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Lipid II must translocate across the cell membrane to deliver and incorporate its disaccharide-pentapeptide "building block" into the peptidoglycan mesh. Lipid II is the target of several antibiotics. A number of analogous compounds are produced via a similar pathway in some bacteria, giving rise to cell wall modifications.
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.
Bacitracin is a polypeptide antibiotic derived from a bacterium, Bacillus subtilis, and acts against bacteria through the inhibition of cell wall synthesis. [6] It does this by inhibiting the removal of phosphate from lipid compounds, thus deactivating its function to transport peptidoglycan; the main component of bacterial cell membranes, to the microbial cell wall.
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 moenomycin family functions as an antibiotic by reversibly binding bacterial transglycosylases, essential enzymes that catalyze the extension of the glycan chain of the cell wall to form a stable peptidoglycan layer. The moenomycins mimic and thus compete with the natural substrate of the enzyme, inhibiting growth of the cell wall.
Since peptidoglycan is also lacking in L-form bacteria and in mycoplasmas, both are resistant against penicillin. Other steps of peptidoglycan synthesis can also be targeted. The topical antibiotic bacitracin targets the utilization of C55-isoprenyl pyrophosphate. Lantibiotics, which includes the food preservative nisin, attack lipid II. [36]
It is speculated that the added side chain mimics a longer segment of the peptidoglycan chain, more than ampicillin, and thus would bind more easily to the penicillin-binding proteins. Ureidopenicillins are not resistant to beta-lactamases. [citation needed]
Teicoplanin is a glycopeptide antibiotic that inhibits bacterial cell wall synthesis. It binds to the D-alanyl-D-alanine (D-Ala-D-Ala) terminus of the peptidoglycan precursor, preventing the transpeptidation reaction necessary for cell wall cross-linking.
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