EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.1.6.1 | glycoprotein |
- |
135522, 135525 |
| 3.1.6.1 | glycoprotein |
ASG is a glycoprotein that binds specifically to mannose 6-phosphate receptors, the activity of arylsulfatase G depends on the Cys84 residue that is predicted to be posttranslationally converted to the critical active site Calpha-formylglycine |
693036 |
| 3.1.6.1 | glycoprotein |
contains complex N-linked oligosaccharides |
135517 |
| 3.1.6.1 | glycoprotein |
lowering pH and increasing glycosylation reduces the flexibility of the enzyme. At acidic pH, the glycosylated enzyme presents a higher secondary conformational stability when compared to its nonglycosylated counterpart |
730069 |
| 3.1.6.1 | glycoprotein |
when expressed in human cells, isoform ArsK is detected as a 68-kDa glycoprotein carrying at least four N-glycans of both the complex and high-mannose type. Protein carries mannose 6-phosphate, indicating lysosomal sorting |
730022 |
| 3.1.6.1 | more |
presence of a disulfide bridge between the processed 18-kDa fragment and another smaller polypeptide, probably involving residue Cys195 of the 10-kDa chain |
730056 |
| 3.1.6.1 | no modification |
not a glycoprotein |
135522 |
| 3.1.6.1 | proteolytic modification |
63-kDa single-chain precursor protein localizes to pre-lysosomal compartments and tightly associates with organelle membranes. Proteolytically processed arylsulfatase G fragments of 34-, 18-, and 10-kDa are found in lysosomal fractions and lost their membrane association. Proteases participating in the processing are cathepsins B and L. Proteolytic processing is dispensable for hydrolytic sulfatase activity in vitro |
730056 |
| 3.1.6.1 | proteolytic modification |
the enzyme is synthesized as a higher molecular mass precursor |
135517 |
| 3.1.6.1 | side-chain modification |
formylglycine is generated by posttranslational modification of a conserved cysteine residue. Cysteine is also converted to formylglycine when the gene is expressed in Escherichia coli. Substituting the relevant cysteine by a serine codon in the gene of Pseudomonas aeruginosa leads to expression of inactive sulfatase protein, lacking the formylglycine. The machinery catalyzing the modification of the Pseudomonas sulfatase in E. coli therefore accepts cysteine but not serine as a modification substrate |
662100 |
