EC Number   |
Posttranslational Modification |
Reference  |
|---|
   3.2.1.166 | glycoprotein |
glycosylation of Hpa1 is essential for solubility |
690801 |
| 3.2.1.166 | proteolytic modification |
Hpa1 protein is initially synthesized as an inactive 65000 Da proenzyme and subsequently activated by proteolytic cleavage to generate an active heterodimer of 8000 Da and 50000 Da polypeptides |
690801 |
| 3.2.1.166 | glycoprotein |
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 |
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 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 | glycoprotein |
4 potential N-glycosylation sites |
692954 |
| 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 |
| 3.2.1.166 | glycoprotein |
the enzyme contains six N-linked oligosaccharides |
693320 |
| 3.2.1.166 | proteolytic modification |
heparanase-1 is synthesized as an inactive precursor of about 65000 Da that subsequently undergoes proteolytic cleavage, yielding 8000 Da and 50000 Da protein subunits that heterodimerize to form the active enzyme. The protein contains a putative N-terminal signal peptide (Met1-Ala35) and a C-terminal hydrophobic region (Pro515-Ile534) |
693320 |
| 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 |
