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Literature summary extracted from

  • Fukai, S.; Nureki, O.; Sekine, S.; Shimada, A.; Vassylyev, D.G.; Yokoyama, S.
    Mechanism of molecular interactions for tRNA(Val) recognition by valyl-tRNA synthetase (2003), RNA, 9, 100-111.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.1.1.9 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 Thermus thermophilus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.9 overexpression of wild-type and mutant emnzymes in Escherichia coli strain JM109(DE3) Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.9 enzyme complexed with tRNAVal and valyl-adenylate, hanging-drop vapour diffusion method, 20°C, 1 month, equal volumes of protein and crystallization solution: 50 mM N-(2-acetoamide)iminodiacetic acid sodium salt buffer, pH 6.5, 2% 2-propanol, 0.1 M lithium sulfate, 12% PEG4000, equilibration against reservoir solution: 50 mM N-(2-acetoamide)iminodiacetic acid sodium salt buffer, pH 6.5, 2% propanol, 0.1 M lithium sulfate, and 14% PEG 4000, ligand-free crystals by macro-seeding, X-ray diffraction structure determination at 2.9 A resolution, and analysis Thermus thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.9 additional information a C-treminally truncated mutant enzyme shows highly reduced activity compared to the wild-type enzyme Thermus thermophilus
6.1.1.9 R818A/R843A slightly reduced activity compared to the wild-type enzyme with tRNAValCAC mutant substrate Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.9 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 Thermus thermophilus
6.1.1.9 0.0015
-
tRNAVal wild-type enzyme, pH 7.7, 65°C Thermus thermophilus
6.1.1.9 0.031
-
tRNAVal C-terminally truncated mutant enzyme, pH 7.7, 65°C Thermus thermophilus
6.1.1.9 0.042
-
tRNAVal R818A/R843A mutant enzyme, pH 7.7, 65°C Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.9 ATP + L-valine + tRNAVal Thermus thermophilus
-
AMP + diphosphate + L-valyl-tRNAVal
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.9 Thermus thermophilus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.9 recombinant from Escherichia coli strain JM109(DE3) Thermus thermophilus

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.9 ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal mechanism and structural basis of molecular interactions of the enzyme with the C34A35C36 anticodon for tRNAVal recognition by the enzyme Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.9 ATP + L-valine + tRNAVal
-
Thermus thermophilus AMP + diphosphate + L-valyl-tRNAVal
-
?
6.1.1.9 ATP + L-valine + tRNAVal wild-type tRNAVal substrate and mutant forms, the anticodon loop structure of the tRNA is important for substrate recognition Thermus thermophilus AMP + diphosphate + L-valyl-tRNAVal
-
?
6.1.1.9 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 Thermus thermophilus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.9 G7a
-
Thermus thermophilus
6.1.1.9 Synthetase, valyl-transfer ribonucleate
-
Thermus thermophilus
6.1.1.9 Valine transfer ribonucleate ligase
-
Thermus thermophilus
6.1.1.9 Valine translase
-
Thermus thermophilus
6.1.1.9 Valine--tRNA ligase
-
Thermus thermophilus
6.1.1.9 ValRS
-
Thermus thermophilus
6.1.1.9 Valyl transfer ribonucleic acid synthetase
-
Thermus thermophilus
6.1.1.9 Valyl-transfer ribonucleate synthetase
-
Thermus thermophilus
6.1.1.9 Valyl-transfer RNA synthetase
-
Thermus thermophilus
6.1.1.9 Valyl-tRNA ligase
-
Thermus thermophilus
6.1.1.9 Valyl-tRNA synthetase
-
Thermus thermophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.9 additional information
-
additional information 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 Thermus thermophilus
6.1.1.9 0.36
-
tRNAVal C-terminally truncated mutant enzyme, pH 7.7, 65°C Thermus thermophilus
6.1.1.9 4.3
-
tRNAVal R818A/R843A mutant enzyme, pH 7.7, 65°C Thermus thermophilus
6.1.1.9 6.7
-
tRNAVal wild-type enzyme, pH 7.7, 65°C Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.9 ATP
-
Thermus thermophilus