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・ 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
・ Phosphatosaurus
・ Phosphatrioxa-adamantane
・ Phosphaturic mesenchymal tumor
・ Phosphazene
・ Phosphene
・ Phosphene Dream
・ Phosphichthys
・ Phosphide
・ Phosphila


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Phosphatidylinositol-4-phosphate 3-kinase : ウィキペディア英語版
Phosphatidylinositol-4-phosphate 3-kinase

In enzymology, a phosphatidylinositol-4-phosphate 3-kinase () is an enzyme that catalyzes the chemical reaction
:ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate \rightleftharpoons ADP + 1-phosphatidyl-1D-myo-inositol 3,4-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 3,4-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 3-phosphotransferase. Other names in common use include type II phosphoinositide 3-kinase, C2-domain-containing phosphoinositide 3-kinase, and phosphoinositide 3-kinase. This enzyme participates in phosphatidylinositol signaling system.
==Structural studies==

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .

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