Evidence map›Paper›PMID 36370045›Full record

ArticleProtein engineering, design & selection : PEDS2023

Engineering enzyme activity using an expanded amino acid alphabet.

Zachary Birch-Price, Christopher J Taylor, Mary Ortmayer, Anthony P Green

Abstract read
In one paragraph

Article in Protein engineering, design & selection : PEDS, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Transitioning enzyme catalysis towards photocatalysis.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2025
    Review
  3. Article
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  6. Article
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  11. Review
  12. Genetic Code Expansion inACS synthetic biology · 2024
    Article
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  14. Review
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  16. Review
  17. Review
  18. Article
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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

4 authors.

Zachary Birch-PriceSchool of Chemistry, Manchester Institute of Biotechnology, University of Manchester, Manchester, M1 7DN, UK.
Christopher J TaylorSchool of Chemistry, Manchester Institute of Biotechnology, University of Manchester, Manchester, M1 7DN, UK.
Mary OrtmayerSchool of Chemistry, Manchester Institute of Biotechnology, University of Manchester, Manchester, M1 7DN, UK.
Anthony P GreenSchool of Chemistry, Manchester Institute of Biotechnology, University of Manchester, Manchester, M1 7DN, UK.ORCID 0000-0003-0454-1798

Funding

Biotechnology and Biological Sciences Research CouncilBiotechnology and Biological Sciences Research Council Manchester Doctoral Training PartnershipCentre of Excellence for Biocatalysis, Biotransformations and Biocatalytic Manufacture StudentshipEuropean Research Council (ERC Starter Grant 757991
6 · The paper itself

Abstract

Enzyme design and engineering strategies are typically constrained by the limited size of nature's genetic alphabet, comprised of only 20 canonical amino acids. In recent years, site-selective incorporation of non-canonical amino acids (ncAAs) via an expanded genetic code has emerged as a powerful means of inserting new functional components into proteins, with hundreds of structurally diverse ncAAs now available. Here, we highlight how the emergence of an expanded repertoire of amino acids has opened new avenues in enzyme design and engineering. ncAAs have been used to probe complex biological mechanisms, augment enzyme function and, most ambitiously, embed new catalytic mechanisms into protein active sites that would be challenging to access within the constraints of nature's genetic code. We predict that the studies reviewed in this article, along with further advances in genetic code expansion technology, will establish ncAA incorporation as an increasingly important tool for biocatalysis in the coming years.

Indexed as

Amino AcidsProteinsBiocatalysisCloning, MolecularGenetic CodeAmino AcidsProteinsdirected evolutiongenetic code expansionnon-canonical amino acids

Identifiers

PMID36370045
PMCPMC9863031

What OpenQuestion holds

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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.