Penicillin-binding proteins (PBPs) 5 and 6 of Escherichia coli released the bound penicilloyl moiety at an intermediate rate relative to, e.g., Staphylococcus aureus PBPs 4 (rapid) and 1 or 2 (slow). Each of these E. coli PBPs released the bound penicilloyl moiety as both penicilloic acid (hydrolysis) and phenylacetyl glycine (scission of the C-5--C-6 bond followed by hydrolysis).

All beta-lactam sensitive bacteria contain enzymatic penicillin binding proteins (PBPs), which are membrane-bound enzymes and targets of beta-lactam antibiotics. In this work evaluation of the significance of PBPs in immune response to benzylpenicillin was presented. 35 patients with allergic reactions to penicillin and 17 subjects without penicillin allergy, but exposed, were studied. Prolifer...

The peptidoglycan cell wall is a common target for antibiotic therapy, but its structure and assembly are only partially understood. Peptidoglycan synthesis requires a suite of penicillin-binding proteins (PBPs), the individual roles of which are difficult to determine because each enzyme is often dispensable for growth perhaps due to functional redundancy. To address this challenge, we sought ...

In competition assays for radiolabeled penicillin, penicillin-binding proteins (PBPs) 4, 7a, and 7b showed very high affinities for strong inducers of AmpC beta-lactamase. Loss of PBP 4 resulted in diminished inducibility. This suggests that if PBPs are involved in induction of AmpC beta-lactamase, there is probably a redundancy in function among the different PBPs.

OBJECTIVE Adherence to basic quality improvement principles enhances the implementation of potentially better practices (PBPs) and requires extensive planning and education. Even after PBPs have been identified and acknowledged as desirable, effective implementation of these practices does not occur easily. The objective of this study was to identify and assess implementation strategies that fa...

Penicillin-binding protein 2 (PBP-2) of Escherichia coli K-12 was purified by covalent affinity chromatography using 6-aminopenicillanic acid covalently coupled to carboxymethyl-Sepharose (6-APA-CM-Sepharose). Purification of PBP-2 was accomplished by prebinding the methoxy cephalosporin, cefoxitin, to the Triton X-100-solubilized PBPs of E. coli and then incubating the PBPs with 6-APA-CM-Sepha...

Examination of Bacillus subtilis strains containing multiple mutations affecting the class A high-molecular-weight penicillin-binding proteins (PBPs) 1, 2c, and 4 revealed a significant degree of redundancy in the functions of these three proteins. In rich media, loss of PBPs 2c and 4 resulted in no obvious phenotype. The slight growth and cell morphology defects associated with loss of PBP 1 w...

The high molecular weight penicillin-binding proteins (PBP(s) ) Bacillus subtilis PBPs 1, 2, and 4 and Bacillus stearothermophilus PBPs 1-4 were shown to catalyze peptidoglycan synthesis from the undecaprenol-containing lipid intermediate substrate in two assay systems. In a filter paper assay system, high levels of substrate polymerization occurred when reaction mixtures were incubated on What...

Penicillin-binding proteins (PBPs) are enzymes responsible for the polymerization of the glycan strand and the cross-linking between glycan chains as well as the target proteins for β-lactam antibiotics. Mutational alterations in PBPs can confer resistance either by reducing binding of the antibiotic to the active site or by evolving a β-lactamase activity that degrades the antibiotic. As no sy...

OBJECTIVE Part of the process of deriving and refining the CARE (communication, accountability, respect, empowerment) focus group's potentially better practices (PBPs) for multidisciplinary teamwork was to evaluate and experience the PBPs through implementation. METHODS The 4 neonatal intensive care units (NICUs) in the CARE focus group each worked with implementation of the PBPs. The choice ...