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Literature summary extracted from

  • 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 (2008), J. Biol. Chem., 283, 30699-30706.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.9 expressed in Saccharomyces cerevisiae as a His-tagged fusion protein Homo sapiens
6.1.1.9 expressed in Saccharomyces cerevisiae as a His-tagged fusion protein Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.9 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 Homo sapiens
6.1.1.9 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 Saccharomyces cerevisiae
6.1.1.9 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) Saccharomyces cerevisiae
6.1.1.9 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 Homo sapiens
6.1.1.9 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 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.9 0.0002
-
 L-valyl-tRNAVal
-
 Saccharomyces cerevisiae
6.1.1.9 0.001
-
 L-valyl-tRNAVal DELTA32-71 mutant Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.9 Homo sapiens
-
-
-
6.1.1.9 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.9 using Ni-NTA chromatography Homo sapiens
6.1.1.9 using Ni-NTA chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.9 ATP + L-valine + tRNAVal
-
 Homo sapiens AMP + diphosphate + L-valyl-tRNAVal
-
 ?
6.1.1.9 ATP + L-valine + tRNAVal
-
 Saccharomyces cerevisiae AMP + diphosphate + L-valyl-tRNAVal
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.9 ValRS
-
 Homo sapiens
6.1.1.9 ValRS
-
 Saccharomyces cerevisiae
6.1.1.9 Valyl-tRNA synthetase
-
 Homo sapiens
6.1.1.9 Valyl-tRNA synthetase
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.9 0.06
-
 L-valyl-tRNAVal DELTA32-71 mutant Saccharomyces cerevisiae
6.1.1.9 0.2
-
 L-valyl-tRNAVal
-
 Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.9 7.9
-
 assay at Homo sapiens
6.1.1.9 7.9
-
 assay at Saccharomyces cerevisiae