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β-Lactam antibiotics are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, [ 6 ] especially in gram-positive organisms, being the outermost and primary component of the wall.
The β-lactam ring is part of the core structure of several antibiotic families, the principal ones being the penicillins, cephalosporins, carbapenems, and monobactams, which are, therefore, also called β-lactam antibiotics. Nearly all of these antibiotics work by inhibiting bacterial cell wall biosynthesis.
The bactericidal effects of β-lactam antibiotics are achieved through inhibition of the bacterial cell wall synthesis. The cell wall of both gram-positive and gram-negative bacteria is a tight covalently bound and cross-linked peptidoglycan network and essential for bacterial growth, cell division and cellular structure.
Bacterial cell wall synthesis and the role of PBPs in its synthesis is a very good target for drugs of selective toxicity because the metabolic pathways and enzymes are unique to bacteria. [10] Resistance to antibiotics has come about through overproduction of PBPs and formation of PBPs that have low affinity for penicillins (among other ...
Prevents bacterial cell division by inhibiting cell wall synthesis. Carbapenems; Ertapenem: Invanz: Bactericidal for both Gram-positive and Gram-negative organisms and therefore useful for empiric broad-spectrum antibacterial coverage. (Notes: MRSA resistance to this class. All are active against Pseudomonas aeruginosa except ertapenem.)
Cephalosporins are bactericidal and, like other β-lactam antibiotics, disrupt the synthesis of the peptidoglycan layer forming the bacterial cell wall. The peptidoglycan layer is important for cell wall structural integrity. The final transpeptidation step in the synthesis of the peptidoglycan is facilitated by penicillin-binding proteins ...
The structure of a Streptomyces serine β-lactamase (SBLs) is given by 1BSG.The alpha-beta fold (InterPro: IPR012338) resembles that of a DD-transpeptidase, from which the enzyme is thought to have evolved. β-lactam antibiotics bind to DD-transpeptidases to inhibit bacterial cell wall biosynthesis.
Those that target the bacterial cell wall (penicillins and cephalosporins) or the cell membrane , or interfere with essential bacterial enzymes (rifamycins, lipiarmycins, quinolones, and sulfonamides) have bactericidal activities, killing the bacteria.
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