Evidence map›Paper›PMID 34584960›Full record

ArticleACS central science2021

Phage-Assisted Continuous Evolution and Selection of Enzymes for Chemical Synthesis.

Krysten A Jones, Harrison M Snodgrass, Ketaki Belsare, Bryan C Dickinson, Jared C Lewis

Abstract read
In one paragraph

Article in ACS central science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed.

  1. Review
  2. Phage-assisted continuous evolution of enzymes for noncanonical tyrosine biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Advances in adaptive laboratory evolution applications forSynthetic and systems biotechnology · 2025
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Virus-assisted directed evolution of biomolecules.Current opinion in chemical biology · 2023
    Review
  14. EnzyHTP Computational Directed Evolution with Adaptive Resource Allocation.Journal of chemical information and modeling · 2023
    Article
  15. Article
  16. Review
  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Krysten A JonesDepartment of Chemistry, The University of Chicago, Chicago, Illinois 60637, United States.ORCID https://orcid.org/0000-0003-0711-5516
Harrison M SnodgrassDepartment of Chemistry, Indiana University, Bloomington, Indiana 47401, United States.
Ketaki BelsareDepartment of Chemistry, The University of Chicago, Chicago, Illinois 60637, United States.
Bryan C DickinsonDepartment of Chemistry, The University of Chicago, Chicago, Illinois 60637, United States.ORCID https://orcid.org/0000-0002-9616-1911
Jared C LewisDepartment of Chemistry, Indiana University, Bloomington, Indiana 47401, United States.ORCID https://orcid.org/0000-0003-2800-8330

Funding

Directed Evolution of Halogenases For Small Molecule FunctionalizationR01GM115665 · NIGMS · UNIVERSITY OF CHICAGO · PI LEWIS, JARED C · 2015 to 2022
$2.5M
NIGMS NIH HHS R01 GM115665
6 · The paper itself

Abstract

Ligand-dependent biosensors are valuable tools for coupling the intracellular concentrations of small molecules to easily detectable readouts such as absorbance, fluorescence, or cell growth. While ligand-dependent biosensors are widely used for monitoring the production of small molecules in engineered cells and for controlling or optimizing biosynthetic pathways, their application to directed evolution for biocatalysts remains underexplored. As a consequence, emerging continuous evolution technologies are rarely applied to biocatalyst evolution. Here, we develop a panel of ligand-dependent biosensors that can detect a range of small molecules. We demonstrate that these biosensors can link enzymatic activity to the production of an essential phage protein to enable biocatalyst-dependent phage-assisted continuous evolution (PACE) and phage-assisted continuous selection (PACS). By combining these phage-based evolution and library selection technologies, we demonstrate that we can evolve enzyme variants with improved and expanded catalytic properties. Finally, we show that the genetic diversity resulting from a highly mutated PACS library is enriched for active enzyme variants with altered substrate scope. These results lay the foundation for using phage-based continuous evolution and selection technologies to engineer biocatalysts with novel substrate scope and reactivity.

Identifiers

PMID34584960
PMCPMC8461764

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.