{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84822"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84822","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"A Study of the Mechanistic Diversity Inherent to the Ribulose Phosphate Binding Barrel Superfamily","abstract":"To probe the functional plasticity of the RPBB superfamily, rational design was used to enhance the UPS activity within the KGPDC scaffold. The triple mutant E112D/T169A/R139V had an enhancement in kcat /KM by 260 fold over wild-type KGPDC. Structural studies suggest that little perturbation of the active site occurs with the 3 mutations.","abstract_html":"To probe the functional plasticity of the RPBB superfamily, rational design was used to enhance the UPS activity within the KGPDC scaffold. 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