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Literature summary extracted from
- Cleavage of model substrates by archaeal RNase P: role of protein cofactors in cleavage-site selection (2011), Nucleic Acids Res., 39, 1105-1116.
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.26.5 | Mg2+ | required | Pyrococcus furiosus |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.26.5 | Pyrococcus furiosus | - |
- |
- |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.26.5 | More | archaeal RNase P comprises a catalytic RNase P RNA, RPR, and at least four protein cofactors, RPPs, which function as two binary complexes, POP5/RPP30 and RPP21/RPP29 | Pyrococcus furiosus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.26.5 | RNase P | - |
Pyrococcus furiosus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.26.5 | 37 | - |
assay at | Pyrococcus furiosus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.26.5 | 6.1 | - |
assay at | Pyrococcus furiosus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.26.5 | physiological function | RNase P is a catalytic ribonucleoprotein primarily involved in tRNA biogenesis. Insights into the role of protein cofactors RPPs in substrate recognition and cleavage-site selection. Cleavage of various model hairpin loop substrates in the presence of archaeal RPPs | Pyrococcus furiosus |
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Release 2023.1 (January 2023)
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