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