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Literature summary for 6.1.1.17 extracted from
- Conformation change of tRNAGlu in the complex with glutamyl-tRNA synthetase is required for specific binding of L-glutamate (1986), Biochemistry, 25, 7031-7036.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | as the KCl concentration is raised from 0 to 100 mM, the Km value for L-glutamate in the reaction with E. coli tRNAGlu is remarkably increased wheras the Km value for glutamate with Thermus thermophilus tRNAGlu is slightly increased | Thermus thermophilus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | - |
wild-type and mutant enzymes | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamate + tRNAGlu | in absence of tRNAGlu, GluRS binds to D-glutamate as well as L-glutamate | Thermus thermophilus | AMP + diphosphate + L-glutamyl-tRNAGlu | - |
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