to the antiviral roles of EPRS in regulating MAVS
additional information
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targets for oxidation-based inhibition are cysteines from a SWIM zinc-binding motif located in the tRNA acceptor helix-binding domain. Oxidation of the metal-binding site cysteine of GluRS1 significantly impaired catalysis. Also, binding of ATP or tRNA protects the distant cysteines of the SWIM motif
additional information
analysis of the contributions to aminoacylation efficiency made by the N-terminal Arc1p domain of Saccharomyces cerevisiae GluRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview, overview
additional information
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analysis of the contributions to aminoacylation efficiency made by the N-terminal Arc1p domain of Saccharomyces cerevisiae GluRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview, overview
additional information
homology structure modeling using structures of GluRSs identified from Burkholderia thailandensis and Thermosynechococcus elongatus, Uniprot IDs Q2SX36 and Q8DLI5, respectively, as search template, molecular docking
additional information
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homology structure modeling using structures of GluRSs identified from Burkholderia thailandensis and Thermosynechococcus elongatus, Uniprot IDs Q2SX36 and Q8DLI5, respectively, as search template, molecular docking
additional information
the enzyme is part of a multi-tRNA synthetase complex (MSC)
additional information
the enzyme is part of a multi-tRNA synthetase complex (MSC)
additional information
Saccharomyces cerevisiae ATCC 204508 / S288c
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analysis of the contributions to aminoacylation efficiency made by the N-terminal Arc1p domain of Saccharomyces cerevisiae GluRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview, overview
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Show AA Sequence and Transmembrane Helices (54930 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46000
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1 * 56000 (catalytic subunit) + 1 * 46000 (no detectable enzymatic activity, protective function), SDS-PAGE
54000
55000
56000
58000
62000
65500
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1 * 65500, enzyme copurifies with a 46000 MW polypeptide which increases the affinity for glutamate and ATP, and stabilizes it against heat inactivation, SDS-PAGE
55000
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x * 55000, recombinant enzyme expressed in Bacillus subtilis, SDS-PAGE
56000
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1 * 56000 (catalytic subunit) + 1 * 46000 (no detectable enzymatic activity, protective function), SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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x * 53901, calculation from nucleotide sequence
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dimer
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1 * 56000 (catalytic subunit) + 1 * 46000 (no detectable enzymatic activity, protective function), SDS-PAGE
dimer
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the active forms are dimers, which are in equilibrium with inactive monomers
monomer
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1 * 65500, enzyme copurifies with a 46000 MW polypeptide which increases the affinity for glutamate and ATP, and stabilizes it against heat inactivation, SDS-PAGE
monomer
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1 * 65500, enzyme copurifies with a 46000 MW polypeptide which increases the affinity for glutamate and ATP, and stabilizes it against heat inactivation, SDS-PAGE
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additional information
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Acidithiobacillus ferrooxidans GluRS1 contains cysteines 98, 100 and 125 together with glutamate 127 clustered in the catalytic domain
additional information
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the human EPRS consists of four major domains: an N-terminal elongation factor-1Bgamma-like domain, an ERS catalytic domain, a 300 amino acid linker domain containing three tandem WHEP domains, and a C-terminal PRS catalytic domain
additional information
the enzyme is part of a multi-tRNA synthetase complex (MSC)
additional information
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enzyme is part of a high molecular mass aminoacyl-tRNA synthetase complex, which has a coherent structure, that can be visualized by electron microscopy
additional information
the enzyme is part of a multi-tRNA synthetase complex (MSC)