The enzyme phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase (EC 3.1.3.67) catalyzes the chemical reaction
phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase | |||||||||
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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 | ||||||||
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- 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,[citation needed] MMAC1, and phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase. PTEN also refers to a member of the class, phosphatase and tensin homolog.[citation needed] 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
edit- 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.