Evidence map›Paper›PMID 23672516›Full record

ArticleJournal of the American Chemical Society2013

Mechanistic insights into the LsrK kinase required for autoinducer-2 quorum sensing activation.

Jie Zhu, Mark S Hixon, Daniel Globisch, Gunnar F Kaufmann, Kim D Janda

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Kaempferol restores the susceptibility of ESBLsFrontiers in microbiology · 2024
    Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. LsrF, a coenzyme A-dependent thiolase, catalyzes the terminal step in processing the quorum sensing signal autoinducer-2.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  15. Article
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

5 authors at 2 institutions in 2 countries.

Jie ZhuThe Skaggs Institute for Chemical Biology and Department of Chemistry and the Worm Institute for Research and Medicine (WIRM), the Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California, 92037, USA.
Mark S Hixon
Daniel Globisch
Gunnar F Kaufmann
Kim D Janda
Scripps Research Institute · USTakeda (United States) · US

Funding

Chemical Strategies to Manipulate A1-2 Signaling in Bacterial PathogensR01AI077644 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI JANDA, KIM · 2010 to 2014
$2.3M
NIAID NIH HHS AI077644NIAID NIH HHS R01 AI077644
6 · The paper itself

Abstract

In enteric bacteria, the kinase LsrK catalyzes the phosphorylation of the C5-hydroxyl group in the linear form of 4,5-dihydroxy-2,3-pentanedione (DPD), the precursor of the type II bacterial quorum sensing molecule (AI-2). This phosphorylation is required for AI-2 sequestration in the cytoplasm and subsequent derepression of AI-2-related genes necessary for quorum development. While LsrK is a critical enzyme within the DPD quorum sensing relay system, kinetic details of this kinase have yet to be reported. A continuous UV-vis spectrophotometric assay was developed that allowed steady-state kinetic analysis of LsrK to be undertaken with the substrates ATP and DPD. The data was most consistent with a rapid equilibrium ordered mechanism with ATP binding first: kcat (7.4 ± 0.6 s(-1)), Km,ATP (150 ± 30 μM) and Km(app),DPD (1.0 ± 0.2 mM). The assay also allowed a DPD substrate profile to be conducted, which provided an unexpected biochemical disconnect between the previous agonist/antagonist cell-based reporter assay and the LsrK assay presented herein. Together these findings raise the importance of LsrK and lay the foundation not only for further understanding of this enzyme and its critical biological role but also for the rational design of regulatory molecules targeting AI-2 quorum sensing in pathogenic bacteria.

Indexed as

Quorum SensingAdenosine TriphosphateEscherichia coli ProteinsHomoserineKineticsLactonesNADPhosphotransferases (Alcohol Group Acceptor)Spectrophotometry, UltravioletAdenosine TriphosphateEscherichia coli ProteinsHomoserineLactonesLsrK protein, E coliNADN-octanoylhomoserine lactonePhosphotransferases (Alcohol Group Acceptor)

Identifiers

PMID23672516
PMCPMC3736694
OpenAlexW2007960517

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.