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Literature summary for 6.1.1.12 extracted from
- Binding free energies and free energy components from molecular dynamics and Poisson-Boltzmann calculations. Application to amino acid recognition by aspartyl-tRNA synthetase (2001), J. Mol. Biol., 306, 307-327.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K198L | exchange of the conserved residue leads to a slightly increased binding of Asp, binding of Asn is strongly increased to the level of Asp, no ability to adenylate Asn, molecular dynamic simulation, binding mechansim and free energy | Escherichia coli |
| K198L/D233E | slightly increased binding of Asp, binding of ASn is strongly increased to the level of Asp, no ability to adenylate Asn, molecular dynamic simulation, binding mechansim and free energy | Escherichia coli |
| K198L/Q199E/D233E | binding of Asp is strongly reduced, no ability to adenylate Asn, molecular dynamic simulation, binding mechansim and free energy | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-aspartate + tRNAAsp | Escherichia coli | - |
AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp | Asn binding sites K198 and H449, binding mechanism and free energies | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-asparagine + tRNAAsp | - |
Escherichia coli | AMP + diphosphate + L-asparaginyl-tRNAAsp | - |
? | |
| ATP + L-aspartate + tRNAAsp | - |
Escherichia coli | AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? | |
| additional information | determination of binding free energies | Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Aspartic acid translase | - |
Escherichia coli |
| Aspartyl ribonucleate synthetase | - |
Escherichia coli |
| aspartyl ribonuleic synthetase | - |
Escherichia coli |
| Aspartyl-transfer ribonucleic acid synthetase | - |
Escherichia coli |
| Aspartyl-transfer RNA synthetase | - |
Escherichia coli |
| Aspartyl-tRNA synthetase | - |
Escherichia coli |
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