Evidence map›Paper›PMID 29515200›Full record

ArticleScientific reports2018

Mechanism of the Escherichia coli MltE lytic transglycosylase, the cell-wall-penetrating enzyme for Type VI secretion system assembly.

Byungjin Byun, Kiran V Mahasenan, David A Dik, Daniel R Marous, Enrico Speri, Malika Kumarasiri, Jed F Fisher, Juan A Hermoso, Shahriar Mobashery

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
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  3. A Concise Route to Orthogonally Protected Bulgecinine.The Journal of organic chemistry · 2026
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  15. Review
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  17. Unconventional Antibacterials and Adjuvants.Accounts of chemical research · 2021
    Article
  18. Article
  19. Article
  20. Constructing and deconstructing the bacterial cell wall.Protein science : a publication of the Protein Society · 2020
    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

9 authors at 2 institutions in 2 countries.

Byungjin ByunDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, United States.
Kiran V MahasenanDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, United States.
David A DikDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, United States.
Daniel R MarousDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, United States.
Enrico SperiDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, United States.
Malika KumarasiriDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, United States.
Jed F FisherDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, United States.
Juan A HermosoDepartment of Crystallography and Structural Biology, Instituto de Química-Física "Rocasolano", Consejo Superior de Investigaciones Científicas, 28006, Madrid, Spain.
Shahriar MobasheryDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, United States. mobashery@nd.edu.
University of Notre Dame · USInstituto de Química Física Blas Cabrera · ES

Funding

Penicillin-Binding Proteins, Mechanism and InhibitionR01GM061629 · NIGMS · WAYNE STATE UNIVERSITY · PI MOBASHERY, SHAHRIAR · 2001 to 2018
$5.1M
Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
NIGMS NIH HHS R01 GM061629NIGMS NIH HHS T32 GM075762
6 · The paper itself

Abstract

Lytic transglycosylases (LTs) catalyze the non-hydrolytic cleavage of the bacterial cell wall by an intramolecular transacetalization reaction. This reaction is critically and broadly important in modifications of the bacterial cell wall in the course of its biosynthesis, recycling, manifestation of virulence, insertion of structural entities such as the flagellum and the pili, among others. The first QM/MM analysis of the mechanism of reaction of an LT, that for the Escherichia coli MltE, is undertaken. The study reveals a conformational itinerary consistent with an oxocarbenium-like transition state, characterized by a pivotal role for the active-site glutamic acid in proton transfer. Notably, an oxazolinium intermediate, as a potential intermediate, is absent. Rather, substrate-assisted catalysis is observed through a favorable dipole provided by the N-acetyl carbonyl group of MurNAc saccharide. This interaction stabilizes the incipient positive charge development in the transition state. This mechanism coincides with near-synchronous acetal cleavage and acetal formation.

Indexed as

Models, MolecularCatalytic DomainCell WallEscherichia coliEscherichia coli ProteinsGlycosyltransferasesType VI Secretion SystemsEscherichia coli ProteinsGlycosyltransferasesMltE protein, E coliType VI Secretion Systems

Identifiers

PMID29515200
PMCPMC5841429
OpenAlexW2789376487

What OpenQuestion holds

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LicenceCC BY
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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.