Evidence map›Paper›PMID 23585538›Full record

ArticleJournal of bacteriology2013

Evidence that a metabolic microcompartment contains and recycles private cofactor pools.

Douglas L Huseby, John R Roth

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

45 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
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  5. Electrochemical NAD+ regeneration in bacterial organelles.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. IntegrativemSystems · 2024
    Article
  8. Review
  9. Article
  10. Transcriptomic and phenotype analysis revealed the role ofFrontiers in cellular and infection microbiology · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. 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.

Douglas L HusebyDepartment of Microbiology, University of California, Davis, Davis, California, USA.
John R Roth
University of California, Davis · US

Funding

GENETIC ANALYSIS OF BACTERIAL CHROMSOME STRUCTURER01GM027068 · NIGMS · UNIVERSITY OF UTAH · PI ROTH, JOHN R · 1985 to 2018
$8.9M
The Salmonella biochemistry of inflammationR21AI088122 · NIAID · UNIVERSITY OF CALIFORNIA AT DAVIS · PI BAUMLER, ANDREAS J · 2010 to 2011
$410k
ACQUISITION OF 500 MHZ NMR SPECTROMETERS10RR011973 · NCRR · UNIVERSITY OF CALIFORNIA DAVIS · PI LA MAR, GERD N · 1997 to 1997
–
NCRR NIH HHS NIH RR11973NCRR NIH HHS S10 RR011973NIAID NIH HHS AI088122NIAID NIH HHS R21 AI088122NIGMS NIH HHS GM27068NIGMS NIH HHS R01 GM027068
6 · The paper itself

Abstract

Microcompartments are loose protein cages that encapsulate enzymes for particular bacterial metabolic pathways. These structures are thought to retain and perhaps concentrate pools of small, uncharged intermediates that would otherwise diffuse from the cell. In Salmonella enterica, a microcompartment encloses enzymes for ethanolamine catabolism. The cage has been thought to retain the volatile intermediate acetaldehyde but allow diffusion of the much larger cofactors NAD and coenzyme A (CoA). Genetic tests support an alternative idea that the microcompartment contains and recycles private pools of the large cofactors NAD and CoA. Two central enzymes convert ethanolamine to acetaldehyde (EutBC) and then to acetyl-CoA (EutE). Two seemingly peripheral redundant enzymes encoded by the eut operon proved to be essential for ethanolamine utilization, when subjected to sufficiently stringent tests. These are EutD (acetyl-CoA to acetyl phosphate) and EutG (acetaldehyde to ethanol). Obligatory recycling of cofactors couples the three reactions and drives acetaldehyde consumption. Loss and toxic effects of acetaldehyde are minimized by accelerating its consumption. In a eutD mutant, acetyl-CoA cannot escape the compartment but is released by mutations that disrupt the structure. The model predicts that EutBC (ethanolamine-ammonia lyase) lies outside the compartment, using external coenzyme B12 and injecting its product, acetaldehyde, into the lumen, where it is degraded by the EutE, EutD, and EutG enzymes using private pools of CoA and NAD. The compartment appears to allow free diffusion of the intermediates ethanol and acetyl-PO4 but (to our great surprise) restricts diffusion of acetaldehyde.

Indexed as

Metabolic Networks and PathwaysAcetaldehydeAcetyl Coenzyme ABacterial ProteinsCoenzyme ACoenzymesEthanolamineModels, BiologicalNADSalmonella entericaAcetaldehydeAcetyl Coenzyme ABacterial ProteinsCoenzyme ACoenzymesEthanolamineNAD

Identifiers

PMID23585538
PMCPMC3697265
OpenAlexW2160991221

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.