6.1.1.9: valine-tRNA ligase
This is an abbreviated version!
For detailed information about valine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.9
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6.1.1.9
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synthetases
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aminoacylation
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aminoacyl-trna
-
valylation
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isoleucyl-trna
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anticodon
-
ilers
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turnip
-
noncognate
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leucyl-trna
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mischarged
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trna-like
-
isoleucyl
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misacylated
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misactivated
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post-transfer
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l-shaped
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aarss
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phenylalanyl-trna
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threonylation
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trnaile
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cysrs
-
atp-ppi
-
medicine
- 6.1.1.9
- synthetases
- aminoacylation
- aminoacyl-trna
-
valylation
-
isoleucyl-trna
-
anticodon
- ilers
-
turnip
-
noncognate
- leucyl-trna
-
mischarged
-
trna-like
-
isoleucyl
-
misacylated
-
misactivated
-
post-transfer
-
l-shaped
-
aarss
- phenylalanyl-trna
-
threonylation
- trnaile
- cysrs
-
atp-ppi
- medicine
Reaction
Synonyms
G7a, glp-4, mitochondrial valyl tRNA synthetase, More, MTTV, Os03g0694900, OsValRS2, Synthetase, valyl-transfer ribonucleate, Val-tRNA synthetase, Valine transfer ribonucleate ligase, Valine translase, Valine--tRNA ligase, ValRS, ValRS1, ValRS2, valS, valyl aminoacyl tRNA synthetase, Valyl transfer ribonucleic acid synthetase, Valyl-transfer ribonucleate synthetase, Valyl-transfer RNA synthetase, Valyl-tRNA ligase, Valyl-tRNA synthetase, valyl-tRNAsynthetase, VARS, VARS-2, Vas1, Vas2, white panicle1
ECTree
6.1.1.9 valine-tRNA ligaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 6.1.1.9 - valine-tRNA ligase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-chloroadenosine 5'-triphosphate + L-valine + tRNAVal
2-chloroadenosine 5'-monophosphate + diphosphate + L-valyl-tRNAVal
-
-
-
-
?
ATP + DL-2-amino-3-chlorobutyrate + tRNAVal
AMP + diphosphate + DL-2-amino-3-chlorobutyryl-tRNAVal
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as effective as valine
-
-
?
ATP + DL-2-aminobutyrate + tRNAVal
AMP + diphosphate + DL-2-aminobutyryl-tRNAVal
-
30% of the activity with valine
-
-
?
ATP + DL-allo-2-amino-3-chlorobutyrate + tRNAVal
AMP + diphosphate + DL-allo-2-amino-3-chlorobutyryl-tRNAVal
-
15% of the activity with valine
-
-
?
ATP + L-isoleucine + tRNAVal
AMP + diphosphate + L-isoleucyl-tRNAVal
-
very low activity
-
?
ATP + L-threonine + tRNAVal
?
-
1 step performance of an originally two-step reaction, the enzyme can hardly differentiate between the cognate amino acid valine and others, especially threonine, to minimize misaminoacetylation the enzyme performs a proofreading, socalled editing reaction at a second active site, which is dependent on the presence of cognate tRNAVal whose 3'-end is involved in the editing reaction, a majority of editing by the enzyme entails prior charging of the tRNA, misacylated tRNA is a transient intermediate in the editing reaction
-
?
ATP + L-valine + tRNAiMet,GAC mutant
AMP + diphosphate + L-valyl-tRNAiMet,GAC mutant
-
anticodon CAU to GAC initiator tRNA mutant, i.e. G34C36 mutant, is aminoacylated in vitro and in vivo, its anticodon sequence corresponds to the one of tRNAVal
-
?
ATP + L-valine + tRNAVal,3' 2-aminopurine
AMP + diphosphate + L-valyl-tRNAVal, 3' 2-aminopurine
-
mutant tRNAVal with 3'-terminal 2-aminopurine base analogue substitution
-
?
ATP + L-valine + tRNAVal,3' inosine
AMP + diphosphate + L-valyl-tRNAVal, 3' inosine
-
mutant tRNAVal with 3'-terminal inosine base analogue substitution
-
?
ATP + L-valine + tRNAVal,3' isoguanosine
AMP + diphosphate + L-valyl-tRNAVal, 3' isoguanosine
-
mutant tRNAVal with 3'-terminal isoguanosine base analogue substitution
-
?
ATP + L-valine + tRNAVal,3' purine riboside
AMP + diphosphate + L-valyl-tRNAVal, 3' purine riboside
-
mutant tRNAVal with 3'-terminal purine riboside base analogue substitution
-
?
formycin 5'-triphosphate + L-valine + tRNAVal
formycin 5'-monophosphate + diphosphate + L-valyl-tRNAVal
-
-
-
-
?
L-threonyl-tRNAVal
L-threonine + tRNAVal
-
substrate bound to the enzyme, intermediate in the posttransfer editing reaction
-
ir
L-threonyl-tRNAVal-AMP
L-threonine + tRNAVal + AMP
-
substrate bound to the enzyme, intermediate in the pretransfer editing reaction
-
ir
tubercidin 5'-triphosphate + L-valine + tRNAVal
tubercidin 5'-monophosphate + diphosphate + L-valyl-tRNAVal
-
-
-
-
?
