Sequence determinants of function and evolution in serine proteases.
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.
Krem
M M
MM
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA.
Rose
T
T
Di Cera
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D000818:Animals; D010802:Phylogeny; D017434:Protein Structure, Tertiary / Q000235:genetics; D020539:Sequence Analysis, Protein; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000235:genetics*
D012697:Serine Endopeptidases