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
-
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
- 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 (Engineering
Engineering on EC 6.1.1.9 - valine-tRNA ligase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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)
D279A
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
K270A
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
additional information
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
-
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
