Reference : Interaction between penicillin and the DD-carboxypeptidase of the unstable L-form of Pro...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83044
Interaction between penicillin and the DD-carboxypeptidase of the unstable L-form of Proteus mirabilis strain 19
English
Schilf, Wolfgang [Technische Hochschule (Darmstadt) > Institut fur Mikrobiologie, Fachbereich Biologie > > > >]
Frere, Philippe [Ateliers des Constructions Electriques de Charleroi > Centre de Calcul > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Faculté de Médecine > Service de Microbiologie > >]
Martin, Hans-Herbert [Technische Hochschule Darmstadt > Institut fur Mikrobiologie, Fachbereich Biologie > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine > Service de Microbiologie > >]
Adriaens, Paul [Université Catholique de Louvain - UCL > Rega Instituut > Afdeling Microbiologie > >]
Meesschaert, Boudewijn [Université Catholique de Louvain - UCL > Rega Instituut > Afdeling Microbiologie > >]
17-Apr-1978
European Journal of Biochemistry
Blackwell Science
85
2
325-330
Yes (verified by ORBi)
International
0014-2956
1432-1033
Oxford
United Kingdom
[en] carboxypeptidases/metabolism ; kinetics ; mathematics ; penicillins ; protein binding ; proteus mirabilis/*enzymology ; spheroplasts/enzymology
[en] Binding of penicillin to the DD-carboxypeptidase of the unstable spheroplast L-form of Proteus mirabilis results in the rapid formation of a modified enzyme-inhibitor complex which in turn undergoes rapid decay into reactivated enzyme and an antibiotically inactive penicillin degradation product. Major antibiotic metabolites recovered from such interactions were benzylpenicilloic acid and phenoxymethylpenicilloic acid from benzylpenicillin and phenoxymethylpenicillin, respectively, suggesting a second enzymic function of the DD-carboxypeptidase as a penicillinase of low efficiency. Statistical analyses made with the help of a linear regression program show that the enzyme interacts with the substrate UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-(L)-meso-2,6-diaminopimelyl -(L)-D-alanyl-D-alanine and either benzympenicillin or carbenicillin in a non-competitive manner.
National Institutes of Health - NIH
Researchers ; Professionals
http://hdl.handle.net/2268/83044

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