Polynucleotide phosphorylase from Synechocystis sp.

2.7.7.8 ( BRENDA | IUBMB )

MFCD00131992

NA.54

Polynuclotide phosphorlyase in spinach chloroplasts acts as a exonuclease and a poly(A) polymerase.

Polynucleotide phosphorylase has been used in a study to discover that a major function of PNPase is the synthesis of CDP. It has also been used in a study to investigate the enzyme responsible for RNA 3′-tail synthesis in S. coelicolor.

Polynucleotide phosphorylase localizes to the intermembrane space of mitochondria and has a critical function in regulating mitochondrial homeostasis in human cells.
Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3′ to 5′ exoribonuclease activity and a 3′-terminal oligonucleotide polymerase activity.

Supplied as a solution in 20 mM Hepes buffer pH 7.9, 0.1 mM EDTA, 2 mM DTT, 12.5 mM MgCl₂, 60 mM KCl, 20% (w/v) Glycerol
One unit will polymerize 1.0 μmole of ADP, releasing 1.0 μmole of inorganic phosphate in 15 minutes, at pH 9.1 at 37 ℃.

200

expressed in E. coli

Histidine tagged

solution

≥500 units/mg protein

85 kDa

dry ice

−70℃

12 - Non Combustible Liquids

WGK 1