Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Role of MurT C-Terminal Domain in the Amidation of Staphylococcus aureus Peptidoglycan

26 Jul 2019

Abstract excerpt

Glutamate amidation, a secondary modification of the peptidoglycan, was first identified in Staphylococcus aureus . It is catalyzed by the protein products of the murT and gatD genes, which are conserved and colocalized in the genomes of most sequenced Gram-positive bacterial species. The MurT-GatD complex is required for cell viability, full resistance to β-lactam antibiotics, and resistance to human lysozyme...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antimicrobial Resistance in Staphylococcus
Share to Bacterial Genetics and Biotechnology
Share to Bacteriophages and microbial interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 31358586
DOI: 10.1128/aac.00957-19

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of MurT C-Terminal Domain in the Amidation of Staphylococcus aureus PeptidoglycanPMID 31358586Read ↗

Identification and in vitro analysis of the GatD/MurT enzyme-complex catalyzing lipid II amidation in Staphylococcus aureus.Semantic proximity Read ↗

Cloning and sequencing of Staphylococcus aureus murC, a gene essential for cell wall biosynthesis.Semantic proximity Read ↗

Inactivation of the monofunctional peptidoglycan glycosyltransferase SgtB allows <i>Staphylococcus aureus</i> to survive in the absence of lipoteichoic acidSemantic proximity Read ↗

A modified BCG with depletion of enzymes associated with peptidoglycan amidation induces enhanced protection against tuberculosis in miceSemantic proximity Read ↗

Molecular Basis of Resistance to Muramidase and Cationic Antimicrobial Peptide Activity of Lysozyme in StaphylococciSemantic proximity Read ↗

Functional Characterization of the N-Acetylmuramyl-l-Alanine Amidase, Ami1, from Mycobacterium abscessus.Semantic proximity Read ↗

A Molecular Link between Cell Wall Modification and Stringent Response in a Gram-positive BacteriaSemantic proximity Read ↗

Characterization of Substrate Distribution and Functional Implication of Lysine Acylations in Staphylococcus aureusSemantic proximity Read ↗

A modified BCG with depletion of enzymes associated with peptidoglycan amidation induces enhanced protection against tuberculosis in miceSemantic proximity Read ↗

Structure and cell wall cleavage by modular lytic transglycosylase MltC of Escherichia coli.Semantic proximity Read ↗

Insights into the central role of N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU) in peptidoglycan metabolism and its potential as a therapeutic targetSemantic proximity Read ↗

Purification and biochemical characterization of Mur ligases from Staphylococcus aureus.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.