Evidence map›Paper›PMID 28196894›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Extending enzyme molecular recognition with an expanded amino acid alphabet.

Claire L Windle, Katie J Simmons, James R Ault, Chi H Trinh, Adam Nelson, Arwen R Pearson, Alan Berry

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.1field-weighted citation impact, top 13% of its field
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

12 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Directed Evolution of a Designer Enzyme Featuring an Unnatural Catalytic Amino Acid.Angewandte Chemie (International ed. in English) · 2019
    Article
  10. Review
  11. Adaptive evolution of genomically recodedProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Review
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

7 authors at 1 institution in 1 country.

Claire L WindleAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom.
Katie J SimmonsAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom.
James R AultAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom.
Chi H TrinhAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom.
Adam NelsonAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom; a.berry@leeds.ac.uk a.s.nelson@leeds.ac.uk.
Arwen R PearsonAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom.ORCID 0000-0001-8499-7490
Alan BerryAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom; a.berry@leeds.ac.uk a.s.nelson@leeds.ac.uk.ORCID 0000-0003-3502-0426
University of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L015056/1Biotechnology and Biological Sciences Research Council BB/M012573/1Biotechnology and Biological Sciences Research Council BB/N002091/1Biotechnology and Biological Sciences Research Council B/F01614X/1Wellcome TrustWellcome Trust WT094232MA
6 · The paper itself

Abstract

Natural enzymes are constructed from the 20 proteogenic amino acids, which may then require posttranslational modification or the recruitment of coenzymes or metal ions to achieve catalytic function. Here, we demonstrate that expansion of the alphabet of amino acids can also enable the properties of enzymes to be extended. A chemical mutagenesis strategy allowed a wide range of noncanonical amino acids to be systematically incorporated throughout an active site to alter enzymic substrate specificity. Specifically, 13 different noncanonical side chains were incorporated at 12 different positions within the active site of

Indexed as

CatalysisCatalytic DomainCrystallography, X-RayCysteineEnzyme StabilityKineticsMutagenesis, Site-DirectedOxo-Acid-LyasesSubstrate SpecificityCysteineN-acetylneuraminate lyaseOxo-Acid-Lyasesaldolaseschemical modificationprotein engineering

Identifiers

PMID28196894
PMCPMC5347630
OpenAlexW2588516463

What OpenQuestion holds

Textmetadata
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.