Literature summary for 2.7.7.8 extracted from

Yehudai-Resheff, S.; Portnoy, V.; Yogev, S.; Adir, N.; Schuster, G.
Domain analysis of the chloroplast polynucleotide phosphorylase reveals discrete functions in RNA degradation, polyadenylation, and sequence homology with exosome proteins (2003), Plant Cell, 15, 2003-2019.

Search for more literature for 2.7.7.8

Cloned(Commentary)

Cloned (Comment)	Organism
expression of PNPase lacking the chloroplast transit peptide and several deletion proteins in Escherichia coli	Spinacia oleracea

Localization

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

Organism

Organism	UniProt	Comment	Textmining
Spinacia oleracea	Q41370	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant PNPase, nitrilotriacetic acid agarose, Mono Q	Spinacia oleracea

Reaction

Reaction	Comment	Organism	Reaction ID
RNAn+1 + phosphate = RNAn + a nucleoside diphosphate	analysis of the different PNPase domains for polymerization, degradation, and RNA binding properties	Spinacia oleracea	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
RNAn + a nucleoside diphosphate	-	Spinacia oleracea	RNAn+1 + phosphate	-	r

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Release 2023.1 (January 2023)