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Information on EC 6.1.1.18 - glutamine-tRNA ligase
for references in articles please use BRENDA:EC6.1.1.18
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EC Tree 6 Ligases
6.1 Forming carbon-oxygen bonds
6.1.1 Ligases forming aminoacyl-tRNA and related compounds
6.1.1.18 glutamine-tRNA ligase
The enzyme appears in viruses and cellular organisms
- 6.1.1.18
- synthetases
- aminoacyl-trna
- aminoacylation
-
anticodon
- glutamyl-trna
-
glutaminylation
- gln-trnagln
-
noncognate
-
aarss
-
trna-dependent
-
mischarging
-
transamidation
- asnrs
- aspartyl-trna
- trna2gln
-
nondiscriminating
- trnatyr
-
misaminoacylation
- glurss
-
misacylated
- ilers
- cysrs
-
anticodon-binding
- valrs
- gatcab
-
gln-trna
- drug development
showSynonyms
glnrs, glutaminyl trna synthetase, glutaminyl-transfer rna synthetase, cytosolic glutaminyl-trna synthetase, class i glutaminyl-trna synthetase, glutamyl/glutaminyl-trna synthetase, l-glutamine:trnagln ligase (amp-forming), more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Gln4
GlnRS
Glutamine translase
-
-
-
-
Glutamine--tRNA ligase
-
-
-
-
Glutamine-tRNA synthetase
-
-
-
-
Glutaminyl-transfer ribonucleate synthetase
-
-
-
-
Glutaminyl-transfer RNA synthetase
-
-
-
-
Glutaminyl-tRNA synthetase
glutamyl/glutaminyl-tRNA synthetase
QRS
Synthetase, glutaminyl-transfer ribonucleate
-
-
-
-
Vegetative specific protein H4
-
-
-
-
GlnRS
-
-
-
-
Glutaminyl-tRNA synthetase
-
-
-
-
Glutaminyl-tRNA synthetase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln
active site residues are Tyr240 and Phe90
-
ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln
aminoacylation reaction mechanism, substrate binding sites, Tyr211 and a water molecule are responsible for recognition of both hydrogen atoms of the nitrogen of glutamine sidechain, which is esstial for substrate recognition
ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln
binding of ATP and of tRNAGln induces conformational changes that change the interaction of the enzyme with the cognate tRNA, crucial for substrate recognition and selectivity
-
ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln
structurefunction relationship, overview
ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln
structurefunction relationship, overview
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
esterification
Aminoacylation
-
-
-
-
esterification
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-glutamine:tRNAGln ligase (AMP-forming)
-
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CAS REGISTRY NUMBER
COMMENTARY
9075-59-6
-
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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 + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
Substrates: primary binding pocket structure, overview
Products: -
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?
ATP + L-glutamine + tRNAGln in unfractionated tRNA
?
-
Substrates: -
Products: -
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?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + glutamyl-tRNAGln
Substrates: -
Products: -
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?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + glutamyl-tRNAGln
Substrates: activity also with Gln-RS, EC 6.1.1.18, mutant C229R
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
Products: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
Products: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: -
Products: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
Substrates: -
Products: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
235, 236, 237, 238, 239, 240, 241, 243, 244, 247, 248, 249, 250, 251, 255, 649850, 651246, 653817, 662374, 690792, 703714
Substrates: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
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r
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: specific tRNA-dependent amino acid recognition involves Asp66, Tyr211, and Phe233, which interact with A76 of tRNAGln and glutamine
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ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: two-step reaction: 1. recognition of appropriate amino acid by the enzyme and formation of an enzyme-bound mixed anhydride, the aminoacyl-AMP, under release of diphosphate, 2. transfer of the activated amino acid to the CCA end of the cognate tRNA to form aminoacyl-tRNA and AMP, both steps are tRNA-dependent
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r
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: long-range intramolecular signaling in a tRNA synthetase complex
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ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: the enzyme is electrostatically optimized for binding of its cognate substrates
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: a two-step reaction
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ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: a two-step reaction, with a distinct role in induced-fit for Glu73
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ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: wild-type tRNA, and var-AGGUtRNA, mechanism of the difference in the binding affinity of endogenous tRNAGln to the enzyme caused by noninterface nucleotides in variable loop, overview
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: analysis of domain functions in enzyme-substrate interactions, overview
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Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: primary binding pocket structure, overview
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: tRNA substrate from bovine liver
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ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
Products: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: -
Products: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: a two-step aminoacylation reaction
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Saccharomyces cerevisiae ATCC 204508 / S288c
Substrates: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Saccharomyces cerevisiae ATCC 204508 / S288c
Substrates: a two-step aminoacylation reaction
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Toxoplasma gondii ATCC 50611 / Me49
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
Products: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
Products: -
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?
ATP + L-glutamine + tRNAGln(CUG)
AMP + diphosphate + L-glutaminyl-tRNAGln(CUG)
Substrates: -
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?
ATP + L-glutamine + tRNAGln(CUG)
AMP + diphosphate + L-glutaminyl-tRNAGln(CUG)
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
Substrates: -
Products: -
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?
ATP + L-glutamine + tRNAGln(UUG)
AMP + diphosphate + L-glutaminyl-tRNAGln(UUG)
Substrates: -
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?
ATP + L-glutamine + tRNAGln(UUG)
AMP + diphosphate + L-glutaminyl-tRNAGln(UUG)
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
Substrates: -
Products: -
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?
additional information
?
-
Substrates: the Deinococcus radiodurans GlnRS is a structural hybrid between conventional GlnRS and AdT, EC 6.3.5.6, structurefunction relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the Deinococcus radiodurans GlnRS is a structural hybrid between conventional GlnRS and AdT, EC 6.3.5.6, structurefunction relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview
Products: -
Products: -
?
additional information
?
-
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
Substrates: the Deinococcus radiodurans GlnRS is a structural hybrid between conventional GlnRS and AdT, EC 6.3.5.6, structurefunction relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: several noncognate tRNAs stimulate ATP-diphosphate exchange
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?
additional information
?
-
-
Substrates: lack of tRNA-independent diphosphate exchange
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?
additional information
?
-
-
Substrates: lack of tRNA-independent diphosphate exchange
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?
additional information
?
-
-
Substrates: dimethyl sulfoxide stimulates the charging of several noncognate tRNA's with glutamine
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?
additional information
?
-
-
Substrates: tRNA binding triggers aminoacyl-adenylate formation and diphosphate exchange
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?
additional information
?
-
-
Substrates: importance of the acceptor binding domain for accurate recognition of tRNA
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?
additional information
?
-
-
Substrates: conformational changes are induced by tRNAGln binding not by binding of tRNAGlu
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?
additional information
?
-
-
Substrates: phylogenetic analysis
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?
additional information
?
-
-
Substrates: structure function analysis, overview
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?
additional information
?
-
Substrates: ternary complexed GlnRS bound to tRNAGln and the Gln-AMP analogue is catalytically active and has undergone the first step of the aminoacylation reaction
Products: -
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?
additional information
?
-
-
Substrates: ternary complexed GlnRS bound to tRNAGln and the Gln-AMP analogue is catalytically active and has undergone the first step of the aminoacylation reaction
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?
additional information
?
-
-
Substrates: eukaryotic GlnRS evolves from GluRS by gene duplication and horizontally transfers to bacteria
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?
additional information
?
-
-
Substrates: wild-type GlnRS catalyzes Glu-tRNAGln synthesis 1000000fold less efficiently than the cognate reaction
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?
additional information
?
-
Substrates: wild-type GlnRS catalyzes Glu-tRNAGln synthesis 1000000fold less efficiently than the cognate reaction
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?
additional information
?
-
-
Substrates: GlnRS forms a 1:1 molar complex with tRNAGln
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?
additional information
?
