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Literature summary for 3.1.26.5 extracted from

  • Christian, E.L.; Kaye, N.M.; Harris, M.E.
    Evidence for a polynuclear metal ion binding site in the catalytic domain of ribonuclease P RNA (2002), EMBO J., 21, 2253-2262.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.5

Protein Variants

Protein Variants Comment Organism
additional information the use of Ca2+ as catalytic metal ion is enhanced in nucleotide point mutants C70U and U69 deletion in the P4 helix Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
phosphorothionate modifies nucleotides A67Rp and A67Sp, no remaining activity with Mg2+, complete rescue of activity with 5 mM Mn2+ for A67Rp, partially 65fold for A67Sp Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ coordination to nucleotide A67 of the enzymes RNA Escherichia coli
Mn2+ rescues A67Rp- and A67Sp-phosphorothionate modified inactive enzyme at 5 mM completely and partially, respectively Escherichia coli
additional information at least 2 metal ions per enzyme molecule, one catalytically and one structurally important, interactions of divalent metal cations at the pro-Rp and ProSp non-bridging phosphate oxygens with nucleotide A67 in the universally conserved helix p4 are essential for the folding and function of the enzymes' catalytic RNA component, interaction kinetics Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, secondary structural features, e.g. helix P4, sequence J5/15 or J18/2 in the RNA portion of the enzyme, are important for catalysis Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
tRNA precursor + H2O cleavage of 5'-terminal oligonucleotide Escherichia coli mature tRNA + 5'-oligonucleotide generates 5'-phosphate,3'-hydroxyl-product ?

Subunits

Subunits Comment Organism
More enzyme folding and function are dependent on divalent metal cations, clustered interactions, e.g. with the helix P4 of the enzymes' RNA part, secondary structure of the RNA moiety, overview Escherichia coli

Synonyms

Synonyms Comment Organism
RNase P RNA
-
 Escherichia coli
tRNA processing enzyme
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 assay at Escherichia coli