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Sequence determinants of function and evolution in serine proteases.

M M Krem·T Rose·E Di Cera
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Abstract

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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AnimalsPhylogenyProtein Structure, TertiarySequence Analysis, ProteinSerine EndopeptidasesJournal ArticleReview

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M M Krem, T Rose, E Di Cera. 2000. Sequence determinants of function and evolution in serine proteases.. https://doi.org/10.1016/s1050-1738(00)00068-2

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