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Sequence determinants of function and evolution in serine proteases.

M M Krem1, T Rose, E Di Cera

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

Trends in Cardiovascular Medicine
|March 10, 2001
PubMed
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Serine proteases, vital for functions like blood clotting, show remarkable diversity despite sequence similarity. Their evolution is driven by the protease domain, particularly its C-terminal region, shaping diverse functions.

Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Enzymology

Background:

  • Serine proteases in the chymotrypsin family share a conserved fold across >1 billion years.
  • These enzymes perform critical biological roles including fibrinolysis, blood coagulation, and complement activation.
  • Despite conserved structure, they exhibit diverse substrate specificities.

Purpose of the Study:

  • To investigate the evolutionary drivers of functional diversity in serine proteases.
  • To identify the key structural elements responsible for varied substrate specificities and biological functions.

Main Methods:

  • Comparative sequence analysis of serine proteases.
  • Structural analysis focusing on the protease domain and C-terminal regions.
  • Functional domain mapping studies (inferred).

Related Experiment Videos

Main Results:

  • The conserved fold of chymotrypsin-like serine proteases has persisted for over a billion years.
  • Modest sequence variations within the conserved fold lead to a broad spectrum of substrate specificities.
  • The protease domain, particularly its C-terminal sequence, is the primary determinant of functional diversity.

Conclusions:

  • The C-terminal region of the protease domain is crucial for the evolutionary diversification of serine proteases.
  • Understanding this domain is key to comprehending the evolution of essential biological processes regulated by these enzymes.