ArticleProtein science : a publication of the Protein Society2015
Design of an allosterically regulated retroaldolase.
Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Modulating thermal folded stability and catalytic activity of aRSC advances · 2026Article
- Fishing for Catalysis: Experimental Approaches to Narrowing Search Space in Directed Evolution of Enzymes.JACS Au · 2023Review
- MinimalistACS catalysis · 2019Article
- Article
- A Designed Enzyme Promotes Selective Post-translational Acylation.Chembiochem : a European journal of chemical biology · 2018Article
- Rational and Semirational Protein Design.Methods in molecular biology (Clifton, N.J.) · 2018Review
- Incorporating an allosteric regulatory site in an antibody through backbone design.Protein science : a publication of the Protein Society · 2017Article
- Design of Catalytic Peptides and Proteins Through Rational and Combinatorial Approaches.Annual review of biomedical engineering · 2016Review
- Protein engineering in the 21st century.Protein science : a publication of the Protein Society · 2015Article
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6 authors.
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Abstract
We employed a minimalist approach for design of an allosterically controlled retroaldolase. Introduction of a single lysine residue into the nonenzymatic protein calmodulin led to a 15,000-fold increase in the second order rate constant for retroaldol reaction with methodol as a substrate. The resulting catalyst AlleyCatR is active enough for subsequent directed evolution in crude cell bacterial lysates. AlleyCatR's activity is allosterically regulated by Ca(2+) ions. No catalysis is observed in the absence of the metal ion. The increase in catalytic activity originates from the hydrophobic interaction of the substrate (∼2000-fold) and the change in the apparent pKa of the active lysine residue.
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