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Penicillin-binding protein 1 (PBP1) is a high-molecular-weight, membrane-associated enzyme found in many bacteria, including Staphylococcus aureus. It plays an essential role in the final stages of bacterial cell wall synthesis by catalyzing the cross-linking of peptidoglycan strands—a process critical for cell division and structural integrity. PBP1 is classified as a class B penicillin-binding protein: it has only transpeptidase activity and must partner with a separate transglycosylase like FtsW to complete peptidoglycan synthesis. PBPs are targets for β-lactam antibiotics which inhibit PBPs by covalently binding to their active sites, thereby blocking cell wall cross-linking and leading to bacterial death.
β-lactam antibiotics inhibit PBPs by covalently binding to their active sites, thereby blocking cell wall cross-linking and leading to bacterial death.
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