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1-phosphatidylinositol-3-phosphate 5-kinase

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1-phosphatidylinositol-3-phosphate 5-kinase
Identifiers
EC no.2.7.1.150
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

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

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  • 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. doi:10.1016/S0960-9822(07)00513-1. PMID 9811604.