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Literature summary for 2.7.7.8 extracted from

  • Baginsky, S.; Shteiman-Kotler, A.; Liveanu, V.; Yehudai-Resheff, S.; Bellaoui, M.; Settlage, R.E.; Shabanowitz, J.; Hunt, D.F.; Schuster, G.; Gruissem, W.
    Chloroplast PNPase exists as a homo-multimer enzyme complex that is distinct from the Escherichia coli degradosome (2001), RNA, 7, 1464-1475.
    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 maximal activation of recombinant PNPase RNA-derading activity at 20 mM Spinacia oleracea

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Spinacia oleracea

Localization

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 PNPase, the endoribonuclease RNase E, a DEAD-RNA helicase and the glycolytic enzyme enolase are associated with a high molecular weight complex, the degradosome Escherichia coli
580000 600000 native and recombinant PNPase form a homo-multimer complex, gel filtration Spinacia oleracea

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
poly(G) + GDP GDP second best substrate Spinacia oleracea poly(G)+1 + phosphate
-
 ?