CO-AUTHORED BY IVANA KUTA SMATANOVA AND MARYNA LAHODA FROM CNSB- Dynamics and hydration explain failed functional transformation in dehalogenase design

In their publication the authors 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. Nature Chemical Biology one of the most prestigious scientific journals in the field with an impact factor of 12.948 published the paper online 13 April 2014.

Publication
Jan Sykora, Jan Brezovsky, Tana Koudelakova, Maryna Lahoda, Andrea Fortova, Tatsiana Chernovets, Radka Chaloupkova, Veronika Stepankova, Zbynek Prokop, Ivana Kuta Smatanova, Martin Hof, Jiri Damborsky: Dynamics and hydration explain failed functional transformation in dehalogenase design, Nature Chemical Biology (2014), Published online 13 April 2014, doi:10.1038/nchembio.1502