Title
A water-soluble analogue of glucosaminylphosphatidylinositol distinguishes two activities that palmitoylate inositol on GPI anchors
Document Type
Article
Publication Date
1-7-2000
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. (C) 200 Academic Press.
Publication Source (Journal or Book title)
Biochemical and Biophysical Research Communications
First Page
296
Last Page
299
Recommended Citation
Doerrler, W., & Lehrman, M. (2000). A water-soluble analogue of glucosaminylphosphatidylinositol distinguishes two activities that palmitoylate inositol on GPI anchors. Biochemical and Biophysical Research Communications, 267 (1), 296-299. https://doi.org/10.1006/bbrc.1999.1900