Evidence map›Paper›PMID 21947170›Full record

ArticleArchives of microbiology2012

N-acetylglucosamine-6-phosphate deacetylase (NagA) of Listeria monocytogenes EGD, an essential enzyme for the metabolism and recycling of amino sugars.

Magdalena Popowska, Magdalena Osińska, Magdalena Rzeczkowska

Open access · hybridAbstract read
In one paragraph

Article in Archives of microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.0field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 55 citations in OpenAlex.

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  16. Chitin Attenuates Expression ofFrontiers in microbiology · 2020
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  17. Article
  18. Review
  19. Article
  20. Regulatory network features in Listeria monocytogenes-changing the way we talk.Frontiers in cellular and infection microbiology · 2014
    Review
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.

Magdalena PopowskaDepartment of Applied Microbiology, Institute of Microbiology, Faculty of Biology, University of Warsaw, Poland. magdapop@biol.uw.edu.pl
Magdalena Osińska
Magdalena Rzeczkowska
University of Warsaw · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The main aim of our study was to determine the physiological function of NagA enzyme in the Listeria monocytogenes cell. The primary structure of the murein of L. monocytogenes is very similar to that of Escherichia coli, the main differences being amidation of diaminopimelic acid and partial de-N-acetylation of glucosamine residues. NagA is needed for the deacetylation of N-acetyl-glucosamine-6 phosphate to glucosamine-6 phosphate and acetate. Analysis of the L. monocytogenes genome reveals the presence of two proteins with NagA domain, Lmo0956 and Lmo2108, which are cytoplasmic putative proteins. We introduced independent mutations into the structural genes for the two proteins. In-depth characterization of one of these mutants, MN1, deficient in protein Lmo0956 revealed strikingly altered cell morphology, strongly reduced cell wall murein content and decreased sensitivity to cell wall hydrolase, mutanolysin and peptide antibiotic, colistin. The gene products of operon 150, consisting of three genes: lmo0956, lmo0957, and lmo0958, are necessary for the cytosolic steps of the amino-sugar-recycling pathway. The cytoplasmic de-N-acetylase Lmo0956 of L. monocytogenes is required for cell wall peptidoglycan and teichoic acid biosynthesis and is also essential for bacterial cell growth, cell division, and sensitivity to cell wall hydrolases and peptide antibiotics.

Indexed as

AcetylglucosamineAmidohydrolasesBacterial ProteinsCell WallColistinEndopeptidasesEscherichia coliGlucosamineGlucose-6-PhosphateListeria monocytogenesMutagenesis, InsertionalOperonPeptidoglycanProtein Structure, TertiaryTeichoic AcidsAcetylglucosamineAmidohydrolasesBacterial ProteinsColistinEndopeptidasesGlucosamineglucosamine 6-phosphateGlucose-6-PhosphatemutanolysinN-acetylglucosamine-6-phosphate deacetylasePeptidoglycanTeichoic Acids

Identifiers

PMID21947170
PMCPMC3304070
OpenAlexW1983770647

What OpenQuestion holds

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LicenceCC BY-NC
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.