EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.2.1.166 | proteolytic modification |
synthesized as an inactive 65000 Da glycoprotein that is cleaved at the N-terminus to generate the active enzyme |
692520 |
| 3.2.1.166 | proteolytic modification |
the 65 kDa precursor polypeptide that is enzymatically inactive. Proteolytic activation by cleavage into two fragments |
732436 |
| 3.2.1.166 | proteolytic modification |
the 65 kDa precursor polypeptide that is enzymatically inactive. Proteolytic excision by cathepsin L of a 48 amino acid peptide yields an active heterodimer comprising 8 and 50 kDa subunits |
731586, 731867 |
| 3.2.1.166 | proteolytic modification |
the 8000 Da and 50000 Da chains which make up the active enzyme reside, respectively, at the NH2-terminal and COOH-terminal regions of the inactive precursor, proheparanase. The heparanase heterodimer is produced by excision and loss of an internal linking segment |
692947 |
| 3.2.1.166 | proteolytic modification |
the full-length chicken heparanase cDNA encodes a 60000 Da proenzyme that is processed at the N-terminus into a 45000 Da highly active enzyme. The signal peptide sequence accounts for the chicken heparanase being readily secreted and localized in close proximity to the cell surface |
692954 |
