Evidence map›Paper›PMID 10894724›Full record

ArticleJournal of bacteriology2000

Regulation of acetyl coenzyme A synthetase in Escherichia coli.

S Kumari, C M Beatty, D F Browning, S J Busby, E J Simel, G Hovel-Miner, A J Wolfe

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
4.3field-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

101 citing papers in PubMed, 226 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Metabolic Engineering ofACS synthetic biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Engineering in life sciences · 2023
    Article
  11. Article
  12. Adaptive laboratory evolution ofFrontiers in microbiology · 2023
    Article
  13. Article
  14. Coordinated expression of acetyl CoA synthetase and theMicrobiology (Reading, England) · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

41 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 2 countries.

S KumariDepartment of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, Maywood, Illinois 60153, USA.
C M Beatty
D F Browning
S J Busby
E J Simel
G Hovel-Miner
A J Wolfe
Loyola University Chicago · USUniversity of Birmingham · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cells of Escherichia coli growing on sugars that result in catabolite repression or amino acids that feed into glycolysis undergo a metabolic switch associated with the production and utilization of acetate. As they divide exponentially, these cells excrete acetate via the phosphotransacetylase-acetate kinase pathway. As they begin the transition to stationary phase, they instead resorb acetate, activate it to acetyl coenzyme A (acetyl-CoA) by means of the enzyme acetyl-CoA synthetase (Acs) and utilize it to generate energy and biosynthetic components via the tricarboxylic acid cycle and the glyoxylate shunt, respectively. Here, we present evidence that this switch occurs primarily through the induction of acs and that the timing and magnitude of this induction depend, in part, on the direct action of the carbon regulator cyclic AMP receptor protein (CRP) and the oxygen regulator FNR. It also depends, probably indirectly, upon the glyoxylate shunt repressor IclR, its activator FadR, and many enzymes involved in acetate metabolism. On the basis of these results, we propose that cells induce acs, and thus their ability to assimilate acetate, in response to rising cyclic AMP levels, falling oxygen partial pressure, and the flux of carbon through acetate-associated pathways.

Indexed as

Escherichia coli ProteinsAcetate-CoA LigaseBacterial ProteinsBinding SitesCyclic AMPCyclic AMP Receptor ProteinDNA-Binding ProteinsEnzyme InductionEscherichia coliGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicIron-Sulfur ProteinsModels, ChemicalOxygenPartial PressureTranscription FactorsAcetate-CoA LigaseBacterial ProteinsCyclic AMPCyclic AMP Receptor ProteinDNA-Binding ProteinsEscherichia coli ProteinsFNR protein, E coliIron-Sulfur ProteinsOxygenTranscription Factors

Identifiers

PMID10894724
PMCPMC101899
OpenAlexW2168076793

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.