6.1.1.24: glutamate-tRNAGln ligase
This is an abbreviated version!
For detailed information about glutamate-tRNAGln ligase, go to the full flat file.
Word Map on EC 6.1.1.24
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6.1.1.24
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glutaminyl-trna
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aminoacylation
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gln-trnagln
-
trnaglu
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aminoacyl-trnas
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synthetases
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amidotransferase
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glutamylates
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archaea
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transamidation
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gatcab
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anticodons
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thermautotrophicus
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glutaminylated
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methanothermobacter
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mischarged
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apicoplast
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isoacceptors
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glurss
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eukarya
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anticodon-binding
-
berghei
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heterotrimeric
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arc1p
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lupinus
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luteus
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misaminoacylated
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noncognate
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drug development
- 6.1.1.24
- glutaminyl-trna
- aminoacylation
- gln-trnagln
- trnaglu
- aminoacyl-trnas
- synthetases
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amidotransferase
-
glutamylates
- archaea
-
transamidation
- gatcab
-
anticodons
- thermautotrophicus
-
glutaminylated
-
methanothermobacter
-
mischarged
- apicoplast
-
isoacceptors
- glurss
- eukarya
-
anticodon-binding
- berghei
-
heterotrimeric
- arc1p
-
lupinus
- luteus
-
misaminoacylated
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noncognate
- drug development
Reaction
Synonyms
Glu-Q-RS, GluRS, GluRS1, GluRS2, GluRSND, glutamyl-queuosine tRNAAsp synthetase, Glutamyl-tRNA synthetase, GlxRS, ND-GluRS, non-discriminating GluRS, non-discriminating glutamyl-tRNA synthetase, nondiscriminating GluRS, nondiscriminating glutamyl-tRNA synthetase, Pf3D7_1357200, TM1875
ECTree
6.1.1.24 glutamate-tRNAGln ligaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 6.1.1.24 - glutamate-tRNAGln ligase
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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 + glutamyl-tRNAGln
-
-
-
-
?
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + glutamyl-tRNAGlx
-
-
-
-
?
ATP + L-glutamine + tRNAGln
AMP + diphosphate + glutaminyl-tRNAGln
-
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
-
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS1 charges tRNAGln(CUG)
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS2 preferetially charges tRNAGln(UUG)
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS1 charges tRNAGln(CUG)
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS2 preferetially charges tRNAGln(UUG)
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS1 charges tRNAGln(CUG)
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS2 preferetially charges tRNAGln(UUG)
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
GluRS2
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS2 is specific solely for tRNAGln
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
GluRS2
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS2 is specific solely for tRNAGln
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
GluRS2 is specific solely for tRNAGln
-
-
?
ATP + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
the glutamylation ability of tRNAGln by ND-GluRS is measured in the presence of the bacterial Glu-tRNAGln amidotransferase GatCAB. Glutamylation efficiency is not affected even in the presence of excess GatCAB
-
-
?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
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GluRS1
-
-
?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
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GluRS1
-
-
?
ATP + Glu + tRNAGlU
AMP + diphosphate + L-glutamyl-tRNAGlU
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GluRS1
-
-
?
ATP + L-Glu + tRNAGln
AMP + diphosphate + Glu-tRNAGln
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synthesis of Glu-tRNAGln by engineered, not natural GlnRS, overview
-
-
?
ATP + L-Glu + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
-
-
-
?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
-
the L-glutamyl-queuosine tRNAAsp synthetase, Glu-Q-RS from Escherichia coli is a paralogue of the catalytic core of glutamyl-tRNA synthetase, GluRS, that catalyzes glutamylation of queuosine in the wobble position of tRNAAsp
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-
?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
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the L-glutamyl-queuosine tRNAAsp synthetase, Glu-Q-RS from Escherichia coli is a paralogue of the catalytic core of glutamyl-tRNA synthetase, GluRS, that catalyzes glutamylation of queuosine in the wobble position of tRNAAsp. Activation of Glu to form Glu-AMP, the intermediate of tRNA aminoacylation, in the absence of tRNA. Glu-Q-RS transfers the activated Glu to Q34 located in the anticodon loop of the noncognate tRNAAsp. A C in position 38 is crucial for glutamylation of Q34
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
the enzyme aminoacylates tRNAGLU and tRNASGln in Bacillus subtilis and efficiently misacylates Escherichia coli tRNA1Gln in vitro
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + Glu-tRNAGln
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the enzyme efficiently charges E. coli tRNAGlu and both tRNAGlu and tRNAGln from chloroplasts, no activity with the two E. coli tRNAGln species
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + Glu-tRNAGln
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + Glu-tRNAGln
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the enzyme is capable of mischarging plastidal tRNAGln from barley with glutamate as well as regularly charges the plastidal tRNAGlu from Scenedesmus. The mischarged glutamyl-tRNAGln is subsequently amidated by glutamyl-tRNA amidotransferase to form the glutaminyl-tRNAGln required for plastidal protein biosynthesis
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
activity also with Gln-RS, EC 6.1.1.18, mutant C229R
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
-
-
-
?
