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
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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
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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
-
amidotransferase
-
glutamylates
- archaea
-
transamidation
- gatcab
-
anticodons
- thermautotrophicus
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glutaminylated
-
methanothermobacter
-
mischarged
- apicoplast
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isoacceptors
- glurss
- eukarya
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anticodon-binding
- berghei
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heterotrimeric
- arc1p
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lupinus
- luteus
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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
results (
results (Engineering
Engineering on EC 6.1.1.24 - glutamate-tRNAGln ligase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L1L2
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site-directed mutagenesis, construction of a hybrid enzyme, kinetic comparison to wild-type enzyme and other hybrid enzyme mutants
T231L
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site-directed mutagenesis, construction of a hybrid enzyme, kinetic comparison to wild-type enzyme and other hybrid enzyme mutants
V218S
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site-directed mutagenesis, construction of a hybrid enzyme, kinetic comparison to wild-type enzyme and other hybrid enzyme mutants
W256Y
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site-directed mutagenesis, construction of a hybrid enzyme, kinetic comparison to wild-type enzyme and other hybrid enzyme mutants
Y240D/D241F
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site-directed mutagenesis, construction of a hybrid enzyme, kinetic comparison to wild-type enzyme and other hybrid enzyme mutants
E334R/G417T/
mutant of GluRS2 specifically and more robustly aminoacylates tRNAGlu1 instead of tRNAGln
E334R/G417T/
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mutant of GluRS2 specifically and more robustly aminoacylates tRNAGlu1 instead of tRNAGln
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additional information
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
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construction of a hybrid enzyme in which 23 amino acids from the catalytic domain of Escherichia coli glutaminyl-tRNA synthetase, GlnRS, are replaced with the corresponding residues of human glutamyl-tRNA synthetase, GluRS. Further introduction of two distal surface loops bridging core secondary structural elements of the Rossmann fold then produces a hybrid enzyme GlnRS S1/L1/L2. The engineered hybrid GlnRS S1/L1/L2 synthesizes Glu-tRNAGln over 104fold more efficiently than GlnRS, overview. The simultaneous optimization of paired amino acid and tRNA binding sites found in a naturally occurring enzyme is not recapitulated in a hybrid that is successfully engineered for amino acid complementarity. Design and characterization of four additional hybrids identify further residues involved in improving complementarity for glutamate and in communicating between amino acid and tRNA binding sites, complementarity for tRNA, mutant enzyme structure, overview. Relationship between tRNA and amino acid binding sites in the hybrid enzymes, overview
