Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-aspartate + tRNAAsp | Homo sapiens | - |
AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? | |
additional information | Homo sapiens | the N-terminal extension of the enzyme is involved in the transfer of Asp-tRNAAsp to elongation factor alpha1, the structural switch model supports the direct transfer mechanism | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-aspartate + tRNAAsp | - |
Homo sapiens | AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? | |
additional information | the N-terminal extension of the enzyme is involved in the transfer of Asp-tRNAAsp to elongation factor alpha1, the structural switch model supports the direct transfer mechanism | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | secondary structure determination, structural switch model, the C-terminus adopts a regular alpha-helix with amphiphilicity, while the N-terminus shows a less-ordered structure with a flexible beta turn | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
Aspartic acid translase | - |
Homo sapiens |
Aspartyl ribonucleate synthetase | - |
Homo sapiens |
aspartyl ribonuleic synthetase | - |
Homo sapiens |
Aspartyl-transfer ribonucleic acid synthetase | - |
Homo sapiens |
Aspartyl-transfer RNA synthetase | - |
Homo sapiens |
Aspartyl-tRNA synthetase | - |
Homo sapiens |
DRS | - |
Homo sapiens |