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Literature summary for 2.3.2.12 extracted from
- Linezolid and tiamulin cross-resistance in Staphylococcus aureus mediated by point mutations in the peptidyl transferase center (2008), Antimicrob. Agents Chemother., 52, 1737-1742.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| linezolid | - |
Thermus thermophilus |  |
| tiamulin | - |
Thermus thermophilus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | deletion of ribosomal protein L27 is predicted to give only a minor reaction rate reduction. The N-terminus of L27 interacts with the A76 phosphate group of the A-site tRNA, explaining the observed impairment of A-site substrate binding for ribosomes lacking L27. The calculated energetics show that substrate puromycin can cause a downward pKa shift of L27 and that the reaction proceeds faster with the L27 N-terminus deprotonated, in contrast to the situation with aminoacyl-tRNA substrates. These results could explain the observed differences in pH dependence between the puromycin and C-puromycin reactions, where the former reaction has been seen to depend on an additional ionizing group besides the attacking amine, and this ionizing group is predicted to be the N-terminal amine of L27 | Thermus thermophilus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ribosomal protein L27 | - |
Thermus thermophilus |
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