Evidence map›Paper›PMID 35785499›Full record

ArticleMolecular microbiology2022

Localization and interaction studies of the Salmonella enterica ethanolamine ammonia-lyase (EutBC), its reactivase (EutA), and the EutT corrinoid adenosyltransferase.

Flavia G Costa, Jorge C Escalante-Semerena

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. IntegrativemSystems · 2024
    Article
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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

2 authors at 1 institution in 1 country.

Flavia G CostaDepartment of Microbiology, University of Georgia, Athens, Georgia, USA.ORCID 0000-0001-7058-6009
Jorge C Escalante-SemerenaDepartment of Microbiology, University of Georgia, Athens, Georgia, USA.ORCID 0000-0001-7428-2811
University of Georgia · US

Funding

Analysis of the Metabolic Capabilities of Prokaryotic CellsR35GM130399 · NIGMS · UNIVERSITY OF GEORGIA · PI JORGE C ESCALANTE · 2019 to 2026
$5.5M
Studies of metal-containing and metal-less EutT adenosyltransferasesF31GM122394 · NIGMS · UNIVERSITY OF GEORGIA · PI COSTA, FLAVIA GISELA · 2017 to 2020
$176k
NIGMS NIH HHS F31 GM122394NIGMS NIH HHS R35 GM130399
6 · The paper itself

Abstract

Some prokaryotes compartmentalize select metabolic capabilities. Salmonella enterica subspecies enterica serovar Typhimurium LT2 (hereafter S. Typhimurium) catabolizes ethanolamine (EA) within a proteinaceous compartment that we refer to as the ethanolamine utilization (Eut) metabolosome. EA catabolism is initiated by the adenosylcobalamin (AdoCbl)-dependent ethanolamine ammonia-lyase (EAL), which deaminates EA via an adenosyl radical mechanism to yield acetaldehyde plus ammonia. This adenosyl radical can be quenched, requiring the replacement of AdoCbl by the ATP-dependent EutA reactivase. During growth on ethanolamine, S. Typhimurium synthesizes AdoCbl from cobalamin (Cbl) using the ATP:Co(I)rrinoid adenosyltransferase (ACAT) EutT. It is known that EAL localizes to the metabolosome, however, prior to this work, it was unclear where EutA and EutT localized, and whether they interacted with EAL. Here, we provide evidence that EAL, EutA, and EutT localize to the Eut metabolosome, and that EutA interacts directly with EAL. We did not observe interactions between EutT and EAL nor between EutT and the EutA/EAL complex. However, growth phenotypes of a ΔeutT mutant strain show that EutT is critical for efficient ethanolamine catabolism. This work provides a preliminary understanding of the dynamics of AdoCbl synthesis and its uses within the Eut metabolosome.

Indexed as

Ethanolamine Ammonia-LyaseSalmonella entericaAdenosine TriphosphateCobamidesEthanolamineSalmonella typhimuriumAdenosine TriphosphateCobamidesEthanolamineEthanolamine Ammonia-Lyasebacterial microcompartmentsethanolamine ammonia-lyaseethanolamine catabolismEutA reactivaseEutT corrinoid adenosyltransferaseprotein-protein interactions

Identifiers

PMID35785499
PMCPMC9481676
OpenAlexW4283812786

What OpenQuestion holds

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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.