Cloning of human choline ethanolaminephospho transferases synthesis of phosphatidyl choline phosphatidyle thanolamine and platelet activating factor
US6451568B1 · kind B1 · utility
Assignee
Inventors
Key dates
| Filing date | Dec 8, 2000 |
| Grant date | Sep 17, 2002 |
| Priority date | — |
| Expiry date | Dec 8, 2020 |
Classification
- Technology area (CPC C)Chemistry; Metallurgy
- CPC primaryC12Q1/6883
- WIPO fieldBiotechnology
- WIPO sectorChemistry
Abstract
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.
Source: USPTO / EPO open patent data. Objective bibliographic and citation counts.