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Literature summary for 2.7.7.8 extracted from

  • Lisitsky, I.; Schuster, G.
    Preferential degradation of polyadenylated and polyuridinylated RNAs by the bacterial exoribonuclease polynucleotide phosphorylase (1999), Eur. J. Biochem., 261, 468-474.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
diphosphate activation of PNPase RNA synthesis activity at very low concentrations of phosphate Escherichia coli
phosphate 1-10 mM, strong activation of PNPase exonuclease activity Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
86000
-
3 * 86000, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
RNAn+1 + phosphate PNPase prefers degradation of polyadenylated and polyuridinylated RNAs due to the high binding affinities for poly(A) and poly(U), no activity with polyguanylated RNA Escherichia coli RNAn + a nucleoside diphosphate
-
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Subunits

Subunits Comment Organism
trimer 3 * 86000, SDS-PAGE Escherichia coli