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Information on EC 6.1.1.18 - glutamine-tRNA ligase
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6.1.1.18 glutamine-tRNA ligaseSpecify your search results
Word Map
- 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
The enzyme appears in viruses and cellular organisms
Synonyms
glnrs, glutaminyl trna synthetase, cytosolic glutaminyl-trna synthetase, class i glutaminyl-trna synthetase, glutaminyl-transfer rna synthetase, glutamyl/glutaminyl-trna synthetase, l-glutamine:trnagln ligase (amp-forming), 
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
primary binding pocket structure, overview
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + glutamyl-tRNAGln
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + glutamyl-tRNAGln
activity also with Gln-RS, EC 6.1.1.18, mutant C229R
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
r
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
r
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
specific tRNA-dependent amino acid recognition involves Asp66, Tyr211, and Phe233, which interact with A76 of tRNAGln and glutamine
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
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
-
r
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
long-range intramolecular signaling in a tRNA synthetase complex
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
the enzyme is electrostatically optimized for binding of its cognate substrates
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
a two-step reaction
-
-
r
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
a two-step reaction, with a distinct role in induced-fit for Glu73
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
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
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
analysis of domain functions in enzyme-substrate interactions, overview
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
primary binding pocket structure, overview
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
tRNA substrate from bovine liver
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
a two-step aminoacylation reaction
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Saccharomyces cerevisiae ATCC 204508 / S288c
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Saccharomyces cerevisiae ATCC 204508 / S288c
a two-step aminoacylation reaction
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Toxoplasma gondii ATCC 50611 / Me49
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln(CUG)
AMP + diphosphate + L-glutaminyl-tRNAGln(CUG)
-
-
-
?
ATP + L-glutamine + tRNAGln(CUG)
AMP + diphosphate + L-glutaminyl-tRNAGln(CUG)
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
-
?
ATP + L-glutamine + tRNAGln(UUG)
AMP + diphosphate + L-glutaminyl-tRNAGln(UUG)
-
-
-
?
ATP + L-glutamine + tRNAGln(UUG)
AMP + diphosphate + L-glutaminyl-tRNAGln(UUG)
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
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
-
-
?
additional information
?
-
-
several noncognate tRNAs stimulate ATP-diphosphate exchange
-
-
?
additional information
?
-
-
lack of tRNA-independent diphosphate exchange
-
-
?
additional information
?
-
-
lack of tRNA-independent diphosphate exchange
-
-
?
additional information
?
-
-
dimethyl sulfoxide stimulates the charging of several noncognate tRNA's with glutamine
-
-
?
additional information
?
-
-
tRNA binding triggers aminoacyl-adenylate formation and diphosphate exchange
-
-
?
additional information
?
-
-
importance of the acceptor binding domain for accurate recognition of tRNA
-
-
?
additional information
?
-
-
conformational changes are induced by tRNAGln binding not by binding of tRNAGlu
-
?
additional information
?
-
ternary complexed GlnRS bound to tRNAGln and the Gln-AMP analogue is catalytically active and has undergone the first step of the aminoacylation reaction
-
-
?
additional information
?
-
-
ternary complexed GlnRS bound to tRNAGln and the Gln-AMP analogue is catalytically active and has undergone the first step of the aminoacylation reaction
-
-
?
additional information
?
-
-
eukaryotic GlnRS evolves from GluRS by gene duplication and horizontally transfers to bacteria
-
-
?
additional information
?
-
-
wild-type GlnRS catalyzes Glu-tRNAGln synthesis 1000000fold less efficiently than the cognate reaction
-
-
?
additional information
?
-
wild-type GlnRS catalyzes Glu-tRNAGln synthesis 1000000fold less efficiently than the cognate reaction
-
-
?
additional information
?
-
-
GlnRS forms a 1:1 molar complex with tRNAGln
-
-
?
additional information
?
-
GlnRS has adetectable tRNA-acylation activity for its D-amino acid substrate
-
-
?
additional information
?
-
-
GlnRS has adetectable tRNA-acylation activity for its D-amino acid substrate
-
-
?
additional information
?
-
-
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
-
?
additional information
?
-
human GlnRS cannot aminoacylate bacterial tRNAGln from Escherichia coli, but recognition of tRNAGln by human and yeast GlnRSs may be conserved
-
-
?
additional information
?
-
-
human GlnRS cannot aminoacylate bacterial tRNAGln from Escherichia coli, but recognition of tRNAGln by human and yeast GlnRSs may be conserved
-
-
?
additional information
?
-
-
glutamine-dependent ATP-diphosphate exchange
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate + tRNAGln
AMP + diphosphate + glutamyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
r
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
r
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
long-range intramolecular signaling in a tRNA synthetase complex
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Saccharomyces cerevisiae ATCC 204508 / S288c
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
Toxoplasma gondii ATCC 50611 / Me49
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
-
?
additional information
?
-
-
eukaryotic GlnRS evolves from GluRS by gene duplication and horizontally transfers to bacteria
-
-
?
additional information
?
-
-
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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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
Cl-