Phosphatidylinositol-3-phosphatase

In enzymology, a phosphatidylinositol-3-phosphatase (EC 3.1.3.64) is an enzyme that catalyzes the chemical reaction

1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O 1-phosphatidyl-1D-myo-inositol + phosphate
phosphatidylinositol-3-phosphatase
Identifiers
EC number3.1.3.64
CAS number124248-47-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Thus, the two substrates of this enzyme are 1-phosphatidyl-1D-myo-inositol 3-phosphate and H2O, whereas its two products are 1-phosphatidyl-1D-myo-inositol and phosphate.

This enzyme 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-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

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1LW3 and 1M7R.

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gollark: Hydronitrogen has loads of stuff *anyway*, I don't think we need to centralize power even more...
gollark: I added much of ale's insanity to potatOS.
gollark: Please DON'T send them to hydronitrogen.
gollark: You should use PotatOS Bin instead.

References

    • 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. 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. PMID 1655747.


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