Protein Flexibility and Preorganization in the Design of Enzymes. The Kemp Elimination Catalyzed by HG3.17
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Other documents of the author: Świderek, Katarzyna; Tuñón, Iñaki; Moliner, Vicent; Bertran, Joan
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http://dx.doi.org/10.1021/cs501904w |
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Title
Protein Flexibility and Preorganization in the Design of Enzymes. The Kemp Elimination Catalyzed by HG3.17Date
2015Publisher
ACS PublicationsBibliographic citation
SWIDEREK, Katarzyna; TUÑÓN, Iñaki; MOLINER IBÁÑEZ, Vicente; BERTRAN, Joan. Protein Flexibility and Preorganization in the Design of Enzymes. The Kemp Elimination Catalyzed by HG3.17. ACS Catalysis (2015), v. 4, n. 5, pp. 2587-2595Type
info:eu-repo/semantics/articlePublisher version
http://pubs.acs.org/doi/abs/10.1021/cs501904wSubject
Abstract
A recently designed enzyme, HG3.17, obtained by directed evolution, has shown a catalytic activity close to natural enzymes. Hybrid QM/MM molecular dynamics simulations for the Kemp elimination in this new enzyme have ... [+]
A recently designed enzyme, HG3.17, obtained by directed evolution, has shown a catalytic activity close to natural enzymes. Hybrid QM/MM molecular dynamics simulations for the Kemp elimination in this new enzyme have provided a deep insight into the origin of its catalytic efficiency. In this case, we have first demonstrated the presence of different conformations with significantly different reactivity. The larger reactivity is related with a better electrostatic preorganization of the environment that creates a more favorable electrostatic potential for the reaction to proceed. In HG3.17, efforts to improve the catalytic properties must be focused in possible mutations increasing the preorganization and decreasing the reorganization around the oxyanion hole. Mutations should be considered not only in the first shell of residues but in further shells since protein electrostatics is a long-range property. The present work stresses the fact that not all features of catalysis can be revealed of a single structure derived from X-ray diffraction. [-]
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ACS Catalysis (2015), v. 4, n. 5Rights
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