| protein-serine/threonine phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Protein serine/threonine phosphatase dodecamer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 3.1.3.16 | ||||||||
| CAS no. | 9025-75-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDBPDBePDBsum | ||||||||
| |||||||||
The enzymeprotein serine/threonine phosphatase (EC 3.1.3.16; systematic nameprotein-serine/threonine-phosphate phosphohydrolase)[1] is a form ofphosphoprotein phosphatase that acts upon phosphorylated serine/threonine residues:
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate
Serine andthreonine phosphates are stable under physiological conditions, so a phosphatase enzyme has to remove the phosphate to reverse the regulation signal. Ser/Thr-specific protein phosphatases are regulated partly by their location within thecell and by specificinhibitor proteins.
Serine and threonine are amino acids which have similar side-chain compositions that contain a hydroxyl group and thus can be phosphorylated by enzymes calledserine/threonine protein kinases. The addition of the phosphate group can be reversed by enzymes called serine/threonine phosphatases. The addition and removal of phosphate groups regulates many cellular pathways involved in cell proliferation, programmed cell death (apoptosis), embryonic development, and cell differentiation.
There are several known groups with numerous members in each:
(links are to the catalytic subunit)
