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Literature summary for 2.7.7.8 extracted from

  • Raj, R.; Mitra, S.; Gopal, B.
    Characterization of Staphylococcus epidermidis polynucleotide phosphorylase and its interactions with ribonucleases RNase J1 and RNase J2 (2018), Biochem. Biophys. Res. Commun., 495, 2078-2084 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structure reveals a bound phosphate in the PH2 domain of each protomer coordinated by three adjacent serine residues. Phosphate coordination by these serine residues is essential to maintain the catalytic center in an active conformation Staphylococcus epidermidis

Protein Variants

Protein Variants Comment Organism
S441A catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure Staphylococcus epidermidis
S442A catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure Staphylococcus epidermidis
S443A catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure Staphylococcus epidermidis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
poly(A)n Km value 21.95 microg/ml, phosphorolysis reaction, pH 8.2, 37°C Staphylococcus epidermidis
0.0536
-
ADP polyadenylation reaction, pH 7.5, 26°C Staphylococcus epidermidis

Organism

Organism UniProt Comment Textmining
Staphylococcus epidermidis Q8CST1
-
-
Staphylococcus epidermidis ATCC 12228 Q8CST1
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein structure reveals a bound phosphate in the PH2 domain of each protomer coordinated by three adjacent serine residues Staphylococcus epidermidis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
poly(A)(n-1) + ADP
-
Staphylococcus epidermidis poly(A)n + phosphate
-
r
poly(A)(n-1) + ADP
-
Staphylococcus epidermidis ATCC 12228 poly(A)n + phosphate
-
r
poly(A)n + phosphate
-
Staphylococcus epidermidis poly(A)(n-1) + ADP
-
r
poly(A)n + phosphate
-
Staphylococcus epidermidis ATCC 12228 poly(A)(n-1) + ADP
-
r

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.22
-
ADP polyadenylation reaction, pH 7.5, 26°C Staphylococcus epidermidis
15.88
-
poly(A)n phosphorolysis reaction, pH 8.2, 37°C Staphylococcus epidermidis

General Information

General Information Comment Organism
physiological function PNPase forms a complex with RNase J1 and RNase J2 without substantially altering either exo-ribonuclease or polyadenylation activity of the enzyme Staphylococcus epidermidis