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Structure, biosynthesis, and function of asparagine‐linked glycans on plant glycoproteins
Author(s) -
Faye Loïc,
Johnson Kenneth D.,
Sturm Arnd,
Chrispeels Maarten J.
Publication year - 1989
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1989.tb06187.x
Subject(s) - asparagine , golgi apparatus , glycan , endoplasmic reticulum , glycoprotein , biochemistry , vacuole , mannose , residue (chemistry) , biosynthesis , biology , membrane glycoproteins , glycosylation , yeast , microbiology and biotechnology , chemistry , amino acid , gene , cytoplasm
In plants, glycoproteins with asparagine‐linked glycans (oligosaccharides) are found in vacuoles, in the extracellular space or matrix, and associated with the endo‐membrane system (endoplasmic reticulum, Golgi apparatus, plasma membrane, tonoplast). These glycans are of the high‐mannose type, with a structure identical to that found in other organisms (mammals, yeast), or of the complex type with a β1–2 linked xylosyl residue not found in mammalian complex glycans. Asparagine‐linked glycans play multiple roles by modifying the physicochemical properties of the polypeptides to which they are attached.