Evidence map›Paper›PMID 36044980›Full record

ArticleACS chemical biology2022

Proof-Reading Thioesterase Boosts Activity of Engineered Nonribosomal Peptide Synthetase.

Farzaneh Pourmasoumi, Sayantan De, Huiyun Peng, Felix Trottmann, Christian Hertweck, Hajo Kries

Open access · bronzeAbstract read
In one paragraph

Article in ACS chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed, 25 citations in OpenAlex.

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  8. A discrete intermediate for the biosynthesis of both the enediyne core and the anthraquinone moiety of enediyne natural products.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

6 authors at 1 institution in 1 country.

Farzaneh PourmasoumiIndependent Junior Research Group Biosynthetic Design of Natural Products, Leibniz Institute for Natural Product Research and Infection Biology e.V., Hans Knöll Institute (HKI Jena), Beutenbergstr. 11a, 07745 Jena, Germany.
Sayantan DeIndependent Junior Research Group Biosynthetic Design of Natural Products, Leibniz Institute for Natural Product Research and Infection Biology e.V., Hans Knöll Institute (HKI Jena), Beutenbergstr. 11a, 07745 Jena, Germany.ORCID 0000-0001-8683-3836
Huiyun PengIndependent Junior Research Group Biosynthetic Design of Natural Products, Leibniz Institute for Natural Product Research and Infection Biology e.V., Hans Knöll Institute (HKI Jena), Beutenbergstr. 11a, 07745 Jena, Germany.
Felix TrottmannBiomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology e.V., Hans Knöll Institute (HKI Jena), Beutenbergstr. 11a, 07745 Jena, Germany.
Christian HertweckBiomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology e.V., Hans Knöll Institute (HKI Jena), Beutenbergstr. 11a, 07745 Jena, Germany.
Hajo KriesIndependent Junior Research Group Biosynthetic Design of Natural Products, Leibniz Institute for Natural Product Research and Infection Biology e.V., Hans Knöll Institute (HKI Jena), Beutenbergstr. 11a, 07745 Jena, Germany.ORCID 0000-0002-4919-2811
Leibniz-Institut für Naturstoff-Forschung und Infektionsbiologie e. V. - Hans-Knöll-Institut (HKI) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nonribosomal peptide synthetases (NRPSs) are a vast source of valuable natural products, and re-engineering them is an attractive path toward structurally diversified active compounds. NRPS engineering often requires heterologous expression, which is hindered by the enormous size of NRPS proteins. Protein splitting and docking domain insertion have been proposed as a strategy to overcome this limitation. Here, we have applied the splitting strategy to the gramicidin S NRPS: Despite better production of the split proteins, gramicidin S production almost ceased. However, the addition of type II thioesterase GrsT boosted production. GrsT is an enzyme encoded in the gramicidin S biosynthetic gene cluster that we have produced and characterized for this purpose. We attribute the activity enhancement to the removal of a stalled intermediate from the split NRPS that is formed due to misinitiation. These results highlight type II thioesterases as useful tools for NRPS engineering.

Indexed as

Biological ProductsGramicidinMultigene FamilyPeptide SynthasesBiological ProductsGramicidinnon-ribosomal peptide synthasePeptide Synthases

Identifiers

PMID36044980
PMCPMC9486807
OpenAlexW4294124094

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.