Kinetic features of L,D-transpeptidase inactivation critical for β-lactam antibacterial activity (Q28534519)

7

Mélanie Ethève-Quelquejeu

0 references

Jean-Emmanuel Hugonnet

Jean-Emmanuel Hugonnet

11

0 references

Jean-Luc Mainardi

Jean-Luc Mainardi

5

0 references

Michel Arthur

Michel Arthur

13

0 references

Vincent Dubée

Vincent Dubée

2

1 reference

ORCID Public Data File 2021

author name string

Sébastien Triboulet

1

0 references

Lauriane Lecoq

3

0 references

Catherine Bougault

4

0 references

Louis B Rice

6

0 references

Mélanie Ethève-Quelquejeu

7

0 references

Laurent Gutmann

8

0 references

Arul Marie

9

0 references

Lionel Dubost

10

0 references

Jean-Pierre Simorre

Creative Commons Attribution 4.0 International

12

0 references

language of work or name

English

0 references

publication date

2013

0 references

published in

PLOS One

0 references

volume

8

0 references

issue

7

0 references

page(s)

e67831

0 references

copyright license

start time

4 July 2013

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

0 references

cites work

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Structure of Enterococcus faecium l , d -Transpeptidase Acylated by Ertapenem Provides Insight into the Inactivation Mechanism

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Structural basis for the inhibition ofMycobacterium tuberculosisL,D-transpeptidase by meropenem, a drug effective against extensively drug-resistant strains

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Targeting the Cell Wall of Mycobacterium tuberculosis: Structure and Mechanism of L,D-Transpeptidase 2

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Dynamics induced by β-lactam antibiotics in the active site of Bacillus subtilis L,D-transpeptidase

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Meropenem-Clavulanate Is Effective Against Extensively Drug-Resistant Mycobacterium tuberculosis

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The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L,D-transpeptidation

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Novel mechanism of beta-lactam resistance due to bypass of DD-transpeptidation in Enterococcus faecium

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Inactivation of Mycobacterium tuberculosis l,d-transpeptidase LdtMt₁ by carbapenems and cephalosporins

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Clostridium difficile has an original peptidoglycan structure with a high level of N-acetylglucosamine deacetylation and mainly 3-3 cross-links

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Inactivation kinetics of a new target of beta-lactam antibiotics

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The peptidoglycan of Mycobacterium abscessus is predominantly cross-linked by L,D-transpeptidases

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The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin.

29 September 2017

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Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine

29 September 2017

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Effects of nucleophiles on the breakdown of the benzylpenicilloyl–enzyme complex EI formed between benzylpenicillin and the exocellular DD-carboxypeptidase–transpeptiase of Streptomyces strain R61

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A novel peptidoglycan cross-linking enzyme for a beta-lactam-resistant transpeptidation pathway

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Balance between two transpeptidation mechanisms determines the expression of beta-lactam resistance in Enterococcus faecium

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Unexpected Inhibition of Peptidoglycan LD-Transpeptidase fromEnterococcus faeciumby the β-Lactam Imipenem

21 January 2018

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Crystal Structure of a Novel β-Lactam-insensitive Peptidoglycan Transpeptidase

21 January 2018

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Fighting resistant tuberculosis with old compounds: the carbapenem paradigm

21 January 2018

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Fate of thiazolidine ring during fragmentation of penicillin by exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23861815

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1371/JOURNAL.PONE.0067831

1 reference

ADS bibcode

2013PLoSO...867831T

0 references

1 reference

1 reference

PubMed publication ID

23861815

1 reference