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Cloning of human choline ethanolaminephospho transferases synthesis of phosphatidyl choline phosphatidyle thanolamine and platelet activating factor
Cloning of human choline ethanolaminephospho transferases synthesis of phosphatidyl choline phosphatidyle thanolamine and platelet activating factor
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机译:人胆碱乙醇胺磷酸转移酶的克隆磷脂酰胆碱磷脂酰三醇胺的合成及血小板活化因子
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摘要
We report the first cloning and expression, from a mammalian source, of proteins capable of catalyzing choline- and ethanolaminephosphotransferase reactions (hCEPT1 and hCEPT2). Both coding regions predict highly hydrophobic proteins of 43-46.5 kDa with several predicted membrane spanning domains. A CDP-alcohol phosphotransferase motif, DG(x)2AR(x)8G(x)3D(x)3D, has been identified in both hCEPT1 and hCEPT2 choline- and ethanolamine-phosphotransferases (and several other lipid synthesizing enzymes that catalyze the formation of a phosphoester bond by the displacement of CMP from a CDP-alcohol by a second alcohol). Site-directed mutagenesis was used to differentiate the residues responsible for choline- versus ethanolamine-phosphotransferase activity. Mutation of glycine 156 of hCEPT1 abolished ethanolaminephosphotransferase activity, while cholinephosphotransferase activity remained intact.
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