Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
Reaction(IUBMB)
Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys
Comment
The enzyme is activated by removal of an N-terminal prepropeptide [2,4]. The highest amidolytic activity is observed using Boc-Val-Pro-Arg!7-amido-4-methylcoumarin, which is a substrate of alpha-thrombin [2,4]. Substrates lacking basic amino acids in the P1 position are not cleaved [4]. The enzyme degrades casein, fibronectin, gelatin, collagen type IV, fibrinogen, and high-molecular-mass kininogen [3] and is associated with diseases such as ovarian cancer and Alzheimer's disease [4]. Belongs in peptidase family S1A.