Evidence map›Paper›PMID 38959423›Full record

ReviewChemical reviews2024

Noncanonical Amino Acids in Biocatalysis.

Zachary Birch-Price, Florence J Hardy, Thomas M Lister, Anna R Kohn, Anthony P Green

Abstract readReview
In one paragraph

Review in Chemical reviews, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. 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
  2. Article
  3. Article
  4. Article
  5. Applications and limitations of AI tools in enzyme design.Protein science : a publication of the Protein Society · 2026
    Review
  6. Reprogramming NAD(P)Angewandte Chemie (International ed. in English) · 2026
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Exploring PadR Proteins for Artificial Enzyme Design.Chembiochem : a European journal of chemical biology · 2026
    Article
  16. Article
  17. l-Arg@ZY-FeNanoscale advances · 2026
    Article
  18. Article
  19. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  20. 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.

Zachary Birch-PriceManchester Institute of Biotechnology, School of Chemistry, University of Manchester, Manchester M1 7DN, U.K.ORCID 0000-0002-2024-3005
Florence J HardyManchester Institute of Biotechnology, School of Chemistry, University of Manchester, Manchester M1 7DN, U.K.ORCID 0000-0003-0671-0209
Thomas M ListerManchester Institute of Biotechnology, School of Chemistry, University of Manchester, Manchester M1 7DN, U.K.
Anna R KohnManchester Institute of Biotechnology, School of Chemistry, University of Manchester, Manchester M1 7DN, U.K.
Anthony P GreenManchester Institute of Biotechnology, School of Chemistry, University of Manchester, Manchester M1 7DN, U.K.ORCID 0000-0003-0454-1798

Funding

Biotechnology and Biological Sciences Research Council BB/M027023/1Biotechnology and Biological Sciences Research Council BB/W014483/1Biotechnology and Biological Sciences Research Council BB/X000974/1European Research Council 757991
6 · The paper itself

Abstract

In recent years, powerful genetic code reprogramming methods have emerged that allow new functional components to be embedded into proteins as noncanonical amino acid (ncAA) side chains. In this review, we will illustrate how the availability of an expanded set of amino acid building blocks has opened a wealth of new opportunities in enzymology and biocatalysis research. Genetic code reprogramming has provided new insights into enzyme mechanisms by allowing introduction of new spectroscopic probes and the targeted replacement of individual atoms or functional groups. NcAAs have also been used to develop engineered biocatalysts with improved activity, selectivity, and stability, as well as enzymes with artificial regulatory elements that are responsive to external stimuli. Perhaps most ambitiously, the combination of genetic code reprogramming and laboratory evolution has given rise to new classes of enzymes that use ncAAs as key catalytic elements. With the framework for developing ncAA-containing biocatalysts now firmly established, we are optimistic that genetic code reprogramming will become a progressively more powerful tool in the armory of enzyme designers and engineers in the coming years.

Indexed as

Amino AcidsBiocatalysisEnzymesGenetic CodeProtein EngineeringAmino AcidsEnzymes

Identifiers

PMID38959423
PMCPMC11273360

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.