-
Substrates: GlnRS has adetectable tRNA-acylation activity for its D-amino acid substrate
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?
additional information
?
-
-
Substrates: GlnRS has adetectable tRNA-acylation activity for its D-amino acid substrate
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?
additional information
?
-
-
Substrates: the enzyme interacts with the apoptosis signal-regulating kinase ASK1, which involves the active sites of the enzymes and inhibits AKS1, the association is mediated and enhanced by glutamine, it is inhibited by Fas ligation, the enzyme inhibits ASK1-induced apoptosis
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?
additional information
?
-
Substrates: human GlnRS cannot aminoacylate bacterial tRNAGln from Escherichia coli, but recognition of tRNAGln by human and yeast GlnRSs may be conserved
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?
additional information
?
-
-
Substrates: human GlnRS cannot aminoacylate bacterial tRNAGln from Escherichia coli, but recognition of tRNAGln by human and yeast GlnRSs may be conserved
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?
additional information
?
-
-
Substrates: glutamine-dependent ATP-diphosphate exchange
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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
AMP + diphosphate + glutamyl-tRNAGln
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
Products: -
Products: -
r
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: long-range intramolecular signaling in a tRNA synthetase complex
Products: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
Products: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
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ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Saccharomyces cerevisiae ATCC 204508 / S288c
Substrates: -
Products: -
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?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Toxoplasma gondii ATCC 50611 / Me49
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: phylogenetic analysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: eukaryotic GlnRS evolves from GluRS by gene duplication and horizontally transfers to bacteria
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme interacts with the apoptosis signal-regulating kinase ASK1, which involves the active sites of the enzymes and inhibits AKS1, the association is mediated and enhanced by glutamine, it is inhibited by Fas ligation, the enzyme inhibits ASK1-induced apoptosis
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
binding of ATP induces conformational changes that change the interaction of the enzyme with the cognate tRNA
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutaminyl-beta-ketophosphonate-adenosine
-
i.e. Gln-KPA, selective, competitive inhibition of GlnRS, contrast, Gln-KPA inhibits GlnRS by binding competitively but weakly at two distinct sites on the enzyme, the glutamine and the AMP modules of Gln-KPA, connected by the beta-ketophosphonate linker, cannot bind GlnRS simultaneously, and that one Gln-KPA molecule binds the AMP-binding site of GlnRS through its AMP module, whereas another Gln-KPA molecule binds the glutamine-binding site through its glutamine module, mechanism, overview
glutamyl-beta-ketophosphonate-adenosine
-
i.e. Glu-KPA, competitive inhibition, non-cognate, binds weakly at one site on the monomeric enzyme
L-Glutamic acid
-
competitive inhibition of the wild-type and mutant enzymes
5'-O-[N-(L-glutaminyl)sulfamoyl] adenosine
-
i.e. QSI, competitive to glutamine
5'-O-[N-(L-glutaminyl)sulfamoyl] adenosine
i.e. QSI, glutaminyl-adenylate analogue, competitive to glutamine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
putrescine
-
can partially replace Mg2+ in activation, with 32% efficiency
spermidine
-
can partially replace Mg2+ in activation, with 12% efficiency
spermine
-
significant stimulation of ATP-diphosphate exchange and aminoacylation in presence of limited MgCl2 concentrations, cannot totally replace Mg2+
spermine
-
can partially replace Mg2+ in activation, with 35% efficiency
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brain Diseases
The crystal structure of human GlnRS provides basis for the development of neurological disorders.
Nervous System Diseases
The crystal structure of human GlnRS provides basis for the development of neurological disorders.
Tuberculosis
Atypical OmpR/PhoB subfamily response regulator GlnR of actinomycetes functions as a homodimer, stabilized by the unphosphorylated conserved Asp-focused charge interactions.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.7
L-glutamine
pH and temperature not specified in the publication
0.00019
tRNAGln
pH and temperature not specified in the publication
additional information
additional information
effect of the isolated Yqey domain on the kinetic properties of GlnRS, overview
-
additional information
additional information
-
effect of the isolated Yqey domain on the kinetic properties of GlnRS, overview
-
additional information
additional information
kinetics, tRNA substrate binding: calculation of the enthalpic and entropic contributions to the binding free energy with the molecular mechanics-Poisson-Boltzmann/surface area method, the entropic difference plays an important role in the difference in binding free energies, overview
-
additional information
additional information
-
single turnover kinetics, and steady-state kinetics of recombinant mutant enzymes, overview
-
additional information
additional information
-
kinetics of the mutant enzyme compared to wild-type GlnRS, EC 6.1.1.18, overview
-
additional information
additional information
kinetics of the mutant enzyme compared to wild-type GlnRS, EC 6.1.1.18, overview
-
additional information
additional information
-
no KM value for L-glutamate with the wild-type enzyme due to no saturation, kinetics of wild-type and mutant enzymes, overview. Kinetics of extended-loop GlnRS mutants, overview
-
additional information
additional information
no KM value for L-glutamate with the wild-type enzyme due to no saturation, kinetics of wild-type and mutant enzymes, overview. Kinetics of extended-loop GlnRS mutants, overview
-
additional information
additional information
-
pre-steady-state kinetics, negative allosteric coupling, overview
-
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
1.4
L-glutamine
pH and temperature not specified in the publication
1.4
tRNAGln
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.824
L-glutamine
pH and temperature not specified in the publication
7368.4
tRNAGln
pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.65
glutaminyl-beta-ketophosphonate-adenosine
-
pH 7.2, 37°C, versus L-glutamine
2.8
glutamyl-beta-ketophosphonate-adenosine
-
pH 7.2, 37°C, versus L-glutamine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00024 - 0.00033
recombinant mutant Y57H/R515W enzyme in crude cell extract, pH 7.5, 37°C
0.00028
recombinant mutant G45V/R403W enzyme in crude cell extract, pH 7.5, 37°C
0.00041
recombinant mutant G45V enzyme in crude cell extract, pH 7.5, 37°C
0.00051
recombinant mutant R515W enzyme in crude cell extract, pH 7.5, 37°C
0.00058
recombinant mutant Y57H enzyme in crude cell extract, pH 7.5, 37°C
0.00079 - 0.00083
recombinant wild-type enzyme in crude cell extract, pH 7.5, 37°C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain HAPPY101, plasmid-mediated expression of detrimental GlnRS mutants, which cannot complement the chromosomal glnS deletion in Escherichia coli strain X3R2
-
-
brenda
strains UT172 and X3R2, and deletion mutants with C-terminal truncations and N-terminal truncations
-
-
brenda
full-length and truncated enzyme form lacking the NH2-terminal domain
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
QARS is highly expressed in the developing fetal human cerebral cortex in many cell types
brenda
QARS is widely expressed in fetal human brain during early development
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme DNA sequence contains a lysine-rich nuclear targeting sequence motif
brenda
-
localization of cytoplasmic GlnRS in mitochondrial Gln-tRNA synthesis
brenda
-
localization of cytoplasmic GlnRS in mitochondrial Gln-tRNA synthesis. Saccharomyces cerevisiae imports the cytosolic pathway for Gln-tRNA synthesis into the mitochondrion
brenda
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
physiological function
additional information
evolution
-
the architecture of the GlnRS RNP has differentiated over evolutionary time to maintain glutamine-binding affinity at a weak level, and provides strong evidence for long-distance communication
