Reference : Δ2- and Δ3-Cephalosporins, penicillinate, and 6-unsubstituted penems. Intrinsic react...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83025
Δ2- and Δ3-Cephalosporins, penicillinate, and 6-unsubstituted penems. Intrinsic reactivity and interaction with β-lactamases and D-alanyl-D-alanine-cleaving serine peptidases
English
Frère, Jean-Marie mailto [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > >]
Kelly, Judith A [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > > >]
Klein, Daniel [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > > >]
Claes, Paul [Katholieke Universiteit Leuven - KUL > Rega Instituut > > >]
Vanderhaeghe, Hubert [Katholieke Universiteit Leuven - KUL > Rega Instituut > > >]
1-Apr-1982
Biochemical Journal
Portland Press
203
1
223-234
Yes (verified by ORBi)
International
0264-6021
1470-8728
London
United Kingdom
[en] actinomycetaceae/enzymology ; amides ; anti-bacterial agents/*metabolism ; carboxypeptidases/*metabolism ; cephalosporins/*metabolism ; chemical phenomena ; chemistry ; hydrolysis ; kinetics ; penicillins/*metabolism ; serine-type d-ala-d-ala carboxypeptidase ; streptomyces/enzymology ; structure-activity relationship ; beta-Lactamases/*metabolism ; beta-Lactams/metabolism
[en] The intrinsic reactivity of delta 2- and delta 3-deacetoxy-7-phenylacetamidocephalosporanates, penicillanate, unsubstituted, 2-methyl- and 2-phenyl-penems and other beta-lactam antibiotics has been expressed in terms of the second-order rate constant (M-1.s-1(OH-)) for the hydrolysis of the beta-lactam amide bond by OH- at 37 degrees C. The values thus obtained have been compared with the second-order rate constants (M-1.s-1(enzyme) for the opening of the same beta-lactam amide bond during interaction with the beta-lactamases of Streptomyces albus G and Actinomadura R39 and the D-alanyl-D-alanine-cleaving serine peptidases of Streptomyces R61 and Actinomadura R39. Depending on the cases, the accelerating effect due to enzyme action and expressed by the ratio M-1.s-1(enzyme)/M-1.s-1(OH) varies from less than 2 to more than 1 x 10(6). The primary parameter that governs enzyme action is the goodness of fit of the beta-lactam molecule to the enzyme cavity rather than its intrinsic reactivity. With the D-alanyl-D-alanine-cleaving serine peptidases, the three penems studied form intermediate complexes characterized by very short half lives of 14-100 s, values significantly lower than those exhibited by most beta-lactam compounds.
Fonds de la Recherche Scientifique Médicale - FRSM ; National Institutes of Health - NIH
Researchers ; Professionals
http://hdl.handle.net/2268/83025

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