1-phosphatidylinositol-4-phosphate 5-kinase

{{infobox enzyme

| Name = 1-phosphatidylinositol-4-phosphate 5-kinase

| EC_number = 2.7.1.68

| CAS_number = 104645-76-3

| GO_code = 0016308

| image =

| width =

| caption =

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In enzymology, 1-phosphatidylinositol-4-phosphate 5-kinase ({{EC number|2.7.1.68}}) is an enzyme that catalyzes the chemical reaction

:ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate $\rightleftharpoons$ ADP + 1-phosphatidyl-1D-myo-inositol 4,5-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-4-phosphate 5-phosphotransferase. Other names in common use include diphosphoinositide kinase, PIP kinase, phosphatidylinositol 4-phosphate kinase, phosphatidylinositol-4-phosphate 5-kinase, and type I PIP kinase. This enzyme participates in 3 metabolic pathways: inositol phosphate metabolism, phosphatidylinositol signaling system, and regulation of the actin cytoskeleton.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1BO1}} and {{PDB link|2GK9}}.

{{cite journal |vauthors=Kai M, Salway JG, Hawthorne JN | date = 1968 | title = The diphosphoinositide kinase of rat brain | journal = Biochem. J. | volume = 106 | pages = 791–801 | pmid = 4295336 | issue = 4 | doi = 10.1042/bj1060791 | pmc = 1198582 }}
{{cite journal |vauthors=Kai M, Salway JG, Michell RH, Hawthorne JN | date = 1966 | title = The biosynthesis of triphosphoinositide by rat brain in vitro | journal = Biochem. Biophys. Res. Commun. | volume = 22 | pages = 370–375 | doi = 10.1016/0006-291X(66)90655-3 | issue = 4 }}
{{cite journal |vauthors=Rameh LE, Tolias KF, Duckworth BC, Cantley LC | date = 1997 | title = A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate | journal = Nature | volume = 390 | pages = 192–6 | pmid = 9367159 | doi = 10.1038/36621 | issue = 6656 | bibcode = 1997Natur.390..192R | s2cid = 4403301 }}