ArticleProtein science : a publication of the Protein Society2005
Simultaneous optimization of enzyme activity and quaternary structure by directed evolution.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- An in vivo selection system with tightly regulated gene expression enables directed evolution of highly efficient enzymes.Scientific reports · 2021Article
- Dependence of the Enzymatic Velocity on the Substrate Dissociation Rate.The journal of physical chemistry. B · 2017Article
- Dynamic dissociating homo-oligomers and the control of protein function.Archives of biochemistry and biophysics · 2012Review
- Design, selection, and characterization of a split chorismate mutase.Protein science : a publication of the Protein Society · 2010Article
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5 authors.
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Abstract
Natural evolution has produced efficient enzymes of enormous structural diversity. We imitated this natural process in the laboratory to augment the efficiency of an engineered chorismate mutase with low activity and an unusual hexameric topology. By applying two rounds of DNA shuffling and genetic selection, we obtained a 400-fold more efficient enzyme, containing three non-active-site mutations. Detailed biophysical characterization of the evolved variant suggests that it exists predominantly as a trimer in solution, but is otherwise similarly stable as the parent hexamer. The dramatic structural and functional effects achieved by a small number of seemingly innocuous substitutions highlights the utility of directed evolution for modifying protein-protein interactions to produce novel quaternary states with optimized activities.
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