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  • Title: Converting an esterase into an epoxide hydrolase.
    Author: Jochens H, Stiba K, Savile C, Fujii R, Yu JG, Gerassenkov T, Kazlauskas RJ, Bornscheuer UT.
    Journal: Angew Chem Int Ed Engl; 2009; 48(19):3532-5. PubMed ID: 19350592.
    Abstract:
    Entering the fold: A common structural motif in hydrolytic enzymes is the alpha,beta-hydrolase fold. The interconversion of one enzyme into another by introduction of mechanistically important residues is not enough; only substitution of a loop allows epoxide hydrolase activity in the esterase scaffold to be formed (see picture; structure comparison of epoxide hydrolases (green) with the esterase (orange)). The result is an enantioselective chimeric enzyme.
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