6.1.1.5: isoleucine-tRNA ligase
This is an abbreviated version!
For detailed information about isoleucine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.5
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6.1.1.5
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synthetases
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aminoacyl-trna
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aminoacylation
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isoleucylation
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valyl-trna
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misactivated
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methionyl-trna
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leurs
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mischarged
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pseudomonic
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post-transfer
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noncognate
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valrs
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mupirocin-resistant
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misacylated
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anticodons
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aarss
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kmsks
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glnrs
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trna-dependent
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pretransfer
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lysyl-trna
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molecular biology
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medicine
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drug development
- 6.1.1.5
- synthetases
- aminoacyl-trna
- aminoacylation
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isoleucylation
- valyl-trna
-
misactivated
- methionyl-trna
- leurs
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mischarged
-
pseudomonic
-
post-transfer
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noncognate
- valrs
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mupirocin-resistant
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misacylated
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anticodons
-
aarss
-
kmsks
- glnrs
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trna-dependent
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pretransfer
- lysyl-trna
- molecular biology
- medicine
- drug development
Reaction
Synonyms
EcIleRS, IARS2, Ile-tRNA synthetase, IleRS, ileS, ileS1, ileS2, IRS, Isoleucine translase, Isoleucine--tRNA ligase, Isoleucine-transfer RNA ligase, Isoleucine-tRNA synthetase, isoleucyl tRNA synthetase, Isoleucyl-transfer ribonucleate synthetase, Isoleucyl-transfer RNA synthetase, Isoleucyl-tRNA synthetase, mitochondrial isoleucyl-tRNA synthetase, More, mt isoleucyl-tRNA synthetase, mt-IleRS, Mupirocin resistance protein, ScIleRS, SgIleRS, Synthetase, isoleucyl-transfer ribonucleate
ECTree
6.1.1.5 isoleucine-tRNA ligaseAdvanced search results
results (
results (KM Value
KM Value on EC 6.1.1.5 - isoleucine-tRNA ligase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.00000004
L-isoleucine
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pH and temperature not specified in the publication
additional information
additional information
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Km value of structural analogs of adenosine 5'-triphosphate in the aminoacylation reaction
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additional information
additional information
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Km value of mutant enzynes with altered metal-binding sites
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additional information
additional information
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steady-state parameters for tRNA-independent pre-transfer editing by IleRS and its mutants determined by varying concentrations of noncognate valine, overview. Kinetic method to distinguish among three models for pre-transfer editing by IleRS, overview
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additional information
additional information
kinetic analysis, rapid equilibrium determinations, steady-state kinetics. The analysis strongly suggests an additional activation step, formation of a new isoleucyl-AMP before the isoleucyl-tRNA is freed from the enzyme. The removal of Ile-tRNA is possible without the formation of Ile-AMP if both isoleucine and ATP are bound to the E-Ile-tRNA complex, but this route covers only 11% of the total formation of Ile-tRNA. In addition to the Mg2+ in MgATP or Mg-diphosphate, only two tRNA-bound Mg2+ are required to explain the magnesium dependence in the best-fit mechanism. The first Mg2+ might be present in all steps before the second activation and is obligatory in the first reorganizing step and transfer step. The second Mg2+ is present only at the transfer step, whereas elsewhere it prevents the reaction, including the activation reaction
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additional information
additional information
single-turnover kinetic analysis
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additional information
additional information
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single-turnover kinetic analysis
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additional information
additional information
single-turnover kinetic analysis, activation kinetics of isoleucine and valine by ScIleRS at 30°C
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additional information
additional information
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single-turnover kinetic analysis, activation kinetics of isoleucine and valine by ScIleRS at 30°C
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additional information
additional information
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single-turnover kinetic analysis, activation kinetics of isoleucine and valine by SgIleRS at 30°C
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additional information
additional information
steady-state kinetics of activation of cognate L-Ile and noncognate amino acid L-Val by Y59 IleRS mutant variants, and transfer kinetics, as well as tRNA-dependent hydrolysis of cognate isoleucyl-AMP, overview
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additional information
additional information
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steady-state kinetics of activation of cognate L-Ile and noncognate amino acid L-Val by Y59 IleRS mutant variants, and transfer kinetics, as well as tRNA-dependent hydrolysis of cognate isoleucyl-AMP, overview
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