6.1.1.18: glutamine-tRNA ligase
This is an abbreviated version!
For detailed information about glutamine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.18
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6.1.1.18
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synthetases
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aminoacyl-trna
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aminoacylation
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anticodon
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glutamyl-trna
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glutaminylation
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gln-trnagln
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noncognate
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aarss
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trna-dependent
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mischarging
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transamidation
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asnrs
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aspartyl-trna
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trna2gln
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nondiscriminating
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trnatyr
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misaminoacylation
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glurss
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misacylated
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ilers
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cysrs
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anticodon-binding
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valrs
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gatcab
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gln-trna
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drug development
- 6.1.1.18
- synthetases
- aminoacyl-trna
- aminoacylation
-
anticodon
- glutamyl-trna
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glutaminylation
- gln-trnagln
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noncognate
-
aarss
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trna-dependent
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mischarging
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transamidation
- asnrs
- aspartyl-trna
- trna2gln
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nondiscriminating
- trnatyr
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misaminoacylation
- glurss
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misacylated
- ilers
- cysrs
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anticodon-binding
- valrs
- gatcab
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gln-trna
- drug development
Reaction
Synonyms
class I glutaminyl-tRNA synthetase, cytosolic glutaminyl-tRNA synthetase, Gln-RS, Gln4, GlnRS, Glutamine translase, Glutamine--tRNA ligase, Glutamine-tRNA synthetase, glutaminyl tRNA synthetase, Glutaminyl-transfer ribonucleate synthetase, Glutaminyl-transfer RNA synthetase, Glutaminyl-tRNA synthetase, glutaminyltRNA synthetase, glutamyl/glutaminyl-tRNA synthetase, QARS, QRS, Synthetase, glutaminyl-transfer ribonucleate, Vegetative specific protein H4
ECTree
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KM Value
KM Value on EC 6.1.1.18 - glutamine-tRNA ligase
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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
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additional information
additional information
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effect of the isolated Yqey domain on the kinetic properties of GlnRS, overview
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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
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additional information
additional information
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single turnover kinetics, and steady-state kinetics of recombinant mutant enzymes, overview
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additional information
additional information
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kinetics of the mutant enzyme compared to wild-type GlnRS, EC 6.1.1.18, overview
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additional information
additional information
kinetics of the mutant enzyme compared to wild-type GlnRS, EC 6.1.1.18, overview
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additional information
additional information
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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
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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
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additional information
additional information
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pre-steady-state kinetics, negative allosteric coupling, overview
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additional information
additional information
steady-state and transient kinetic analysis
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additional information
additional information
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steady-state and transient kinetic analysis
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