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Literature summary for 6.1.1.4 extracted from
- Crystal structure of leucyl-tRNA synthetase from the archaeon Pyrococcus horikoshii reveals a novel editing domain orientation (2005), J. Mol. Biol., 346, 57-71.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging-drop vapour-diffusion method, resolution 2.1 A, C-terminally truncated LeuRS (amino acids 1-810), crystals belong to the Rhombohedral space group R3, with unit-cell parameters a = b = 186.23 A, c = 91.45 A, alpha = beta = 90°, gamma = 120° for the native form and a = b = 185.8 A, c = 91.19 A, alpha = beta = 90°, and gamma = 120° for the SeMet crystal | Pyrococcus horikoshii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D332A | unlike the wild-type enzyme the mutant enzyme synthesizes the incorrect product Ile-tRNALeu, unlike the wild-type enzyme, the mutant enzyme cannot deacylate Ile-tRNALeu | Pyrococcus horikoshii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus horikoshii | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant C-terminally truncated LeuRS (amino acids 1-819) | Pyrococcus horikoshii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-isoleucine + tRNALeu | activity with mutant enzyme D332A, no activity with wild-type full-length enzyme | Pyrococcus horikoshii | AMP + diphosphate + L-isoleucyl-tRNALeu | - |
? |  |
| ATP + L-leucine + tRNALeu | - |
Pyrococcus horikoshii | AMP + diphosphate + L-leucyl-tRNALeu | - |
? | |
| additional information | wild-type, full-length enzyme deacylates the pre-formed Ile-tRNALeu | Pyrococcus horikoshii | ? | - |
? | |
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