ATP + L-threonine + tRNAVal
AMP + diphosphate + L-threonyl-tRNAVal
-
28% of the activity with valine
-
-
?
ATP + L-threonine + tRNAVal
AMP + diphosphate + L-threonyl-tRNAVal
-
noncognate isosteric substrate, low activity, posttransfer editing occurs
-
ir
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
ir
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
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enzyme contains 2 tRNA binding sites involved in aminoacetylation and editing reactions, misacetylated tRNAVal is edited by the enzyme to avoid accumulation, the 3'-end of the tRNA is involved
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
two-step reaction, covalent valylation of the enzyme
-
ir
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
two-step reaction, the enzyme can hardly differentiate between the cognate amino acid valine and others, especially threonine, to minimize misaminoacetylation the enzyme performs a proofreading, socalled editing reaction at a second active site, which is dependent on the presence of cognate tRNAVal whose 3'-end is involved in the editing reaction, a majority of editing by the enzyme entails prior charging of the tRNA, misacylated tRNA is a transient intermediate in the editing reaction
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
charging of tRNAVal by ValS occurs in two steps: firstly, valine is activated with ATP to form Val-AMP leading to the release of pyrophosphate, and secondly, the valine is then transferred to the tRNAVal to form Val-tRNAVal, with a concomitant release of AMP
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
chloroplastic enzyme charges E. coli tRNA and not yeast tRNA, cytoplasmic enzyme is able to aminoacylate yeast tRNA but not E. coli tRNA
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
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tRNA recognition mechanism, the anticodon sequence is important for the aminoacylation
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?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
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tRNA from E. coli or Mycobacterium smegmatis
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?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
the enzyme is strictly specific for the cognate L-valine and discriminates from the larger L-isoleucine and L-threonine by the tRNA-dependent double sieve mechanism
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
wild-type tRNAVal substrate and mutant forms, the anticodon loop structure of the tRNA is important for substrate recognition
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
ATP + L-valine + tRNAVal(GAC)
AMP + diphosphate + L-valyl-tRNAVal(GAC)
-
-
-
-
?
ATP + L-valine + tRNAVal(GAC)
AMP + diphosphate + L-valyl-tRNAVal(GAC)
-
-
-
-
?
ATP + L-valine + tRNAVal(UAC)
AMP + diphosphate + L-valyl-tRNAVal(UAC)
-
-
-
-
?
ATP + L-valine + tRNAVal(UAC)
AMP + diphosphate + L-valyl-tRNAVal(UAC)
-
-
-
-
?
ATP + L-valine + tRNAVal(UAC-2)
AMP + diphosphate + L-valyl-tRNAVal(UAC-2)
-
-
-
-
?
ATP + L-valine + tRNAVal(UAC-2)
AMP + diphosphate + L-valyl-tRNAVal(UAC-2)
-
-
-
-
?
additional information
?
-
functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
-
-
?
additional information
?
-
-
valine-dependent ATP-diphosphate exchange: valine + ATP + enzyme /Val-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
-
catalytic activity with L-valine and diverse tRNA analogues with functional group substitutions at the terminal nucleoside of the 3'-end, some of which stimulate the editing reaction, overview
-
?
additional information
?
-
-
substrate specificity with diverse Escherichia coli tRNAs and tRNA mutants in editing and aminoacylation reaction, overview
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction, labeling of the enzyme by methionyladenylate, determination of lysine residues involved in binding
-
?
additional information
?
-
-
tRNAVal variants in position 76, i.e. U76, C76, G76 activate the editing activity, misactivation of threonine, alanine, serine, cysteine, alpha-aminobutyrate, and to a low extent of norvaline activates the editing reaction at different rates, overview, the enzyme is unable to deacylate misacylated tRNAVal terminating in 3'-pyrimidines but does deacylate mischarged tRNAVal terminating in adenosine or guanosine, no misactivation of methionine, leucine, glycine, glutamic acid, lysine, tyrosine, and phenylalanine
-
?
additional information
?
-
functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
-
-
?
additional information
?
-
-
valine-dependent ATP-diphosphate exchange: valine + ATP + enzyme /Val-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
interaction of membrane-anchored ValRS with ATP synthase, analysis of the impact of the interaction on the activity of ValRS by measuring aminoacylation activity in whole cell extracts of the wild-type strain and the Anabaena 1C mutant, where the interaction between ValRS and ATP synthase is not expected to occur, analysis of aminoacyl-tRNA synthetases protein interactions, overview
-
-
?
additional information
?
-
functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
-
-
?
additional information
?
-
-
functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
-
-
?
additional information
?
-
-
redundancy of non-AUG initiators is a mechanism to enhance the efficiency of translation in yeast
-
-
?
additional information
?
-
functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
-
-
?
additional information
?
-
-
loss of the electrostatically interactions between the coiled-coil domain of the enzyme and base A20 and tertiary bas pair G19.C56 increases the Km for the tRNA by 28fold and the kcat for aminoacylation by 19fold
-
?
additional information
?
-
-
substitutions in the anticodon loop of turnip yellow mosaic virus RNA diminish the viral RNA's ability to be valylated by wheat germ ValRS
-
-
?
additional information
?
-
-
valine-dependent ATP-diphosphate exchange: valine + ATP + enzyme /Val-AMP-enzyme + diphosphate
-
-
?
