Penicillin-binding proteins 5 and 6 of Escherichia coli have been identified as d-alanine carboxypeptidase IA.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC233099PMC
http://dx.doi.org/10.1128/jb.127.1.660-663.1976DOI Listing

Publication Analysis

Top Keywords

penicillin-binding proteins
8
proteins escherichia
8
escherichia coli
8
d-alanine carboxypeptidase
8
identification major
4
major penicillin-binding
4
coli d-alanine
4
carboxypeptidase penicillin-binding
4
coli identified
4
identified d-alanine
4

Similar Publications

Enterococcus faecalis is responsible for numerous serious infections, and treatment options often include ampicillin combined with an aminoglycoside or dual beta-lactam therapy with ampicillin and a third-generation cephalosporin. The mechanism of dual beta-lactam therapy relies on the saturation of penicillin-binding proteins (PBPs). Ceftobiprole exhibits high affinity binding to nearly all E.

View Article and Find Full Text PDF

Potential Antibacterial of Leaf Sirih Merah Against Enterococcus Faecalis ATCC 29212 Bacteria.

Comb Chem High Throughput Screen

January 2025

Department of Chemistry, Faculty of Mathematics and Natural Science, Universitas Padjadjaran, Sumedang, Indonesia.

Background: Dental root canal failure is a disease caused by gram-positive bacteria, Enterococcus faecalis. The disease is caused by the bacterial cell wall consisting of a peptidoglycan layer that protects the bacteria from internal osmotic pressure. Peptidoglycan biosynthesis includes many enzymes, such as MurA, Penicillin-binding protein (PBP), and SrtA.

View Article and Find Full Text PDF

In Silico Subtractive Proteome Analysis to Design Multi-Epitope-Based Subunit Vaccine against .

J Microbiol Biotechnol

November 2024

Fatemah AlMalki, Biology Department, College of Science and Humanities- Al Quwaiiyah, Shaqra University, Al Quwaiiyah 19257, Saudi Arabia.

is a gram-negative, facultatively anaerobic bacterium typically found in the oropharynx and respiratory tract of humans. It is responsible for various infections, including head-and-neck infections, pericarditis, and abscesses of the deltoid, perirenal tissue, brain, and liver. Increasing antibiotic resistance requires urgent identification of novel drug targets to fight this bacterium.

View Article and Find Full Text PDF

Purpose: To evaluate the clinical characteristics, antimicrobial resistance (AMR) phenotypes and genotypes, and homology features of carbapenem-resistant (CRAB) in intensive care unit (ICU) and to provide basis for effectively prevention, control and treatment of nosocomial infections caused by CRAB.

Methods: A total of 39 CRAB strains isolated from hospitalized patients in the ICU and neurosurgical ICU (NICU) between 2020 and 2023 were subjected to antimicrobial susceptibility testing and whole-genome sequencing (WGS). Virulence factor genes (VFGs), antimicrobial resistance genes (ARGs), multilocus sequencing typing (MLST), complete genome multilocus sequencing typing (cgMLST), average nucleotide identity (ANI), and single nucleotide polymorphism (SNP) analyses were performed using WGS.

View Article and Find Full Text PDF

Type III protein secretion systems (T3SSs) function as multiprotein devices that span the envelope of Gram-negative bacteria using the peptidoglycan (PG) layer as scaffold. This spatial arrangement explains why modifications in PG structure can alter T3SS activity. In incorporation of non-canonical D-amino acids in the PG was shown to decrease the activity of the T3SS encoded by the pathogenicity island-1 (SPI-1) without affecting other T3SS, like the flagellum apparatus.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!