Description
The enzyme is activated by removal of an N-terminal prepropeptide. The highest amidolytic activity is observed using Boc-Val-Pro-Arg┼7-amido-4-methylcoumarin, which is a substrate of α-thrombin. Substrates lacking basic amino acids in the P1 position are not cleaved. The enzyme degrades casein, fibronectin, gelatin, collagen type IV, fibrinogen, and high-molecular-mass kininogen and is associated with diseases such as ovarian cancer and Alzheimer's disease. Belongs in peptidase family S1A