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 |
EC Number | Cloned (Comment) | Organism |
---|---|---|
6.1.1.9 | overexpression of wild-type and mutant emnzymes in Escherichia coli strain JM109(DE3) | Thermus thermophilus |
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 |
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 |
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 |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.1.1.9 | Thermus thermophilus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
6.1.1.9 | recombinant from Escherichia coli strain JM109(DE3) | Thermus thermophilus |
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 |
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 | ? | - |
? |
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 |
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 |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.9 | ATP | - |
Thermus thermophilus |