phosphoprotein phosphatase

Human genes that encode proteins with phosphoprotein phosphatase activity include:

Phosphoprotein phosphatase is an enzyme that dephosphorylates certain phosphorylated proteins.

Phosphoprotein phosphatases are just enzymes.

Phosphoprotein phosphatase is activated by the hormone insulin, which indicates that there is a high concentration of glucose in the blood.

Phosphoprotein phosphatase 1 (PP1) belongs to a certain class of phosphatases known as protein serine/ threonine phosphatases.

As a phosphoprotein phosphatase, insulin dephosphorylates the enzyme, thus activating the PFK-2 and inhibiting the FBPase-2 activities.

Finally, after purifying the phosphorylated form of the enzyme, phosphorylase a, from rabbit liver, ion exchange chromatography was used to identify phosphoprotein phosphatase I and II.

These can be classed into groups: phosphoprotein phosphatases, metallo-dependent protein phosphatases, protein tyrosine phosphatases and NLI interacting factor-like phosphatases.

The opposite action of PDK, namely the dephosphorylation and activation of pyruvate dehydrogenase, is catalyzed by a phosphoprotein phosphatase called pyruvate dehydrogenase phosphatase.