3.1.26.5: ribonuclease P
This is an abbreviated version!
For detailed information about ribonuclease P, go to the full flat file.
Word Map on EC 3.1.26.5
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3.1.26.5
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ribonucleoproteins
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pre-trnas
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endoribonuclease
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endonucleolytic
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eculizumab
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aminoacylation
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rna-based
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stem-loops
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phosphodiester
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nucleolar
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nocturnal
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eubacterial
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paroxysmal
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gene-targeting
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anticodon
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base-pairing
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rna-protein
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sars-cov-2
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c5a
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horikoshii
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hemoglobinuria
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trna-like
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pyrococcus
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swab
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3'-terminal
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5\'-leader
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riboswitches
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trnatyr
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2'-hydroxyls
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trnahis
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trailer
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cloverleaf
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rna-rna
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self-splicing
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protein-rna
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tmrna
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micrococcal
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self-cleaving
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t-loops
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p-mediated
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complement-mediated
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ncrnas
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pseudoknots
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watson-crick
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eukaryal
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oligoribonucleotides
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analysis
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pharmacology
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snornps
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synthesis
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medicine
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biotechnology
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trnase
- 3.1.26.5
- ribonucleoproteins
- pre-trnas
-
endoribonuclease
-
endonucleolytic
- eculizumab
- aminoacylation
-
rna-based
-
stem-loops
-
phosphodiester
-
nucleolar
-
nocturnal
-
eubacterial
-
paroxysmal
-
gene-targeting
-
anticodon
-
base-pairing
-
rna-protein
- sars-cov-2
- c5a
- horikoshii
- hemoglobinuria
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trna-like
- pyrococcus
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swab
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3'-terminal
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5\'-leader
- riboswitches
- trnatyr
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2'-hydroxyls
- trnahis
- trailer
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cloverleaf
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rna-rna
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self-splicing
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protein-rna
- tmrna
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micrococcal
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self-cleaving
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t-loops
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p-mediated
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complement-mediated
- ncrnas
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pseudoknots
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watson-crick
-
eukaryal
- oligoribonucleotides
- analysis
- pharmacology
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snornps
- synthesis
- medicine
- biotechnology
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trnase
Reaction
endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor =
Synonyms
Aq_880, aRpp29, aRpp29 protein, AtPop1p, AtPRORP1, AtPRORP2, AtPRORP3, C5 protein, CrPRORP, hPOP1, hPOP4, hPOP7, M1 RNA, M1GS, M1GS RNA, mitochondrial RNase P protein 1, MRPP1, MRPP2, MRPP3, nuclear ribonclease P ribonucleoprotein, nuclease, ribo-, P, Pfu Pop5, PhoPRNA, POP1, Pop1p, Pop5, Pop6, Pop7, PRORP, PRORP1, PRORP2, PRORP3, Protein C5, protein-only ribonuclease P, protein-only RNase P, protein-only RNase P enzyme, proteinaceous RNase P, ribonuclease MRP, ribonuclease P, ribonuclease P ribozyme, ribosomal RNA processing ribonucleoprotein, Ribunuclease P, RNA processing protein POP1, RNA processing protein POP5, RNA processing protein POP6, RNA processing protein POP7, RNA processing protein POP8, RNase MRP, RNase P, RNase P holoenzyme, RNase P protein, RNase P ribozyme, RNase P RNA, RNase P/MRP, RNase P/MRP protein, RNaseP protein, RNaseP protein p20, RNaseP protein p30, RNaseP protein p38, RNaseP protein p40, RNases P, RNP, Rpm2p, RPP, RPP14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, RPP40, RPR, RPR1, transfer RNA 5' maturation enzyme, transfer RNA processing enzyme, tRNA processing enzyme, tRNA-processing endonuclease, tRNA-processing enzyme
