Evidence map›Paper›PMID 28504677›Full record

ArticleNature chemical biology2017

β-Lactone formation during product release from a nonribosomal peptide synthetase.

Jason E Schaffer, Margaret R Reck, Neha K Prasad, Timothy A Wencewicz

Abstract read
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Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
–field-weighted citation impact
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

58 citing papers in PubMed.

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  16. Natural Products That Contain Higher Homologated Amino Acids.Chembiochem : a European journal of chemical biology · 2024
    Review
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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

4 authors.

Jason E SchafferDepartment of Chemistry, Washington University in St. Louis, St. Louis, Missouri, USA.
Margaret R ReckDepartment of Chemistry, Washington University in St. Louis, St. Louis, Missouri, USA.
Neha K PrasadDepartment of Chemistry, Washington University in St. Louis, St. Louis, Missouri, USA.
Timothy A WencewiczDepartment of Chemistry, Washington University in St. Louis, St. Louis, Missouri, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nonribosomal peptide synthetases (NRPSs) are multidomain modular biosynthetic assembly lines that polymerize amino acids into a myriad of biologically active nonribosomal peptides (NRPs). NRPS thioesterase (TE) domains employ diverse release strategies for off-loading thioester-tethered polymeric peptides from termination modules typically via hydrolysis, aminolysis, or cyclization to provide mature antibiotics as carboxylic acids/esters, amides, and lactams/lactones, respectively. Here we report the enzyme-catalyzed formation of a highly strained β-lactone ring during TE-mediated cyclization of a β-hydroxythioester to release the antibiotic obafluorin (Obi) from an NRPS assembly line. The Obi NRPS (ObiF) contains a type I TE domain with a rare catalytic cysteine residue that plays a direct role in β-lactone ring formation. We present a detailed genetic and biochemical characterization of the entire Obi biosynthetic gene cluster in plant-associated Pseudomonas fluorescens ATCC 39502 that establishes a general strategy for β-lactone biogenesis.

Indexed as

Anti-Bacterial AgentsBiocatalysisLactonesPeptide SynthasesPseudomonas fluorescensAnti-Bacterial AgentsLactonesnon-ribosomal peptide synthaseobafluorinPeptide Synthases

Identifiers

PMID28504677

What OpenQuestion holds

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Registered trials

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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.