Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
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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In enzymology, a phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase (EC 3.1.3.67) is an enzyme that catalyzes the chemical reaction
- phosphatidylinositol 3,4,5-trisphosphate + H2O phosphatidylinositol 4,5-bisphosphate + phosphate
Thus, the two substrates of this enzyme are phosphatidylinositol 3,4,5-trisphosphate and H2O, whereas its two products are phosphatidylinositol 4,5-bisphosphate and phosphate.
This enzyme class belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is 1-phosphatidyl-1D-myo-inositol-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 class 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.
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