EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.2.1.76 | glycoprotein |
- |
171555, 171557, 171564 |
| 3.2.1.76 | glycoprotein |
contains glucosamine |
171554 |
| 3.2.1.76 | glycoprotein |
N-glycosylation at N110, N190, N336, N372, N415, and N451 in subunit A, and at N110, N190, N336, N372, N415, and N451 in subunit B, glycan structures, overview. The enzyme uses its own N-glycan as a substrate binding and catalytic module. The mannose residue of the N-glycan attached to N372 constitutes a part of the substrate-binding pocket and interacts directly with a substrate. The kinetics of native and deglycosylated hIDUA suggest that the N-glycan is also involved in catalytic processes. Deglycosylation of the enzyme with endoglycosidase H, but not peptide-N-glycosidase F, reduces the enzyme's activity. Concanavalin A pull-down assay shows that PNGase F-resistant N-glycans are essential for the enzyme activity |
732821 |
| 3.2.1.76 | glycoprotein |
N-glycosylation, deglycoslyation b peptide N-glycosidase F from Flavobacterium meningosepticum and neuraminidase from Clostridium perfringens. The N-glycan pools consists of oligomannosidic glycans (mainly Man7, Man8, Man9 as well as Man9 + Glc), complex type glycans with up to three antennae. Sialylation as well as fucosylation are observed on almost all complex type glycans |
732391 |
| 3.2.1.76 | glycoprotein |
oligomannose 7-bisphosphate is bound to the enzyme, with a much higher amount on the recombinant wild-type enzyme compared to the recombinant RAP fusion enzyme |
665552 |
| 3.2.1.76 | glycoprotein |
six potential N-glycosylation sites |
731075 |
| 3.2.1.76 | glycoprotein |
the enzyme has 6 N-glycosylation sites |
751839 |
| 3.2.1.76 | glycoprotein |
the enzyme is N-glycosylated. The carboxy-terminal endoplasmic reticulum-retention motif, SEKDEL, influences the N-linked glycosylation of the recombinant enzyme |
710326 |
| 3.2.1.76 | phosphoprotein |
phosphorylations on S59 and S482, phosphatase treatment |
732391 |
| 3.2.1.76 | proteolytic modification |
- |
171559, 171568, 171569 |
