Phosphatidylinositol-3-phosphatase
Appearance
phosphatidylinositol-3-phosphatase | |||||||||
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Identifiers | |||||||||
EC no. | 3.1.3.64 | ||||||||
CAS no. | 124248-47-1 | ||||||||
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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The enzyme phosphatidylinositol-3-phosphatase (EC 3.1.3.64) catalyzes the reaction
- 1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O 1-phosphatidyl-1D-myo-inositol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 1-phosphatidyl-1D-myo-inositol-3-phosphate 3-phosphohydrolase. Other names in common use include inositol-1,3-bisphosphate 3-phosphatase, inositol 1,3-bisphosphate phosphatase, inositol-polyphosphate 3-phosphatase, D-myo-inositol-1,3-bisphosphate 3-phosphohydrolase, and phosphatidyl-3-phosphate 3-phosphohydrolase. This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system.
Structural studies
[edit]As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1LW3 and 1M7R.
References
[edit]- Lips DL, Majerus PW (1989). "The discovery of a 3-phosphomonoesterase that hydrolyzes phosphatidylinositol 3-phosphate in NIH 3T3 cells". J. Biol. Chem. 264 (33): 19911–5. doi:10.1016/S0021-9258(19)47197-4. PMID 2555336.
- Caldwell KK, Lips DL, Bansal VS, Majerus PW (1991). "Isolation and characterization of two 3-phosphatases that hydrolyze both phosphatidylinositol 3-phosphate and inositol 1,3-bisphosphate". J. Biol. Chem. 266 (27): 18378–86. doi:10.1016/S0021-9258(18)55281-9. PMID 1655747.