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Information on EC 6.1.1.9 - valine-tRNA ligase and Organism(s) Homo sapiens and UniProt Accession P26640

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Homo sapiens
UNIPROT: P26640 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
valyl-trna synthetase, valrs, glp-4, val-trna synthetase, valyl-transfer rna synthetase, osvalrs2, valine-trna ligase, valyl-trna ligase, valyl transfer ribonucleic acid synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Valyl-tRNA synthetase
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G7a
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-
-
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mitochondrial valyl tRNA synthetase
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MTTV
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Synthetase, valyl-transfer ribonucleate
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-
-
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Valine transfer ribonucleate ligase
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-
-
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Valine translase
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-
-
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Valine--tRNA ligase
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-
-
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ValRS
Valyl transfer ribonucleic acid synthetase
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-
-
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Valyl-transfer ribonucleate synthetase
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-
-
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Valyl-transfer RNA synthetase
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-
-
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Valyl-tRNA ligase
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Valyl-tRNA synthetase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
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Aminoacylation
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-
-
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PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
L-valine:tRNAVal ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-47-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-valine + tRNAVal
AMP + diphosphate + L-valyl-tRNAVal
show the reaction diagram
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-
-
-
?
additional information
?
-
functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.9
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cytoplasmic valRS; gene VARS
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SYVC_HUMAN
1264
0
140476
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
-
gel filtration
additional information
-
three-dimensional structure of the valyl-tRNA synthetase/elongation factor-1H complex
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme possesses N terminal alpha-helices with basic residues distributed asymmetrically, on a single face of the helix, termed basic faced alpha helices, BFAHs, which are unique to the aminoacyl-tRNA synthetases, structural analysis, determination of distribution of basic residues within protein secondary structure by Fourier analysis, functional and evolutionary aspects of these structural features, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C25T
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site-directed mutagenesis
DELTA1-97
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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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae as a His-tagged fusion protein
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gene VARS2
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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a C25U point mutation in the MTTV gene, gene encoding tRNAVal, is associated with a metabolic disorder resulting in the neonatal deaths of numerous siblings. In primary myoblasts and transmitochondrial cybrids established from the proband and offspring, the steady-state levels of the mutated mt-tRNAVal are greater than in the biopsy material, but are still lower than in control myoblasts. Decrease in steady-state mt-tRNAVal observed cell lines is caused by a rapid degradation of the deacylated form of the abnormal mt-tRNAVal. By both establishing the identity of the human mitochondrial valyltRNA synthetase then inducing its overexpression in transmitochondrial cell lines, steady-state levels of the mutated mt-tRNAVal can be partially restored
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jiang, S.; Wolfe, C.L.; Warrington, J.A.; Norcum, M.T.
Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the delta subunit
FEBS Lett.
579
6049-6054
2005
Homo sapiens
Manually annotated by BRENDA team
Massey, S.E.
Basic faced alpha-helices are widespread in the peptide extensions of the eukaryotic aminoacyl-tRNA synthetases
In Silico Biol.
6
259-273
2006
Saccharomyces cerevisiae, Homo sapiens (P26640), Takifugu rubripes (P49696), Arabidopsis thaliana (P93736), Oryza sativa (Q851K9)
Manually annotated by BRENDA team
Chang, C.P.; Lin, G.; Chen, S.J.; Chiu, W.C.; Chen, W.H.; Wang, C.C.
Promoting the formation of an active synthetase/tRNA complex by a nonspecific tRNA-binding domain
J. Biol. Chem.
283
30699-30706
2008
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Rorbach, J.; Yusoff, A.A.; Tuppen, H.; Abg-Kamaludin, D.P.; Chrzanowska-Lightowlers, Z.M.; Taylor, R.W.; Turnbull, D.M.; McFarland, R.; Lightowlers, R.N.
Overexpression of human mitochondrial valyl tRNA synthetase can partially restore levels of cognate mt-tRNAVal carrying the pathogenic C25U mutation
Nucleic Acids Res.
36
3065-3074
2008
Homo sapiens
Manually annotated by BRENDA team
Montanari, A.; De Luca, C.; Frontali, L.; Francisci, S.
Aminoacyl-tRNA synthetases are multivalent suppressors of defects due to human equivalent mutations in yeast mt tRNA genes
Biochim. Biophys. Acta
1803
1050-1057
2010
Homo sapiens
Manually annotated by BRENDA team