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Literature summary for 3.1.26.5 extracted from

  • Yandek, L.E.; Lin, H.C.; Harris, M.E.
    Alternative substrate kinetics of Escherichia coli ribonuclease P: determination of relative rate constants by internal competition (2013), J. Biol. Chem., 288, 8342-8354.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten steady-state reaction kinetics of two tRNA precursors showing fast substrate cleavage relative to dissociation, and competitive substrate kinetics of the enzyme, overview. Reactions containing two or more ptRNAs follow simple competitive alternative substrate kinetics in which the relative rates of processing are determined by ptRNA concentration and their V/K. Rates of ptRNA processing by RNase P are tuned for uniform specificity and consequently optimal coupling to precursor biosynthesis. Multiple turnover reactions and competitive multiple turnover reactions, detailed overview Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the enzyme processes the 5' ends of tRNA precursors, the substrate population includes over 80 different competing ptRNAs in Escherichia coli, sequence and secondary structure of representative ptRNAs, overview. Its mode of molecular recognition differs from other catalytic RNAs in two important ways. First, its biological role in ptRNA processing requires that it act in trans as a multiple turnover enzyme, whereas other ribozymes, with the exceptions of the ribosome and spliceosome, undergo single turnover self-splicing or self-cleavage reactions. Second, RNase P processes multiple RNA substrates, including all ptRNAs in the cell, whereas other ribozymes, again with the exceptions of the ribosome and spliceosome, have one specific substrate ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
ribonucleoprotein the enzyme is a ribonlucleoprotein, the RNAsubunit, termed P RNA, contains the active site, whereas the smaller protein subunit is required for optimal molecular recognition and catalysis in vitro and is essential in vivo Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme processes the 5' ends of tRNA precursors, the substrate population includes over 80 different competing ptRNAs in Escherichia coli, sequence and secondary structure of representative ptRNAs, overview. Its mode of molecular recognition differs from other catalytic RNAs in two important ways. First, its biological role in ptRNA processing requires that it act in trans as a multiple turnover enzyme, whereas other ribozymes, with the exceptions of the ribosome and spliceosome, undergo single turnover self-splicing or self-cleavage reactions. Second, RNase P processes multiple RNA substrates, including all ptRNAs in the cell, whereas other ribozymes, again with the exceptions of the ribosome and spliceosome, have one specific substrate Escherichia coli ?
-
?
additional information the ptRNA substrates are 5'-end-labeled with [gamma-32P]ATP and T4 polynucleotide kinase, after dephosphorylation by alkaline phosphatase, in reaction with RNase P holoenzyme Escherichia coli ? formation of products from two substrates independently in the same reaction, ptRNAfMet47 and ptRNAMet82 are modified for eparation by PAGE by the addition of two extra G nucleotides to the 5' end of the leader sequence, giving rise to ptRNAfMet47(+2) and ptRNAMet82(+2) ?

Subunits

Subunits Comment Organism
More the enzyme is a ribonlucleoprotein, the RNAsubunit, termed P RNA, contains the active site, whereas the smaller protein subunit, i.e. C5 protein, is required for optimal molecular recognition and catalysis in vitro and is essential in vivo Escherichia coli

Synonyms

Synonyms Comment Organism
RNase P
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Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Escherichia coli

General Information

General Information Comment Organism
additional information the enzyme is a ribonlucleoprotein, the RNAsubunit, termed P RNA, contains the active site, whereas the smaller protein subunit is required for optimal molecular recognition and catalysis in vitro and is essential in vivo Escherichia coli
physiological function the enzyme is an essential ribonucleoprotein enzyme that is responsible for catalyzing the maturation of the 5' end of transfer RNAs through site-specific hydrolysis of a phosphodiester bond in precursor tRNAs. The single enzyme processes the 5' ends of tRNA precursors in cells and organelles that carry out tRNA biosynthesis. Rates of ptRNA processing by RNase P are tuned for uniform specificity and consequently optimal coupling to precursor biosynthesis Escherichia coli