Open AccessExocellular β-Lactamases of Streptomyces albus G and Strains R39 and K11
Author(s) -
Kenneth G. Johnson,
Jean Dusart,
James N. Campbell,
JeanMarie Ghuysen
Publication year - 1973
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.3.2.289
Subject(s) - benzylpenicillin , streptomyces albus , streptomyces , carboxypeptidase , strain (injury) , streptomycetaceae , biochemistry , actinomycetales , chemistry , enzyme , microbiology and biotechnology , cephalosporin , bacteria , stereochemistry , biology , antibiotics , penicillin , anatomy , genetics
The β-lactamases excreted by the highly benzylpenicillin-susceptibleStreptomyces strain R39 and the highly benzylpenicillin-resistantStreptomyces albus G were isolated and purified. Neither β-lactamase exhibiteddd -carboxypeptidase activity. Both were anionic atp H 8.3, did not require metal ions, and were not sensitive to iodine, but were inhibited by Cu2+ and readily inactivated by heat.p -Chloromercuribenzoate, iodoacetate,p -aminobenzoate, and substrates and inhibitors ofdd -carboxypeptidase had no effect on β-lactamase activity. TheK m andV max values for β-lactamase activity were studied with 6-aminopenicillanic acid and with various penicillins and cephalosporins. The β-lactamase from the related strain K11 ofStreptomyces , which is intermediate in its susceptibility to benzylpenicillin, was partially purified, and its activity was compared on the various substrates.