Reengineering Enzymes

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Science  16 Jul 2010:
Vol. 329, Issue 5989, pp. 285-287
DOI: 10.1126/science.1192224

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The versatility and proficiency of enzymes makes them promising catalysts for the laboratory and for industrial synthesis of organic molecules, yet natural biocatalysts often do not meet the scientists and engineers' expectations in regards to stability, selectivity, and specificity. On pages 309 and 305 of this issue, two different approaches show how enzymes can be engineered to make them part of the organic chemist's toolkit. Using a first-principles approach, Siegel et al. (1) applied the Rosetta design software to create an enzyme that performs the stereoselective, intermolecular Diels-Alder cycloaddition, a reaction of great value to organic synthetic chemistry. In contrast, Savile et al. (2) used structure-based rational design and directed evolution to reprogram the substrate specificity and stability of a native transaminase to replace a rhodium-based hydrogenation catalyst in the production of an antidiabetes compound, sitagliptin.