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Literature summary 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

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

Cloned(Commentary)

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

Inhibitors

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.26.11 Cd2+ with 0.2 mM, at 37°C, pH 7.4, 28% relative activity when compared to Co2+ Escherichia coli
3.1.26.11 Co2+ 100% relative activity at 0.2 mM Escherichia coli
3.1.26.11 Cu2+ with 0.2 mM, at 37°C, pH 7.4, 8% relative activity when compared to Co2+ Escherichia coli
3.1.26.11 Fe2+ with 0.2 mM, at 37°C, pH 7.4, 34% relative activity when compared to Co2+ Escherichia coli
3.1.26.11 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
3.1.26.11 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
3.1.26.11 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

EC Number Organism UniProt Comment Textmining
3.1.26.11 Escherichia coli
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.26.11 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
-
 ?
3.1.26.11 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

EC Number Synonyms Comment Organism
3.1.26.11 3'-tRNase
-
 Escherichia coli
3.1.26.11 Elac
-
 Escherichia coli
3.1.26.11 RNase BN RNase Z homologue Escherichia coli
3.1.26.11 RNase Z
-
 Escherichia coli