関: phosphatidylinositol 4-kinase、PI 4-kinase、PtdIns 4-kinase

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an enzyme that catalyzes the conversion of a proenzyme to an active enzyme
the basic unit of money in Papua New Guinea

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/08/13 17:31:40」(JST)

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In enzymology, a 1-phosphatidylinositol 4-kinase (EC 2.7.1.67) is an enzyme that catalyzes the chemical reaction

ATP + 1-phosphatidyl-1D-myo-inositol ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate

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

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-phosphotransferase. Other names in common use include phosphatidylinositol kinase (phosphorylating), phosphatidylinositol 4-kinase, phosphatidylinositol kinase, type II phosphatidylinositol kinase, PI kinase, and PI 4-kinase. This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system.

Structural studies

As of late 2007, the structure has only been solved for this enzyme. Part of the enyzme was crystallized with its activating partner frequenin.^[1]

References

^ Strahl T, Huttner IG, Lusin JD et al. (October 2007). "Structural insights into activation of phosphatidylinositol 4-kinase (Pik1) by yeast frequenin (Frq1)". J. Biol. Chem. 282 (42): 30949–59. doi:10.1074/jbc.M705499200. PMID 17720810.

Colodzin M, Kennedy EP (1965). "Biosynthesis of diphosphoinositide in brain". J. Biol. Chem. 240 (10): 3771–80. PMID 4284712.
Kai M, White GL, Hawthorne JN (1966). "The phosphatidylinositol kinase of rat brain". Biochem. J. 101 (2): 328–37. PMC 1270113. PMID 4290722.
Walker DH, Dougherty N, Pike LJ (1988). "Purification and characterization of a phosphatidylinositol kinase from A431 cells". Biochemistry. 27 (17): 6504–11. doi:10.1021/bi00417a046. PMID 2851325.
Whitman M, Downes CP, Keeler M, Keller T, Cantley L (1988). "Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate". Nature. 332 (6165): 644–6. doi:10.1038/332644a0. PMID 2833705.
Barylko B; Gerber, SH; Binns, DD; Grichine, N; Khvotchev, M; Südhof, TC; Albanesi, JP (2001). "A novel family of phosphatidylinositol 4-kinases conserved from yeast to humans". J. Biol. Chem. 276 (11): 7705–8. doi:10.1074/jbc.C000861200. PMID 11244087.

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English Journal

Sanguinarine suppresses IgE induced inflammatory responses through inhibition of type II PtdIns 4-kinase(s).

Bojjireddy N, Sinha RK, Panda D, Subrahmanyam G.SourceDepartment of Biosciences and Bioengineering, Wadhwani Research Centre, Indian Institute of Technology, Bombay, Powai, Mumbai 400076, India. naveenb@u.washington.edu
Archives of biochemistry and biophysics.Arch Biochem Biophys.2013 Sep 15;537(2):192-7. doi: 10.1016/j.abb.2013.07.017. Epub 2013 Jul 27.
The effects of sanguinarine on IgE mediated early signaling mechanisms leading to inflammatory mediators release were investigated. Pretreatment of RBL 2H3 cells with sanguinarine inhibited IgE induced activation of type II PtdIns 4-kinase activity. Concomitant with type II PtdIns 4-kinase inhibitio
PMID 23899475

Evolutionarily conserved structural changes in phosphatidylinositol 5-phosphate 4-kinase (PI5P4K) isoforms are responsible for differences in enzyme activity and localization.

Clarke JH, Irvine RF.SourceDepartment of Pharmacology, Tennis Court Road, Cambridge CB2 1PD, U.K. jhc30@cam.ac.uk
The Biochemical journal.Biochem J.2013 Aug 15;454(1):49-57. doi: 10.1042/BJ20130488.
Mammals have genes coding for three PI5P4Ks (PtdIns5P 4-kinases), and these have different cellular localizations, tissue distributions and lipid kinase activities. We describe in the present paper a detailed molecular exploration of human PI5P4Ks α, β and γ, as well as their fly and worm homolog
PMID 23758345

The lipid kinase phosphatidylinositol-4 kinase III alpha regulates the phosphorylation status of hepatitis C virus NS5A.

Reiss S, Harak C, Romero-Brey I, Radujkovic D, Klein R, Ruggieri A, Rebhan I, Bartenschlager R, Lohmann V.SourceDepartment of Infectious Diseases, Molecular Virology, University of Heidelberg, Heidelberg, Germany.
PLoS pathogens.PLoS Pathog.2013 May;9(5):e1003359. doi: 10.1371/journal.ppat.1003359. Epub 2013 May 9.
The lipid kinase phosphatidylinositol 4-kinase III alpha (PI4KIIIα) is an essential host factor of hepatitis C virus (HCV) replication. PI4KIIIα catalyzes the synthesis of phosphatidylinositol 4-phosphate (PI4P) accumulating in HCV replicating cells due to enzyme activation resulting from its inte
PMID 23675303

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★リンクテーブル★

リンク元	「PI 4-kinase」「PtdIns 4-kinase」「phosphatidylinositol 4-kinase」「1-ホスファチジルイノシトール-4-キナーゼ」
関連記事	「kinase」「phosphatidylinositol」

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1-phosphatidylinositol 4-kinase
Identifiers
EC number	2.7.1.67
CAS number	37205-54-2
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 / EGO
Search
PMC	articles
PubMed	articles
NCBI	proteins