EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.3.2.12 | linezolid | - |
Thermus thermophilus | |
2.3.2.12 | tiamulin | - |
Thermus thermophilus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.2.12 | Thermus thermophilus | - |
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EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.2.12 | 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 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.2.12 | ribosomal protein L27 | - |
Thermus thermophilus |