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• W2019959532 abstract "Dihydroceramide desaturase is responsible for the introduction of the 4,5-trans double bond into ceramide. Here, we describe the localization of this enzyme in the endoplasmic reticulum (ER) using ER- and Golgi-enriched fractions from rat liver. Furthermore, enzyme topology was studied. Mild proteolysis of ER-derived vesicles under conditions which assure membrane integrity (latency of mannose 6-phosphatase was at least 91%) resulted in an up to 90% inactivation of dihydroceramide desaturase activity. This indicates a cytosolic orientation of dihydroceramide desaturase activity in the ER membrane." @default.
• W2019959532 created "2016-06-24" @default.
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• W2019959532 date "1997-10-20" @default.
• W2019959532 modified "2023-10-15" @default.
• W2019959532 title "Conversion of dihydroceramide to ceramide occurs at the cytosolic face of the endoplasmic reticulum" @default.
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• W2019959532 doi "https://doi.org/10.1016/s0014-5793(97)01187-3" @default.
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