Evidence map›Paper›PMID 28827772›Full record

ArticleNature communications2017

A three enzyme system to generate the Strychnos alkaloid scaffold from a central biosynthetic intermediate.

Evangelos C Tatsis, Inês Carqueijeiro, Thomas Dugé de Bernonville, Jakob Franke, Thu-Thuy T Dang, Audrey Oudin, Arnaud Lanoue, Florent Lafontaine, Anna K Stavrinides, Marc Clastre and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
14.3field-weighted citation impact, top 1% 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

53 citing papers in PubMed, 146 citations in OpenAlex.

  1. Tuning reductase activity in monoterpene indole alkaloid biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  9. Oxidative Rearrangements of the Alkaloid Intermediate Geissoschizine.Angewandte Chemie (International ed. in English) · 2025
    Article
  10. Review
  11. Genome-based discovery of pachysiphine synthases in Tabernaemontana elegans.The Plant journal : for cell and molecular biology · 2024
    Article
  12. Chromosome-leveliScience · 2024
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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

12 authors at 2 institutions in 2 countries.

Evangelos C TatsisJohn Innes Centre, Department of Biological Chemistry, Norwich Research Park, Norwich, NR4 7UH, UK.ORCID http://orcid.org/0000-0002-4013-1537
Inês CarqueijeiroUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, Parc de Grandmont, 37200, Tours, France.ORCID http://orcid.org/0000-0001-9576-5556
Thomas Dugé de BernonvilleUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, Parc de Grandmont, 37200, Tours, France.ORCID http://orcid.org/0000-0002-2205-2886
Jakob FrankeJohn Innes Centre, Department of Biological Chemistry, Norwich Research Park, Norwich, NR4 7UH, UK.
Thu-Thuy T DangJohn Innes Centre, Department of Biological Chemistry, Norwich Research Park, Norwich, NR4 7UH, UK.
Audrey OudinUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, Parc de Grandmont, 37200, Tours, France.
Arnaud LanoueUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, Parc de Grandmont, 37200, Tours, France.
Florent LafontaineUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, Parc de Grandmont, 37200, Tours, France.
Anna K StavrinidesJohn Innes Centre, Department of Biological Chemistry, Norwich Research Park, Norwich, NR4 7UH, UK.ORCID http://orcid.org/0000-0001-7351-8116
Marc ClastreUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, Parc de Grandmont, 37200, Tours, France.
Vincent CourdavaultUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, Parc de Grandmont, 37200, Tours, France. vincent.courdavault@univ-tours.fr.ORCID http://orcid.org/0000-0001-8902-4532
Sarah E O'ConnorJohn Innes Centre, Department of Biological Chemistry, Norwich Research Park, Norwich, NR4 7UH, UK. sarah.oconnor@jic.ac.uk.ORCID http://orcid.org/0000-0003-0356-6213
Université de Tours · FRJohn Innes Centre · GB

Funding

Biotechnology and Biological Sciences Research Council BB/N007905/1Biotechnology and Biological Sciences Research Council BBS/E/J/000CA512Biotechnology and Biological Sciences Research Council BBS/E/J/000PR9790European Research Council 311363
6 · The paper itself

Abstract

Monoterpene indole alkaloids comprise a diverse family of over 2000 plant-produced natural products. This pathway provides an outstanding example of how nature creates chemical diversity from a single precursor, in this case from the intermediate strictosidine. The enzymes that elicit these seemingly disparate products from strictosidine have hitherto been elusive. Here we show that the concerted action of two enzymes commonly involved in natural product metabolism-an alcohol dehydrogenase and a cytochrome P450-produces unexpected rearrangements in strictosidine when assayed simultaneously. The tetrahydro-β-carboline of strictosidine aglycone is converted into akuammicine, a Strychnos alkaloid, an elusive biosynthetic transformation that has been investigated for decades. Importantly, akuammicine arises from deformylation of preakuammicine, which is the central biosynthetic precursor for the anti-cancer agents vinblastine and vincristine, as well as other biologically active compounds. This discovery of how these enzymes can function in combination opens a gateway into a rich family of natural products.The biosynthetic pathway of preakuammicine, a monoterpene precursor of the anti-cancer agent vinblastine, has remained largely unexplored. Here, the authors provide transcriptomic and biochemical data to identify two enzymes that, in tandem, convert strictosidine to akuammicine, the stable shunt product of preakuammicine.

Indexed as

Alcohol DehydrogenaseAlkaloidsBase SequenceBiological ProductsBiosynthetic PathwaysCytochrome P-450 Enzyme SystemIndolesIsoenzymesModels, ChemicalMolecular StructurePlant ProteinsStrychnosVinca AlkaloidsakuammicineAlcohol DehydrogenaseAlkaloidsBiological ProductsCytochrome P-450 Enzyme SystemIndolesIsoenzymesPlant ProteinsstrictosidineVinca Alkaloids

Identifiers

PMID28827772
PMCPMC5566405
OpenAlexW2746450705

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.