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Literature summary for 6.1.1.4 extracted from
- Functional role of C-terminal domain of Thermus thermophilus leucyl-tRNA synthetase (2010), Biopolym. Cell, 26, 478-485.
No PubMed abstract available
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | deletion of the C-terminal domain lowering the kcat by 152fold | Thermus thermophilus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | equilibrium kinetics of wild-type and mutant enzymes, overview | Thermus thermophilus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Leucyl-tRNA synthetase | - |
Thermus thermophilus |
| LeuRSTT | - |
Thermus thermophilus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | activating role of C-terminal domain in the reactions of aminoacylation and editing, and its contribution to interaction with tRNALeu, overview. The C-terminal domain does is not critical for the manifestation of specificity of the enzyme of homologous RNAs, but is required for to enhance the rate of catalysis in aminoacylation and editing reaction | Thermus thermophilus |
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