The presence of dolichol in a lipid diphosphate N-acetylglucosamine from Saccharomyces cerevisiae (baker's yeast).
The lipid moiety of a lipid diphosphate N-acetylglucosamine, an intermediate in glycosylation of proteins, was studied. Ozonolysis of the compound gave evidence for an alpha-saturated isoprene unit. Alkaline hydrolysis of the glycolipid, followed by high-pressure liquid chromatography, showed the presence of a series of polyprenol homologues identical with those isolated directly from Saccharomyces cerevisiae (baker's yeast). No particular homologue was preferred in the enzymic transfer of N-acetylglucosamine 1-phosphate to endogenous dolichol monophosphate.
D000117:Acetylglucosamine / Q000031:analogs & derivatives / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D002855:Chromatography, Thin Layer; D004224:Diterpenes / Q000032:analysis*; D004286:Dolichols / Q000032:analysis*; D006868:Hydrolysis; D011103:Polyisoprenyl Phosphate Monosaccharides / Q000032:analysis*; D011105:Polyisoprenyl Phosphate Sugars / Q000032:analysis*; D012441:Saccharomyces cerevisiae / Q000032:analysis*
D004224:Diterpenes; D004286:Dolichols; D011103:Polyisoprenyl Phosphate Monosaccharides; D011105:Polyisoprenyl Phosphate Sugars; D000117:Acetylglucosamine