Evidence map›Paper›PMID 9287002›Full record

ArticleJournal of bacteriology1997

Outer membrane localization of murein hydrolases: MltA, a third lipoprotein lytic transglycosylase in Escherichia coli.

J Lommatzsch, M F Templin, A R Kraft, W Vollmer, J V Höltje

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

47 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
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  5. Revealing Cell Envelope Heterogeneity in Two StableInternational journal of molecular sciences · 2026
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  9. Measure of Peptidoglycan Degradation Activity.Methods in molecular biology (Clifton, N.J.) · 2024
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  17. Review
  18. Regulation of peptidoglycan synthesis and remodelling.Nature reviews. Microbiology · 2020
    Review
  19. Review
  20. 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 1 institution in 1 country.

J LommatzschAbteilung Biochemie, Max-Planck-Institut für Entwicklungsbiologie, Tübingen, Germany.
M F Templin
A R Kraft
W Vollmer
J V Höltje
Max Planck Institute for Developmental Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lytic transglycosylases are a unique lysozyme-like class of murein hydrolases believed to be important for growth of Escherichia coli. A membrane-bound lytic transglycosylase with an apparent molecular mass of 38 kDa, which was designated Mlt38, has previously been purified and characterized (A. Ursinus and J.-V. Höltje, J. Bacteriol. 176:338-343, 1994). On the basis of four tryptic peptides, the gene mltA was mapped at 63 min on the chromosomal map of E. coli K-12 and cloned by reverse genetics. The open reading frame was found to contain a typical lipoprotein consensus sequence, and the lipoprotein nature of the gene product was demonstrated by [3H]palmitate labeling. On the basis of the distribution of MltA in membrane fractions obtained by sucrose gradient centrifugation, a localization in the outer membrane is indicated. Overexpression of MltA at 30 degrees C, the optimal temperature for enzyme activity, but not at 37 degrees C results in the formation of spheroplasts. Not only a deletion mutant in mltA, but also double mutants in mltA and one of the two other well-characterized lytic transglycosylases (either sltY or mltB), as well as a triple mutant in all three enzymes, showed no obvious phenotype. However, dramatic changes in the structure of the murein sacculus indicate that lytic transglycosylases are involved in maturation of the murein sacculus.

Indexed as

Amino Acid SequenceBase SequenceCell MembraneCloning, MolecularEscherichia coliGenes, BacterialGlycosyltransferasesLipoproteinsMolecular Sequence DataOpen Reading FramesPeptide FragmentsPeptidoglycanRestriction MappingSequence Analysis, DNAGlycosyltransferasesLipoproteinsMltA protein, bacteriaPeptide FragmentsPeptidoglycan

Identifiers

PMID9287002
PMCPMC179418
OpenAlexW2118761676

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.