evolution
human GlnRS is a monomeric class I aminoacyl-tRNA synthetase family member
evolution
the enzyme belongs to the class I aminoacyl-tRNA synthetase family
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. 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
Saccharomyces cerevisiae ATCC 204508 / S288c
-
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. 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
-
malfunction
heterozygous mutations in GlnRS cause severe brain disorders. Pathological mutations mapping in the N-terminal domain alter the domain structure, and decrease catalytic activity and stability of GlnRS, whereas missense mutations in the catalytic domain induce misfolding of the enzyme. The reduced catalytic efficiency and a propensity of GlnRS mutants to misfold trigger the disease development
malfunction
mutations in QARS, encoding glutaminyl-tRNA synthetase, cause progressive microcephaly, cerebral-cerebellar atrophy, and intractable seizures
physiological function
-
negative allosteric coupling plays a key role in enforcing the selective RNA-amino acid pairing at the heart of the genetic code
physiological function
cytosolic glutaminyl-tRNA synthetase (GlnRS) is the singular enzyme responsible for translation of glutamine codons
additional information
-
generation of a comprehensive mapping of intramolecular communication in the glutaminyl-tRNA synthetase:tRNAGln complex, interaction analysis, detailed overview. Distinct coupling amplitudes for glutamine binding and aminoacyl-tRNA formation on the enzyme, respectively, implying the existence of multiple signaling pathways. Signaling from binding of the tRNA inner elbow, overview. Seven protein contacts with the distal tRNA vertical arm each weaken glutamine binding affinity across distances up to 40 A
additional information
analysis of the contributions to aminoacylation efficiency made by the N-terminal Yqey domain of Saccharomyces cerevisiae GlnRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview
additional information
-
analysis of the contributions to aminoacylation efficiency made by the N-terminal Yqey domain of Saccharomyces cerevisiae GlnRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview
additional information
in the multisynthetase complex (MSC) subcomplex (RQA1 subcomplex) comprising arginyl-tRNA synthetase (ArgRS), glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 ((AIMP1)/p43), the N-terminal domain of ArgRS forms a long coiled-coil structure with the N-terminal helix of AIMP1 and anchors the C-terminal core of GlnRS, thereby playing a central role in assembly of the three components. Mutation of AIMP1 destabilizes the N-terminal helix of ArgRS and abrogates its catalytic activity. The MSC complex is comprised of nine different aminoacyl-tRNA synthetases (ARSs) and three accessary proteins. Mutation of the N-terminal helix of ArgRS liberates GlnRS, which is known to control cell death. This ternary RQA1 complex is further anchores to AIMP2/p38 through interaction with AIMP1. Importance of interactions between the N-terminal domains of ArgRS and AIMP1 for the catalytic and noncatalytic activities of ArgRS and for the assembly of the higher-order MSC protein complex. The N-terminal domain of human GlnRS interacts with ArgRS in the MSC, GlnRS is anchored to the complex by the interaction of its C-terminal core with the Hb helix of ArgRS, structure-function analysis, overview. The RQA1 subcomplex also can form a hexameric structure
additional information
molecular dynamics modeling of L-GlnAMP using the PDB ID 1QTQ X-ray structure, superimposed based on their protein/tRNA environment, enzyme molecular dynamics simulation amd modeling, structure-function analysis, detailed overview
additional information
-
molecular dynamics modeling of L-GlnAMP using the PDB ID 1QTQ X-ray structure, superimposed based on their protein/tRNA environment, enzyme molecular dynamics simulation amd modeling, structure-function analysis, detailed overview
additional information
structure-function analysis, importance of the N-terminal domain for GlnRS function, overview
additional information
-
structure-function analysis, importance of the N-terminal domain for GlnRS function, overview
additional information
Saccharomyces cerevisiae ATCC 204508 / S288c
-
analysis of the contributions to aminoacylation efficiency made by the N-terminal Yqey domain of Saccharomyces cerevisiae GlnRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
68500
-
electrophoresis of the native enzyme in polyacrylamide gels of various concentrations
additional information
additional information
-
structural similarities in glutaminyl-tRNA synthetase and methionyl-tRNA synthetase outside the respective dinucleotide-fold domains
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
monomer
the enzyme adopts a boomerang-like shaped structure built of 5 domains, domain organization of the intact enzyme and structure of the functionally important N-terminal domain, modeling of overall structure and domain organization of wild-type, full-length enzyme, structure-function analysis, overview
additional information
-
determination of glutamyl/glutaminyl-tRNA synthetase domain sequences in the proteosome of the organism, classification of proteins into homologous groups by determination and validation of Markov clusters of homologous subsequences, MACHOS, for structure-function analysis, method evaluation, overview
additional information
the enzyme possesses a C-terminal extension of 215 residues appending the anticodon-binding domain, the Yqey domain, which constitutes a paralog of the Saccharomyces cerevisiae Yqey protein, structure-function relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview
additional information
-
the enzyme possesses a C-terminal extension of 215 residues appending the anticodon-binding domain, the Yqey domain, which constitutes a paralog of the Saccharomyces cerevisiae Yqey protein, structure-function relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview
additional information
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
the enzyme possesses a C-terminal extension of 215 residues appending the anticodon-binding domain, the Yqey domain, which constitutes a paralog of the Saccharomyces cerevisiae Yqey protein, structure-function relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview
-
additional information
-
determination of glutamyl/glutaminyl-tRNA synthetase domain sequences in the proteosome of the organism, classification of proteins into homologous groups by determination and validation of Markov clusters of homologous subsequences, MACHOS, for structure-function analysis, method evaluation, overview
additional information
GlnRS structure networks, detection method development for accounting side chain interactions, yet providing a global view of the ligand-induced conformational changes, and understand allosteric changes mediated by the binding of ligands, usage of crystal structures: PDB IDs 1nyl, 1qtq, 1o0b, and 1o0c, overview
additional information
-
GlnRS structure networks, detection method development for accounting side chain interactions, yet providing a global view of the ligand-induced conformational changes, and understand allosteric changes mediated by the binding of ligands, usage of crystal structures: PDB IDs 1nyl, 1qtq, 1o0b, and 1o0c, overview
additional information
molecular dynamics simulations on wild-type tRNA, var-AGGUtRNA, and tRNA-GlnRS complexes, overview
additional information
-
long-range signal propagation from the tRNA anticodon is dynamically driven, whereas shorter pathways are mediated by induced-fit rearrangements, structure modelling, overview
additional information
-
targeting into the multienzyme complex is mediated by the C-terminal catalytic domain
additional information
-
determination of glutamyl/glutaminyl-tRNA synthetase domain sequences in the proteosome of the organism, classification of proteins into homologous groups by determination and validation of Markov clusters of homologous subsequences, MACHOS, for structure-function analysis, method evaluation, overview
additional information
