EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.1.6.12 | glycoprotein |
fucosylated complex, reaction with lectins |
135561 |
| 3.1.6.12 | 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 |
| 3.1.6.12 | more |
conversion of an active-site cysteine into a formylglycine |
663938 |
| 3.1.6.12 | phosphoprotein |
compared to degree of mannose-phosphorylation of the wild-type enzyme the mutant enzyme K457R has 33%, mutant enzyme K457S has 50%, mutant enzyme K457G has 31% mutant enzyme K433A has 95%, mutant enzyme K367A has 106% and mutant enzyme K393A has 123% of mannose-phosphorylation |
652443 |
| 3.1.6.12 | proteolytic modification |
33% of the intracellular Y210C mutant enzyme remains as a precursor form, for at least 8 h post labeling and is not processed to the mature lysosomal form. A significant amount of the mutant enzyme escapes the endoplasmic reticulum and is either secreted from the expression cells or undergoes delayed intracellular traffic. 67% of the intracellular Y210C mutant enzyme is processed to the mature form by a proteolytic processing step known to occur in lysosomes |
654646 |
