protease involved in the degradation of extra-cellular matrix macromolecules, including collagens.

A family of proteases, characterized by a serine amino acid at its active site.

an endoprotease which catalyzes the hydrolysis of a peptide bond in which there is an essential serine residue at the active site

a protease involved in the degradation of extracellular matrix macromolecules, including collagens.

In biochemistry, serine proteases or serine endopeptidases (newer name) are a class of peptidases (enzymes that cleave peptide bonds in proteins) that are characterised by the presence of a serine residue in the active site of the enzyme. Serine proteases are grouped into clans that share structural homology and then further subgrouped into families that share close sequence homology. The major clans found in humans include the chymotrypsin-like, the subtilisin-like, the alpha/beta hydrolase, and signal peptidase clans.