ExplorEnz: EC 2.7.8.48

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2.7.8.48

Accepted name:

ceramide phosphoethanolamine synthase

Reaction:

(1) CDP-ethanolamine + a ceramide = a ceramide phosphorylethanolamine + CMP
(2) a phosphatidylethanolamine + a ceramide = a ceramide phosphorylethanolamine + a 1,2-diacyl-sn-glycerol

Other name(s):

CPE synthase; Cpes (gene name); SGMS1 (gene name); SGMS2 (gene name); SAMD8 (gene name)

Systematic name:

CDP-ethanolamine:ceramide phosphoethanolaminyltransferase

Comments:

The enzyme from invertebrates, best studied from the fly Drosophila melanogaster, is common in arthropods, worms, bees, spiders, and scorpions, and has also been reported in deep-sea mussels and some sea snails, as well as protozoans and oomycetes. Its product, ceramide phosphoethanolamine, is the main sphingolipid in cell membranes of arthropods, such as Drosophila and Musca. The invertebrate enzyme requires a Mn(II) cofactor. In mammals the activity has been shown to be catalysed by members of the EC 2.7.8.27, sphingomyelin synthase, family, such as SGMS1, SGMS2, and SAMD8.

Links to other databases:

BRENDA, EXPASY, GENE, KEGG, MetaCyc

References:

1.	Vacaru, A.M., Tafesse, F.G., Ternes, P., Kondylis, V., Hermansson, M., Brouwers, J.F., Somerharju, P., Rabouille, C. and Holthuis, J.C. Sphingomyelin synthase-related protein SMSr controls ceramide homeostasis in the ER. J. Cell Biol. 185 (2009) 1013–1027. [DOI] [PMID: 19506037]
2.	Ternes, P., Brouwers, J.F., van den Dikkenberg, J. and Holthuis, J.C. Sphingomyelin synthase SMS2 displays dual activity as ceramide phosphoethanolamine synthase. J. Lipid Res. 50 (2009) 2270–2277. [DOI] [PMID: 19454763]
3.	Vacaru, A.M., van den Dikkenberg, J., Ternes, P. and Holthuis, J.C. Ceramide phosphoethanolamine biosynthesis in Drosophila is mediated by a unique ethanolamine phosphotransferase in the Golgi lumen. J. Biol. Chem. 288 (2013) 11520–11530. [DOI] [PMID: 23449981]
4.	Kol, M., Panatala, R., Nordmann, M., Swart, L., van Suijlekom, L., Cabukusta, B., Hilderink, A., Grabietz, T., Mina, J.GM., Somerharju, P., Korneev, S., Tafesse, F.G. and Holthuis, J.CM. Switching head group selectivity in mammalian sphingolipid biosynthesis by active-site-engineering of sphingomyelin synthases. J. Lipid Res. 58 (2017) 962–973. [DOI] [PMID: 28336574]
5.	Suzuki, R., Murakami, C., Dilimulati, K., Atsuta-Tsunoda, K., Kawai, T. and Sakane, F. Human sphingomyelin synthase 1 generates diacylglycerol in the presence and absence of ceramide via multiple enzymatic activities. FEBS Lett. 597 (2023) 2672–2686. [DOI] [PMID: 37715942]

[EC 2.7.8.48 created 2022, modified 2025]