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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
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 | 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 | 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 | Comment | Organism |
---|---|---|
RNase P | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Escherichia coli |
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 |