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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
-
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 + DL-threonine + tRNAVal
AMP + diphosphate + DL-threonyl-tRNAVal
-
-
-
-
?
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-threonine + tRNAVal
AMP + diphosphate + L-threonyl-tRNAVal
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
AMP + diphosphate + L-valyl-tRNAVal
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-2)
AMP + diphosphate + L-valyl-tRNAVal(UAC-2)
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
-
-
-
-
?
additional information
?
-
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
-
-
-
?
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
-
-
-
ir
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
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
-
-
-
?
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
-
tRNA recognition mechanism, the anticodon sequence is important for the aminoacylation
-
?
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
-
tRNA from E. coli or Mycobacterium smegmatis
-
?
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
-
-
-
-
?
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
-
-
-
?
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
-
-
-
?
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
?
-
-
-
-
-
?
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
?
-
-
-
-
-
?
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
?
-
-
no activity with dATP
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.33
DL-2-amino-3-chlorobutyrate
-
-
3.7
DL-2-aminobutyrate
-
-
1
DL-allo-2-amino-3-chlorobutyrate
-
-
1.9
L-isoleucine
-
pH 7.5, 37°C
0.3
L-threonine
-
ATP-diphosphate exchange reaction, native wild-type enzyme, pH 7.5, 25°C
0.0002 - 0.001
L-valyl-tRNAVal
0.00061
tRNAVal(GAC)
-
in 100 mM HEPES (pH 7.2), 20 mM KCl, 30 mM MgCl2, at 30°C
-
0.00208
tRNAVal(UAC)
-
in 100 mM HEPES (pH 7.2), 20 mM KCl, 30 mM MgCl2, at 30°C
-
0.00108
tRNAVal(UAC-2)
-
in 100 mM HEPES (pH 7.2), 20 mM KCl, 30 mM MgCl2, at 30°C
-
additional information
additional information
-
0.029
ATP
-
tetrameric enzyme form
0.07
ATP
-
cytoplasmic enzyme
0.071
ATP
-
monomeric enzyme form
0.11
ATP
-
ATP-diphosphate exchange reaction, His-tagged wild-type and mutant enzymes, pH 7.5, 25°C
0.2005
ATP
-
in 100 mM HEPES (pH 7.2), 20 mM KCl, 30 mM MgCl2, at 30°C
5.8
ATP
-
pH 7.5, 37°C, mutant D286A, in presence of tRNA
9.4
ATP
-
pH 7.5, 37°C, wild-type ValRS, in presence of tRNA
10.7
ATP
-
pH 7.5, 37°C, mutant K277P/D286A, in presence of tRNA
13.4
ATP
-
pH 7.5, 37°C, mutant K277P, in presence of tRNA
0.0019
L-valine
-
aminoacylation reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C
0.002
L-valine
-
with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C
0.0043
L-valine
-
with wild-type tRNAVal, pH 7.5, 37°C
0.0048
L-valine
-
with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C
0.005
L-valine
-
with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C
0.0088
L-valine
-
with mutant tRNAVal with 3'-terminal purine riboside base analogue, pH 7.5, 37°C
0.015
L-valine
-
chloroplastic enzyme
0.0395
L-valine
-
pH 7.5, 37°C
0.047
L-valine
-
aminoacylation reaction, His-tagged wild-type enzyme, pH 7.5, 25°C
0.05
L-valine
-
cytoplasmic enzyme
0.05
L-valine
-
ATP, cytoplasmic enzyme
0.062
L-valine
-
ATP-diphosphate exchange reaction, native wild-type enzyme, pH 7.5, 25°C
0.07
L-valine
-
ATP-diphosphate exchange reaction, His-tagged wild-type enzyme, pH 7.5, 25°C
0.072
L-valine
-
ATP-diphosphate exchange reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C
0.1926
L-valine
-
in 100 mM HEPES (pH 7.2), 20 mM KCl, 30 mM MgCl2, at 30°C
0.0002
L-valyl-tRNAVal
-
-
0.001
L-valyl-tRNAVal
-
DELTA32-71 mutant
0.00005
tRNAVal
-
of Euglena gracilis
0.00005
tRNAVal
