Amoxicillin is a semi-synthetic β-lactam antibiotic. Amoxicillin inhibits cross-linkage between the linear peptidoglycan polymer chains that make up a major component of the cell walls of both gram-positive and gram-negative bacteria.
Amoxicillin binds to penicillin-binding protein 1A (PBP-1A) located inside the bacterial cell well. Penicillins acylate the penicillin-sensitive transpeptidase C-terminal domain by opening the lactam ring. This inactivation of the enzyme prevents the formation of a cross-link of two linear peptidoglycan strands, inhibiting the third and last stage of bacterial cell wall synthesis. Cell lysis is then mediated by bacterial cell wall autolytic enzymes such as autolysins; it is possible that amoxicillin interferes with an autolysin inhibitor.
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