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Computational Design of a Biologically Active Enzyme
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Journal Article
Computational Design of a Biologically Active Enzyme
2004
Overview
Rational design of enzymes is a stringent test of our understanding of protein chemistry and has numerous potential applications. Here, we present and experimentally validate the computational design of enzyme activity in proteins of known structure. We have predicted mutations that introduce triose phosphate isomerase activity into ribosebinding protein, a receptor that normally lacks enzyme activity. The resulting designs contain 18 to 22 mutations, exhibit$10^5- to 10^6-fold$rate enhancements over the uncatalyzed reaction, and are biologically active, in that they support the growth of Escherichia coli under gluconeogenic conditions. The inherent generality of the design method suggests that many enzymes can be designed by this approach.
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science
