Evidence map›Paper›PMID 29633774›Full record

ReviewNatural product reports2018

C-C bond forming radical SAM enzymes involved in the construction of carbon skeletons of cofactors and natural products.

Kenichi Yokoyama, Edward A Lilla

Open access · greenAbstract readReview
In one paragraph

Review in Natural product reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

54 citing papers in PubMed, 103 citations in OpenAlex.

  1. Article
  2. Article
  3. RadicalJournal of the American Chemical Society · 2026
    Article
  4. Mechanism of controlled radical initiation in radical SAM GTP 3',8-cyclase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Nitric Oxide Inhibition of Glycyl Radical Enzymes and Their Activases.Journal of the American Chemical Society · 2025
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Biomolecules · 2023
    Article
  14. Biosynthesis and Genome Mining Potentials of Nucleoside Natural Products.Chembiochem : a European journal of chemical biology · 2023
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. 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

2 authors at 2 institutions in 1 country.

Kenichi YokoyamaDepartment of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA. ken.yoko@duke.edu.
Edward A Lilla
Duke University · USDurham Technical Community College · US

Funding

Biosynthesis of peptidyl nucleoside antifungal antibioticsR01GM115729 · NIGMS · DUKE UNIVERSITY · PI YOKOYAMA, KENICHI · 2015 to 2023
$3.1M
Mechanism of cofactor biosynthesis required for chronic bacterial infectionR01GM112838 · NIGMS · DUKE UNIVERSITY · PI YOKOYAMA, KENICHI · 2015 to 2023
$2.8M
NIGMS NIH HHS R01 GM112838NIGMS NIH HHS R01 GM115729
6 · The paper itself

Abstract

Covering: up to the end of 2017 C-C bond formations are frequently the key steps in cofactor and natural product biosynthesis. Historically, C-C bond formations were thought to proceed by two electron mechanisms, represented by Claisen condensation in fatty acids and polyketide biosynthesis. These types of mechanisms require activated substrates to create a nucleophile and an electrophile. More recently, increasing number of C-C bond formations catalyzed by radical SAM enzymes are being identified. These free radical mediated reactions can proceed between almost any sp3 and sp2 carbon centers, allowing introduction of C-C bonds at unconventional positions in metabolites. Therefore, free radical mediated C-C bond formations are frequently found in the construction of structurally unique and complex metabolites. This review discusses our current understanding of the functions and mechanisms of C-C bond forming radical SAM enzymes and highlights their important roles in the biosynthesis of structurally complex, naturally occurring organic molecules. Mechanistic consideration of C-C bond formation by radical SAM enzymes identifies the significance of three key mechanistic factors: radical initiation, acceptor substrate activation and radical quenching. Understanding the functions and mechanisms of these characteristic enzymes will be important not only in promoting our understanding of radical SAM enzymes, but also for understanding natural product and cofactor biosynthesis.

Indexed as

AdenineBacterial ProteinsBacteriochlorophyllsBiological ProductsCarbonCoenzymesEndopeptidasesEnzymesHydrolasesMolybdenumS-AdenosylmethionineTunicamycinVitamin K 2AdenineBacterial ProteinsBacteriochlorophyllsBiological ProductsCarbonCoenzymesEndopeptidasesEnzymesHydrolasesMolybdenumoxetanocinPqqE protein, Methylobacterium extorquensS-AdenosylmethionineS-adenosylmethionine enzyme MoaA, Staphylococcus aureusTunicamycinVitamin K 2

Identifiers

PMID29633774
PMCPMC6051890
OpenAlexW2798220330

What OpenQuestion holds

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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.