Evidence map›Paper›PMID 37881531›Full record

ArticleNature catalysis2023

The catalytic role of glutathione transferases in heterologous anthocyanin biosynthesis.

Michael Eichenberger, Thomas Schwander, Sean Hüppi, Jan Kreuzer, Peer R E Mittl, Francesca Peccati, Gonzalo Jiménez-Osés, Michael Naesby, Rebecca M Buller

Open access · hybridAbstract read
In one paragraph

Article in Nature catalysis, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
10.2field-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

33 citing papers in PubMed, 64 citations in OpenAlex.

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  18. The Light-RegulatedInternational journal of molecular sciences · 2025
    Article
  19. Article
  20. Overlooked and misunderstood: can glutathione conjugates be clues to understanding plant glutathione transferases?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    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

9 authors at 4 institutions in 3 countries.

Michael EichenbergerCompetence Center for Biocatalysis, Zurich University of Applied Sciences, Wädenswil, Switzerland.
Thomas SchwanderCompetence Center for Biocatalysis, Zurich University of Applied Sciences, Wädenswil, Switzerland.ORCID 0000-0001-9201-3017
Sean HüppiCompetence Center for Biocatalysis, Zurich University of Applied Sciences, Wädenswil, Switzerland.ORCID 0000-0002-8310-9364
Jan KreuzerCompetence Center for Biocatalysis, Zurich University of Applied Sciences, Wädenswil, Switzerland.
Peer R E MittlDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID 0000-0002-3348-3147
Francesca PeccatiCenter for Cooperative Research in Biosciences, Basque Research and Technology Alliance, Derio, Spain.
Gonzalo Jiménez-OsésCenter for Cooperative Research in Biosciences, Basque Research and Technology Alliance, Derio, Spain.ORCID 0000-0003-0105-4337
Michael NaesbyLantana Bio, Toulouse, France.ORCID 0000-0001-9422-3077
Rebecca M BullerCompetence Center for Biocatalysis, Zurich University of Applied Sciences, Wädenswil, Switzerland.ORCID 0000-0002-5997-1616
ZHAW Zurich University of Applied Sciences · CHCIC bioGUNE · ESIkerbasque · ESUniversity of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Anthocyanins are ubiquitous plant pigments used in a variety of technological applications. Yet, after over a century of research, the penultimate biosynthetic step to anthocyanidins attributed to the action of leucoanthocyanidin dioxygenase has never been efficiently reconstituted outside plants, preventing the construction of heterologous cell factories. Through biochemical and structural analysis, here we show that anthocyanin-related glutathione transferases, currently implicated only in anthocyanin transport, catalyse an essential dehydration of the leucoanthocyanidin dioxygenase product, flavan-3,3,4-triol, to generate cyanidin. Building on this knowledge, introduction of anthocyanin-related glutathione transferases into a heterologous biosynthetic pathway in baker's yeast results in >35-fold increased anthocyanin production. In addition to unravelling the long-elusive anthocyanin biosynthesis, our findings pave the way for the colourants' heterologous microbial production and could impact the breeding of industrial and ornamental plants.

Indexed as

BiocatalysisMechanism of actionSynthetic biologyX-ray crystallography

Identifiers

PMID37881531
PMCPMC10593608
OpenAlexW4386325035

What OpenQuestion holds

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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.