Cloning of human choline/ethanolaminephosphotransferases;...

Details Cloning of human choline/ethanolaminephosphotransferases;... Cloning of human choline/ethanolaminephosphotransferases;...

C - Chemistry, Metallurgy

12

N

C12N 15/54 (2006.01) A23L 1/30 (2006.01) C07F 9/10 (2006.01) C07K 16/40 (2006.01) C12N 9/12 (2006.01) C12N 15/11 (2006.01) C12P 7/64 (2006.01) C12Q 1/68 (2006.01) G01N 33/50 (2006.01) G01N 33/53 (2006.01)

Patent

CA 2330733

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.

Il est rendu compte, dans cette invention, du premier clonage et de l'expression, à partir d'un mammifère source, de protéines capables de catalyser des réactions de la cholinephosphotransférase et de l'éthanolaminephosphotransférase (hCEPT1 et hCEPT2). Les deux régions codantes permettent de prévoir des protéines hautement hydrophobes de 43 à 46,5 kDa ayant plusieurs domaines prévus de recouvrement membranaire. Un motif CDP-alcool phosphotransférase DG(x)2AR(x)8G(x)3D(x)3D a été identifié dans les hCEPT1 et hCEPT2, cholinephosphotransférase et éthanolaminephospho-transférase, (ainsi que dans plusieurs autres enzymes synthétisant des lipides, lesquelles enzymes catalysent la formation de liaison phospho-ester par le déplacement de la CMP depuis un CDP-alcool par un second alcool). Il a été utilisé une mutagenèse dirigée sur un site pour différencier les restes responsables d'une activité cholinephosphotransférase contre éthanolaminephosphotransférase. La mutation de la glycine 156 de hCEPT1 a supprimé l'activité de l'éthanolaminephosphotransférase alors que celle de la cholinephosphotransférase se maintenait intacte.

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