6.1.1.4: leucine-tRNA ligase
This is an abbreviated version!
For detailed information about leucine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.4
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6.1.1.4
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aminoacyl-trna
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synthetases
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aminoacylation
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fidelity
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leucylation
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aarss
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mischarged
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post-transfer
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norvaline
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perrault
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anticodon
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aeolicus
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isoacceptors
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misactivated
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aquifex
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ilers
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noncognate
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valrs
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benzoxaborole
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isoleucyl-trna
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misaminoacylated
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hsd17b4
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kmsks
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metrs
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pour
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trnaser
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clinique
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trnaleuuur
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valyl-trna
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isoleucyl
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trna-dependent
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pre-transfer
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drug development
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medicine
- 6.1.1.4
- aminoacyl-trna
- synthetases
- aminoacylation
-
fidelity
-
leucylation
-
aarss
-
mischarged
-
post-transfer
- norvaline
-
perrault
-
anticodon
- aeolicus
-
isoacceptors
-
misactivated
-
aquifex
- ilers
-
noncognate
- valrs
-
benzoxaborole
-
isoleucyl-trna
-
misaminoacylated
- hsd17b4
-
kmsks
- metrs
-
pour
- trnaser
-
clinique
- trnaleuuur
- valyl-trna
-
isoleucyl
-
trna-dependent
-
pre-transfer
- drug development
- medicine
Reaction
Synonyms
AaLeuRS, alphabeta-LeuRS, b0642, cytoplasmic LeuRS, EcLeuRS, GlLeuRS, HcleuRS, hs mt LeuRS, JW0637, LARS, LARS1, LARS2, Leucine translase, Leucine--tRNA ligase, Leucyl-transfer ribonucleate synthetase, Leucyl-transfer ribonucleic acid synthetase, Leucyl-transfer RNA synthetase, leucyl-tRNA ligase, leucyl-tRNA syntethase, Leucyl-tRNA synthetase, leucyl-tRNA synthetase 1, leucyl—tRNA synthetase, LeuRS, LeuRS1, LeuRS2, LeuRSTT, leuS, LRS, MmLeuRS, More, mt leucyl-tRNA synthetase, mt-LeuRS, mtLeuRS, PhLeuRS, Synthetase, leucyl-transfer ribonucleate, ycLeuRS
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Reaction
Reaction on EC 6.1.1.4 - leucine-tRNA ligase
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ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu
bi uni uni bi ping-pong mechanism with ordered addition of ATP and leucine and random release of AMP and leucyl-tRNALeu
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ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu
each amino acid is bound through its carboxyl group to the terminal nucleotide (2'- or 3'-hydroxyl end) of specific polynucleotide chains
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ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu
ATP and tRNA are bound to the enzyme in almost random order, and diphosphate is dissociated before the rate-limiting step
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ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu
A293 is important for the stability of the enzyme conformation and the editing function and probably is involved in the ATP binding
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ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu
active site structure and mechanism, the editing active site binds the two different substrates using a single amino acid discriminatory pocket while preserving he same mode of adenine recognition, Asp347 is involved in the editing process, mechanism of hydrolysis
ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu
Asp345 is involved in the editing process, mechanism of hydrolysis
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ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu
Asp419 is involved in the editing process, mechanism of hydrolysis
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ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu
recognition of the tRNALeu requires the discriminator base A73 and the long variable arm of appropriate stem length, especially the Haloferax volcanii-specific loop sequence A47CG47D and U47H at the base of the helix
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ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu
residue E292 is important for aminoacylation activity
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