6.3.5.7: glutaminyl-tRNA synthase (glutamine-hydrolysing)
This is an abbreviated version!
For detailed information about glutaminyl-tRNA synthase (glutamine-hydrolysing), go to the full flat file.
Word Map on EC 6.3.5.7
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6.3.5.7
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gln-trnagln
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gatcabs
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archaea
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aminoacyl-trnas
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trna-dependent
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transamidation
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misacylated
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mischarged
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asp-trnaasn
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aspartyl-trna
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asparaginyl-trna
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aminoacylation
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gln-trna
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methanothermobacter
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glutaminase
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thermautotrophicus
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trnaasn
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non-discriminating
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transamidase
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misaminoacylated
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glnrs
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analysis
- 6.3.5.7
- gln-trnagln
- gatcabs
- archaea
- aminoacyl-trnas
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trna-dependent
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transamidation
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misacylated
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mischarged
- asp-trnaasn
- aspartyl-trna
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asparaginyl-trna
- aminoacylation
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gln-trna
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methanothermobacter
- glutaminase
- thermautotrophicus
- trnaasn
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non-discriminating
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transamidase
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misaminoacylated
- glnrs
- analysis
Reaction
Synonyms
aa-tRNA amidotransferase, AdT, amidotransferase B, amidotransferase C, amidotransferase, glutamyl-transfer ribonucleate (glutamine-specific), aminoacyl-tRNA amidotransferase, BANKA_112750, gatA, GatB, GatCAB, GatCAB amidotransferase, GatDE, Gln4, GlnRS, Glu-AdT, Glu-amidotransferase, Glu-tRNAGln amidotransferase, Glu-tRNAGlnAT, GluAdT GatDE, GluRS, glutamyl-tRNA(Gln) amidotransferase, glutamyl-tRNAGln amidotransferase, nondiscriminating GluRS, PBANKA_071810, PF3D7_0416100, PF3D7_0628800, Qrsl1
ECTree
6.3.5.7 glutaminyl-tRNA synthase (glutamine-hydrolysing)Advanced search results
results (
results (Engineering
Engineering on EC 6.3.5.7 - glutaminyl-tRNA synthase (glutamine-hydrolysing)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K236E/E328A
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mutant used for crystallization, secondary structure contents and enzymatic activities similar to wild-type
S128T
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mutant protein retains significant glutaminase activity and transamidase activity in the presence of Gln
D178E
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glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
D178N
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glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
K254E
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glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
T101A
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glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
T101S
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hydrolyzes about 10% of glutamine compared to wild-type enzyme. Compared to wild-type enzyme, the mutant enzyme converts approximately half as much mischarged tRNA substrate to product
T177S
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mutant enzyme hydrolyzes the same amount of glutamine as the wild-type enzyme. As the wild-type enzyme, the mutant enzyme transforms most of Glu-tRNAGln to Gln-tRNAGln
T177V
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glutamine hydrolysis is negligible. Gln-tRNAGln formation is undetectable
E125D
mutation in subunit B, molecular dynamics simulations
E125Q
mutation in subunit B, molecular dynamics simulations
K88R
mutation in subunit B, molecular dynamics simulations
T175V
mutation in subunit B, molecular dynamics simulations
additional information
additional information
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activity of the engineered enzyme variants indicates that the acceptor stem loop is the principle discrimination element because insertion of this loop alone enhances the specificity of the archaeal enzyme toward tRNAGln2
additional information
construction of an an N-terminal deletion mutant lacking amino acids 1-186 corresponding to the eukaryote-specific protein domains. The 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
additional information
Saccharomyces cerevisiae ATCC 204508 / S288c
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construction of an an N-terminal deletion mutant lacking amino acids 1-186 corresponding to the eukaryote-specific protein domains. The 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
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