EC Number |
General Information |
Reference |
---|
2.4.99.18 | physiological function |
N-linked glycosylation of nascent polypeptides in the lumen of the endoplasmic reticulum |
707520 |
2.4.99.18 | physiological function |
O-glycosylation of type IV pilins in bacteria |
708997 |
2.4.99.18 | physiological function |
oligosaccharyltransferase (OST) catalyzes the transfer of a high-mannose glycan onto secretory proteins in the endoplasmic reticulum. Mammals express two distinct oligosaccharyltransferase complexes that act in a cotranslational (OST-A) or posttranslocational (OST-B) manner. The distinct functions of the two human complexes are based on structural differences of their catalytic subunits STT3A and STT3B, which result in interactions with distinct subunits and different affinities for acceptor peptides |
760197 |
2.4.99.18 | physiological function |
oligosaccharyltransferase transfers glycan to asparagine in the N-glycosylation sequon, the lysine and isoleucine residues in the DK/MI motif participate in the Ser/Thr recognition in the sequon |
-, 718929 |
2.4.99.18 | physiological function |
subunits Ost3p and Ost6p are necessary for efficient glycosylation of distinct defined glycosylation sites |
709952 |
2.4.99.18 | physiological function |
TbSTT3A and TbSTT3B N-glycosylation together is essential for infectivity in mice |
708330 |
2.4.99.18 | physiological function |
the catalytic subunit of the eukaryotic OST and catalyzes the transfer of a highly defined, lipid-linked oligosaccharide (LLO) donor substrate to a multitude of peptide acceptor sequences located in different substrate proteins |
720164 |
2.4.99.18 | physiological function |
the catalytic subunit of the eukaryotic OST and catalyzes the transfer of a highly defined, lipid-linked oligosaccharide (LLO) donor substrate to a multitude of peptide acceptor sequences located in different substrate proteins. The Stt3 subunit of OST harbors the catalytic center of the enzyme, and some components of the OST complex are involved in the recognition and utilization of glycosylation sites in specific glycoproteins. The oxidoreductase activity of subunits N33/Tusc3 and IAP is required for glycosylation of a subset of proteins essential for brain development |
720164 |