Asparagine-linked glycosylation is the most ubiquitous protein co-translational modification in the endoplasmic reticulum (ER).1 The enzyme that catalyzes this process is called oligosaccharyl transferase (OT). It catalyzes the transfer of an oligosaccharyl moiety (Glc3Man9GlcNAc2) from the dolichol-linked pyrophosphate donor to the side chain of Asn within a consensus sequence of Asn-X-Thr/Ser, where X can be any amino acid residue except for Pro (1–3). This modification serves as a primary determinant for specific molecular recognition as well as protein folding and stability (4, 5) and therefore is an essential and highly conserved protein modification pathway in eukaryotic cells.
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Yan et al. (2004) studied this question.
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