in the multisynthetase complex (MSC) subcomplex (RQA1 subcomplex) comprising arginyl-tRNA synthetase (ArgRS), glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 ((AIMP1)/p43), the N-terminal domain of ArgRS forms a long coiled-coil structure with the N-terminal helix of AIMP1 and anchors the C-terminal core of GlnRS, thereby playing a central role in assembly of the three components. The MSC complex is comprised of nine different aminoacyl-tRNA synthetases (ARSs) and three accessary proteins. This ternary RQA1 complex is further anchores to AIMP2/p38 through interaction with AIMP1. Importance of interactions between the N-terminal domains of ArgRS and AIMP1 for the assembly of the higher-order MSC protein complex. The N-terminal domain of human GlnRS interacts with ArgRS in the MSC, GlnRS is anchored to the complex by the interaction of its C-terminal core with the Hb helix of ArgRS, structure-function analysis, overview. ArgRS, GlnRS, and AIMP1 form a 1:1:1 ternary complex in the asymmetric unit, besides a trimeric, the RQA1 subcomplex also can form a hexameric structure
additional information
-
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
-
determination of glutamyl/glutaminyl-tRNA synthetase domain sequences in the proteosome of the organism, classification of proteins into homologous groups by determination and validation of Markov clusters of homologous subsequences, MACHOS, for structure-function analysis, method evaluation, overview
additional information
-
determination of glutamyl/glutaminyl-tRNA synthetase domain sequences in the proteosome of the organism, classification of proteins into homologous groups by determination and validation of Markov clusters of homologous subsequences, MACHOS, for structure-function analysis, method evaluation, overview
additional information
-
determination of glutamyl/glutaminyl-tRNA synthetase domain sequences in the proteosome of the organism, classification of proteins into homologous groups by determination and validation of Markov clusters of homologous subsequences, MACHOS, for structure-function analysis, method evaluation, overview
additional information
Saccharomyces cerevisiae GlnRS contains an N-terminal domain that is conserved in eukaryotic enzymes and is not present in bacterial homologues, The N-terminal domain consists of 187 amino acids organized in two helical subdomains and is followed by an unstructured 26-residue linker that links it with the main catalytic portion of the enzyme, the C-terminal domain, computational modeling
additional information
-
Saccharomyces cerevisiae GlnRS contains an N-terminal domain that is conserved in eukaryotic enzymes and is not present in bacterial homologues, The N-terminal domain consists of 187 amino acids organized in two helical subdomains and is followed by an unstructured 26-residue linker that links it with the main catalytic portion of the enzyme, the C-terminal domain, computational modeling
additional information
Saccharomyces cerevisiae ATCC 204508 / S288c
-
Saccharomyces cerevisiae GlnRS contains an N-terminal domain that is conserved in eukaryotic enzymes and is not present in bacterial homologues, The N-terminal domain consists of 187 amino acids organized in two helical subdomains and is followed by an unstructured 26-residue linker that links it with the main catalytic portion of the enzyme, the C-terminal domain, computational modeling
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant full-length GlnRS grown in microbatch in the presence of PEG 3350, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement
vapour-diffusion method. Orthorombic crystals are obtained that belong to space group P2(1)2(1)2(1) and diffract to 2.3 A resolution
-
analysis of the crystal structure of GlnRS-tRNAGln complex bound to the glutaminyl adenylate analogue 5'-O-[N-(L-Gln)sulfamoyl] adenosine
-
cocrystallization of the purified enzyme with tRNAGln and inhibitor QSI, X-ray diffraction structure determination at 2.4 A resolution and analysis
crystal structure of three misacylating mutants of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNAGln and ATP
-
crystals of the GlnRS-tRNA(2'H)Gln complex bound to the ATP analog AMPCPP and glutamine are grown by microseeding with crystals of the GlnRS-tRNAGln-ATP ternary complex. Crystals grew in 1-2 weeks by vapor diffusion over a reservoir containing 2 M ammonium sulfate, 10 mM Pipes, pH 7.5, 10 mM MgCl2 and 2 mM DTT
-
detailed structural comparison between Met-tRNA synthetase and Gln-tRNA synthetase
-
GlnRS-tRNAGln complex, 6.6 mg/ml protein in 10 mM PIPES, pH 7.5, 10 mM MgCl2, and 1.8-5.4 mM tRNA. The tRNA/analog solution is then mixed with equal volumes of a 6.3 mg/ml solution of GlnRS, containing 5mM PIPES, pH 7.0, and 5 mM 2-mercaptoethanol, X-ray diffraction structure determination and analysis at 2.6 A resolution
purified recombinant GlnRS C229R-tRNAGln complex, a protein solution containing 6.3mg/ml GlnRS prepared in 5 mM PIPES, pH 7.0, 5 mM 2-mercaptoethanol, is mixed with the tRNAGln solution, X-ray diffraction structure determination and analysis at 2.6 A resolution
the entire anticodon loop provides essential sites for glutaminyl tRNA synthetase discrimination among tRNA molecules
-
purified multisynthetase complex (MSC) subcomplex comprising ArgRS, glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)/p43, X-ray diffraction structure determination and analysis
purified recombinant His-tagged wild-type and mutant enzymes, sitting drop vapour diffusion method, apo wild-type GlnRS crystallizes from 0.1 M calcium acetate, 0.1 M Tris, pH 6.0, 12.5% w/v PEG 3350, and 60 mM Gly-Gly-Gly, the Y57H mutant crystallizes from 0.1 M ammonium acetate, 0.1 M Bis-Tris, pH 5.5, and 17% w/v PEG 10 000, and the G45V mutant crystallizes from 0.15 M ammonium acetate, 0.1 M Bis-Tris, pH 5.5, 3% w/v PEG 20 000, and 10 mM EDTA, 16°C, X-ray diffraction strutcure determination and analysis at 2.4 A, 3.3 A, and 2.7 A resolution, respectively
microbatch-under-oil method, using 50 mM NH4Br, 50 mM KC2H3O2, 100 mM HEPES (pH 7.5), and 20% (w/v) polyethylene glycol 20000
purified recombinant His-tagged N-terminal and C-terminal domain fragments, sitting drop vapour diffusion method, mixing of 20 mg/ml protein in 25 mM Tris pH 7.5, 150 mM KCl, and 10 mM MgCl2, with 2 M ammonium sulfate, 5% isopropanol for the N-terminal fragment and 2 M ammonium sulfate for the C-terminal fragment, X-ray diffraction structure determination and analysis. No crystallization conditions can be identified for the full-length protein
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C229R
site-directed mutagenesis, transplanting the conserved arginine residue from glutamyl-tRNA synthetase, EC 6.1.1.17, to glutaminyltRNA synthetase improves the KM of GlnRS for noncognate glutamate
C229R/Q255I
site-directed mutagenesis, comparison of mutant activity with glutamate and glutamine to charge tRNAGln to the wild-type activity, the mutant shows no activity with L-Gln, but weakly with L-Glu
C229R/Q255I/S227A/F233Y
site-directed mutagenesis, comparison of mutant activity with glutamate and glutamine to charge tRNAGln to the wild-type activity, the mutant shows no activity with L-Gln, but activity with L-Glu
cGluGlnRS
-
a chimeric protein, consisting of the catalytic domain of GluRS and the anticodon-binding domain of GlnRS, is constructed
D235A
-
saturation mutagenesis, only little complementation of glnS-deficient strain
D486R/L488Q
the double mutant causes a relaxed tRNA anticodon specificity
D66E
-
saturation mutagenesis, 18fold increased Km for glutamine, decreased turnover
D66F
-
saturation mutagenesis, highly increased Km for glutamine, 1200fold decrease in activity
D66G
-
saturation mutagenesis, only little complementation of glnS-deficient strain
D66H
-
saturation mutagenesis, only little complementation of glnS-deficient strain
D66R
-
saturation mutagenesis, only little complementation of glnS-deficient strain
D81Q
site-diretced mutagenesis, the mutant has and increased, inverted stereospecificity. D81Q is predicted to lead to a rotated ligand backbone and an increased, not a decreased L-Tyr preference
E222K
site-directed mutagenesis, mutational structure-function study, the residue is part of the invariant Hub, the mutation leads to mischarging and affected cognate tRNAGln recognition
E323A
-
site-directed mutagenesis, the mutation produces small but consistent 2 to 3fold improvements in glutamine-binding affinity compared to the wild-type enzyme
E34A
-
site-directed mutagenesis, the mutant shows highly increased Km and reduced kcat and activity compared to the wild-type enzyme
E34D
-
site-directed mutagenesis, the mutant shows highly increased Km and reduced kcat and activity compared to the wild-type enzyme
E34Q
-
site-directed mutagenesis, the mutant shows highly increased Km and reduced kcat and activity compared to the wild-type enzyme
E73A
-
site-directed mutagenesis, the mutant shows highly increased Km and reduced kcat and activity compared to the wild-type enzyme
E73Q
-
site-directed mutagenesis, the mutant shows highly increased Km and reduced kcat and activity compared to the wild-type enzyme, product release remains the rate-limiting step in E73Q
