Dynamics and Hydration Explain Failed Functional Transformation in Dehalogenase Design.

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Authors

SYKORA J. BREZOVSKÝ Jan KOUDELÁKOVÁ Táňa LAHODA M. FOŘTOVÁ Andrea CHERNOVETS T. CHALOUPKOVÁ Radka ŠTĚPÁNKOVÁ Veronika PROKOP Zbyněk KUTA SMATANOVA I. HOF M. DAMBORSKÝ Jiří

Year of publication 2014
Type Article in Periodical
Magazine / Source Nature Chemical Biology
MU Faculty or unit

Faculty of Science

Citation
Field Biochemistry
Keywords haloalkane dehalogenase
Description We emphasize the importance of dynamics and hydration for enzymatic catalysis and protein design by transplanting the active site from a haloalkane dehalogenase with high enantioselectivity to nonselective dehalogenase. Protein crystallography confirms that the active site geometry of the redesigned dehalogenase matches that of the target, but its enantioselectivity remains low. Time-dependent fluorescence shifts and computer simulations revealed that dynamics and hydration at the tunnel mouth differ substantially between the redesigned and target dehalogenase.
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