EC Number   |
Posttranslational Modification |
Reference |
|---|
    3.6.1.1 | phosphoprotein |
phosphorylation of the Family I PPase from the flowering plant, Papaver rhoeas, suppresses PPase activity and is a key event in preventing self-fertilization |
756721 |
| 3.6.1.1 | phosphoprotein |
the canonical Family II PPase of Streptococcus agalactiae is reversibly phosphorylated by endogenous Stk1/Stp1 protein kinase/phosphatase producing effects on cell behavior |
756721 |
| 3.6.1.1 | phosphoprotein |
the enzyme is inhibited by in vitro phosphorylation, self-incompatibility induces Ca21-dependent phosphorylation of p26.1 |
689148 |
| 3.6.1.1 | phosphoprotein |
the enzyme is probably phosphorylated at Ser150 and Ser296 near the active site, and at Ser194 and Ser195 near the hinge region |
684143 |
| 3.6.1.1 | phosphoprotein |
the enzyme shares the catalytic mechanism of the HAD superfamily including a phosphorylated enzyme intermediate |
-, 718979 |
| 3.6.1.1 | proteolytic modification |
PPase2 contains a mitochondrial import siganl sequence |
668747 |
| 3.6.1.1 | proteolytic modification |
the chloroplast isozyme I contains a precursor sequence, the recombinant enzyme is processed in bacterial cells |
667527 |
| 3.6.1.1 | proteolytic modification |
the N-terminal peptide is autocatalytically cleaved |
756011 |
| 3.6.1.1 | proteolytic modification |
the N-terminal peptide is autocatalytically cleaved, presence of three N-terminal variants, truncated at Leu23, Ser25 and Leu26. The growth of AtPPA1 crystal iis strongly correlated with the progression of proteolysis |
756011 |
