Penicillin-binding proteins (PBPs) have been scrutinized for over 40 years. Recent structural
information on PBPs together with the ongoing long-term biochemical experimental …

Although it is estimated that 20-30% of the general human population are carriers of
Staphylococcus aureus, this bacterium is one of the most important etiological agents …

Bacterial cell division and daughter cell formation are complex mechanisms whose details
are orchestrated by at least a dozen different proteins. Penicillin-binding proteins (PBPs) …

Peptidoglycan (PG) is an essential component in the cell wall of nearly all bacteria, forming
a continuous, mesh-like structure, called the sacculus, around the cytoplasmic membrane to …

Peptidoglycan glycosyltransferases (GTs) catalyze the polymerization step of cell-wall
biosynthesis, are membrane-bound, and are highly conserved across all bacteria. Long …

This review is an attempt to bring together and critically evaluate the now-abundant but
dispersed data concerning the lipid intermediates of the biosynthesis of bacterial …

The β-lactams are the most important class of antibiotics in clinical use. Their lethal targets
are the transpeptidase domains of penicillin binding proteins (PBPs), which catalyze the …

Abstract β-Lactamases (Bla) and low-affinity penicillin-binding proteins (PBP2A) are
responsible for β-lactam resistance in the genera Macrococcus, Mammaliicoccus and …

ABSTRACT Lactococcin 972 (Lcn972) is a nonlantibiotic bacteriocin that inhibits septum
biosynthesis in Lactococcus lactis rather than forming pores in the cytoplasmic membrane …

In Escherichia coli, the bifunctional penicillin-binding proteins (PBPs), PBP1A and PBP1B,
play critical roles in the final stage of peptidoglycan (PG) biosynthesis. These synthetic …