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Literature summary for 3.1.26.11 extracted from

  • Dutta, T.; Deutscher, M.P.
    Catalytic properties of RNase BN/RNase Z from Escherichia coli: RNase BN is both an exo- and endoribonuclease (2009), J. Biol. Chem., 284, 15425-15431.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
EDTA with 0.2 mM, at 37°C, pH 7.4, 11% relative activity when compared to Co2+ Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
Escherichia coli strain BL21I-II-(DE3)/pLys carrying the pET-ElaC(His) plasmid Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information RNase BN is strongly inhibited by the presence of a 3'-CCA sequence or a 3'-phosphoryl group Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Cd2+ with 0.2 mM, at 37°C, pH 7.4, 28% relative activity when compared to Co2+ Escherichia coli
Co2+ 100% relative activity at 0.2 mM Escherichia coli
Cu2+ with 0.2 mM, at 37°C, pH 7.4, 8% relative activity when compared to Co2+ Escherichia coli
Fe2+ with 0.2 mM, at 37°C, pH 7.4, 34% relative activity when compared to Co2+ Escherichia coli
Mg2+ with 0.2 mM, at 37°C, pH 7.4, 54% relative activity when compared to Co2+. When the existing metal ion of the apoenzyme is removed with EDTA, with 0.2 mM, at 37°C, pH 7.4, 15% relative activity when compared to Co2+ after 60 min of incubation Escherichia coli
Mn2+ with 0.2 mM, at 37°C, pH 7.4, 95% relative activity when compared to Co2+. When the existing metal ion of the apoenzyme is removed with EDTA, with 0.2 mM, at 37°C, pH 7.4, 23% relative activity when compared to Co2+ after 60 min of incubation Escherichia coli
Zn2+ with 0.2 mM, at 37°C, pH 7.4, 28% relative activity when compared to Co2+. When the existing metal ion of the apoenzyme is removed with EDTA, with 0.2 mM, at 37°C, pH 7.4, 26% relative activity when compared to Co2+ after 60 min of incubation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by centrifugation, on nickel column and by ultrafiltration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
bis(p-nitrophenyl)phosphate + H2O displays efficient phosphodiesterase activity against bis(p-nitrophenyl) phosphate, which is unusual among the RNase Z family of enzymes Escherichia coli p-nitrophenol + p-nitrophenyl phosphate
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?
additional information RNase BN is active on both double- and single-stranded RNA but duplex RNA is preferred. Displays a profound base specificity, showing no activity on runs of C residues. Digestion by RNase BN leads to 3-mers as the limit products, but the rate slows on molecules shorter than 10 nucleotides in length. RNase BN acts as a distributive exoribonuclease on some substrates, releasing mononucleotides and a ladder of digestion products. RNase BN also cleaves endonucleolytically, releasing 3' fragments as short as 4 nucleotides Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
3'-tRNase
-
Escherichia coli
Elac
-
Escherichia coli
RNase BN RNase Z homologue Escherichia coli
RNase Z
-
Escherichia coli