Dynamics and Hydration Explain Failed Functional Transformation in Dehalogenase Design.
| Authors | |
|---|---|
| Year of publication | 2014 |
| Type | Article in Periodical |
| Magazine / Source | Nature Chemical Biology |
| MU Faculty or unit | |
| 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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