Protein Ser/Thr Phosphatases

Protein Ser/Thr phosphatases are a group of enzymes that catalyze the removal of phosphate groups from serine and/or threonine residues by the hydrolysis of phosphoric acid monoesters. They directly oppose the actions of kinases and phosphorylases and therefore play an integral role in many signal transduction pathways.

There are two groups of serine/threonine phosphatases: phosphoprotein phosphatases (e.g. PP1, calcineurin), which are sensitive to okadaic acid; and metallo-phosphatases (e.g. PP2C), which require a divalent cation, commonly Mg²⁺, for catalytic activity. Dephosphorylation, depending on the residue that the phosphate group is removed from, can have a stimulatory or inhibitory effect on the target molecule. This makes protein Ser/Thr phosphatases essential for many signal transduction pathways, including histone dephosphorylation during epigenetic modification. Protein Ser/Thr phosphatase are regulated by their subcellular localization and by inhibitor proteins, which are subtype-specific.

External sources of pharmacological information for Protein Ser/Thr Phosphatases :

• BJP Guide

Protein Ser/Thr Phosphatase Gene Data