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Penicillinase was the first β-lactamase to be identified. It was first isolated by Abraham and Chain in 1940 from E. coli (which are gram-negative) even before penicillin entered clinical use, [ 5 ] but penicillinase production quickly spread to bacteria that previously did not produce it or produced it only rarely.
β-Lactam antibiotics are indicated for the prevention and treatment of bacterial infections caused by susceptible organisms. At first, β-lactam antibiotics were mainly active only against gram-positive bacteria, yet the recent development of broad-spectrum β-lactam antibiotics active against various gram-negative organisms has increased their usefulness.
Penicillin resistance in Staphylococcus aureus [3] appeared very soon after penicillin entered general clinical use in 1943, and the mechanism of resistance was the production of β-lactamase. Modification of the penicillin molecule so that it was resistant to being broken down by β-lactamase was able to temporarily overcome this problem.
Penicillin can easily enter bacterial cells in the case of Gram-positive species. This is because Gram-positive bacteria do not have an outer cell membrane and are simply enclosed in a thick cell wall. [45] Penicillin molecules are small enough to pass through the spaces of glycoproteins in the cell wall.
Some sources identify them with antipseudomonal penicillins, [2] others consider these types to be distinct. [3] This group includes the carboxypenicillins and the ureidopenicillins . Aminopenicillins , in contrast, do not have activity against Pseudomonas species, as their positively charged amino group does not hinder degradation by ...
PBPs normally catalyze the cross-linking of the bacterial cell wall, but they can be permanently inhibited by penicillin and other β-lactam antibiotics. (NAM = N-acetylmuramic acid; NAG = N-acetylglucosamine) [2] Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin.
Penicillinase is a bacterial enzyme produced by bacteria resistant to other β-lactam antibiotics which hydrolyses the antibiotic, rendering it non-functional. Methicillin is not bound and hydrolysed by penicillinase, meaning it can kill the bacteria, even if this enzyme is present.
The Eagle effect, Eagle phenomenon, or paradoxical zone phenomenon, named after Harry Eagle who first described it, originally referred to the paradoxically reduced antibacterial effect of penicillin at high doses, [1] [2] though recent usage generally refers to the relative lack of efficacy of beta lactam antibacterial drugs on infections having large numbers of bacteria. [3]