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- W2110991863 abstract "2-Palmitoylation of the inositol residue occurs during biosynthesis of glycosylphosphatidylinositol (GPI) anchors, but the enzymology of this step has been enigmatic. With endogenously synthesized glucosamine-PI (GlcN-PI; a GPI intermediate), a CoA-dependent palmitoyl-CoA-independent acyltransfer activity (AT-1) has been reported in rodent preparations. In contrast, a palmitoyl-CoA-dependent GlcN-PI acyltransferase activity (AT-2) was reported in both rodent and yeast preparations with a novel water-soluble dioctanoyl GlcN-PI analogue, GlcN-PI(C8). We report that AT-1, as well as AT-2, can be detected in rodent microsomes with GlcN-PI(C8), thus demonstrating the coexistence of these activities in a single membrane preparation and the general utility of GlcN-PI(C8) for studying the GPI pathway. Unexpectedly, AT-2 was peripherally associated with microsomes, a property atypical for GPI biosynthetic enzymes." @default.
- W2110991863 created "2016-06-24" @default.
- W2110991863 creator A5023906955 @default.
- W2110991863 creator A5055538365 @default.
- W2110991863 date "2000-01-01" @default.
- W2110991863 modified "2023-09-24" @default.
- W2110991863 title "A Water-Soluble Analogue of Glucosaminylphosphatidylinositol Distinguishes Two Activities That Palmitoylate Inositol on GPI Anchors" @default.
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- W2110991863 doi "https://doi.org/10.1006/bbrc.1999.1900" @default.
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