EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.22.15 | glycoprotein |
- |
731095 |
| 3.4.22.15 | glycoprotein |
above 25% carbohydrate content |
667321 |
| 3.4.22.15 | glycoprotein |
sequence contains a potential N-glycosylation site at the Asn223 residue |
698021 |
| 3.4.22.15 | glycoprotein |
the enzyme contains a potential N-glycosylation site |
753600 |
| 3.4.22.15 | phosphoprotein |
investigation of the phosphorylation status of the secreted and lysosomal cathepsin L forms by treatment with alkaline phosphatase (ALP). The 32-kDa form of cathepsin L is phosphorylated, while the 34-kDa form is already dephosphorylated. The 32-kDa form might migrate to the anode faster than the dephosphorylated 34-kDa form because of the retention of the negative charge by the phosphate moiety. Acid phosphatase might remove the phosphorus group from the 32-kDa form as soon as it enters the lysosomes, thereby converting it to the 34-kDa form. The phosphorylated status of 32-kDa cathepsin L suggests that the secreted form has never enters lysosomes |
755110 |
| 3.4.22.15 | proteolytic modification |
activation of enzyme may require the cleavage of the propeptide |
697539 |
| 3.4.22.15 | proteolytic modification |
autoproteolytic maturation of 68000 Da precursor to 61000 Da mature enzyme in presence of dithiothreitol or trypsin |
-, 727746 |
| 3.4.22.15 | proteolytic modification |
calculated molecular mass including prepro-domains is 38000 Da |
696545 |
| 3.4.22.15 | proteolytic modification |
cathepsin L is a lysosomal enzyme that is synthesized as a preproform and processed into a 41-kDa proform in the Golgi apparatus. An acidic pH of 4.8 is sufficient to initiate the autoactivation of single-chain cathepsin L intermediates into the mature double-chain form, this process is inhibited by leupeptin |
755110 |
| 3.4.22.15 | proteolytic modification |
during secretion the polypeptide is cleaved between amino acids 17 and 18 |
647911 |
