dd -Carboxypeptidase-Transpeptidase and Killing Site of β-Lactam Antibiotics in Streptomyces Strains R39, R61, and K11
Copyright policy )dd -Carboxypeptidase-Transpeptidase and Killing Site of β-Lactam Antibiotics in Streptomyces Strains R39, R61, and K11
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 β-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, β-lactamase activity was not involved in susceptibility to β-lactam antibiotics.
- Spanish National Research Council Spain
- Service de Microbiologie France
- National Academies of Sciences, Engineering, and Medicine United States
- University of Liège Belgium
- National Institute for Medical Research Tanzania (United Republic of)
Carboxypeptidases, Biochimie, biophysique & biologie moléculaire, beta-Lactams, Microbiology, anti-bacterial agents, Microbiologie, acyltransferases metabolism, streptomyces/, penicillinase metabolism, beta-lactams, Penicillinase, Life sciences, carboxypeptidases, Streptomyces, Anti-Bacterial Agents, antagonists & inhibitors, drug effects, Sciences du vivant, pharmacology, metabolism, Acyltransferases, Biochemistry, biophysics & molecular biology
Carboxypeptidases, Biochimie, biophysique & biologie moléculaire, beta-Lactams, Microbiology, anti-bacterial agents, Microbiologie, acyltransferases metabolism, streptomyces/, penicillinase metabolism, beta-lactams, Penicillinase, Life sciences, carboxypeptidases, Streptomyces, Anti-Bacterial Agents, antagonists & inhibitors, drug effects, Sciences du vivant, pharmacology, metabolism, Acyltransferases, Biochemistry, biophysics & molecular biology
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