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Literature summary for 3.1.26.12 extracted from

  • Jiang, X.; Belasco, J.G.
    Catalytic activation of multimeric RNase E and RNase G by 5'-monophosphorylated RNA (2004), Proc. Natl. Acad. Sci. USA, 101, 9211-9216.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information 5' monphosphorylation of RNA substrates increases the enzyme activity Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
expression of N-terminal enzyme half, comprising residues 1-499, as C-terminally His6- and Myc-tagged or maltose-binding protein-fused protein in strain BL21(DE3) Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of the reaction with 5' monophosphorylated RNA substrates Escherichia coli
0.00023
-
5' monophosphorylated fluorogenic oligonucleotide pH 7.5, 25°C, recombinant N-terminal domain Escherichia coli
0.00033
-
5' hydroxylated fluorogenic oligonucleotide pH 7.5, 25°C, recombinant N-terminal domain Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
NaCl stimulates at 20 mM Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally His6- and Myc-tagged N-terminal enzyme half and maltose-binding protein-fused N-terminal half from strain BL21(DE3) by affinity chromatography on a metal chelating resin and an amylose resin, respectively Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
development of a highly sensitive quantitative assay method using fluorescent 5' monophosphorylated RNA substrates Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5'-hydroxylated fluorogenic oligonucleotide + H2O
-
Escherichia coli ?
-
?
5'-monophosphorylated fluorogenic oligonucleotide + H2O
-
Escherichia coli ?
-
?
fluorogenic oligonucleotides + H2O 5' monophosphorylated or 5' hydroxylated substrates, P-BR14-FD or OH-BR14-FD Escherichia coli ?
-
?
additional information RNase E shows preference for 5' monophosphorylated RNA substrates rather than RNA with a triphosphate or hydroxyl at the 5' end, the enzyme needs to be in a multimeric state for activation by 5' monophosphorylated RNA substrates Escherichia coli ?
-
?
RNA I.26 + H2O 5' mono- or triphosphorylated, or 5' hydroxylated substrate Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
More the enzyme needs to be in a multimeric state for activation by 5' monophosphorylated RNA substrates, possible multimerization mechanism dependent on 5' activation, overview Escherichia coli

Synonyms

Synonyms Comment Organism
RNase E
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.014
-
5' monophosphorylated fluorogenic oligonucleotide pH 7.5, 25°C, recombinant N-terminal domain Escherichia coli
0.015
-
5' hydroxylated fluorogenic oligonucleotide pH 7.5, 25°C, recombinant N-terminal domain Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli