Abstract
Background: Many invertebrates contain ceramide phosphoethanolamine (CPE) rather than sphingomyelin as key membrane component. Results: Insect-specific CPE synthase belongs to a novel branch of CDP-alcohol phosphotransferases with unique membrane topology. Conclusion: CPE production is catalyzed by a CDP-ethanolamine:ceramide ethanolamine phosphotransferase in the Golgi lumen. Significance: Identification of CPE synthase provides a novel opportunity to elucidate the biological role of an enigmatic but widespread sphingolipid. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
| Original language | English |
|---|---|
| Pages (from-to) | 11520-11530 |
| Number of pages | 11 |
| Journal | Journal of Biological Chemistry |
| Volume | 288 |
| Issue number | 16 |
| DOIs | |
| Publication status | Published - 19 Apr 2013 |
Keywords
- ceramide
- ceramide ethanolamine phosphotransferase
- ceramide phosphoethanolamine
- ceramide phosphoethanolamine synthase
- cytidine diphosphate ethanolamine
- ethanolamine
- ethanolamine phosphotransferase
- phosphoethanolamine
- synthetase
- unclassified drug
- animal cell
- arthropod
- article
- biosynthesis
- Cnidaria
- controlled study
- Drosophila
- enzyme active site
- enzyme localization
- enzyme structure
- Golgi complex
- human
- human cell
- invertebrate
- marine species
- molecular cloning
- mollusc
- nonhuman
- priority journal
- protein function
- sequence homology