Phosphatase (null)

Phosphatases are a broad class of enzymes that catalyze the hydrolytic removal of phosphate groups from a variety of molecules, including proteins, nucleotides, lipids, and carbohydrates. They play critical roles in cellular regulation by reversing the actions of kinases and controlling signal transduction pathways, metabolism, cell cycle, apoptosis, and other physiological processes. Protein phosphatases, in particular, are divided into major subclasses such as serine/threonine phosphatases, tyrosine phosphatases, and dual specificity phosphatases, each recognizing different phosphorylated amino acid substrates. Because of their wide distribution and substrate specificity, phosphatases are essential for modulating cell function, but the use of "phosphatase" as a drug target is generally too broad, as therapeutics are developed against specific phosphatase subtypes (e.g., calcineurin, PP1, PTP1B) rather than the general class

Other names

Phosphatasesprotein phosphatasePPprotein tyrosine phosphatase (PTP)serine/threonine phosphataseacid phosphatasealkaline phosphatasedual specificity phosphataselipid phosphatasenucleotidasecarbohydrate phosphatase

Inhibition of dephosphorylation of target proteins (e.g., phosphatase inhibitors block removal of phosphate groups, sustaining phosphorylation-dependent signaling) Activation or inhibition of metabolic or signaling pathways through modulation of protein phosphorylation status