1-phosphatidylinositol-4-phosphate 5-kinase

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

1-phosphatidylinositol-4-phosphate 5-kinase
Identifiers
EC no.2.7.1.68
CAS no.104645-76-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate

Thus, the two substrates of this enzyme are ATP and 1-phosphatidyl-1D-myo-inositol 4-phosphate, whereas its two products are ADP and 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

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

References

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  • Kai M, Salway JG, Hawthorne JN (1968). "The diphosphoinositide kinase of rat brain". Biochem. J. 106 (4): 791–801. doi:10.1042/bj1060791. PMC 1198582. PMID 4295336.
  • Kai M, Salway JG, Michell RH, Hawthorne JN (1966). "The biosynthesis of triphosphoinositide by rat brain in vitro". Biochem. Biophys. Res. Commun. 22 (4): 370–375. doi:10.1016/0006-291X(66)90655-3.
  • Rameh LE, Tolias KF, Duckworth BC, Cantley LC (1997). "A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate". Nature. 390 (6656): 192–6. Bibcode:1997Natur.390..192R. doi:10.1038/36621. PMID 9367159. S2CID 4403301.