EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.1.6.8 | glycoprotein |
- |
135554, 135666 |
| 3.1.6.8 | glycoprotein |
5-10% carbohydrate content |
135681 |
| 3.1.6.8 | glycoprotein |
A350G mutation results in a loss of a N-glycosylation site |
135691 |
| 3.1.6.8 | glycoprotein |
enzyme possess different number of glycans |
135511 |
| 3.1.6.8 | glycoprotein |
high-mannose-type oligosaccharide chains |
135692 |
| 3.1.6.8 | glycoprotein |
liver: 4.6% carbohydrate |
135684 |
| 3.1.6.8 | glycoprotein |
neuraminic acid residues involved in microheterogeneity |
135669 |
| 3.1.6.8 | glycoprotein |
testis: 20% neutral sugar, 0.8% N-acetylneuraminic acid |
135683 |
| 3.1.6.8 | glycoprotein |
the wild-type enzyme has three N-glycosylation sites. Only oligosaccharides at the first, Asn158, and the third, Asn350, glycosylation site are phosphorylated, whereas the second, Asn184 is not |
652443 |
| 3.1.6.8 | glycoprotein |
three N-glycosylation sites and three N-linked oligosaccharide side chains at asparagine residues 158, 184, and 350, the recombinantly expressed enzyme shows a high variability of the high-mannose-type N-glycans, which prevail at all glycosylation sites, depending on the culture conditions and the cell line expressing the enzyme, overview. The composition of the glycans is largely determined by substantial trimming in the medium, the susceptibility for trimming is different for the glycans at the three N-glycosylation sites, which of the glycans is most susceptible to trimming also depends on production conditions. Structure and ligand binding analysis, overview |
708615 |
