The affinity of impienem (N-formimidoylthienamycin) for the penicillin-binding proteins of Staphylococcus aureus. Binding and release.
Terutaka Hashizume, Wan Park, Michio Matsuhashi
Abstract
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Terutaka Hashizume, Wan Park, Michio Matsuhashi
Abstract
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Penicillin-binding proteins 1, 2 and 3 in Staphylococcus aureus were found to possess common properties. All have very strong affinities for both benzylpenicillin and imipenem (N-formimidoylthienamycin), and all have an activity which releases bound imipenem, but not bound benzylpenicillin. Lower molecular weight penicillin-binding protein 4, which has a rather weak affinity for benzylpenicillin and also weak penicillinase activity showed an extraordinarily high affinity for imipenem but no antibiotic-releasing activity.
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Penicillin-binding proteins 1, 2 and 3 in Staphylococcus aureus were found to possess common properties. All have very strong affinities for both benzylpenicillin and imipenem (N-formimidoylthienamycin), and all have an activity which releases bound imipenem, but not bound benzylpenicillin. Lower molecular weight penicillin-binding protein 4, which has a rather weak affinity for benzylpenicillin and also weak penicillinase activity showed an extraordinarily high affinity for imipenem but no antibiotic-releasing activity.
Key concepts: Benzylpenicillin, Imipenem, Penicillin binding proteins, Penicillin, Staphylococcus aureus, Microbiology, Chemistry, Antibiotics