Reference : Interactions between beta-lactam antibiotics and isolated membranes of Streptococcus fae...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83079
Interactions between beta-lactam antibiotics and isolated membranes of Streptococcus faecalis ATCC 9790
English
Coyette, Jacques [Université de Liège - ULg > Faculté de Médecine > Service de Microbiologie > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine > Service de Microbiologie > > >]
Binot, Françoise [Université de Liège - ULg > Faculté de Médecine > Service de Microbiologie > >]
Adriaens, Paul [Katholieke Universiteit Leuven - KUL > Rega Instituut > > > >]
Meesschaert, Boudewijn [Katholieke Universiteit Leuven - KUL > Rega Instituut > > > >]
Vanderhaeghe, Hubert [Katholieke Universiteit Leuven - KUL > Rega Instituut > > > >]
2-May-1977
European Journal of Biochemistry
Blackwell Science
75
1
231-239
Yes (verified by ORBi)
International
0014-2956
1432-1033
Oxford
United Kingdom
[en] binding sites ; carboxypeptidases/*metabolism ; cell membrane/*enzymology ; enterococcus faecalis/*enzymology ; kinetics ; muramoylpentapeptide carboxypeptidase/*metabolism ; penicillin g/analogs & derivatives/*metabolism ; penicillins/*metabolism ; protein binding ; structure-activity relationship
[en] The DD-carboxypeptidase-exchange membrane-bound enzyme in Streptococcus faecalis ATCC 9790 reacts with beta-lactam antibiotics to form complexes with rather long half-lives. Depending upon the antibiotic, the second-order rate constants for complex formation range from 0.75-560 M-1 S-1 (at 37 degrees C and in water) and the first-order rate constants for complex breakdown range from 1.3 to 26 x 10(-5) s-1 (at 37 degrees C and in 5 mM phosphate buffer pH 7.5). There are about 30 pmol of DD-carboxypeptidase-exchange enzyme per mg of membrane protein. The degradation products arising from benzylpenicillin are phenylacetylglycine and probably N-formyl-D-penicillamine. Isolated membranes also contain other penicillin binding sites (about 70 pmol/mg membrane protein). That part of benzylpenicillin which reacts with at least some of these latter sites is slowly degraded into penicilloic acid. Normal functioning of the DD-carboxypeptidase-exchange membrane-bound enzyme is important, if not essential, for cell growth. With the beta-lactam antibiotics tested inhibition of cell growth is mainly related to the rates of formation of the inactive enzyme-antibiotic complexes. The relationship, however, is not a direct one probably due to the competitive effect exerted by the other penicillin binding sites.
National Institutes of Health - NIH ; Fonds de la Recherche Fondamentale Collective
Researchers ; Professionals
http://hdl.handle.net/2268/83079

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