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4.F.1 The Choline/Ethanolaminephosphotransferase 1 (CEPT1) Family 

These phosphotransfer enzymes catalyze both phosphatidylcholine (PC) and phosphatidylethanolamine (PE) biosynthesis from CDP-choline and CDP-ethanolamine, respectively, plus diglycerides, in a process coupled to transmembrane phospholipid transport to distribute phosphatidyl choline to the lumenal surface of the endoplasmic reticulum (Henneberry et al. 2000).

The human CEPT1 uses diradylglycerols (diacylglycerols) as substrates, and the fatty acyl specificities of CEPT1 for these molecules in a mixed micellar assay have been studied (Wright and McMaster 2002). CEPT1 displayed an apparent Km of 36 microM for CDP-choline and 4.2 mol% for di-18:1 DAG with a Vmax of 14.3 nmol/min/mg. When CDP-ethanolamine was used as substrate, the apparent Km was 98 microM for CDP-ethanolamine and 4.3 mol% for di-18:1 DAG with a Vmax of 8.2 nmol/min/mg. The preferred diradylglycerol substrates used by CEPT1 with CDP-choline as the phosphobase donor were di-18:1 DAG, di-16:1 DAG, and 16:0/18:1 DAG.  When CDP-ethanolamine was used as the phosphobase donor, 16:0/18:1 DAG, di-18:1 DAG, and di-16:1 DAG were the preferred substrates. The mixed micelle assay allowed the lipid activation of CEPT to be measured, and both the cholinephosphotransferase and ethanolaminephosphotransferase activities displayed the unusual property of product activation. The protein kinase C inhibitor chelerythrine and the human DAG kinase inhibitor R59949 both inhibited CEPT1 activity with IC50 values of 40 microM (Wright and McMaster 2002).

References associated with 4.F.1 family:

Chauhan, N., L. Farine, K. Pandey, A.K. Menon, and P. B├╝tikofer. (2016). Lipid topogenesis - 35years on. Biochim. Biophys. Acta. [Epub: Ahead of Print] 26946259
Dewey, R.E., R.F. Wilson, W.P. Novitzky, and J.H. Goode. (1994). The AAPT1 gene of soybean complements a cholinephosphotransferase-deficient mutant of yeast. Plant Cell 6: 1495-1507. 7994181
Henneberry, A.L., G. Wistow, and C.R. McMaster. (2000). Cloning, genomic organization, and characterization of a human cholinephosphotransferase. J. Biol. Chem. 275: 29808-29815. 10893425
Parsons, W.H., M.J. Kolar, S.S. Kamat, A.B. Iii, J.J. Hulce, E. Saez, B.B. Kahn, A. Saghatelian, and B.F. Cravatt. (2016). AIG1 and ADTRP are atypical integral membrane hydrolases that degrade bioactive FAHFAs. Nat Chem Biol 12: 367-372. 27018888
Sciara, G., O.B. Clarke, D. Tomasek, B. Kloss, S. Tabuso, R. Byfield, R. Cohn, S. Banerjee, K.R. Rajashankar, V. Slavkovic, J.H. Graziano, L. Shapiro, and F. Mancia. (2014). Structural basis for catalysis in a CDP-alcohol phosphotransferase. Nat Commun 5: 4068. 24923293
Wright, M.M. and C.R. McMaster. (2002). PC and PE synthesis: mixed micellar analysis of the cholinephosphotransferase and ethanolaminephosphotransferase activities of human choline/ethanolamine phosphotransferase 1 (CEPT1). Lipids 37: 663-672. 12216837