| phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.3.67 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase (EC 3.1.3.67) catalyzes the chemical reaction
- 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O = 1-phosphatidyl-1D-myoinositol 4,5-bisphosphate + phosphate
This enzyme class belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 1-phosphatidyl-D-myoinositol-3,4,5-trisphosphate 3-phosphohydrolase. Other names in common use include PTEN, MMAC1, and phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase. PTEN also refers to a member of the class, phosphatase and tensin homolog. This enzyme participates in 10 metabolic pathways: inositol phosphate metabolism, phosphatidylinositol signaling system, p53 signaling pathway, focal adhesion, tight junction, endometrial cancer, glioma, prostate cancer, melanoma, and small cell lung cancer. It employs one cofactor, magnesium.
References
- Kabuyama Y, Nakatsu N, Homma Y, Fukui Y (1996). "Purification and characterization of the phosphatidylinositol-3,4,5-trisphosphate phosphatase in bovine thymus". Eur. J. Biochem. 238 (2): 350–6. doi:10.1111/j.1432-1033.1996.0350z.x. PMID 8681945.
- Maehama T, Dixon JE (1998). "The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate". J. Biol. Chem. 273 (22): 13375–8. doi:10.1074/jbc.273.22.13375. PMID 9593664.