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
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valylation
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isoleucyl-trna
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anticodon
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ilers
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turnip
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noncognate
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leucyl-trna
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mischarged
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trna-like
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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
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atp-ppi
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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
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threonylation
- trnaile
- cysrs
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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
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results (General Information
General Information on EC 6.1.1.9 - valine-tRNA ligase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
a single base change in OsValRS2 causes virescent to albino mutant phenotypes in seedlings and white panicles at heading, termed the white panicle 1 (wp1) mutant. The white panicle1 mutant form of a Val-tRNA synthetase 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
physiological function
additional information
evolution
glp-4 VARS-2 is a cytoplasmic class I valyl aminoacyl tRNA synthetase
evolution
the enzyme belongs to the class I aminoacyl-tRNA synthetases
evolution
the proline triplet in ValS, the tRNA synthetase that charges tRNAVal with valine, is the only single polyproline stretch that is invariant across all domains of life. The critical role of the proline triplet for ValS activity may explain why bacterial cells co-evolved the EF-P rescue system. Nature has evolved not only specialized translation factors to overcome stalling at polyproline stretches, but also evolved independent sets of modification enzymes to activate these factors. This in itself implies that the benefits of retaining polyproline stretches significantly outweigh the cost of implementing and maintaining the EF-P and a/eIF5A rescue systems
physiological function
gene is active and essential for the survival of the yeast
physiological function
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hydrolytic editing activities are present in aminoacyl-tRNA synthetases possessing reduced amino acid discrimination in the synthetic reactions. Post-transfer hydrolysis of misacylated tRNA in class I editing enzymes, e.g. ValRS, occurs in a spatially separate domain inserted into the catalytic Rossmann fold, location and mechanisms of pre-transfer hydrolysis of misactivated amino acids, overview. The rates of amino acid transfer to tRNA are similar for cognate and noncognate aminoacyl-adenylates. Editing by ValRS occurs nearly exclusively by post-transfer hydrolysis in the editing domain
physiological function
glp-4 VARS-2 is a cytoplasmic class I valyl aminoacyl tRNA synthetase that catalyzes the transfer of valine to its cognate tRNA for protein synthesis
physiological function
in Anabaena sp. PCC 7120, ValRS acts as a hub for the nucleation of a translational complex by attracting other aaRSs to the membranes
physiological function
the proline triplet located in the active site of ValS is important for efficient charging of tRNAVal with valine preventing formation of mischarged Thr-tRNAVal, as well as for efficient growth of Escherichia coli in vivo. The critical role of the proline triplet for ValS activity may explain why bacterial cells co-evolved the EF-P rescue system
physiological function
the Val-tRNA synthetase OsValRS2 regulates chloroplast ribosome biogenesis in rice and is essential for early chloroplast development
additional information
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human valyl-tRNA synthetase and mitochondrial protein elongation factor EF-Tu show suppressing cross-activity on different tRNA mutants in humans and Saccharomyces cerevisiae, mechanism and specificity of suppression, overview. Suppressive activities of wild-type and mutant enzymes, overview
additional information
molecular trigger for pre-transfer editing pathway in valyl-tRNA synthetase, molecular dynamics simulations using ValRS structure, PDB ID 1GAX, overview. Structural models of the complexes ValRS-tRNAval-Val-AMP and ValRS-tRNAval-Thr-AMP
additional information
analysis of aminoacyl-tRNA synthetases protein interactions, overview. The Anabaena sp. ValRs is a CAAD-containing aaRSs, the CAAD domain possesses an inherent membrane targeting ability
additional information
expression of ValS is strictly dependent on the presence of active elongation factor P (EF-P) in vivo and in vitro
additional information
structure homology modeling using the valine tRNA-synthetase (valRS) from Thermus thermophilius, PDB ID 1IVS, as a template, also with bound valyl-adenylate substrate
additional information
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structure homology modeling using the valine tRNA-synthetase (valRS) from Thermus thermophilius, PDB ID 1IVS, as a template, also with bound valyl-adenylate substrate