-
cytoplasmic enzyme
0.00006
tRNAVal
-
of Euglena gracilis, , chloroplastic enzyme
0.00008
tRNAVal
-
tRNA, of E. coli, , chloroplasmic enzyme
0.00008
tRNAVal
-
tRNA, of yeast, , cytoplasmic enzyme
0.00008
tRNAVal
-
of Euglena, , cytoplasmic enzyme
0.00008
tRNAVal
-
aminoacylation reaction with L-valine, wild-type enzyme, pH 7.5, 25°C
0.0001
tRNAVal
-
aminoacylation reaction with L-valine, His-tagged wild-type enzyme, pH 7.5, 25°C
0.0001
tRNAVal
-
aminoacylation reaction with L-valine, K277A mutant enzyme, pH 7.5, 25°C
0.00018
tRNAVal
-
substrate from cytoplasm, , cytoplasmic enzyme
0.00019
tRNAVal
-
substrate from cytoplasm, , mitochondrial enzyme
0.00026
tRNAVal
-
aminoacylation reaction with L-valine, His-tagged K277A mutant enzyme, pH 7.5, 25°C
0.0009
tRNAVal
-
tetrameric enzyme form
0.00092
tRNAVal
-
monomeric enzyme form
0.0015
tRNAVal
-
wild-type enzyme, pH 7.7, 65°C
0.00165
tRNAVal
-
substrate from mitochondria, , mitochondrial and cytoplasmic enzyme
0.031
tRNAVal
-
C-terminally truncated mutant enzyme, pH 7.7, 65°C
0.042
tRNAVal
-
R818A/R843A mutant enzyme, pH 7.7, 65°C
0.001
valine
-
-
0.0082
valine
-
monomeric enzyme form
0.01
valine
-
tetrameric enzyme form
0.023
valine
-
enzyme expressed on E. coli
additional information
additional information
-
Km-values of ATP analogs
-
additional information
additional information
-
Km of anticodon loop mutants of turnip yellow mosaic virus RNA
-
additional information
additional information
-
Km for tRNAVal mutants, 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
-
additional information
additional information
-
steady-state parameters for tRNA-independent pre-transfer editing by ValRS and its mutants determined by varying concentrations of noncognate threonine, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.06 - 0.2
L-valyl-tRNAVal
additional information
additional information
-
0.28
ATP
-
pH 7.5, 37°C, mutant D286A, in presence of tRNA
0.34
ATP
-
pH 7.5, 37°C, mutant K277P, in presence of tRNA
0.48
ATP
-
pH 7.5, 37°C, mutant K277P/D286A, in presence of tRNA
12.9
ATP
-
pH 7.5, 37°C, wild-type ValRS, in presence of tRNA
50
ATP
-
ATP-diphosphate exchange reaction, His-tagged wild-type enzyme, pH 7.5, 25°C
57
ATP
-
ATP-diphosphate exchange reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C
0.064
L-valine
-
aminoacylation reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C
0.074
L-valine
-
at pH and °C
0.68
L-valine
-
with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C
0.99
L-valine
-
with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C
1.06
L-valine
-
with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C
1.5
L-valine
-
aminoacylation reaction, His-tagged wild-type enzyme, pH 7.5, 25°C
6.08
L-valine
-
with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C
6.08
L-valine
-
with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C
6.08
L-valine
-
with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C
13.9
L-valine
-
with wild-type tRNAVal, pH 7.5, 37°C
14.4
L-valine
-
with mutant tRNAVal with 3'-terminal purine riboside base analogue, pH 7.5, 37°C
0.06
L-valyl-tRNAVal
-
DELTA32-71 mutant
0.36
tRNAVal
-
C-terminally truncated mutant enzyme, pH 7.7, 65°C
1.5
tRNAVal
-
aminoacylation reaction with L-valine, K277A mutant enzyme, pH 7.5, 25°C
1.7
tRNAVal
-
aminoacylation reaction with L-valine, wild-type enzyme, pH 7.5, 25°C
4.3
tRNAVal
-
R818A/R843A mutant enzyme, pH 7.7, 65°C
6.7
tRNAVal
-
wild-type enzyme, pH 7.7, 65°C
50
tRNAVal
-
ATP-diphosphate exchange reaction, K277A mutant enzyme, pH 7.5, 25°C
51
tRNAVal
-
ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.5, 25°C
2.9
valine
-
-
5.65
valine
-
enzyme expressed in E. coli
additional information
additional information
