Title : DD-carboxypeptidase-transpeptidase and killing site of beta-lactam antibiotics in Streptomyces strains R39, R61, and K11
Language : English
Author, co-author : Dusart, Jean [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
Marquet, Alberto [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
Frère, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > >]
Moreno, Ramon [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
Leyh-Bouille, Mélina [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
Johnson, Kenneth [National Research Council of Canada (Ottawa) > Division of Biological Sciences > > > >]
Lucchi, Chantal [> > > > >]
Perkins, Harnold R. [National Institute for Medical Research > > > > >]
Nieto, Manuel [Instituto de Biologia Celular > Centro de Investigaciones Biologicas > > > >]
Publication date : 2-Feb-1973
Journal title : Antimicrobial Agents and Chemotherapy
Publisher : American Society for Microbiology (ASM)
Volume : 3
Issue/season : 2
Pages : 181-187
Audience : International
ISSN : 0066-4804
e-ISSN : 1098-6596
City : Washington
Country : DC
Keywords : [en] acyltransferases metabolism ; anti-bacterial agents ; carboxypeptidases ; penicillinase metabolism ; streptomyces/ ; beta-lactams ; pharmacology ; antagonists & inhibitors ; metabolism ; drug effects
Abstract : [en] 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.
Funders : Fonds de la Recherche Fondamentale Collective
Target : Researchers ; Professionals
Permalink : http://hdl.handle.net/2268/83536