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Trends Cardiovasc Med. 2000 May;10(4):171-6.

Sequence determinants of function and evolution in serine proteases.

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  • 1Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA.


Serine proteases of the chymotrypsin family have maintained a common fold over an evolutionary span of more than one billion years. Notwithstanding modest changes in sequence, this class of enzymes has developed a wide variety of substrate specificities and important biological functions such as fibrinolysis, blood coagulation, and complement activation. Recently it has become apparent that the protease domain, especially its C-terminal sequence, accounts fully for this functional diversity and is the most important element in shaping serine protease evolution.

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