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kcat for tRNAVal mutants, loss of the electrostatically interactions between the coiled-coil domain of the enzyme and base A20 and tertiary bas pair G19.C56 increases the kcat for aminoacylation by 19fold
-
additional information
additional information
-
rate of hydrolysis of Thr-tRNAVal and Val-tRNAVal by wild-type and mutant enzyme, incorporation of amino acids valine and threonine into the enzyme
-
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G296D
naturally occuring mutation bn2, the mutant glp-4(bn2ts) shows partial loss of function. Aspartate 296 in the editing pocket induces inappropriate deacylation of correctly charged Val-tRNAval. Intragenic suppressor mutations are predicted to displace aspartate 296 so that it is less able to catalyze inappropriate deacylation. Thus glp-4(bn2ts) likely causes reduced protein translation due to decreased levels of Val-tRNAval. glp-4(bn2ts) mutants are widely used to generate germline deficient mutants for organismal studies, under the assumption that the soma is unaffected. As reduced translation has also been demonstrated to alter organismal properties, it is unclear whether changes in aging, stress resistance etc. observed in glp-4(bn2ts) mutants are the result of germline deficiency or reduced translation. The G296D mutation lies just inside a region of the valyl-tRNA synthetase called the CP1 domain
D286A
-
site-directed mutagenesis, the ValRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations
K277A
-
site-directed mutagenesis, mutant exhibits a reduced posttransfer editing activity compared to the wild-type, also the specificiy of the editing reaction is modulated, the mutant hydrolyzes the correctly formed Val-tRNAVal, increased sensitivity to Mg2+, high concentrations inactivate
K277P
-
site-directed mutagenesis, the ValRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations
K277P/D286A
-
site-directed mutagenesis, the ValRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations
C25T
-
site-directed mutagenesis
DELTA1-97
-
an N-domain-deleted yeast valyltRNA synthetase mutant (DELTA1-97) form Saccharomyces cerevisiae can be rescued by fusion of the equivalent domain from its human homologue
D750G
-
the mutation is associated with a temperature-sensitive phenotype. Although depicting slower growth at 26°C, the mutant strain is unable to grow at 37°C
DELTA1-97
-
deletion of N-terminal polypeptide extension of 97 residues, which is absent in bacteria, severely impairs tRNA binding, aminoacylation, and complementation activities of the enzyme. This N-domain-deleted yeast valyl-tRNA synthetase mutant can be rescued by fusion of the equivalent domain from its human homologue
DELTA32-71
-
deletion of a lysine rich insert impairs aminoacylation activity of the enzyme in vitro but aminoacylation activity is still significantly higher than in DELTA1-97 mutant. Km: 0.001 mM (L-valyl-tRNAVal), kcast: 0.06/sec (L-valyl-tRNAVal)
D276A
valylation activity is similar to that of wild-type enzyme
F264A
valylation activity is similar to that of wild-type enzyme, about 15% decrease in ATP consumption rate compared to wild-type enzyme, somewhat reduced deacylation activityith Thr-tRNAVal, mutation impairs editing activity of ValRS
R216A
valylation activity is similar to that of wild-type enzyme, about 15% decrease in ATP consumption rate compared to wild-type enzyme, somewhat reduced deacylation activity with Thr-tRNAVal
R818A/R843A
-
slightly reduced activity compared to the wild-type enzyme with tRNAValCAC mutant substrate
T272A
valylation activity is similar to that of wild-type enzyme, about 15% decrease in ATP consumption rate compared to wild-type enzyme, somewhat reduced deacylation activity with Thr-tRNAVal
D279A
valylation activity is similar to that of wild-type enzyme, efficiently produces Thr-tRNAVal, drastic decrease in ATP consumption rate, severe deficiency in deacylation activity with Thr-tRNAVal compared to wild-type enzyme
