Phosphatase

In biochemistry, a phosphatase is an enzyme that uses water to cleave a phosphoric acid monoester into a phosphate ion and an alcohol.

Together, kinases and phosphatases direct a form of post-translational modification that is essential to the cell's regulatory network.

The net result of the reaction is the destruction of a phosphomonoester and the creation of both a phosphate ion and a molecule with a free hydroxyl group.

[6] Studies reveal that so called "docking interactions" play a significant role in substrate binding.

In contrast to kinases, phosphatase enzymes recognize and catalyze a wider array of substrates and reactions.

[4] To some extent, this disparity results from incomplete knowledge of the human phosphatome, that is, the complete set of phosphatases expressed in a cell, tissue, or organism.

The tandem work of kinases and phosphatases constitute a significant element of the cell's regulatory network.

PP2B, also called calcineurin, is involved in the proliferation of T cells; because of this, it is the target of some drugs that seek to suppress the immune system.

[12] Nucleotidases are essential for cellular homeostasis, because they are partially responsible for maintaining a balanced ratio of nucleotides to nucleosides.

A ball and stick model of a phosphate anion.
The general reaction catalyzed by a phosphatase enzyme
Calcineurin (PP2B) is a protein phosphatase enzyme involved in immune system function.
Nucleosides and nucleotides differ by one phosphate, which is cleaved from nucleotides by nucleotidases.