Proteases (Serine)

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[1].


[1] L. Hedstrom. Serine Protease Mechanism and Specificity. Chem. Rev. 2002, 102, 4501-4524.

Items 16 to 19 of 19 total

per page
Page:
  1. 1
  2. 2
Axon ID Name Description From price
2344 TM 5275 Selective and orally active inhibitor of PAI-1 €105.00
2734 TM 5441 Orally active inhibitor of PAI-1 €95.00
3173 Velpatasvir Hepatitis C virus NS5A inhibitor €50.00
2911 Y 29794 tosylate Orally active, brain penetrant, potent and specific prolyl endopeptidase (PPCE) inhibitor €125.00

Items 16 to 19 of 19 total

per page
Page:
  1. 1
  2. 2
Please wait...