D279A
editing site mutation, severely affects the binding ability of pre-transfer substrate Thr-AMP
K270A
slight reduction of valylation activity, efficiently produces Thr-tRNAVal, drastic decrease in ATP consumption rate, severe deficiency in deacylation activity with Thr-tRNAVal compared to wild-type enzyme
K270A
editing site mutation, severely affects the binding ability of pre-transfer substrate Thr-AMP
additional information
a knockout mutation causes early larval lethality
additional information
-
a knockout mutation causes early larval lethality
additional information
-
substitution of base 75 of C by U or A leads to effective stimulation of the editing activity at lower rates, substitution with G leads to reduction of the editing activity by 95%, mutational exchange of the discriminator base A73 to U73 or C73 does not alter enzyme activity but exchange to G73 stimulates editing activity of the catalytically inactive mutant
additional information
generation of three single ValS Pro-to-Gly mutants, ValS-GPP, ValS-PGP, and ValS-PPG, as well as a triple PPP-to-GGG mutant (ValS-GGG). The ability of the ValS mutants to charge tRNAVal with [14C]valine is assessed and compared to wild-type ValS. All ValS mutants are less efficient than the wild-type, the ValS-PPG and ValS-GGG mutants are completely devoid of activity, whereas the ValS-PGP and ValS-GPP mutants retain some activity but at lower levels than the wild-type enzyme
additional information
-
construction of mutant tRNAs
additional information
-
construction of mutant tRNAs
-
additional information
-
fusion of the N-terminal 97 residue domain of human ValRS to Escherichia coli glutaminyl-tRNA synthetase enables the otherwise inactive prokaryotic enzyme to function as a yeast enzyme in vivo. Different from the native yeast enzyme, which shows different affinities toward mixed tRNA populations, the fusion enzyme exhibites similar binding affinities for all yeast tRNAs
additional information
a single base change in OsValRS2, changing a Trp into a Cys, causes virescent to albino mutant phenotypes in seedlings and white panicles at heading, the mutant is termed the white panicle 1 (wp1) mutant. The white panicle1 mutant form of a Val-tRNA synthetase (OsValRS2) from Oryza sativa is targeted to both chloroplasts and mitochondria. The wp1 mutants are defective in early chloroplast development, and wp1 is impaired in chloroplast ribosome biogenesis. Expression of nuclear-encoded photosynthetic genes is significantly repressed, while expression of many chloroplast-encoded genes also changed significantly in wp1 mutants, although mRNA levels of some genes are higher in wp1 than in wild-type. Phenotype, overview
additional information
-
substitution of the AUG initiator of the mitochondrial ValRS isozyme, ATG1 of VAS1, with redundant ACG triplets, mutation of ATG1 to GCG deprived the construct of its mitochondrial activity, redundant ACG triplets could effectively substitute for ATG1 in initiation of the mitochondrial enzyme, while a single ACG triplet could hardly do so
additional information
-
fusion of the N-terminal 97 residue domain of the yeast enzyme or its human counterpart to Escherichia coli glutaminyl-tRNA synthetase enables the otherwise inactive prokaryotic enzyme to function as a yeast enzyme in vivo. Different from the native yeast enzyme, which shows different affinities toward mixed tRNA populations, the fusion enzyme exhibites similar binding affinities for all yeast tRNAs
additional information
-
a C-treminally truncated mutant enzyme shows highly reduced activity compared to the wild-type enzyme
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5
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