F233D
-
saturation mutagenesis, highly increased Km for glutamine, 3700fold decrease in activity
F233L
-
saturation mutagenesis, 19fold increased Km for glutamine, decreased turnover
F233Y
-
saturation mutagenesis, increased Km for glutamine, increased turnover
F90L
K194A
-
site-directed mutagenesis, the mutation perturbs the dissociation constant in ATP binding
K401A
-
site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme
L136A
-
site-directed mutagenesis, the mutation perturbs the dissociation constant in ATP binding
N320A
-
site-directed mutagenesis, the mutation produces small but consistent 2 to 3fold improvements in glutamine-binding affinity compared to the wild-type enzyme
N336A
-
site-directed mutagenesis, the mutation removes contact with the ribose at U38, but does not significantly influence glutamine affinity
N370A
-
site-directed mutagenesis, the mutation removes contact with the base of U38, but does not significantly influence glutamine affinity
Q255I
site-directed mutagenesis, mutational structure-function study, the residue is part of the invariant Hub, the mutation leads to reduced specificity for cognate Gln recognition and increased Glu recognition
Q318A
-
site-directed mutagenesis, the mutation produces small but consistent 2 to 3fold improvements in glutamine-binding affinity compared to the wild-type enzyme
Q517A
-
site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme
R260Q
site-diretced mutagenesis, mutating Arg260 to the homologous but neutral Gln does not reduce the L-GlnAMP preference, instead, the mutation produces a change in the DELTADELTAG value that is much smaller than the wild-type free energy component
R30A
site-directed mutagenesis, comparison of mutant activity with glutamate and glutamine to charge tRNAGln to the wild-type activity, the mutant shows no activity with L-Glu
R30K
site-directed mutagenesis, comparison of mutant activity with glutamate and glutamine to charge tRNAGln to the wild-type activity, the mutant shows weak activity with L-Glu
R341A
R410A
-
site-directed mutagenesis, the mutation removes contact with the base of C34, but does not significantly influence glutamine affinity
R520A
-
site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme
R545A
-
site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme
T316A
-
site-directed mutagenesis, the mutation produces small but consistent 2 to 3fold improvements in glutamine-binding affinity compared to the wild-type enzyme
T547A
-
site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme
Y211F
-
saturation mutagenesis, 60fold increased Km for glutamine, decreased turnover
Y211F/F233Y
-
saturation mutagenesis, increased Km for glutamine, about 6fold decreased activity
Y211G
-
saturation mutagenesis, only little complementation of glnS-deficient strain
Y211H
site-directed mutagenesis, mutational structure-function study, the residue is part of the connection in the quaternary cognate-complex, the mutants shows slow solvation dynamics in the active site
Y211L
-
saturation mutagenesis, unaffected Km for glutamine, decreased turnover
Y240E
-
site-directed mutagenesis, active site mutant, 5fold improved glutamic acid recognition in vitro, partial complementation of an enzyme-deficient strain
Y240E/G
site-directed mutagenesis, mutational structure-function study, the residue is part of the Hub common to ligand-free and quaternary cognate-complex, the mutant shows increased Glu recognition in vitro and in vivo
Y240G
-
site-directed mutagenesis, active site mutant, 3fold improved glutamic acid recognition in vitro, partial complementation of an enzyme-deficient strain
G45V
G45V/R403W
naturally occuring mutation involved in progressive microcephaly, severe seizures in infancy, atrophy of the cerebral cortex and cerebellar vermis, and mild atrophy of the cerebellar hemispheres, the mutant shows a highly reduced aminoacylation activity, heterozygous mutations
K496stop
naturally occuring mutation involved in early-onset epileptic encephalopathy (EOEE), heterozygous mutation leading to a deletion of part of the catalytic domain and the entire anticodon-binding domain, a loss-of-function mutant
R403W
R515W
Y57H
Y57H/R515W
occuring mutation involved in progressive microcephaly, severe seizures in infancy, atrophy of the cerebral cortex and cerebellar vermis, and mild atrophy of the cerebellar hemispheres, the mutant shows a highly reduced aminoacylation activity, heterozygous mutations
additional information
F90L
-
site-directed mutagenesis, active site mutant, 5fold improved glutamic acid recognition in vitro, in vivo the mutant shows a 40% reduced growth rate, partial complementation of an enzyme-deficient strain
F90L
site-directed mutagenesis, mutational structure-function study, the residue is part of the connection in the active site network, the mutant shows increased Glu recognition in vitro and in vivo
R341A
site-directed mutagenesis, mutational structure-function study, the residue is part of the Hub common to all liganded complex, the mutation affects anticodon recognition
R341A
-
site-directed mutagenesis, the mutation deletes a hydrogen bond made with the O4 moiety of the U35 base
R341A
-
site-directed mutagenesis, the mutation removes contact with the base of U35, but does not significantly influence glutamine affinity
G45V
naturally occuring mutation involved in development of brain disorder, modestly affects the conformation of the N-terminal domain and the stability of GlnRS, the mutant shows reduced activity compared to the wild-type. Gly45 is in the solvent-flexible loop between helices alpha4 and alpha5
G45V
naturally occuring mutation involved in progressive microcephaly, severe seizures in infancy, atrophy of the cerebral cortex and cerebellar vermis, and mild atrophy of the cerebellar hemispheres, the mutation is located in the N-terminal domain required for QARS interaction with proteins in the multisynthetase complex and potentially with glutamine tRNA, the mutant shows an over 10fold reduction in aminoacylation activity, heterozygous mutation
R403W
inactive mutant, the mutant is bound to GroEL when recombinantly expressed in Escherichi coli suggesting that it is misfolded
R403W
naturally occuring mutation involved in progressive microcephaly, severe seizures in infancy, atrophy of the cerebral cortex and cerebellar vermis, and mild atrophy of the cerebellar hemispheres, the mutation renders QARS less soluble and disrupts the domain structure and overall folding of QARS, the mutant shows no aminoacylation activity in vitro, heterozygous mutation
R515W
inactive mutant, the mutant is bound to GroEL when recombinantly expressed in Escherichi coli suggesting that it is misfolded
R515W
naturally occuring mutation involved in progressive microcephaly, severe seizures in infancy, atrophy of the cerebral cortex and cerebellar vermis, and mild atrophy of the cerebellar hemispheres, the mutation renders QARS less soluble, the mutation disrupts QARS-RARS (arginyl-tRNA synthetase 1) interaction and disrupts the domain structure and overall folding of QARS, the mutant shows no aminoacylation activity in vitro, heterozygous mutation
Y57H
naturally occuring mutation involved in development of brain disorder, modestly affects the conformation of the N-terminal domain and the stability of GlnRS, the mutant shows reduced activity compared to the wild-type. Tyr57 is in the middle of helix alpha5
Y57H
naturally occuring mutation involved in early-onset epileptic encephalopathy (EOEE), heterozygous mutation, a loss-of-function missense mutation
Y57H
naturally occuring mutation involved in progressive microcephaly, severe seizures in infancy, atrophy of the cerebral cortex and cerebellar vermis, and mild atrophy of the cerebellar hemispheres, the mutation is located in the N-terminal domain required for QARS interaction with proteins in the multisynthetase complex and potentially with glutamine tRNA, the mutant shows an over 10fold reduction in aminoacylation activity, heterozygous mutation
additional information
-
deletion mutants with C-terminal truncations and N-terminal truncations. A C-terminal deletion mutant exhibits sharp reduction in the specificity constant. Reduced stability of some of these mutants
additional information
-
strain HAPPY101 allows plasmid-mediated expression of detrimental GlnRS mutants, which cannot complement the chromosomal glnS deletion in Escherichia coli strain X3R2
additional information
-
3 misacylating mutant enzymes with reduced ability to discriminate between cognate and noncognate base pairs at position 3-70
additional information