ECTree
3.1.26.5 ribonuclease PAdvanced search results
results (
results (KM Value
KM Value on EC 3.1.26.5 - ribonuclease P
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.000244
SupS1 precursor
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in 50 mM Tris /HCl pH 7.5, 100 mM NH4Cl, 5 mM MgCl2, 2.5 mM EGTA and 0.5 U Rnasin
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0.00006
pre-tRNA-Tyr
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pre-tRNA-Tyr without the 3'-UUUUU trailer, at 25°C, pH 8.0, in 10 mM HEPES buffer with 10 mM MgCl2 and 100 mM KCl
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0.0001
pre-tRNA-Tyr
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pre-tRNA-Tyr with the 3'-UUUUU trailer, at 25°C, pH 8.0, in 10 mM HEPES buffer with 10 mM MgCl2 and 100 mM KCl
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0.00000009
pre-tRNATyr
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wild-type enzyme, pH not specified in the publication, 65°C
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0.000044
pre-tRNATyr
37°C, pH 7.5, in the presence of L7Ae
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0.0026
pre-tRNATyr
37°C, pH 7.5, in the absence of L7Ae
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0.00018
ptRNATyr
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from Escherichia coli, enzyme subunit RNase P RNA + Pop5 + RNase P protein 30 + RNase P protein 21 + RNase P protein 29
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0.00653
ptRNATyr
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enzyme subunit RNase P RNA + RNase P protein 21 + RNase P protein 29
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0.0116
ptRNATyr
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from Escherichia coli, emzyme subunit RNase P RNA + Pop5 + RNase P protein 30
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0.00002
tRNA precursor
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derived from the sup S1 and sup3-e tRNASer genes of Schizosaccharomyces pombe
0.0000345
tRNA precursor
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pH 8.0, 65°C, in presence of 800 mM ammonium acetate and 5 mM MgCl2
0.0000684
tRNA precursor
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pH 8.0, 50°C, in presence of 50 mM ammonium acetate and 30 mM MgCl2
0.000012
tRNAPhe (G+1) precursor
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37°C, substrate substituted with phosphothionate from GMPaS
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additional information
additional information
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both pre-steady state and steady state kinetics
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additional information
additional information
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kinetics, the rate constant for the scissile bond cleavage is pH-dependent
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additional information
additional information
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pre-steady state kinetics, nuclear enzyme form
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additional information
additional information
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KM-values for pre-tRNATyr, mutant enzymes
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additional information
additional information
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kinetics of deletion mutants
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additional information
additional information
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the RNR motif enhances the affinity of RNase P for pre-tRNA
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additional information
additional information
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dissociation of the tRNA product from the catalytic RNA usually limits the rate of the RNA-alone reaction under multiple-turnover conditions, single-turnover conditions allow to analyze steps preceding product release
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additional information
additional information
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dissociation of the tRNA product from the catalytic RNA usually limits the rate of the RNA-alone reaction under multiple-turnover conditions, single-turnover conditions allow to analyze steps preceding product release
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additional information
additional information
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dissociation of the tRNA product from the catalytic RNA usually limits the rate of the RNA-alone reaction under multiple-turnover conditions, single-turnover conditions allow to analyze steps preceding product release, pseudo-first-order rate constants of cleavage are calculated by nonlinear regression analysis
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additional information
additional information
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kinetics and kinetic mechanism of reaction and enzyme stablization with metal ions, overview
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additional information
additional information
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kinetics of wild-type and mutant enzymes, affinity of PRNA for P protein, and of RNase P for pre-tRNAAsp substrate, overview. Apparent pKa and pH-independent single-turnover rate constants for wild-type enzyme and mutants R60A and R62A in Mg(II)
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additional information
additional information
Michaelis-Menten single-turnover reaction kinetics of wild-type and mutant enzymes, overview
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additional information
additional information
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Michaelis-Menten single-turnover reaction kinetics of wild-type and mutant enzymes, overview
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additional information
additional information
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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
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