Evidence map›Paper›PMID 27010356›Full record

ArticleMolecular microbiology2016

L-2,3-diaminopropionate generates diverse metabolic stresses in Salmonella enterica.

Dustin C Ernst, Mary E Anderson, Diana M Downs

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  4. RidA proteins contribute to fitness ofMicrobial cell (Graz, Austria) · 2024
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  5. Review
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  9. RidA Proteins Protect against Metabolic Damage by Reactive Intermediates.Microbiology and molecular biology reviews : MMBR · 2020
    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

3 authors at 1 institution in 1 country.

Dustin C ErnstDepartment of Microbiology, University of Georgia, Athens, GA, 30602-2605, USA.
Mary E AndersonDepartment of Microbiology, University of Georgia, Athens, GA, 30602-2605, USA.
Diana M DownsDepartment of Microbiology, University of Georgia, Athens, GA, 30602-2605, USA.
University of Georgia · US

Funding

Rid family members neutralize endogenous metabolic stressorsR01GM095837 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DOWNS, DIANA M. · 2011 to 2023
$3.7M
NIGMS NIH HHS R01 GM095837
6 · The paper itself

Abstract

Unchecked amino acid accumulation in living cells has the potential to cause stress by disrupting normal metabolic processes. Thus, many organisms have evolved degradation strategies that prevent endogenous accumulation of amino acids. L-2,3-diaminopropionate (Dap) is a non-protein amino acid produced in nature where it serves as a precursor to siderophores, neurotoxins and antibiotics. Dap accumulation in Salmonella enterica was previously shown to inhibit growth by unknown mechanisms. The production of diaminopropionate ammonia-lyase (DpaL) alleviated Dap toxicity in S. enterica by catalyzing the degradation of Dap to pyruvate and ammonia. Here, we demonstrate that Dap accumulation in S. enterica elicits a proline requirement for growth and specifically inhibits coenzyme A and isoleucine biosynthesis. Additionally, we establish that the DpaL-dependent degradation of Dap to pyruvate proceeds through an unbound 2-aminoacrylate (2AA) intermediate, thus contributing to 2AA stress inside the cell. The reactive intermediate deaminase, RidA, is shown to prevent 2AA damage caused by DpaL-dependent Dap degradation by enhancing the rate of 2AA hydrolysis. The results presented herein inform our understanding of the effects Dap has on metabolism in S. enterica, and likely other organisms, and highlight the critical role played by RidA in preventing 2AA stress stemming from Dap detoxification.

Indexed as

Amino AcidsAminohydrolasesAmmonia-LyasesBacterial ProteinsProlinePyruvic AcidSalmonella entericaStress, PhysiologicalAmino AcidsAminohydrolasesAmmonia-LyasesBacterial Proteinsdiaminopropionate ammonia-lyaseProlinePyruvic Acid

Identifiers

PMID27010356
PMCPMC5384650
OpenAlexW2311209919

What OpenQuestion holds

Textmetadata
LicenceTDM
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.