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
-
isoleucylation
- valyl-trna
-
misactivated
- methionyl-trna
- leurs
-
mischarged
-
pseudomonic
-
post-transfer
-
noncognate
- valrs
-
mupirocin-resistant
-
misacylated
-
anticodons
-
aarss
-
kmsks
- glnrs
-
trna-dependent
-
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
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results (Metals Ions
Metals Ions on EC 6.1.1.5 - isoleucine-tRNA ligase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Mg2+
Zinc
Zn2+
additional information
polyamines can replace part of the Mg2+ ions in the aminoacyl-tRNA synthetase reactions, spermidine can replace Mg2+ (KME3) and Mg2+ (KME42), which are involved in the forward and backward transfer reaction, while the competition with Mg2+ (KMR) is much weaker, kinetics, overview
Mg2+
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at least 2 bound Mg2+ or spermidines required for the binding of tRNA to the enzyme
Mg2+
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optimum at very low concentration (0.5-0.7 mM), slight inhibition at higher concentration
Mg2+
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enzyme-bound isoleucyl-AMP can be formed in the absence of Mg2+ and spermine
Mg2+
required. 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
Mg2+
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at a concentration of ATP and diphosphate of 3 mM, the optimal Mg2+ concentration is 6-10 mM
Mg2+
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in presence of 50 mM K+ and in absence of polyamines, the optimal Mg2+ concentration for Ile-tRNA formation is 1 mM, an increase in Mg2+ concentration markedly inhibits
Zinc
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a single zinc atom which is coordinated to ligands is contained in the catalytic domain, a second, functionally essential zinc is bound to ligands at the C-terminal end of the 939 amino acid polypeptide, the average zinc environment contains predominantly sulfur ligands with a Zn-S distance of 2.33 A
