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Literature summary for 3.1.26.5 extracted from

  • Brown, J.W.; Haas, E.S.; Pace, N.R.
    Characterization of ribonuclease P RNAs from thermophilic bacteria (1993), Nucleic Acids Res., 21, 671-679.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.5

Cloned(Commentary)

Cloned (Comment) Organism
-
 Thermus aquaticus
-
 Thermotoga neapolitana
-
 Thermotoga maritima
-
 Deinococcus radiodurans

Organism

Organism UniProt Comment Textmining
Deinococcus radiodurans
-
-
-
Escherichia coli
-
-
-
Thermotoga maritima
-
-
-
Thermotoga neapolitana
-
-
-
Thermus aquaticus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pre-tRNA precursor + H2O
-
 Thermus aquaticus tRNA + 5'-oligoribonucleotide
-
 ?
pre-tRNA precursor + H2O
-
 Escherichia coli tRNA + 5'-oligoribonucleotide
-
 ?
pre-tRNA precursor + H2O
-
 Thermotoga neapolitana tRNA + 5'-oligoribonucleotide
-
 ?
pre-tRNA precursor + H2O
-
 Thermotoga maritima tRNA + 5'-oligoribonucleotide
-
 ?
pre-tRNA precursor + H2O
-
 Deinococcus radiodurans tRNA + 5'-oligoribonucleotide
-
 ?

Subunits

Subunits Comment Organism
More active holoenzymes can be reconstituted from the Thermotoga aquaticus and the Thermotoga maritima RNAs and the protein component of RNase P from Escherichia coli Thermus aquaticus
More active holoenzymes can be reconstituted from the Thermotoga aquaticus and the Thermotoga maritima RNAs and the protein component of RNase P from Escherichia coli Escherichia coli
More active holoenzymes can be reconstituted from the Thermotoga aquaticus and the Thermotoga maritima RNAs and the protein component of RNase P from Escherichia coli Thermotoga maritima

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 3 M NH4Cl Thermus aquaticus
60
-
 3 M NH4Cl Escherichia coli
60
-
 3 M NH4Cl Thermotoga neapolitana
60
-
 3 M NH4Cl Thermotoga maritima
60
-
 3 M NH4Cl Deinococcus radiodurans