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Literature summary for 6.1.1.5 extracted from
- Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase (2006), J. Mol. Biol., 359, 901-912.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of His-tagged wild-type and mutants enzymes in Escherichia coli | Thermus thermophilus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| IleRS editing domain complexed with the substrate analogues in the pre and post-transfer modes, X-ray diffraction structure determination and analysis at 1.7 A resolution | Thermus thermophilus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H319A | site-directed mutagenesis, Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain, but the mutant shows detectable editing activities against the cognate isoleucine, mechanism, overview | Thermus thermophilus |
| T223A | site-directed mutagenesis, Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain, but the mutant shows detectable editing activities against the cognate isoleucine, mechanism, overview | Thermus thermophilus |
| W227A | site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme | Thermus thermophilus |
| W227F | site-directed mutagenesis, the mutant shows editing activities which are unaltered compared to the wild-type enzyme | Thermus thermophilus |
| W227H | site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme | Thermus thermophilus |
| W227L | site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme | Thermus thermophilus |
| W227V | site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme | Thermus thermophilus |
| W227Y | site-directed mutagenesis, the mutant shows editing activities which are unaltered compared to the wild-type enzyme | Thermus thermophilus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Thermus thermophilus |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-isoleucine + tRNAIle | Thermus thermophilus | - |
AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | P56690 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type and mutants enzymes from Escherichia coli by nickel affinity chromatography | Thermus thermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-isoleucine + tRNAIle | - |
Thermus thermophilus | AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
| ATP + L-isoleucine + tRNAIle | substrate recognition mechanisms of IleRS are characterized by the active-site rearrangement between the two editing modes, overview, the editing domain contributes to accurate aminoacylation by hydrolyzing the mis-synthesized intermediate, valyl-adenylate, in the pre-transfer editing mode and the incorrect final product, valyl-tRNAIle, in the post-transfer editing mode, Trp227 with its aromatic ring is important | Thermus thermophilus | AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
| additional information | Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain | Thermus thermophilus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| IleRS | - |
Thermus thermophilus |
| Isoleucyl-tRNA synthetase | - |
Thermus thermophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Thermus thermophilus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Thermus thermophilus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Thermus thermophilus | |
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