TY - DATA T1 - Dataset for: Quantum chemical modeling of the reaction path of chorismate mutase based on the experimental substrate/product complex PY - 2017/05/12 AU - Daniel Burschowsky AU - Ute Krengel AU - Einar Uggerud AU - David Balcells UR - https://wiley.figshare.com/articles/dataset/Dataset_for_Quantum_chemical_modeling_of_the_reaction_path_of_chorismate_mutase_based_on_the_experimental_substrate_product_complex/5001902 DO - 10.6084/m9.figshare.5001902.v1 L4 - https://ndownloader.figshare.com/files/8423174 L4 - https://ndownloader.figshare.com/files/8423177 L4 - https://ndownloader.figshare.com/files/8423180 L4 - https://ndownloader.figshare.com/files/8423183 L4 - https://ndownloader.figshare.com/files/8423186 L4 - https://ndownloader.figshare.com/files/8423189 KW - chorismate mutase KW - pericyclic reaction KW - Claisen rearrangement KW - transition state stabilization KW - enzyme catalysis KW - Stem Cells KW - Synthetic Biology KW - Molecular Biology KW - Developmental Biology KW - Structural Biology KW - Proteomics and Intermolecular Interactions (excl. Medical Proteomics) KW - Evolutionary Biology KW - Signal Transduction KW - Cancer Cell Biology KW - Systems Biology KW - Bioinformatics KW - Biostatistics KW - Heat and Mass Transfer Operations N2 - Chorismate mutase is a well-known model enzyme, catalyzing the Claisen rearrangement of chorismate to prephenate. Recent high-resolution crystal structures along the reaction coordinate of this enzyme enable computational analyses at unprecedented detail. Using quantum chemical simulations, we have investigated how the catalytic reaction mechanism is affected by electrostatic and hydrogen bond interactions. Our calculations showed that the transition state was mainly stabilized electrostatically, with Arg90 playing the leading role. The effect was augmented by selective hydrogen bond formation to the transition state in the wild-type enzyme, facilitated by a small-scale local induced fit. We further identified a previously underappreciated water molecule, which separates the negative charges during the reaction. The analysis includes the wild-type enzyme and a non-natural enzyme variant, where the catalytic arginine was replaced with an isosteric citrulline residue. ER -