Structural highlights
Function
CEPT1_HUMAN Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP-ethanolamine, respectively (PubMed:10191259, PubMed:10893425, PubMed:12216837, PubMed:37137909). Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface (PubMed:10191259, PubMed:10893425, PubMed:12216837). Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity (PubMed:10191259, PubMed:12216837).[1] [2] [3] [4]
References
- ↑ Henneberry AL, McMaster CR. Cloning and expression of a human choline/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidylethanolamine. Biochem J. 1999 Apr 15;339 ( Pt 2)(Pt 2):291-8 PMID:10191259
- ↑ Henneberry AL, Wistow G, McMaster CR. Cloning, genomic organization, and characterization of a human cholinephosphotransferase. J Biol Chem. 2000 Sep 22;275(38):29808-15. PMID:10893425 doi:10.1074/jbc.M005786200
- ↑ Wright MM, McMaster CR. PC and PE synthesis: mixed micellar analysis of the cholinephosphotransferase and ethanolaminephosphotransferase activities of human choline/ethanolamine phosphotransferase 1 (CEPT1). Lipids. 2002 Jul;37(7):663-72. PMID:12216837 doi:10.1007/s11745-002-0947-6
- ↑ Wang Z, Yang M, Yang Y, He Y, Qian H. Structural basis for catalysis of human choline/ethanolamine phosphotransferase 1. Nat Commun. 2023 May 3;14(1):2529. PMID:37137909 doi:10.1038/s41467-023-38290-2
