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Literature summary for 6.1.1.17 extracted from
- The catalytic mechanism of glutamyl-tRNA synthetase of Escherichia coli. A steady-state kinetic investigation (1981), Eur. J. Biochem., 115, 29-38.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu | ATP and tRNAGlu bind randomly to the free enzyme, whereas glutamate binds only to the ternary enzyme-tRNAGlu-ATP complex. After interconversion of the quarternary enzyme-substrate complex the end-products dissociate in the order: diphosphate, AMP, Glu-tRNA | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamate + tRNAGlu | - |
Escherichia coli | AMP + diphosphate + L-glutamyl-tRNAGlu | - |
? |  |
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