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Papers In Press, published online ahead of print March 29, 2002
J. Biol. Chem, 10.1074/jbc.C200132200
Submitted on March 6, 2002
Revised on March 28, 2002
Accepted on March 29, 2002

Substrate recognition drives the evolution of serine proteases

Thierry Rose and Enrico Di Cera

Biochemistry and Molecular Biophysics, Washington University School of Medicine, St Louis, MO 63110

Corresponding Author: enrico{at}biochem.wustl.edu

A method is introduced to identify amino acid residues that dictate the functional diversity acquired during evolution in a protein family. Using over 80 enzymes of the chymotrypsin family, we demonstrate that the general organization of the phylogenetic tree and its functional branch points are fully accounted for by a limited number of residues that cluster around the active site of the protein and define the contact region with the P1-P4 residues of substrate.


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