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
Thermosynechococcus vestitus
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tRNAGln is initially mischarged with glutamate by a non-discriminating glutamyl-tRNA synthetase
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
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the enzyme aminoacylates tRNAGlu and tRNAsGln in Bacillus subtilis and efficiently misacylates Escherichia coli tRNA1Gln in vitro, not tRNA2Gln from Escherichia coli or tRNAGlu from Escherichia coli
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
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the enzyme interacts with the G64-C50 or G64-U50 in the Tpsi stem of its tRNA substrate
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
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major recognition element for the enzyme is U at the 34th position of both tRNA1Gln from Bacillus subtilis and tRNA1Gln from E. coli as a modified form
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
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the enzyme efficiently charges E. coli tRNAGlu and both tRNAGlu and tRNAGln from chloroplasts, no activity with the two E. coli tRNAGln species
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + Glu-tRNAGlu
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the enzyme is capable of mischarging plastidal tRNAGln from barley with glutamate as well as regularly charges the plastidal tRNAGlu from Scenedesmus. The mischarged glutamyl-tRNAGln is subsequently amidated by glutamyl-tRNA amidotransferase to form the glutaminyl-tRNAGln required for plastidal protein biosynthesis
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Thermosynechococcus vestitus
-
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
Thermosynechococcus vestitus
-
preferred tRNA substrate
-
-
?
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + Glu-tRNAGlx
-
the enzyme is responsible for the in vivo aminoacylation of both tRNAGlu and tRNAGln in Bacillus subtilis
-
?
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + Glu-tRNAGlx
-
the enzyme aminoacylates both tRNAGlu and tRNAGln because Rhizobium meliloti contains no glutaminyl-tRNAGln ligase
-
?
ATP + L-glutamate + tRNAGlx
AMP + diphosphate + Glu-tRNAGlx
-
the enzyme is capable of mischarging plastidal tRNAGln from barley with glutamate as well as regularly charges the plastidal tRNAGlu from Scenedesmus. The mischarged glutamyl-tRNAGln is subsequently amidated by glutamyl-tRNA amidotransferase to form the glutaminyl-tRNAGln required for plastidal protein biosynthesis
-
?
additional information
?
-
-
Glu-Q-RS binds the noncognate amino acids L-Gln and D-Glu fourfold and sixfold, respectively, weaker than L-Glu. Despite important structural similarities, Glu-Q-RS and GluRS diverge strongly by their functional properties, selection of the cognate amino acid and by the mechanism of its activation, overview. Structural basis of the reaction mechanism, overview
-
-
?
additional information
?
-
-
ND-GluRS recognizes both tRNAGlu and tRNAGln without significantly discriminating between them, tRNA discrimination module, overview. The first point of significant distinction between the GlnRS and ND-GluRS tRNA recognition involves residues contacting the G36 nucleobase. A second distiction involves a beta-hairpin module in the CP domain
-
-
?
additional information
?
-
the glutamyl residue of Glu-tRNAGln is then transamidated by a glutamyl-tRNAGln amidotransferase (Glu-AdT) in the presence of ATP using Gln as an amide donor, producing GlntRNAGln, coupled reaction assay
-
-
?
additional information
?
-
-
the glutamyl residue of Glu-tRNAGln is then transamidated by a glutamyl-tRNAGln amidotransferase (Glu-AdT) in the presence of ATP using Gln as an amide donor, producing GlntRNAGln, coupled reaction assay
-
-
?
additional information
?
-
the non-discriminating GluRS (ND-GluRS) can glutamylate both tRNAGlu and tRNAGln
-
-
?
additional information
?
-
-
the non-discriminating GluRS (ND-GluRS) can glutamylate both tRNAGlu and tRNAGln
-
-
?
additional information
?
-
Thermosynechococcus vestitus
-
the non-discriminating enzyme charges both tRNAGlu and tRNAGln with glutamate, anticodons of tRNAGlu, 34C/UUC36, and tRNAGln, 34C/UUG36, differ only in base 36, residue Gly366 is responsible for allowing both cytosine and the bulkier purine base G36 of tRNAGln to be tolerated, glutamate recognition structure, overview
-
-
?
additional information
?
-
ND-GluRS TM1875 glutamylates both tRNAGlu and tRNAGln
-
-
?
additional information
?
-
-
ND-GluRS TM1875 glutamylates both tRNAGlu and tRNAGln
-
-
?
additional information
?
-
TM1875 glutamylates both the tRNAGlu and tRNAGln transcripts
-
-
?
additional information
?
-
-
TM1875 glutamylates both the tRNAGlu and tRNAGln transcripts
-
-
?
