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Literature summary for 3.1.26.5 extracted from

  • Sinapah, S.; Wu, S.; Chen, Y.; Pettersson, B.M.; Gopalan, V.; Kirsebom, L.A.
    Cleavage of model substrates by archaeal RNase P: role of protein cofactors in cleavage-site selection (2011), Nucleic Acids Res., 39, 1105-1116.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.5

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
RNase P
-
 Pyrococcus furiosus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Pyrococcus furiosus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1
-
 assay at Pyrococcus furiosus

General Information

General Information Comment Organism
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