Evidence map›Paper›PMID 29334382›Full record

ArticleNature chemical biology2018

A de novo enzyme catalyzes a life-sustaining reaction in Escherichia coli.

Ann E Donnelly, Grant S Murphy, Katherine M Digianantonio, Michael H Hecht

Abstract read
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In one paragraph

Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Review
  2. ACS central science · 2025
    Article
  3. Article
  4. Article
  5. Evolution and synthetic biology.Current opinion in microbiology · 2023
    Review
  6. Review
  7. Crystal structure and activity of a de novo enzyme, ferric enterobactin esterase Syn-F4.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. A de novo protein catalyzes the synthesis of semiconductor quantum dots.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Article
  12. Review
  13. De novo proteins from random sequences through in vitro evolution.Current opinion in structural biology · 2021
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. A de novo peroxidase is also a promiscuous yet stereoselective carbene transferase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Ann E DonnellyDepartment of Chemistry, Princeton University, Princeton, New Jersey, USA.ORCID 0000-0002-6296-5401
Grant S MurphyDepartment of Chemistry, Princeton University, Princeton, New Jersey, USA.
Katherine M DigianantonioDepartment of Chemistry, Princeton University, Princeton, New Jersey, USA.
Michael H HechtDepartment of Chemistry, Princeton University, Princeton, New Jersey, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Producing novel enzymes that are catalytically active in vitro and biologically functional in vivo is a key goal of synthetic biology. Here we describe Syn-F4, the first de novo protein that meets both criteria. Purified Syn-F4 hydrolyzes the siderophore ferric enterobactin, and expression of Syn-F4 allows an inviable strain of Escherichia coli to grow in iron-limited medium. These findings demonstrate that entirely new sequences can provide life-sustaining enzymatic functions in living organisms.

Indexed as

CatalysisComputational BiologyCulture MediaDimerizationEnterobactinEscherichia coliEscherichia coli ProteinsHydrolysisIronKineticsMutagenesisMutationPhenotypeProtein FoldingSiderophoresSynthetic BiologyCulture MediaEnterobactinEscherichia coli ProteinsferrienterochelinIronSiderophores

Identifiers

PMID29334382

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.