| EC |
2.7.8.48 |
| Accepted name: |
ceramide phosphoethanolamine synthase |
| Reaction: |
CDP-ethanolamine + a ceramide = a ceramide phosphorylethanolamine + CMP |
| Other name(s): |
Cpes (gene name); CPE synthase |
| Systematic name: |
CDP-ethanolamine:ceramide phosphoethanolaminyltransferase |
| Comments: |
The enzyme, studied from the fly Drosophila melanogaster, has homologues among the invertebrates, but not in other animal phyla. Its product, ceramide phosphoethanolamine, is synthesized as the main sphingolipid in cell membranes of arthropods, such as Drosophila and Musca, and is common in worms, bees, spiders, and scorpions. It has also been reported in deep-sea mussels and some sea snails, as well as protozoans and oomycetes. The enzyme requires a Mn(II) cofactor. |
| Links to other databases: |
BRENDA, EXPASY, 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. |
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] |
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| [EC 2.7.8.48 created 2022] |
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