1-phosphatidylinositol-3-phosphate 5-kinase

1-phosphatidylinositol-3-phosphate 5-kinase
Identifiers
EC no.	2.7.1.150
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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a 1-phosphatidylinositol-3-phosphate 5-kinase (EC 2.7.1.150) is an enzyme that catalyzes the chemical reaction

ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate ⇌ ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate

Thus, the two substrates of this enzyme are ATP and 1-phosphatidyl-1D-myo-inositol 3-phosphate, whereas its two products are ADP and 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1-phosphatidyl-1D-myo-inositol-3-phosphate 5-phosphotransferase. Other names in common use include type III PIP kinase, and phosphatidylinositol 3-phosphate 5-kinase. This enzyme participates in phosphatidylinositol signaling system and regulation of actin cytoskeleton.

References

• Cooke FT, Dove SK, McEwen RK, Painter G, Holmes AB, Hall MN, Michell RH, Parker PJ (November 1998). "The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae". Current Biology. 8 (22): 1219–22. Bibcode:1998CBio....8.1219C. doi: 10.1016/S0960-9822(07)00513-1 . PMID   9811604.