-
temperature-sensitive mutant enzyme, no change in affinity for glutamine
additional information
-
construction of a truncated enzyme form, partial complementation of an enzyme-deficient strain, reduced growth rate in vivo
additional information
-
construction of a chimeric glutamyl:glutaminyl-tRNA synthetase, cGluGlnRS, consisting of the catalytic domain of the GluRS and the anti-codon binding domain of the GlnRS. The chimeric mutant shows detectable glutamylation activity with Escherichia coli tRNAGlu and is capable of complementing a ts-GluRS strain at non-permissive temperatures. The GlnRS anticodon-binding domain in cGluGlnRS enhances kcat for glutamylation, interaction analysis, overview
additional information
-
cumulative replacement of other primary binding site residues than Cys229 in GlnRS, with those of GluRS, only slightly improves the ability of the GlnRS active site to accommodate glutamate. Introduction of 22 amino acid replacements and one deletion, including substitution of the entire primary binding site and two surface loops adjacent to the region disrupted in C229R, improves the capacity of Escherichia coli GlnRS to synthesize misacylated Glu-tRNAGln by 16000fold. This hybrid enzyme recapitulates the function of misacylating GluRS enzymes found in organisms that synthesize Gln-tRNAGln by an alternative pathway, overview
additional information
cumulative replacement of other primary binding site residues than Cys229 in GlnRS, with those of GluRS, only slightly improves the ability of the GlnRS active site to accommodate glutamate. Introduction of 22 amino acid replacements and one deletion, including substitution of the entire primary binding site and two surface loops adjacent to the region disrupted in C229R, improves the capacity of Escherichia coli GlnRS to synthesize misacylated Glu-tRNAGln by 16000fold. This hybrid enzyme recapitulates the function of misacylating GluRS enzymes found in organisms that synthesize Gln-tRNAGln by an alternative pathway, overview
additional information
-
the engineered mutant hybrid C229R Gln-RS, EC 6.1.1.18, shows activity with L-glutamine or L-glutamate and tRNAGln like the nondiscriminating enzyme, EC 6.1.1.24. Introduction of 22 amino acid replacements and one deletion, including substitution of the entire primary binding site and two surface loops adjacent to the region disrupted in the mutant C229R, improves the capacity of the mutant enzyme to synthesize misacylated Glu-tRNAGln by 16000fold, overview
additional information
the engineered mutant hybrid C229R Gln-RS, EC 6.1.1.18, shows activity with L-glutamine or L-glutamate and tRNAGln like the nondiscriminating enzyme, EC 6.1.1.24. Introduction of 22 amino acid replacements and one deletion, including substitution of the entire primary binding site and two surface loops adjacent to the region disrupted in the mutant C229R, improves the capacity of the mutant enzyme to synthesize misacylated Glu-tRNAGln by 16000fold, overview
additional information
-
a deletion mutant comprising only the C-terminal catalytic domain is targeted into the multienzyme complex, while a deletion mutant comprising only the N-terminal domain is not
additional information
generation of truncated mutants DELTAN1 (116-775) with reduced activity compared to the wild-type, and DELTANTD (183-775) with no activity
additional information
-
generation of truncated mutants DELTAN1 (116-775) with reduced activity compared to the wild-type, and DELTANTD (183-775) with no activity
additional information
microcephaly and neurodegeneration in two nonconsanguineous families and the identification of QARS mutations, phenotypes, overview
additional information
-
truncated enzyme form lacking the NH2-terminal domain, with modest increase in Km value for glutamine and ATP and no difference in kcat for aminoacylation or Km for tRNA
additional information
construction of a C-terminal catalytic domain (QRS-C) of the QRS gene, a region corresponding to residues 255-805 of the annotated full-length gene, and of an N-terminal domain contruct
additional information
Toxoplasma gondii ATCC 50611 / Me49
-
construction of a C-terminal catalytic domain (QRS-C) of the QRS gene, a region corresponding to residues 255-805 of the annotated full-length gene, and of an N-terminal domain contruct
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
strain KL301 enzyme is stable, temperature-sensitive mutant enzyme loses about 70% of its activity
additional information
additional information
-
several noncognate tRNAs protect the enzyme against thermal inactivation
additional information
the melting curves of mutant enzymes G45V and Y57H comprise two peaks indicating that these mutants unfold along a more complex trajectory. The (un)folding events occur at 46.5°C and 52°C in G45V, and at 46°C and 51°C in Y57H
additional information
-
the melting curves of mutant enzymes G45V and Y57H comprise two peaks indicating that these mutants unfold along a more complex trajectory. The (un)folding events occur at 46.5°C and 52°C in G45V, and at 46°C and 51°C in Y57H
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM potassium phosphate, pH 7.5, 50 mM KCl, 1 mM DTT, 50% glycerol, stable for 6 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
IgG Sepharose column chromatography and Superdex HiLoad 16/60 gel filtration
recombinant His-tagged chimeric mutant enzyme from strain BL21(DE3) or the temperature sensitive strain JP1449(DE3) by nickel affinity chromatography
-
recombinant His-tagged GlnRS mutants from strain BL21-DE3 by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography and dialysis
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain Rosetta (DE3)pLysS by nickel affinity chromatography and gel filtration
recombinant His6-tagged wild-type full-length enzyme and truncated mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration, optimization of purification conditions
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, enzyme contains a N-terminal lysine-rich sequence KPKKKKEK, that may function as a nuclear targetng signal as well as in regulation of gene expression, since the 8 amino acid peptide derived from the motif interacts with DNA and changes the DNA molecule form from B to Z form
-
expression of full length and C-terminal truncated GlnRS, lacking the the Yqey domain, and of the isolated Yqey protein, in Escherichia coli strain ER2566
expression of the His-tagged chimeric mutant enzyme in Escherichia coli strain BL21(DE3) or the temperature sensitive strain JP1449(DE3)
-
gene glnS, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21
gene QARS, genotyping, recombinant expression of codon-optimized His-tagged wild-type and mutant enzymes in Escherichia coli
gene QARS, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta (DE3)pLysS
overexpression of various Myc-tagged enzyme mutants in human embryonic kidney 293 cells
-
recombinant expression of His6-tagged wild-type full-length enzyme and truncated mutant enzymes in Escherichia coli strain BL21(DE3), optimization of expression conditions
transient expression of the p.Lys496stop mutant in neuroblastoma 2A cells reveals diminished and aberrantly aggregated expression
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
urea induces equilibrium denaturation of glutaminyl-tRNA synthetase, existence of a stable intermediate state at around 2 M urea, existence of an induced molten globule state in a large multidomain protein which is separated from the native and the denatured protein by high activation energy barriers
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
the essential nature of the enzymes makes it an attractive targets for designing of drugs against important pathogenic protozoans like Toxoplasma
drug development
Toxoplasma gondii ATCC 50611 / Me49
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the essential nature of the enzymes makes it an attractive targets for designing of drugs against important pathogenic protozoans like Toxoplasma
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Walker, E.J.; Treacy, G.B.; Jeffrey, P.D.
Molecular weights of mitochondrial and cytoplasmic aminoacyl-tRNA synthetases of beef liver and their complexes
Biochemistry
22
1934-1941
1983
Bos taurus
brenda
Lea, P.J.; Fowden, L.
Amino acid substrate specificity of asparaginyl-, aspartyl- and glutaminyl-tRNA synthetase isolated from higher plants
Phytochemistry
12
1903-1916
1973
Albizia julibrissin, Vigna radiata var. radiata
-
brenda
Norcum, M.T.
Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cells
J. Biol. Chem.
264
15043-15051
1989
Mus musculus
brenda
Rould, M.A.; Perona, J.J.; Sll, D.; Steitz, T.A.
Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNAGln and ATP at 2.8 A resolution
Science
246
1135-1142
1989
Escherichia coli
brenda
Conley, J.; Sherman, J.; Thomann, H.U.; Sll, D.
Domains of E. coli glutaminyl-tRNA synthetase disordered in the crystal structure are essential for function or stability
Nucleosides Nucleotides
13
1581-1595
1994
Escherichia coli
-
brenda
Thomann, H.U.; Ibba, M.; Hong, K.W.; Sll, D.
Homologous expression and purification of mutants of an essential protein by reverse epitope-tagging
Bio/Technology
14
50-55
1996
Escherichia coli
brenda
Rogers, M.J.; Weygand-Durasevic, I.; Schwob, E.; Sherman, J.M.; Rogers, K.C.; Adachi, T.; Inokuchi, H.; Sll, D.
Selectivity and specificity in the recognition of tRNA by E. coli glutaminyl-tRNA synthetase
Biochimie
75
1083-1090
1993
Escherichia coli
brenda
Perona, J.J.; Rould, M.A.; Steitz, T.A.; Risler, J.L.; Zelwer, C.; Brunie, S.
Structural similarities in glutaminyl- and methionyl-tRNA synthetases suggest a common overall orientation of tRNA binding
Proc. Natl. Acad. Sci. USA
88
2903-2907
1991
Escherichia coli
brenda
Rould, M.A.; Perona, J.J.; Steitz, T.A.
Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase
Nature
352
213-218
1991
Escherichia coli
brenda
Bhattacharyya, T.; Bhattacharyya, A.; Roy, S.
A fluorescence spectroscopic study of glutaminyl-tRNA synthetase from Escherichia coli and its implications for the enzyme mechanism
Eur. J. Biochem.
200
739-745
1991
Escherichia coli
brenda
Ludmerer, S.W.; Wright, D.J.; Schimmel, P.
Purification of glutamine tRNA synthetase from Saccharomyces cerevisiae
J. Biol. Chem.
268
5519-5523
1993
Saccharomyces cerevisiae
brenda
Das, B.K.; Bhattacharyya, T.; Roy, S.
Characterization of a urea induced molten globule intermediate state of glutaminyl-tRNA synthetase from Escherichia coli
Biochemistry
34
5242-5247
1995
Escherichia coli
brenda
Arnez, J.G.; Steitz, T.A.
Crystal structures of three misacylating mutants of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNAGln and ATP
Biochemistry
35
14725-14733
1996
Escherichia coli
brenda
Fett, R.; Knippers, R.
The primary structure of human glutaminyl-tRNA synthetase
J. Biol. Chem.
266
1448-1455
1991
Homo sapiens
brenda
Krner, A.; Magee, B.B.; Liska, B.; Low, K.B.; Adelberg, E.A.; Sll, D.
Isolation and partial characterization of a temperature-sensitive Escherichia coli mutant with altered glutaminyl-transfer ribonucleic acid synthetase
J. Bacteriol.
120
154-158
1974
Escherichia coli
brenda
Seno, T.; Nakamura, A.; Fukuhara, S.; Iwata, K.
Interaction of Escherichia coli glutaminyl-tRNA synthetase with noncognate tRNA's
Nucleic Acids Res.
5
1561-1570
1978
Escherichia coli
brenda
Kern, D.; Potier, S.; Lapointe, J.; Boulanger, Y.
The glutaminyl-transfer RNA synthetase of Escherichia coli. Purification, structure and function relationship
Biochim. Biophys. Acta
607
65-80
1980
Escherichia coli
brenda
Yamao, F.; Inokuchi, H.; Cheung, A.; Ozeki, H.; Sll, D.
Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene
J. Biol. Chem.
257
11639-11643
1982
Escherichia coli
brenda
Hoben, P.; Royal, N.; Cheung, A.; Yamao, F.; Biemann, K.; Sll, D.
Escherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product
J. Biol. Chem.
257
11644-11650
1982
Escherichia coli
brenda
Mitchell, A.P.; Ludmerer, S.W.
Identification of a glutaminyl-tRNA synthetase mutation in Saccharomyces cerevisiae
J. Bacteriol.
158
530-534
1984
Saccharomyces cerevisiae
brenda
Ludmerer, S.W.; Schimmel, P.
Cloning of GLN4: an essential gene that encodes glutaminyl-tRNA synthetase in Saccharomyces cerevisiae
J. Bacteriol.
163
763-768
1985
Saccharomyces cerevisiae
brenda
Hoben, P.; Sll, D.
Glutaminyl-tRNA synthetase of Escherichia coli
Methods Enzymol.
113
55-59
1985
Escherichia coli
brenda
Liu, J.; Ibba, M.; Hong, K.W.; Soll, D.
The terminal adenosine of tRNA(Gln) mediates tRNA-dependent amino acid recognition by glutaminyl-tRNA synthetase
Biochemistry
37
9836-9842
1998
Escherichia coli
brenda
Bernier, S.; Dubois, D.Y.; Therrien, M.; Lapointe, J.; Chenevert, R.
Synthesis of glutaminyl adenylate analogues that are inhibitors of glutaminyl-tRNA synthetase
Bioorg. Med. Chem. Lett.
10
2441-2444
2000
Escherichia coli
brenda
Hong, K.W.; Ibba, M.; Soll, D.
Retracing the evolution of amino acid specificity in glutaminyl-tRNA synthetase
FEBS Lett.
434
149-154
1998
Escherichia coli
brenda
Kim, T.; Park, S.G.; Kim, J.E.; Seol, W.; Ko, Y.G.; Kim, S.
Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex
J. Biol. Chem.
275
21768-21772
2000
Homo sapiens
brenda
Ko, Y.G.; Kim, E.Y.; Kim, T.; Park, H.; Park, H.S.; Choi, E.J.; Kim, S.
Glutamine-dependent antiapoptotic interaction of human glutaminyl-tRNA synthetase with apoptosis signal-regulating kinase 1
J. Biol. Chem.
276
6030-6036
2001
Homo sapiens
brenda
Krzyzaniak, A.; Siatecka, M.; Szyk, A.; Mucha, P.; Rekowski, P.; Kupryszewski, G.; Barciszewski, J.
Specific induction of Z-DNA conformation by a nuclear localization signal peptide of lupin glutaminyl tRNA synthetase
Mol. Biol. Rep.
27
51-54
2000
Lupinus luteus
brenda
Mandal, A.K.; Bhattacharyya, A.; Bhattacharyya, S.; Bhattacharyya, T.; Roy, S.
A cognate tRNA specific conformational change in glutaminyl-tRNA synthetase and its implication for specificity
Protein Sci.
7
1046-1051
1998
Escherichia coli
brenda
Rath, V.L.; Silvian, L.F.; Beijer, B.; Sproat, B.S.; Steitz, T.A.
How glutaminyl-tRNA synthetase selects glutamine
Structure
6
439-449
1998
Escherichia coli (P00962)
brenda
Akochy, P.M.; Bernard, D.; Roy, P.H.; Lapointe, J.
Direct glutaminyl-tRNA biosynthesis and indirect asparaginyl-tRNA biosynthesis in Pseudomonas aeruginosa PAO1
J. Bacteriol.
186
767-776
2004
Pseudomonas aeruginosa
brenda
Rinehart, J.; Horn, E.K.; Wei, D.; Soll, D.; Schneider, A.
Non-canonical eukaryotic glutaminyl- and glutamyl-tRNA synthetases form mitochondrial aminoacyl-tRNA in Trypanosoma brucei
J. Biol. Chem.
279
1161-1166
2004
Trypanosoma brucei
brenda
Deniziak, M.A.; Sauter, C.; Becker, H.D.; Giege, R.; Kern, D.
