Serine protease
In biochemistry, a serine proteases or serine endopeptidases (newer name) are a class of peptidases which are characterised by the presence of a serine residue in the active domain of the enzyme.
Genetics
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Physiology
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Serine proteases are inhibited by serine protease inhibitors ("serpins"), a diverse group of enzymes that form a covalent bond with the serine protease, inhibiting its function. The best-studied serpins are antithrombin and alpha 1-antitrypsin, studied for their role in coagulation/thrombosis and emphysema/A1AT respectively.
Role in disease
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