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Literature summary extracted from
- Molecular dynamics investigation into substrate binding and identity of the catalytic base in the mechanism of threonyl-tRNA synthetase (2012), J. Phys. Chem. B, 116, 5205-5212.
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 6.1.1.3 | ATP + L-threonine + tRNAThr | Escherichia coli | - |
AMP + diphosphate + L-threonyl-tRNAThr | - |
? |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 6.1.1.3 | Escherichia coli | P0A8M3 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 6.1.1.3 | ATP + L-threonine + tRNAThr | - |
Escherichia coli | AMP + diphosphate + L-threonyl-tRNAThr | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 6.1.1.3 | Threonyl-tRNA synthetase | - |
Escherichia coli |
| 6.1.1.3 | ThrRS | - |
Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 6.1.1.3 | ATP | - |
Escherichia coli | |
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Release 2023.1 (January 2023)
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