Serine protease

Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the (enzyme's) active site. They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like. In humans, they are responsible for co-ordinating various physiological functions, including digestion, immune response, blood coagulation and reproduction.

Classification

The MEROPS protease classification system counts 16 superfamilies (as of 2013) each containing many families. Each superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the catalytic mechanism. The majority belong to the S1 family of the PA clan (superfamily) of proteases.

For superfamilies, P = superfamily containing a mixture of nucleophile class families, S = purely serine proteases. superfamily. Within each superfamily, families are designated by their catalytic nucleophile (S = serine proteases).

Matriptase

Matriptase (EC 3.4.21.109, serine protease 14, membrane-type serine protease 1, MT-SP1, prostamin, serine protease TADG-15, tumor-associated differentially-expressed gene 15 protein, ST14, breast cancer 80 kDa protease, epithin, serine endopeptidase SNC19) is an enzyme. This enzyme catalyses the following chemical reaction

This trypsin-like integral-membrane serine peptidase has been implicated in breast cancer invasion and metastasis.

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