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- W2037063485 abstract "N-Oligosaccharyltransferase catalyzes the N-glycosylation of asparagine residues of nascent polypeptide chains in the endoplasmic reticulum, a pathway highly conserved in all eukaryotes. An enzymatically active complex was isolated from microsomal membranes from Saccharomyces cerevisiae, which is composed of four proteins: Wbplp and Swplp (previously found to be encoded by two essential genes necessary for N-glycosylation in vivo and in vitro) and two additional proteins with a molecular mass of 60/62 kDa and 34 kDa. The 60/62 component represents differentially glycosylated forms of a protein that has sequence homology to ribophorin I. Wbplp and Swplp reveal homology to mammalian OST 48 and ribophorin II, respectively. Ribophorin I and II and OST 48 were recently shown to be constituents of the mammalian transferase from dog pancreas. The data reveal a high conservation of the organization of this enzyme activity." @default.
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- W2037063485 date "1994-05-09" @default.
- W2037063485 modified "2023-10-14" @default.
- W2037063485 title "The<i>N</i>-oligosaccharyltransferase complex from yeast" @default.
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- W2037063485 doi "https://doi.org/10.1016/0014-5793(94)00356-4" @default.
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