Crystallization and preliminary X-ray characterization of the atypical glutaminyl-tRNA synthetase from Deinococcus radiodurans
Acta Crystallogr. Sect. D
60
2361-2363
2004
Deinococcus radiodurans
brenda
Rinehart, J.; Krett, B.; Rubio, M.A.; Alfonzo, J.D.; Soll, D.
Saccharomyces cerevisiae imports the cytosolic pathway for Gln-tRNA synthesis into the mitochondrion
Genes Dev.
19
583-592
2005
Saccharomyces cerevisiae
brenda
Gruic-Sovulj, I.; Uter, N.; Bullock, T.; Perona, J.J.
tRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting class I aminoacyl-tRNA synthetase
J. Biol. Chem.
280
23978-23986
2005
Escherichia coli
brenda
Green, D.F.; Tidor, B.
Escherichia coli glutaminyl-tRNA synthetase is electrostatically optimized for binding of its cognate substrates
J. Mol. Biol.
342
435-452
2004
Escherichia coli
brenda
Uter, N.T.; Perona, J.J.
Long-range intramolecular signaling in a tRNA synthetase complex revealed by pre-steady-state kinetics
Proc. Natl. Acad. Sci. USA
101
14396-14401
2004
Escherichia coli
brenda
Uter, N.T.; Perona, J.J.
Active-site assembly in glutaminyl-tRNA synthetase by tRNA-mediated induced fit
Biochemistry
45
6858-6865
2006
Escherichia coli
brenda
Balg, C.; Blais, S.P.; Bernier, S.; Huot, J.L.; Couture, M.; Lapointe, J.; Chenevert, R.
Synthesis of beta-ketophosphonate analogs of glutamyl and glutaminyl adenylate, and selective inhibition of the corresponding bacterial aminoacyl-tRNA synthetases
Bioorg. Med. Chem.
15
295-304
2007
Escherichia coli
brenda
Yamasaki, S.; Nakamura, S.; Terada, T.; Shimizu, K.
Mechanism of the difference in the binding affinity of E. coli tRNAGln to glutaminyl-tRNA synthetase caused by noninterface nucleotides in variable loop
Biophys. J.
92
192-200
2007
Escherichia coli (P00962)
brenda
Deniziak, M.; Sauter, C.; Becker, H.D.; Paulus, C.A.; Giege, R.; Kern, D.
Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation
Nucleic Acids Res.
35
1421-1431
2007
Deinococcus radiodurans (P56926), Deinococcus radiodurans, Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 (P56926)
brenda
Sathyapriya, R.; Vishveshwara, S.
Structure networks of E. coli glutaminyl-tRNA synthetase: effects of ligand binding
Proteins
68
541-550
2007
Escherichia coli (P00962), Escherichia coli
brenda
Saha, R.; Dasgupta, S.; Basu, G.; Roy, S.
A chimeric glutamyl: glutaminyl-tRNA synthetase: implications for evolution
Biochem. J.
15
449-455
2008
Escherichia coli
brenda
Wong, S.; Ragan, M.A.
MACHOS: Markov clusters of homologous subsequences
Bioinformatics
24
i77-i85
2008
Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Bullock, T.L.; Rodriguez-Hernandez, A.; Corigliano, E.M.; Perona, J.J.
A rationally engineered misacylating aminoacyl-tRNA synthetase
Proc. Natl. Acad. Sci. USA
105
7428-7433
2008
Escherichia coli, Escherichia coli (P00962)
brenda
Dasgupta, S.; Saha, R.; Dey, C.; Banerjee, R.; Roy, S.; Basu, G.
The role of the catalytic domain of E. coli GluRS in tRNAGln discrimination
FEBS Lett.
583
2114-2120
2009
Escherichia coli
brenda
Rodriguez-Hernandez, A.; Perona, J.J.
Heat maps for intramolecular communication in an RNP enzyme encoding glutamine
Structure
19
386-396
2011
Escherichia coli
brenda
Saha, R.; Dasgupta, S.; Banerjee, R.; Mitra-Bhattacharyya, A.; Soell, D.; Basu, G.; Roy, S.
A functional loop spanning distant domains of glutaminyl-tRNA synthetase also stabilizes a molten globule state
Biochemistry
51
4429-4437
2012
Escherichia coli (P00962)
brenda
Grant, T.D.; Luft, J.R.; Wolfley, J.R.; Snell, M.E.; Tsuruta, H.; Corretore, S.; Quartley, E.; Phizicky, E.M.; Grayhack, E.J.; Snell, E.H.
The structure of yeast glutaminyl-tRNA synthetase and modeling of its interaction with tRNA
J. Mol. Biol.
425
2480-2493
2013
Saccharomyces cerevisiae (P13188), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P13188)
brenda
Zhang, X.; Ling, J.; Barcia, G.; Jing, L.; Wu, J.; Barry, B.J.; Mochida, G.H.; Hill, R.S.; Weimer, J.M.; Stein, Q.; Poduri, A.; Partlow, J.N.; Ville, D.; Dulac, O.; Yu, T.W.; Lam, A.T.; Servattalab, S.; Rodriguez, J.; Boddaert, N.; Munnich, A.; Colleaux, L.; Zon, L.I.; Soell, D.; Walsh, C.A.; Nabbout, R.
Mutations in QARS, encoding glutaminyl-tRNA synthetase, cause progressive microcephaly, cerebral-cerebellar atrophy, and intractable seizures
Am. J. Hum. Genet.
94
547-558
2014
Homo sapiens (P47897)
brenda
Kodera, H.; Osaka, H.; Iai, M.; Aida, N.; Yamashita, A.; Tsurusaki, Y.; Nakashima, M.; Miyake, N.; Saitsu, H.; Matsumoto, N.
Mutations in the glutaminyl-tRNA synthetase gene cause early-onset epileptic encephalopathy
J. Hum. Genet.
60
97-101
2015
Homo sapiens (P47897)
brenda
Hadd, A.; Perona, J.J.
Coevolution of specificity determinants in eukaryotic glutamyl- and glutaminyl-tRNA synthetases
J. Mol. Biol.
426
3619-3633
2014
Saccharomyces cerevisiae (P13188), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 / S288c (P13188)
brenda
Druart, K.; Guennec, M.L.; Palmai, Z.; Simonson, T.
Probing the stereospecificity of tyrosyl- and glutaminyl-tRNA synthetase with molecular dynamics
J. Mol. Graph. Model.
71
192-199
2017
Escherichia coli (P00962), Escherichia coli
brenda
Ognjenovic, J.; Wu, J.; Matthies, D.; Baxa, U.; Subramaniam, S.; Ling, J.; Simonovic, M.
The crystal structure of human GlnRS provides basis for the development of neurological disorders
Nucleic Acids Res.
44
3420-3431
2016
Homo sapiens (P47897), Homo sapiens
brenda
Fu, Y.; Kim, Y.; Jin, K.S.; Kim, H.S.; Kim, J.H.; Wang, D.; Park, M.; Jo, C.H.; Kwon, N.H.; Kim, D.; Kim, M.H.; Jeon, Y.H.; Hwang, K.Y.; Kim, S.; Cho, Y.
Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation
Proc. Natl. Acad. Sci. USA
111
15084-15089
2014
Homo sapiens (P47897)
brenda
van Rooyen, J.M.; Hakimi, M.A.; Belrhali, H.
Recombinant expression, purification, and crystallization of the glutaminyl-tRNA synthetase from Toxoplasma gondii
Protein Expr. Purif.
110
115-121
2015
Toxoplasma gondii (A0A125YXL3), Toxoplasma gondii ATCC 50611 / Me49 (A0A125YXL3)
brenda
EXTERNAL LINKS (specific for EC-Number 6.1.1.18)
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