Serine endopeptidases are a class of proteases that use an active-site serine residue as the nucleophile to hydrolyze peptide bonds within proteins or polypeptides. Their members participate in protein digestion, coagulation and fibrinolysis, complement activation, inflammatory regulation, ...
Subtilisin-class proteases are a family of serine endoproteases predominantly secreted by bacteria, with Bacillus species as the most representative producers.