Serine (Ser) proteases are enzymes that catalyze the hydrolysis of specific peptide bonds in their substrates, and one of the amino acids in the enzyme's active site is always a serine. The trypsin family and the subtilisin family are two families that have received particular attention in research. The process of blood clotting, protein digestion, cell signaling, inflammation, and protein processing are just a few of the numerous cellular and extracellular functions that serine proteases are essential for. A threonine residue is present in the active site of a family of proteolytic enzymes known as thronine (Thr) proteases. Although the catalytic subunits of the proteasome are the prototype members of this class of enzymes, the active site geometry and mechanism of acyltransferases were convergently evolved.
|Acetyltrypsin (acetylated trypsin)
|Avoralstat (formerly also known as BCX-4161) is a novel, potent and orally bioavailable inhibitor of Kallikrein and Bradykinin with the potential for treatment for Hereditary angioedema.
|Benzamidine hydrochloride hydrate (benzamidine hydrochloride hydrate; Benzenecarboximidamide hydrochloride hydrate)
|Berotralstat dihydrochloride (BCX7353 dihydrochloride)
|Bococizumab (PF-04950615; RN316)