The large family of serine proteases (almost one-third of all proteases; EC 3.4.21.-) is characterized by its general mechanism of action to cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the (enzyme's) active site. The members of this family can be divided roughly into four sub-groups based on their structure, being chymotrypsin-like (trypsin-like), subtilisin-like, carboxypeptidase Y-like, and Clp-like.
 L. Hedstrom. Serine Protease Mechanism and Specificity. Chem. Rev. 2002, 102, 4501-4524.
|Axon ID||Name||Description||From price|
|1754||Apixaban||Factor Xa inhibitor||€125.00|
|2093||Daclatasvir dihydrochloride||Hepatitis C virus (HCV) NS5A protein inhibitor||€85.00|
|1669||Danoprevir||HCV NS3/4A serine protease inhibitor||€115.00|
|2364||GW 311616A||Potent, selective and orally active human neutrophil elastase (HNE) inhibitor||€135.00|
|1536||Odiparcil||Thrombin inhibitor (via Heparin CoFII)||€125.00|
|1269||SSR 69071||HLE inhibitor||€145.00|
|1769||T 1776Na||Inhibitor of plasminogen activator inhibitor-1||€95.00|
|1383||Tiplaxtinin||Plasminogen activator inhibitor-1 (PAI-1) inhibitor||€75.00|
|2344||TM 5275||Selective and orally active inhibitor of PAI-1||€105.00|