Evidence map›Paper›PMID 15489439›Full record

ArticleJournal of bacteriology2004

The N-acetyl-D-glucosamine kinase of Escherichia coli and its role in murein recycling.

Tsuyoshi Uehara, James T Park

Abstract read
In one paragraph

Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Uridine diphosphateFEMS microbes · 2026
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  4. Evaluation and Comparison ofBiochemistry · 2025
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  6. Carbapenem-ResistantbioRxiv : the preprint server for biology · 2024
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  7. Review
  8. Article
  9. Article
  10. Production ofSynthetic and systems biotechnology · 2023
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  12. Frontiers in microbiology · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The basis for non-canonical ROK family function in theThe Journal of biological chemistry · 2020
    Article
  18. Activity of Tracheal Cytotoxin ofFrontiers in cellular and infection microbiology · 2020
    Article
  19. Structural and functional determination of homologs of theThe Journal of biological chemistry · 2018
    Article
  20. ThemBio · 2017
    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

2 authors at 1 institution in 1 country.

Tsuyoshi UeharaDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111. tsuyoshi.uehara@tufts.edu
James T Park
Tufts University · US

Funding

MUROPEPTIDE RECYCLING PATHWAY &BETA LACTAMASE INDUCTIONR01GM051610 · NIGMS · TUFTS UNIVERSITY BOSTON · PI PARK, JAMES T · 1996 to 2006
$975k
NIGMS NIH HHS GM 51610NIGMS NIH HHS R01 GM051610
6 · The paper itself

Abstract

N-acetyl-D-glucosamine (GlcNAc) is a major component of bacterial cell wall murein and the lipopolysaccharide of the outer membrane. During growth, over 60% of the murein of the side wall is degraded, and the major products, GlcNAc-anhydro-N-acetylmuramyl peptides, are efficiently imported into the cytoplasm and cleaved to release GlcNAc, anhydro-N-acetylmuramic acid, murein tripeptide (L-Ala-D-Glu-meso-diaminopimelic acid), and D-alanine. Like murein tripeptide, GlcNAc is readily recycled, and this process was thought to involve phosphorylation, since GlcNAc-6-phosphate (GlcNAc-6-P) is efficiently used to synthesize murein or lipopolysaccharide or can be metabolized by glycolysis. Since the gene for GlcNAc kinase had not been identified, in this work we purified GlcNAc kinase (NagK) from Escherichia coli cell extracts and identified the gene by determining the N-terminal sequence of the purified kinase. A nagK deletion mutant lacked phosphorylated GlcNAc in its cytoplasm, and the cell extract of the mutant did not phosphorylate GlcNAc, indicating that NagK is the only GlcNAc kinase expressed in E. coli. Unexpectedly, GlcNAc did not accumulate in a nagK nagEBACD mutant, though both GlcNAc and GlcNAc-6-P accumulate in the nagEBACD mutant, suggesting the existence of an alternative pathway (presumably repressed by GlcNAc-6-P) that reutilizes GlcNAc without the involvement of NagK.

Indexed as

AcetylglucosamineCytoplasmEscherichia coliEscherichia coli ProteinsMutationPeptidoglycanPhosphotransferases (Alcohol Group Acceptor)Substrate SpecificityAcetylglucosamineEscherichia coli ProteinsN-acetylglucosamine kinasePeptidoglycanPhosphotransferases (Alcohol Group Acceptor)

Identifiers

PMID15489439
PMCPMC523203
OpenAlexW2134632174

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.