Serine peptidases: classification, structure and function.
Serine peptidases play key roles in human health and disease and their biochemical properties shaped the molecular evolution of these processes. Of known proteolytic enzymes, the serine peptidase family is the major cornerstone of the vertebrate degradome. We describe the known diversity of serine peptidases with respect to structure and function. Particular emphasis is placed on the S1 peptidase family, the trypsins, which underwent the most predominant genetic expansion yielding the enzymes responsible for vital processes in man such as digestion, blood coagulation, fibrinolysis, development, fertilization, apoptosis and immunity.
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M J
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Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA.
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D000494:Allosteric Regulation; D000596:Amino Acids / Q000378:metabolism; D006801:Humans; D017433:Protein Structure, Secondary; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D012964:Sodium / Q000378:metabolism; D013917:Thrombin / Q000737:chemistry / Q000378:metabolism
D000596:Amino Acids; D012964:Sodium; D012697:Serine Endopeptidases; D013917:Thrombin