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・ Phosphonoacetaldehyde hydrolase
・ Phosphonoacetaldehyde reductase (NADH)
・ Phosphonoacetate hydrolase
・ Phosphonopyruvate decarboxylase
・ Phosphonopyruvate hydrolase
・ Phosphopantetheine
・ Phosphatidylinositol 4,5-bisphosphate
・ Phosphatidylinositol 4-phosphate
・ Phosphatidylinositol 5-phosphate
・ Phosphatidylinositol a-mannosyltransferase
・ Phosphatidylinositol bisphosphate
・ Phosphatidylinositol deacylase
・ Phosphatidylinositol diacylglycerol-lyase
・ Phosphatidylinositol N-acetylglucosaminyltransferase
・ Phosphatidylinositol phosphate
Phosphatidylinositol phosphate kinases
・ Phosphatidylinositol transfer protein
・ Phosphatidylinositol transfer protein, alpha
・ Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
・ Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase
・ Phosphatidylinositol-3,4-bisphosphate 4-phosphatase
・ Phosphatidylinositol-3-phosphatase
・ Phosphatidylinositol-4,5-bisphosphate 3-kinase
・ Phosphatidylinositol-4,5-bisphosphate 4-phosphatase
・ Phosphatidylinositol-4-phosphate 3-kinase
・ Phosphatidylmyo-inositol mannosides
・ Phosphatidylserine
・ Phosphatidylserine decarboxylase
・ Phosphatocopida
・ Phosphatodraco


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Phosphatidylinositol phosphate kinases : ウィキペディア英語版
Phosphatidylinositol phosphate kinases
Phosphatidylinositol phosphate kinases (PIPK) are kinases that phosphorylate the phosphoinositides PtdIns''P'' and PtdIns''P''2 that are derivatives of phosphatidylinositol (PtdIns). It has been found that PtdIns is only phosphorylated on three (3,4,5) of its five hydroxyl groups, possibly because D-2 and D-6 hydroxyl groups cannot be phosphorylated because of steric hindrance.〔Pettitt TR, Dove SK, Lubben A, Calaminus SDJ, Wakelam MJO. Analysis of intact phosphoinositides in biological samples. American Soc f Biochem and Mol Biol 2006; 47:1588-1596〕 All 7 combinations of phosphorylated PtdIns have been found in animals, all except PtdIns(3,4,5)''P''3 have been found in plants.〔Muller-Roeber B, Pical C. Inositol Phospholipid Metabolism in Arabidopsis. Characterized and Putative Isoforms of Inositol Phospholipid Kinase and Phosphoinositide-Specific Phospholipase C. Plant Physiol 2002 130:22–46〕
PIPKs are today divided into three groups, type I, II and III that share significant sequence homology but differ in the substrate specificities, subcellular localisations and functions.〔Anderson RA, Boronenkov IV, Doughman SD, Kunz J, Loijens JC . Phosphatidylinositol phosphate kinases, a multifaceted family of signalling enzymes. J Biol Chem 1999; 274:9907-9910〕
Type 1 are PIPKs that phosphorylate PtdIns4''P'' to PtdIns(4,5)''P''2 and are called PtdIns4''P'' 5-kinases because they phosphorylate on the D-5 hydroxyl group. Type II PIPKs phosphorylate PtdIns5''P'' at the D-4 site and are called PtdIns5''P'' 4-kinases. And finally PIPKs of type III are PtdIns3''P'' 5-kinases that phosphorylate PtdIns to PtdIns(3,5)''P''2, which prototype is Fab1 in yeast (see () for descriptive picture). The substrate specificity of type I and II depends on the so-called activation loop. The activation loop is a segment of 22 to 27 amino acid residues, located close to the C-terminal end of the catalytic domain in all PIPKs. When the activation loops of a type I and a type II PIPK were swapped, the chimera with type I backbone showed specificity for type II substrate, and vice versa for the other chimera.〔Kunz J, Wilson MP, Kisseleva M, Hurley JH, Majerus PW, Anderson RA. The activation loop of phosphatidylinositol phosphate kinases determines signaling specificity. Mol Cell 2000 5:1-11〕
==References==


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