Penicillin-binding proteins of Streptomyces cacaoi, Streptomyces olivaceus, and Streptomyces clavuligerus.
Penicillin-binding proteins of three Streptomyces strains, S. cacaoi, S. olivaceus, and S. clavuligerus, were examined by gel electrophoresis and fluorography. In a beta-lactamase producer, S. cacaoi, at least five membrane-bound penicillin-binding proteins were detected, but in two beta-lactam producers, S. olivaceus and S. clavuligerus, fewer penicillin-binding proteins were detected. Mecillinam and methicillin bound selectively to some penicillin-binding proteins in S. cacaoi, whereas they did not bind at all to those in S. olivaceus and S. clavuligerus. Clavulanic acid bound to penicillin-binding proteins only at a very high concentration in S. cacoi. This compound did not bind to those of S. olivaceus and S. clavuligerus. Penicillin-binding proteins in culture supernatant and cytoplasm and minimum inhibitory concentrations of these strains against benzylpenicillin were also examined.
D000560:Amdinocillin / Q000494:pharmacology; D008565:Membrane Proteins / Q000032:analysis*; D008712:Methicillin / Q000494:pharmacology; D010400:Penicillin G / Q000378:metabolism*; D010403:Penicillin Resistance; D011485:Protein Binding; D013302:Streptomyces / Q000032:analysis* / Q000187:drug effects; D001618:beta-Lactamases / Q000096:biosynthesis
D008565:Membrane Proteins; D001618:beta-Lactamases; D010400:Penicillin G; D008712:Methicillin; D000560:Amdinocillin