Evidence map›Paper›PMID 35618928›Full record

ArticleNature chemical biology2022

Biosynthesis of cyanobacterin, a paradigm for furanolide core structure assembly.

Paul M D'Agostino, Catharina J Seel, Xiaoqi Ji, Tanja Gulder, Tobias A M Gulder

Abstract read
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In one paragraph

Article in Nature chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

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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

5 authors at 3 institutions in 1 country.

Paul M D'Agostino *Technische Universität Dresden, Chair of Technical Biochemistry, Dresden, Germany.ORCID http://orcid.org/0000-0002-8323-5416
Catharina J Seel *Biomimetic Catalysis, Department of Chemistry and Catalysis Research Center (CRC), Technische Universität München, Garching bei München, Germany.
Xiaoqi JiTechnische Universität Dresden, Chair of Technical Biochemistry, Dresden, Germany.
Tanja GulderBiomimetic Catalysis, Department of Chemistry and Catalysis Research Center (CRC), Technische Universität München, Garching bei München, Germany. tanja.gulder@uni-leipzig.de.ORCID http://orcid.org/0000-0003-4870-2266
Tobias A M GulderTechnische Universität Dresden, Chair of Technical Biochemistry, Dresden, Germany. tobias.gulder@tu-dresden.de.ORCID http://orcid.org/0000-0001-6013-3161
Leipzig University of Applied Sciences · DETechnische Universität Dresden · DEKlinikum Leverkusen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The γ-butyrolactone motif is found in many natural signaling molecules and other specialized metabolites. A prominent example is the potent aquatic phytotoxin cyanobacterin, which has a highly functionalized γ-butyrolactone core structure. The enzymatic machinery that assembles cyanobacterin and structurally related natural products (herein termed furanolides) has remained elusive for decades. Here, we elucidate the biosynthetic process of furanolide assembly. The cyanobacterin biosynthetic gene cluster was identified by targeted bioinformatic screening and validated by heterologous expression in Escherichia coli. Full functional evaluation of the recombinant key enzymes in vivo and in vitro, individually and in concert, provided in-depth mechanistic insights into a streamlined C-C bond-forming cascade that involves installation of compatible reactivity at seemingly unreactive Cα positions of amino acid precursors. Our work extends the biosynthetic and biocatalytic toolbox for γ-butyrolactone formation, provides a general paradigm for furanolide biosynthesis and sets the stage for their targeted discovery, biosynthetic engineering and enzymatic synthesis.

Indexed as

4-ButyrolactoneBiological ProductsEscherichia coliMultigene Family4-ButyrolactoneBiological Productscyanobacterin

Identifiers

PMID35618928
OpenAlexW4281553480

What OpenQuestion holds

Textmetadata
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.