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See detailBeta-lactamases (Actinomycetes species)
Johnson, Kenneth; Duez, Colette ULg; Frère, Jean-Marie ULg et al

in Methods in Enzymology (1975), XLIII

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See detailDD-carboxypeptidase-transpeptidase and killing site of β-lactam antibiotics in Streptomyces strains R39, R61, and K11
Dusart, Jean; Marquet, Alberto; Ghuysen, Jean-Marie ULg et al

in Antimicrobial Agents and Chemotherapy (1973), 3(2), 181-187

Additional evidence is given that in Streptomyces strains R39, R61, and K11 the same enzyme performs dd-carboxypeptidase and transpeptidase activities and that this enzyme is the killing site of beta ... [more ▼]

Additional evidence is given that in Streptomyces strains R39, R61, and K11 the same enzyme performs dd-carboxypeptidase and transpeptidase activities and that this enzyme is the killing site of beta-lactam antibiotics. With strain R61, it was found that the exocellular enzyme has a sensitivity towards some antibiotics different from that of the membrane-bound enzyme. Under the growth conditions used in the present investigations, beta-lactamase activity was not involved in susceptibility to beta-lactam antibiotics. [less ▲]

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See detailExocellular β-lactamases of Streptomyces albus G and strains R39 and K11
Johnson, Kenneth; Dusart, Jean; Campbell, James N. et al

in Antimicrobial Agents and Chemotherapy (1973), 3(2), 289-298

The beta-lactamases excreted by the highly benzylpenicillin-susceptible Streptomyces strain R39 and the highly benzylpenicillin-resistant Streptomyces albus G were isolated and purified. Neither beta ... [more ▼]

The beta-lactamases excreted by the highly benzylpenicillin-susceptible Streptomyces strain R39 and the highly benzylpenicillin-resistant Streptomyces albus G were isolated and purified. Neither beta-lactamase exhibited dd-carboxypeptidase activity. Both were anionic at pH 8.3, did not require metal ions, and were not sensitive to iodine, but were inhibited by Cu(2+) and readily inactivated by heat. p-Chloromercuribenzoate, iodoacetate, p-aminobenzoate, and substrates and inhibitors of dd-carboxypeptidase had no effect on beta-lactamase activity. The K(m) and V(max) values for beta-lactamase activity were studied with 6-aminopenicillanic acid and with various penicillins and cephalosporins. The beta-lactamase from the related strain K11 of Streptomyces, which is intermediate in its susceptibility to benzylpenicillin, was partially purified, and its activity was compared on the various substrates. [less ▲]

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See detailPenicillin-sensitive DD-carboxypeptidases from Streptomyces strains R39 and K11
Leyh-Bouille, Mélina; Nakel, Marlies; Frère, Jean-Marie ULg et al

in Biochemistry (1972), 11(7), 1290-1298

The two penicillin-sensitive DD-carboxypeptidases from Streptomyces R39 and K11 are anionic at pH 8. They specifically recognize a C-terminal L-R3-D-alanyl-D sequence with a long side chain at the R3 ... [more ▼]

The two penicillin-sensitive DD-carboxypeptidases from Streptomyces R39 and K11 are anionic at pH 8. They specifically recognize a C-terminal L-R3-D-alanyl-D sequence with a long side chain at the R3 position. The two enzymes differ from each other with respect to: (1) the effects of ionic strength on activity, (2) the influence exerted on activity by the presence of a free amino group at the end of the L-R3 side chain, (3) the K3 and Vmax values. Enzyme K11 has Km values which are high for both good and poor substrates. The enzyme efficiency reflects itself in Vmax values which are high for good substrates and low for poor substrates. Enzyme R39 has Km values which are low for good substrates. The enzyme efficiency toward various substrates reflects itself in the Km and, to a lesser extent, in the Vmax values, (4) the effects of penicillin. Kinetically, inhibition of enzyme K11 by penicillin is competitive. On the contrary, inhibition of enzyme R39 by penicillin is noncompetitive and increasing penicillin concentrations cause disproportionate decreases in the catalytic rate. Noncompetitiveness cannot be attributed to an irreversible inactivation of the enzyme by penicillin. [less ▲]

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