ArticleScientific reports2021
An in vivo selection system with tightly regulated gene expression enables directed evolution of highly efficient enzymes.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Directed evolution of a beta-lactamase samples a wide variety of conformational states.Protein science : a publication of the Protein Society · 2025Article
- Catalytic Residue Reprogramming Enhances Enzyme Activity at Alkaline pH via Phenolate-Mediated Proton Transfer.ACS synthetic biology · 2025Article
- A growth-based screening strategy for engineering the catalytic activity of an oxygen-sensitive formate dehydrogenase.Applied and environmental microbiology · 2024Article
- A growth selection system for sucrose synthases (SuSy): design and test.AMB Express · 2024Article
- Growth-Coupled Evolutionary Pressure Improving Epimerases for D-Allulose Biosynthesis Using a Biosensor-Assisted In Vivo Selection Platform.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Directed Evolution of 4-Hydroxyphenylpyruvate Biosensors Based on a Dual Selection System.International journal of molecular sciences · 2024Article
- A growth selection system for the directed evolution of amine-forming or converting enzymes.Nature communications · 2022Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In vivo selection systems are powerful tools for directed evolution of enzymes. The selection pressure of the systems can be tuned by regulating the expression levels of the catalysts. In this work, we engineered a selection system for laboratory evolution of highly active enzymes by incorporating a translationally suppressing cis repressor as well as an inducible promoter to impart stringent and tunable selection pressure. We demonstrated the utility of our selection system by performing directed evolution experiments using TEM β-lactamase as the model enzyme. Five evolutionary rounds afforded a highly active variant exhibiting 440-fold improvement in catalytic efficiency. We also showed that, without the cis repressor, the selection system cannot provide sufficient selection pressure required for evolving highly efficient TEM β-lactamase. The selection system should be applicable for the exploration of catalytic perfection of a wide range of enzymes.
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