Evidence map›Paper›PMID 22383957›Full record

ArticlePloS one2012

F420H2-dependent degradation of aflatoxin and other furanocoumarins is widespread throughout the actinomycetales.

Gauri V Lapalikar, Matthew C Taylor, Andrew C Warden, Colin Scott, Robyn J Russell, John G Oakeshott

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

28 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. On the diversity of FProteins · 2021
    Article
  9. Article
  10. Potency boost of aProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Toxins · 2021
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Coenzyme FJournal of bacteriology · 2018
    Article
  17. Discovery and characterization of an FApplied microbiology and biotechnology · 2017
    Article
  18. Mycobacterial FFrontiers in microbiology · 2017
    Article
  19. The methanogenic redox cofactor FThe ISME journal · 2017
    Article
  20. The Redox Cofactor FApplied and environmental microbiology · 2016
    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

6 authors at 3 institutions in 1 country.

Gauri V LapalikarEcosystem Sciences, Commonwealth Science and Industrial Research Organisation, Canberra, Australian Capital Territory, Australia.
Matthew C Taylor
Andrew C Warden
Colin Scott
Robyn J Russell
John G Oakeshott
Ecosystem Sciences · AUCommonwealth Scientific and Industrial Research Organisation · AUACT Government

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two classes of F(420)-dependent reductases (FDR-A and FDR-B) that can reduce aflatoxins and thereby degrade them have previously been isolated from Mycobacterium smegmatis. One class, the FDR-A enzymes, has up to 100 times more activity than the other. F(420) is a cofactor with a low reduction potential that is largely confined to the Actinomycetales and some Archaea and Proteobacteria. We have heterologously expressed ten FDR-A enzymes from diverse Actinomycetales, finding that nine can also use F(420)H(2) to reduce aflatoxin. Thus FDR-As may be responsible for the previously observed degradation of aflatoxin in other Actinomycetales. The one FDR-A enzyme that we found not to reduce aflatoxin belonged to a distinct clade (herein denoted FDR-AA), and our subsequent expression and analysis of seven other FDR-AAs from M. smegmatis found that none could reduce aflatoxin. Certain FDR-A and FDR-B enzymes that could reduce aflatoxin also showed activity with coumarin and three furanocoumarins (angelicin, 8-methoxysporalen and imperatorin), but none of the FDR-AAs tested showed any of these activities. The shared feature of the compounds that were substrates was an α,β-unsaturated lactone moiety. This moiety occurs in a wide variety of otherwise recalcitrant xenobiotics and antibiotics, so the FDR-As and FDR-Bs may have evolved to harness the reducing power of F(420) to metabolise such compounds. Mass spectrometry on the products of the FDR-catalyzed reduction of coumarin and the other furanocoumarins shows their spontaneous hydrolysis to multiple products.

Indexed as

Gene Expression RegulationAflatoxinsAnti-Bacterial AgentsBacterial ProteinsCoumarinsFlavinsFurocoumarinsHydrolysisKhellinMass SpectrometryMethoxsalenMycobacterium smegmatisOxidoreductasesPhylogenySpecies SpecificityXenobioticsAflatoxinsangelicinAnti-Bacterial AgentsBacterial ProteinscoumarinCoumarinsF420H2 dehydrogenaseFlavinsFurocoumarinsimperatorinKhellinMethoxsalenOxidoreductasesXenobiotics

Identifiers

PMID22383957
PMCPMC3288000
OpenAlexW2091385951

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.