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Substrate Recognition Drives the Evolution of Serine Proteases*

https://doi.org/10.1074/jbc.C200132200Get rights and content
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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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Published, JBC Papers in Press, March 29, 2002, DOI 10.1074/jbc.C200132200

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This work was supported in part by National Institutes of Health Research Grants HL49413 and HL58141. The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.