Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of several enzyme mutants with deleted stem loops in their RNA part. The mutants show reduced activity | Pyrococcus horikoshii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of deletion mutants | Pyrococcus horikoshii | |
0.00000009 | - |
pre-tRNATyr | wild-type enzyme, pH not specified in the publication, 65°C | Pyrococcus horikoshii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Pyrococcus horikoshii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | - |
- |
- |
Pyrococcus horikoshii OT-3 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pre-tRNATyr + H2O | activity assay using in vitro reconstituted particles | Pyrococcus horikoshii | tRNATyr + 5' leader of tRNA | - |
? | |
pre-tRNATyr + H2O | activity assay using in vitro reconstituted particles | Pyrococcus horikoshii OT-3 | tRNATyr + 5' leader of tRNA | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PhoPRNA | - |
Pyrococcus horikoshii |
RNase P RNA | - |
Pyrococcus horikoshii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
the deletion mutants show a slightly reduced optimal temperature compared to the wild-type enzyme | Pyrococcus horikoshii |
65 | 70 | wild-type enzyme | Pyrococcus horikoshii |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.009 | - |
pre-tRNATyr | wild-type enzyme, pH not specified in the publication, 65°C | Pyrococcus horikoshii |
General Information | Comment | Organism |
---|---|---|
physiological function | the stem loops of the RNase P RNA are required as binding sites for the proteins, their interactions are predominantly involved in stabilizing the active conformation of the enzyme | Pyrococcus horikoshii |