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Literature summary for 2.7.7.8 extracted from

  • Yehudai-Resheff, S.; Hirsh, M.; Schuster, G.
    Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts (2001), Mol. Cell. Biol., 21, 5408-5416.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.8

Activating Compound

Activating Compound Comment Organism Structure
phosphate
-
 Escherichia coli
phosphate degradation activity of chloroplast PNPase is dramatically enhanced, polymerization activity in the absence of phosphate Spinacia oleracea

Inhibitors

Inhibitors Comment Organism Structure
phosphate inhibition of chloroplast PNPase polymerization activity Spinacia oleracea
Poly(G) inhibition of exoribonuclease activity due to its formation of a strong tertiary structure Spinacia oleracea

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
 Spinacia oleracea 9507
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
RNAn + a nucleoside diphosphate Escherichia coli
-
 RNAn+1 + phosphate
-
 r
RNAn + a nucleoside diphosphate Spinacia oleracea chloroplast PNPase is most probably responsible for polyadenylation of RNA RNAn+1 + phosphate
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Spinacia oleracea
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
poly(A) + ADP
-
 Escherichia coli poly(A)+1 + phosphate
-
 r
poly(A) + ADP chloroplast PNPase has both exonuclease and poly(A) polymerase activity, phosphate enhances RNA degradation activity, ADP inhibits degradation and enhances poly(A) polymerization, ADP best substrate Spinacia oleracea poly(A)+1 + phosphate
-
 r
poly(G) + GDP
-
 Escherichia coli poly(G)+1 + phosphate
-
 r
poly(G) + GDP
-
 Spinacia oleracea poly(G)+1 + phosphate
-
 r
RNA + ATP polymerization in the absence of phosphate Spinacia oleracea RNA+1 + diphosphate
-
 r
RNA + CTP polymerization in the absence of phosphate Spinacia oleracea RNA+1 + diphosphate
-
 r
RNA + GTP polymerization in the absence of phosphate Spinacia oleracea RNA+1 + diphosphate
-
 r
RNA + UTP polymerization in the absence of phosphate Spinacia oleracea RNA+1 + diphosphate
-
 r
RNAn + a nucleoside diphosphate
-
 Escherichia coli RNAn+1 + phosphate
-
 r
RNAn + a nucleoside diphosphate chloroplast PNPase is most probably responsible for polyadenylation of RNA Spinacia oleracea RNAn+1 + phosphate
-
 r