Reference : Interaction between beta-lactam antibiotics and exocellular DD-carboxypeptidase-trans...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83087
Interaction between beta-lactam antibiotics and exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61
English
Frère, Jean-Marie mailto [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 > > >]
Ghuysen, Jean-Marie [ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
Perkins, Harnold R [National Institute for Medical Research > > > > >]
16-Dec-1974
European Journal of Biochemistry
Blackwell Science
50
1
203-214
Yes (verified by ORBi)
International
0014-2956
1432-1033
Oxford
United Kingdom
[en] acyltransferases/*metabolism ; anti-bacterial agents/*pharmacology ; carbenicillin/pharmacology ; carboxypeptidases/*metabolism ; cephalosporins/pharmacology ; kinetics ; penicillin g/pharmacology ; penicillin v/pharmacology ; peptidoglycan ; protein binding ; streptomyces/*enzymology ; beta-lactams/*pharmacology
[en] On the basis of steady-state kinetics, inhibition of the exocellular dd-carboxypeptidase-trans-peptidase of Streptomyces R61 by β-lactam antibiotics was competitive with regard to the donor substrate. However, the complexes formed between the Streptomyces R61 enzyme and various β-lactam antibiotics were relatively stable, exhibiting half-lives of 40 to 80 min at 37°C and neutral pH. During breakdown of the complexes the protein underwent reactivation, whereas the released antibiotic molecule was chemically altered. With [14C]benzylpenicillin, the released compound was neither benzylpenicillin nor benzylpenicilloic acid. The properties of the Streptomyces R61 enzyme β-lactam antibiotic complexes were compared with those of the complexes formed between the same antibiotics and either the membrane-bound transpeptidase from Streptomyces R61 or the exocellular dd-carboxypeptidase-transpeptidase of Streptomyces R39.
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/83087
also: http://hdl.handle.net/2268/83121
10.1111/j.1432-1033.1974.tb03889.x

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