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Literature summary for 6.1.1.12 extracted from
- Yeast tRNA(Asp) charging accuracy is threatened by the N-terminal extension of aspartyl-tRNA synthetase (2003), J. Biol. Chem., 278, 9683-9690.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of wild-type enzyme, amino acid residues 1-557, and a truncated mutant enzyme, amino acid resdiues 71-557, as His-tagged proteins in Escherichia coli | Saccharomyces cerevisiae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics of several tRNAAsp variants | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-aspartate + tRNAAsp | Saccharomyces cerevisiae | - |
AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
activity with several tRNAAsp variants | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-aspartate + tRNAAsp | - |
Saccharomyces cerevisiae | AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? | |
| ATP + L-aspartate + tRNAAsp | specificty of tRNA recognition by the enzyme is primarily ensured by the tRNA identity determinants, the discriminator base G37, four bases in the anticodon loop G34, U35, C36, and C38, and G10-U25 base pair in the core region of the tRNA, substrate specificity of wild-type and truncated mutant enzymes, overview | Saccharomyces cerevisiae | AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the N-terminal appendix of 70 amino acid residues adopts a helical structure and encompasses the RNA binding motif XSKXXLKKXK | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Aspartic acid translase | - |
Saccharomyces cerevisiae |
| Aspartyl ribonucleate synthetase | - |
Saccharomyces cerevisiae |
| aspartyl ribonuleic synthetase | - |
Saccharomyces cerevisiae |
| Aspartyl-transfer ribonucleic acid synthetase | - |
Saccharomyces cerevisiae |
| Aspartyl-transfer RNA synthetase | - |
Saccharomyces cerevisiae |
| Aspartyl-tRNA synthetase | - |
Saccharomyces cerevisiae |
| AspRS | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Saccharomyces cerevisiae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | catalytic efficiency of several tRNAAsp variants | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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